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Conserved domains on  [gi|110735404|ref|NP_573439|]
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receptor-type tyrosine-protein phosphatase U isoform 1 precursor [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
933-1137 6.10e-160

catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


:

Pssm-ID: 350480 [Multi-domain]  Cd Length: 205  Bit Score: 479.55  E-value: 6.10e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  933 YINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPEDSDTYGDIKIMLVKTETL 1012
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDTYGDIKITLLKTETL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1013 AEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLDVML 1092
Cdd:cd14632    81 AEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYIVLDVML 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 110735404 1093 DMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLC 1137
Cdd:cd14632   161 DMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACLC 205
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
1222-1428 6.31e-153

PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


:

Pssm-ID: 350485 [Multi-domain]  Cd Length: 207  Bit Score: 461.30  E-value: 6.31e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1222 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAWPCLQYWPEPGRQQYGLMEVEFMSGT 1301
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAWPCLQYWPEPGLQQYGPMEVEFVSGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1302 ADEDLVARVFRVQNISRLQEGHLLVRHFQFLRWSAYRDTPDSKKAFLHLLAEVDKWQAESGDGRTIVHCLNGGGRSGTFC 1381
Cdd:cd14637    81 ADEDIVTRLFRVQNITRLQEGHLMVRHFQFLRWSAYRDTPDSKKAFLHLLASVEKWQRESGEGRTVVHCLNGGGRSGTYC 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 110735404 1382 ACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1428
Cdd:cd14637   161 ASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
22-186 7.08e-57

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


:

Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 194.10  E-value: 7.08e-57
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404     22 TPAAGCTFEEASdpavPCEYSQAQYDDFQWEQVRIHPGTRAP---ADLPHGSYLMVNTSQHAPGQRAHVIFQSLSEN-DT 97
Cdd:smart00137    1 TSPGNCDFEEGS----TCGWHQDSNDDGHWERVSSATGIPGPnrdHTTGNGHFMFFETSSGAEGQTARLLSPPLYENrST 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404     98 HCVQFSYFLYsrdGHSPGTLGVYVRVNGGPLGSAVWNMTGSHGRQWHQAELAVSTfWPNEYQVLFEALISPDRRGYMGLD 177
Cdd:smart00137   77 HCLTFWYYMY---GSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALD 152

                    ....*....
gi 110735404    178 DILLLSYPC 186
Cdd:smart00137  153 DILLSNGPC 161
fn3 pfam00041
Fibronectin type III domain;
494-577 3.85e-14

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 68.98  E-value: 3.85e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404   494 LTFTPL-EDMIFLKWEEPQEPNGLITQYEISYQSIESSDPAVNVPGPRrtisklrNETYHVFSNLHPGTTYLFSVRARTG 572
Cdd:pfam00041    6 LTVTDVtSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPG-------TTTSVTLTGLKPGTEYEVRVQAVNG 78

                   ....*
gi 110735404   573 KGFGQ 577
Cdd:pfam00041   79 GGEGP 83
FN3 super family cl27307
Fibronectin type 3 domain [General function prediction only];
347-624 1.37e-11

Fibronectin type 3 domain [General function prediction only];


The actual alignment was detected with superfamily member COG3401:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 69.26  E-value: 1.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  347 LDPDTEYEISVLLTrpGDGGTGRPGPPlISRTKCAEPMRAPKGLAFAEIQARQLTLQWEP------LGYNVTRchtytvs 420
Cdd:COG3401   199 IEPGTTYYYRVAAT--DTGGESAPSNE-VSVTTPTTPPSAPTGLTATADTPGSVTLSWDPvtesdaTGYRVYR------- 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  421 lcyhytlGSSHNQTIREcVKTEQGVSrYTIKNLLPYRNVHVRLVLTNPEGRKEGK--EVTFQTDEDVPSgiAAESLTFTP 498
Cdd:COG3401   269 -------SNSGDGPFTK-VATVTTTS-YTDTGLTNGTTYYYRVTAVDAAGNESAPsnVVSVTTDLTPPA--APSGLTATA 337
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  499 LEDM-IFLKWEEPQEPNglITQYEIsYQSIESSdpavnvpGPRRTISKLRNETYHVFSNLHPGTTYLFSVRARTGKGfgq 577
Cdd:COG3401   338 VGSSsITLSWTASSDAD--VTGYNV-YRSTSGG-------GTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAG--- 404
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 110735404  578 aalteittNISAPSFDYADMPSPLGESENTITVLLRPAQGRGAPISV 624
Cdd:COG3401   405 --------NESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATA 443
fn3 pfam00041
Fibronectin type III domain;
291-365 2.92e-06

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 46.64  E-value: 2.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404   291 PPQLLRA---GPTYLIIQLNTNSIiGDGPIVRKEIEYRMARGPWAEVHAV---SLQTYKLWHLDPDTEYEISVlLTRPGD 364
Cdd:pfam00041    2 APSNLTVtdvTSTSLTVSWTPPPD-GNGPITGYEVEYRPKNSGEPWNEITvpgTTTSVTLTGLKPGTEYEVRV-QAVNGG 79

                   .
gi 110735404   365 G 365
Cdd:pfam00041   80 G 80
 
Name Accession Description Interval E-value
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
933-1137 6.10e-160

catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350480 [Multi-domain]  Cd Length: 205  Bit Score: 479.55  E-value: 6.10e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  933 YINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPEDSDTYGDIKIMLVKTETL 1012
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDTYGDIKITLLKTETL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1013 AEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLDVML 1092
Cdd:cd14632    81 AEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYIVLDVML 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 110735404 1093 DMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLC 1137
Cdd:cd14632   161 DMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACLC 205
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
1222-1428 6.31e-153

PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350485 [Multi-domain]  Cd Length: 207  Bit Score: 461.30  E-value: 6.31e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1222 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAWPCLQYWPEPGRQQYGLMEVEFMSGT 1301
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAWPCLQYWPEPGLQQYGPMEVEFVSGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1302 ADEDLVARVFRVQNISRLQEGHLLVRHFQFLRWSAYRDTPDSKKAFLHLLAEVDKWQAESGDGRTIVHCLNGGGRSGTFC 1381
Cdd:cd14637    81 ADEDIVTRLFRVQNITRLQEGHLMVRHFQFLRWSAYRDTPDSKKAFLHLLASVEKWQRESGEGRTVVHCLNGGGRSGTYC 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 110735404 1382 ACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1428
Cdd:cd14637   161 ASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
908-1133 2.73e-104

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 331.13  E-value: 2.73e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404   908 RQEPMPAYDRHRVKLHPmlGDPNADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVK 987
Cdd:pfam00102    6 RYKDVLPYDHTRVKLTG--DPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKGREK 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404   988 CSRYWP---EDSDTYGDIKIMLVKTET-LAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKAS 1063
Cdd:pfam00102   84 CAQYWPeeeGESLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLRKVRKS 163
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110735404  1064 TP-PDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1133
Cdd:pfam00102  164 SLdGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
883-1133 1.59e-103

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 330.01  E-value: 1.59e-103
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404    883 GFKQEYESFFEGWDATKKKDKvkGSRQEPM--------PAYDRHRVKLHPMLGDPNaDYINANYIDGYHRSNHFIATQGP 954
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCTV--AAFPENRdknrykdvLPYDHTRVKLKPPPGEGS-DYINASYIDGPNGPKAYIATQGP 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404    955 KPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPEDSD---TYGDIKIMLVKTETLAEYVVRTFALERRGYSARH 1031
Cdd:smart00194   78 LPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGeplTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETR 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404   1032 EVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLC 1111
Cdd:smart00194  158 TVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELR 237
                           250       260
                    ....*....|....*....|..
gi 110735404   1112 SRRVNMIQTEEQYIFIHDAILE 1133
Cdd:smart00194  238 SQRPGMVQTEEQYIFLYRAILE 259
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1165-1428 1.35e-84

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 277.23  E-value: 1.35e-84
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404   1165 QLREEFQTLNSVTPplDVEECSIALLPRNRDKNRSMDVLPPDRCLPFLISTDGDSNNYINAALTDSYTRSAAFIVTLHPL 1244
Cdd:smart00194    1 GLEEEFEKLDRLKP--DDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPL 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404   1245 QSTTPDFWRLVYDYGCTSIVMLNQLNqSNSAWPCLQYWPEPGR--QQYGLMEVEFMSGTADEDLVARVFRVQNISrlQEG 1322
Cdd:smart00194   79 PSTVEDFWRMVWEQKVTVIVMLTELV-EKGREKCAQYWPDEEGepLTYGDITVTLKSVEKVDDYTIRTLEVTNTG--CSE 155
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404   1323 HLLVRHFQFLRWSaYRDTPDSKKAFLHLLAEVDKWQaESGDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAA 1402
Cdd:smart00194  156 TRTVTHYHYTNWP-DHGVPESPESILDLIRAVRKSQ-STSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIV 233
                           250       260
                    ....*....|....*....|....*.
gi 110735404   1403 KTLRNYKPNMVETMDQYHFCYDVALE 1428
Cdd:smart00194  234 KELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1193-1428 2.52e-71

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 238.30  E-value: 2.52e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  1193 NRDKNRSMDVLPPDRCLPFLISTDGDSNnYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQS 1272
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGPSD-YINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  1273 NSAwPCLQYWPEP--GRQQYGLMEVEFMSGTADE-DLVARVFRVQNISRlQEGHLlVRHFQFLRWSAyRDTPDSKKAFLH 1349
Cdd:pfam00102   80 GRE-KCAQYWPEEegESLEYGDFTVTLKKEKEDEkDYTVRTLEVSNGGS-EETRT-VKHFHYTGWPD-HGVPESPNSLLD 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110735404  1350 LLAEVDKWQAESGDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1428
Cdd:pfam00102  156 LLRKVRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
22-186 7.08e-57

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 194.10  E-value: 7.08e-57
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404     22 TPAAGCTFEEASdpavPCEYSQAQYDDFQWEQVRIHPGTRAP---ADLPHGSYLMVNTSQHAPGQRAHVIFQSLSEN-DT 97
Cdd:smart00137    1 TSPGNCDFEEGS----TCGWHQDSNDDGHWERVSSATGIPGPnrdHTTGNGHFMFFETSSGAEGQTARLLSPPLYENrST 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404     98 HCVQFSYFLYsrdGHSPGTLGVYVRVNGGPLGSAVWNMTGSHGRQWHQAELAVSTfWPNEYQVLFEALISPDRRGYMGLD 177
Cdd:smart00137   77 HCLTFWYYMY---GSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALD 152

                    ....*....
gi 110735404    178 DILLLSYPC 186
Cdd:smart00137  153 DILLSNGPC 161
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
27-187 9.29e-51

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 176.40  E-value: 9.29e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404    27 CTFEEASDpavpCEYSQAQYDDFQWEQVRIHPGTRAPA-----DLPHGSYLMVNTSQHAPGQRAHVIFQSLSENDT-HCV 100
Cdd:pfam00629    1 CDFEDGNL----CGWTQDSSDDFDWERVSGPSVKTGPSsdhtqGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSpQCL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404   101 QFSYFLYsrdGHSPGTLGVYVRVNGGPLGSAVWNMTGSHGRQWHQAELAVSTFwPNEYQVLFEALISPDRRGYMGLDDIL 180
Cdd:pfam00629   77 RFWYHMS---GSGVGTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSS-TQPFQVVFEGIRGGGSRGGIALDDIS 152

                   ....*..
gi 110735404   181 LLSYPCA 187
Cdd:pfam00629  153 LSSGPCP 159
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
27-186 8.26e-48

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 167.94  E-value: 8.26e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404   27 CTFEEAsdpavPCEYSQAQYDDFQWEQVRIHPGTRAPADL-----PHGSYLMVNTSQHAPGQRAHVIFQSLSEN-DTHCV 100
Cdd:cd06263     1 CDFEDG-----LCGWTQDSTDDFDWTRVSGSTPSPGTPPDhthgtGSGHYLYVESSSGREGQKARLLSPLLPPPrSSHCL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  101 QFSYFLYsrdGHSPGTLGVYVRVNGGPLGSAVWNMTGSHGRQWHQAELAVSTFWpNEYQVLFEALISPDRRGYMGLDDIL 180
Cdd:cd06263    76 SFWYHMY---GSGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASS-KPFQVVFEGVRGSGSRGDIALDDIS 151

                  ....*.
gi 110735404  181 LLSYPC 186
Cdd:cd06263   152 LSPGPC 157
PHA02738 PHA02738
hypothetical protein; Provisional
895-1131 2.10e-46

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 170.11  E-value: 2.10e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  895 WDATKKKDKVkgSRQEPMPAYDRHRVKLhPMLGDpNADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSI 974
Cdd:PHA02738   43 FNAEKKNRKL--NRYLDAVCFDHSRVIL-PAERN-RGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQII 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  975 VMITKLVEVGRVKCSRYWP--EDSD-TYGDIKIMLVKTETLAEYVVRTFALErRGYSARHEVRQFHFTAWPEHGVPYHAT 1051
Cdd:PHA02738  119 VMLCKKKENGREKCFPYWSdvEQGSiRFGKFKITTTQVETHPHYVKSTLLLT-DGTSATQTVTHFNFTAWPDHDVPKNTS 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1052 GLLAFIRRVKA----------------STPPdagPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRV 1115
Cdd:PHA02738  198 EFLNFVLEVRQcqkelaqeslqighnrLQPP---PIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRY 274
                         250
                  ....*....|....*.
gi 110735404 1116 NMIQTEEQYIFIHDAI 1131
Cdd:PHA02738  275 YSLFIPFQYFFCYRAV 290
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
929-1127 3.83e-34

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 133.29  E-value: 3.83e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  929 PNADYINANYIDGYhRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVG--RVKCSRYWPEDSDtYG--DIKI 1004
Cdd:COG5599    61 ANLGYLNANYIQVI-GNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISkpKVKMPVYFRQDGE-YGkyEVSS 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1005 MLVKTETLAEYV-VRTFALERRGYSAR-HEVRQFHFTAWPEHGVPyHATGLLAFIRRVKAS---TPPDAGPIVIHCSAGT 1079
Cdd:COG5599   139 ELTESIQLRDGIeARTYVLTIKGTGQKkIEIPVLHVKNWPDHGAI-SAEALKNLADLIDKKekiKDPDKLLPVVHCRAGV 217
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 110735404 1080 GRTGCYIVLDVMLDM--AECEGVVDIYNCVKTL-CSRRVNMIQTEEQYIFI 1127
Cdd:COG5599   218 GRTGTLIACLALSKSinALVQITLSVEEIVIDMrTSRNGGMVQTSEQLDVL 268
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
1191-1430 2.09e-23

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 102.77  E-value: 2.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1191 PRNRDKNRSMDVLPPDRCLPFLISTDGDSNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLN 1270
Cdd:PHA02747   49 PENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPTK 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1271 QSNSAWPCLQYW--PEPGRQQYGLMEVEFMSGTADEDLVARVFRVQNisRLQEGHLLVRHFQFLRWSAYrDTPDSKKAFL 1348
Cdd:PHA02747  129 GTNGEEKCYQYWclNEDGNIDMEDFRIETLKTSVRAKYILTLIEITD--KILKDSRKISHFQCSEWFED-ETPSDHPDFI 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1349 HLLAEVDKWQAESGDGRT---------IVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQY 1419
Cdd:PHA02747  206 KFIKIIDINRKKSGKLFNpkdallcpiVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDY 285
                         250
                  ....*....|....
gi 110735404 1420 HF---CYDVALEYL 1430
Cdd:PHA02747  286 LFiqpGYEVLHYFL 299
fn3 pfam00041
Fibronectin type III domain;
494-577 3.85e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 68.98  E-value: 3.85e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404   494 LTFTPL-EDMIFLKWEEPQEPNGLITQYEISYQSIESSDPAVNVPGPRrtisklrNETYHVFSNLHPGTTYLFSVRARTG 572
Cdd:pfam00041    6 LTVTDVtSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPG-------TTTSVTLTGLKPGTEYEVRVQAVNG 78

                   ....*
gi 110735404   573 KGFGQ 577
Cdd:pfam00041   79 GGEGP 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
484-585 1.68e-13

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 67.52  E-value: 1.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  484 DVPSGIAAESLTftplEDMIFLKWEEPQEPNGLITQYEISYQSIESSDPA-VNVPGPrrtisklrNETYHVFSNLHPGTT 562
Cdd:cd00063     2 SPPTNLRVTDVT----STSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKeVEVTPG--------SETSYTLTGLKPGTE 69
                          90       100
                  ....*....|....*....|....
gi 110735404  563 YLFSVRARTGKGFGQAA-LTEITT 585
Cdd:cd00063    70 YEFRVRAVNGGGESPPSeSVTVTT 93
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
347-624 1.37e-11

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 69.26  E-value: 1.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  347 LDPDTEYEISVLLTrpGDGGTGRPGPPlISRTKCAEPMRAPKGLAFAEIQARQLTLQWEP------LGYNVTRchtytvs 420
Cdd:COG3401   199 IEPGTTYYYRVAAT--DTGGESAPSNE-VSVTTPTTPPSAPTGLTATADTPGSVTLSWDPvtesdaTGYRVYR------- 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  421 lcyhytlGSSHNQTIREcVKTEQGVSrYTIKNLLPYRNVHVRLVLTNPEGRKEGK--EVTFQTDEDVPSgiAAESLTFTP 498
Cdd:COG3401   269 -------SNSGDGPFTK-VATVTTTS-YTDTGLTNGTTYYYRVTAVDAAGNESAPsnVVSVTTDLTPPA--APSGLTATA 337
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  499 LEDM-IFLKWEEPQEPNglITQYEIsYQSIESSdpavnvpGPRRTISKLRNETYHVFSNLHPGTTYLFSVRARTGKGfgq 577
Cdd:COG3401   338 VGSSsITLSWTASSDAD--VTGYNV-YRSTSGG-------GTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAG--- 404
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 110735404  578 aalteittNISAPSFDYADMPSPLGESENTITVLLRPAQGRGAPISV 624
Cdd:COG3401   405 --------NESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATA 443
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
486-576 1.55e-10

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 58.78  E-value: 1.55e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404    486 PSGIAAESLTftplEDMIFLKWEEPQEPNGL--ITQYEISYQSIESSDPAVNVPGprrtisklrNETYHVFSNLHPGTTY 563
Cdd:smart00060    4 PSNLRVTDVT----STSVTLSWEPPPDDGITgyIVGYRVEYREEGSEWKEVNVTP---------SSTSYTLTGLKPGTEY 70
                            90
                    ....*....|...
gi 110735404    564 LFSVRARTGKGFG 576
Cdd:smart00060   71 EFRVRAVNGAGEG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
386-481 4.77e-07

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 49.03  E-value: 4.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  386 APKGLAFAEIQARQLTLQWEPLGYNVTRCHTYTVSLCyhytlgSSHNQTIRECVKTEQGVSRYTIKNLLPYRNVHVRLVL 465
Cdd:cd00063     3 PPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYR------EKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRA 76
                          90
                  ....*....|....*..
gi 110735404  466 TNPEGR-KEGKEVTFQT 481
Cdd:cd00063    77 VNGGGEsPPSESVTVTT 93
fn3 pfam00041
Fibronectin type III domain;
291-365 2.92e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 46.64  E-value: 2.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404   291 PPQLLRA---GPTYLIIQLNTNSIiGDGPIVRKEIEYRMARGPWAEVHAV---SLQTYKLWHLDPDTEYEISVlLTRPGD 364
Cdd:pfam00041    2 APSNLTVtdvTSTSLTVSWTPPPD-GNGPITGYEVEYRPKNSGEPWNEITvpgTTTSVTLTGLKPGTEYEVRV-QAVNGG 79

                   .
gi 110735404   365 G 365
Cdd:pfam00041   80 G 80
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
386-471 1.25e-04

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 42.22  E-value: 1.25e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404    386 APKGLAFAEIQARQLTLQWEPLGYNVTRChtYTVslcyHYTLGSSHNQTIRECVKTEQGVSRYTIKNLLPYRNVHVRLVL 465
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDGITG--YIV----GYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRA 76

                    ....*.
gi 110735404    466 TNPEGR 471
Cdd:smart00060   77 VNGAGE 82
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
286-357 1.58e-04

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 41.83  E-value: 1.58e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110735404    286 PTPIAPPQLLRAGPTYLIIQ-LNTNSIIGDGPIVRKEIEYRMARGPWAEVHAVSLQT-YKLWHLDPDTEYEISV 357
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSwEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTsYTLTGLKPGTEYEFRV 74
fn3 pfam00041
Fibronectin type III domain;
386-467 9.30e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 39.71  E-value: 9.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404   386 APKGLAFAEIQARQLTLQWEP--------LGYNVTRCHTYTVSLCYHYTLGSSHNqtirecvkteqgvsRYTIKNLLPYR 457
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPppdgngpiTGYEVEYRPKNSGEPWNEITVPGTTT--------------SVTLTGLKPGT 67
                           90
                   ....*....|
gi 110735404   458 NVHVRLVLTN 467
Cdd:pfam00041   68 EYEVRVQAVN 77
 
Name Accession Description Interval E-value
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
933-1137 6.10e-160

catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350480 [Multi-domain]  Cd Length: 205  Bit Score: 479.55  E-value: 6.10e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  933 YINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPEDSDTYGDIKIMLVKTETL 1012
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDTYGDIKITLLKTETL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1013 AEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLDVML 1092
Cdd:cd14632    81 AEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYIVLDVML 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 110735404 1093 DMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLC 1137
Cdd:cd14632   161 DMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACLC 205
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
1222-1428 6.31e-153

PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350485 [Multi-domain]  Cd Length: 207  Bit Score: 461.30  E-value: 6.31e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1222 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAWPCLQYWPEPGRQQYGLMEVEFMSGT 1301
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAWPCLQYWPEPGLQQYGPMEVEFVSGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1302 ADEDLVARVFRVQNISRLQEGHLLVRHFQFLRWSAYRDTPDSKKAFLHLLAEVDKWQAESGDGRTIVHCLNGGGRSGTFC 1381
Cdd:cd14637    81 ADEDIVTRLFRVQNITRLQEGHLMVRHFQFLRWSAYRDTPDSKKAFLHLLASVEKWQRESGEGRTVVHCLNGGGRSGTYC 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 110735404 1382 ACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1428
Cdd:cd14637   161 ASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
933-1136 8.95e-147

catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The type II (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350403 [Multi-domain]  Cd Length: 204  Bit Score: 444.74  E-value: 8.95e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  933 YINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPEDSDTYGDIKIMLVKTETL 1012
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEVYGDIKVTLVETEPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1013 AEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLDVML 1092
Cdd:cd14555    81 AEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYIVIDIML 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 110735404 1093 DMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACL 1136
Cdd:cd14555   161 DMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILEACL 204
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
868-1136 9.33e-140

catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350481 [Multi-domain]  Cd Length: 273  Bit Score: 429.08  E-value: 9.33e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  868 DLLQHINQMKTAEGYGFKQEYESFFEG----WDATKKKDKVKGSRQEPMPAYDRHRVKLHPMLGDPNADYINANYIDGYH 943
Cdd:cd14633     1 DLLQHITQMKCAEGYGFKEEYESFFEGqsapWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  944 RSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPEDSDTYGDIKIMLVKTETLAEYVVRTFALE 1023
Cdd:cd14633    81 RPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1024 RRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDI 1103
Cdd:cd14633   161 KRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDI 240
                         250       260       270
                  ....*....|....*....|....*....|...
gi 110735404 1104 YNCVKTLCSRRVNMIQTEEQYIFIHDAILEACL 1136
Cdd:cd14633   241 YNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 273
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
919-1136 2.46e-123

catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350479 [Multi-domain]  Cd Length: 218  Bit Score: 382.45  E-value: 2.46e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  919 RVKLHPMLGDPNADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPEDSDT 998
Cdd:cd14631     1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  999 YGDIKIMLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAG 1078
Cdd:cd14631    81 YGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAG 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 110735404 1079 TGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACL 1136
Cdd:cd14631   161 AGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 218
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
1222-1424 3.19e-122

PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The type IIb (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350404 [Multi-domain]  Cd Length: 201  Bit Score: 378.67  E-value: 3.19e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1222 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSnsAWPCLQYWPEPGRQQYGLMEVEFMSGT 1301
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPK--DQSCPQYWPDEGSGTYGPIQVEFVSTT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1302 ADEDLVARVFRVQNISRLQEGHLLVRHFQFLRWSAYRDTPDSKKAFLHLLAEVDKWQAESGDGRTIVHCLNGGGRSGTFC 1381
Cdd:cd14556    79 IDEDVISRIFRLQNTTRPQEGYRMVQQFQFLGWPRDRDTPPSKRALLKLLSEVEKWQEQSGEGPIVVHCLNGVGRSGVFC 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 110735404 1382 ACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCYD 1424
Cdd:cd14556   159 AISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
914-1137 1.29e-118

catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350478 [Multi-domain]  Cd Length: 237  Bit Score: 370.51  E-value: 1.29e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  914 AYDRHRVKLHPMLGDPNADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWP 993
Cdd:cd14630    14 SYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVEVGRVKCVRYWP 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  994 EDSDTYGDIKIMLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVI 1073
Cdd:cd14630    94 DDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVRQVKFLNPPDAGPIVV 173
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110735404 1074 HCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLC 1137
Cdd:cd14630   174 HCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILEACLC 237
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
914-1137 2.16e-112

catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350401 [Multi-domain]  Cd Length: 238  Bit Score: 353.62  E-value: 2.16e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  914 AYDRHRVKLHPMLGDPNADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWP 993
Cdd:cd14553    14 AYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEERSRVKCDQYWP 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  994 -EDSDTYGDIKIMLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIV 1072
Cdd:cd14553    94 tRGTETYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKACNPPDAGPIV 173
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110735404 1073 IHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLC 1137
Cdd:cd14553   174 VHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLEAVTC 238
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
908-1133 2.73e-104

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 331.13  E-value: 2.73e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404   908 RQEPMPAYDRHRVKLHPmlGDPNADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVK 987
Cdd:pfam00102    6 RYKDVLPYDHTRVKLTG--DPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKGREK 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404   988 CSRYWP---EDSDTYGDIKIMLVKTET-LAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKAS 1063
Cdd:pfam00102   84 CAQYWPeeeGESLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLRKVRKS 163
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110735404  1064 TP-PDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1133
Cdd:pfam00102  164 SLdGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
883-1133 1.59e-103

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 330.01  E-value: 1.59e-103
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404    883 GFKQEYESFFEGWDATKKKDKvkGSRQEPM--------PAYDRHRVKLHPMLGDPNaDYINANYIDGYHRSNHFIATQGP 954
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCTV--AAFPENRdknrykdvLPYDHTRVKLKPPPGEGS-DYINASYIDGPNGPKAYIATQGP 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404    955 KPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPEDSD---TYGDIKIMLVKTETLAEYVVRTFALERRGYSARH 1031
Cdd:smart00194   78 LPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGeplTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETR 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404   1032 EVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLC 1111
Cdd:smart00194  158 TVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELR 237
                           250       260
                    ....*....|....*....|..
gi 110735404   1112 SRRVNMIQTEEQYIFIHDAILE 1133
Cdd:smart00194  238 SQRPGMVQTEEQYIFLYRAILE 259
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
867-1137 6.23e-102

catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350474 [Multi-domain]  Cd Length: 276  Bit Score: 326.61  E-value: 6.23e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  867 ADLLQHINQMKTAEGYGFKQEYESFFEG----WDATKKKDKVKGSRQEPMPAYDRHRVKLHPMLGDPNADYINANYIDGY 942
Cdd:cd14626     1 SDLADNIERLKANDGLKFSQEYESIDPGqqftWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  943 HRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWP-EDSDTYGDIKIMLVKTETLAEYVVRTFA 1021
Cdd:cd14626    81 RKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPiRGTETYGMIQVTLLDTVELATYSVRTFA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1022 LERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVV 1101
Cdd:cd14626   161 LYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTV 240
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 110735404 1102 DIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLC 1137
Cdd:cd14626   241 DIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAATC 276
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
861-1138 2.38e-96

catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type tyrosine-protein phosphatase D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350472 [Multi-domain]  Cd Length: 284  Bit Score: 311.28  E-value: 2.38e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  861 HPAVRVADLLQHINQMKTAEGYGFKQEYESFFEG----WDATKKKDKVKGSRQEPMPAYDRHRVKLHPMLGDPNADYINA 936
Cdd:cd14624     1 HPPIPILELADHIERLKANDNLKFSQEYESIDPGqqftWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  937 NYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWP-EDSDTYGDIKIMLVKTETLAEY 1015
Cdd:cd14624    81 NYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPsRGTETYGLIQVTLLDTVELATY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1016 VVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMA 1095
Cdd:cd14624   161 CVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERI 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 110735404 1096 ECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLCG 1138
Cdd:cd14624   241 KHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAVTCG 283
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
861-1137 3.40e-96

catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350473 [Multi-domain]  Cd Length: 282  Bit Score: 310.87  E-value: 3.40e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  861 HPAVRVADLLQHINQMKTAEGYGFKQEYESFFEG----WDATKKKDKVKGSRQEPMPAYDRHRVKLHPMLGDPNADYINA 936
Cdd:cd14625     1 HPPIPISELAEHTERLKANDNLKLSQEYESIDPGqqftWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  937 NYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWP-EDSDTYGDIKIMLVKTETLAEY 1015
Cdd:cd14625    81 NYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPsRGTETYGMIQVTLLDTIELATF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1016 VVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMA 1095
Cdd:cd14625   161 CVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERI 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 110735404 1096 ECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLC 1137
Cdd:cd14625   241 KHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAVAC 282
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
933-1129 1.36e-93

catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr (pTyr) residues, instead of pSer or pThr. This family has a distinctive active site signature motif, HCSAGxGRxG, and are characterized as either transmembrane, receptor-like or non-transmembrane (soluble) PTPs. Receptor-like PTP domains tend to occur in two copies in the cytoplasmic region of the transmembrane proteins, only one copy may be active.


Pssm-ID: 350343 [Multi-domain]  Cd Length: 200  Bit Score: 299.97  E-value: 1.36e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  933 YINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPEDSD---TYGDIKIMLVKT 1009
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGkplEYGDITVTLVSE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1010 ETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLD 1089
Cdd:cd00047    81 EELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTFIAID 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 110735404 1090 VMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHD 1129
Cdd:cd00047   161 ILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
933-1129 2.30e-92

catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350397 [Multi-domain]  Cd Length: 204  Bit Score: 296.96  E-value: 2.30e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  933 YINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPED-SDTYGDIKIMLVKTET 1011
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEgTETYGNIQVTLLSTEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1012 LAEYVVRTFAL------ERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCY 1085
Cdd:cd14549    81 LATYTVRTFSLknlklkKVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTGTY 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 110735404 1086 IVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHD 1129
Cdd:cd14549   161 IVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
1222-1428 1.62e-91

PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350482 [Multi-domain]  Cd Length: 206  Bit Score: 294.62  E-value: 1.62e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1222 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNqsnSAWPCLQYWPEPGRQQYGLMEVEFMSGT 1301
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMD---AAQLCMQYWPEKTSCCYGPIQVEFVSAD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1302 ADEDLVARVFRVQNISRLQEGHLLVRHFQFLRWSAYRDTPDSKKAFLHLLAEVDKWQAE--SGDGRTIVHCLNGGGRSGT 1379
Cdd:cd14634    78 IDEDIISRIFRICNMARPQDGYRIVQHLQYIGWPAYRDTPPSKRSILKVVRRLEKWQEQydGREGRTVVHCLNGGGRSGT 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 110735404 1380 FCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1428
Cdd:cd14634   158 FCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
1222-1428 3.01e-90

PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350484 [Multi-domain]  Cd Length: 206  Bit Score: 291.16  E-value: 3.01e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1222 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSawpCLQYWPEPGRQQYGLMEVEFMSGT 1301
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQG---CPQYWPEEGMLRYGPIQVECMSCS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1302 ADEDLVARVFRVQNISRLQEGHLLVRHFQFLRWSAYRDTPDSKKAFLHLLAEVDKWQAE--SGDGRTIVHCLNGGGRSGT 1379
Cdd:cd14636    78 MDCDVISRIFRICNLTRPQEGYLMVQQFQYLGWASHREVPGSKRSFLKLILQVEKWQEEcdEGEGRTIIHCLNGGGRSGM 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 110735404 1380 FCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1428
Cdd:cd14636   158 FCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
915-1128 5.47e-89

catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar proteins; R3 subfamily receptor-type phosphotyrosine phosphatases (RPTP) are characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. Vertebrate members include receptor-type tyrosine-protein phosphatase-like O (PTPRO), J (PTPRJ), Q (PTPRQ), B (PTPRB), V (PTPRV) and H (PTPRH). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Most members are PTPs, except for PTPRQ, which dephosphorylates phosphatidylinositide substrates. PTPRV is characterized only in rodents; its function has been lost in humans. Both vertebrate and invertebrate R3 subfamily RPTPs are involved in the control of a variety of cellular processes, including cell growth, differentiation, mitotic cycle and oncogenic transformation.


Pssm-ID: 350396 [Multi-domain]  Cd Length: 222  Bit Score: 288.10  E-value: 5.47e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  915 YDRHRVKLHPMLGDPNADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPE 994
Cdd:cd14548     8 YDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVKCDHYWPF 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  995 DSD--TYGDIKIMLVKTETLAEYVVRTFALERRGYSarHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIV 1072
Cdd:cd14548    88 DQDpvYYGDITVTMLSESVLPDWTIREFKLERGDEV--RSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIKQEKGPTI 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 110735404 1073 IHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIH 1128
Cdd:cd14548   166 VHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1165-1428 1.35e-84

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 277.23  E-value: 1.35e-84
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404   1165 QLREEFQTLNSVTPplDVEECSIALLPRNRDKNRSMDVLPPDRCLPFLISTDGDSNNYINAALTDSYTRSAAFIVTLHPL 1244
Cdd:smart00194    1 GLEEEFEKLDRLKP--DDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPL 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404   1245 QSTTPDFWRLVYDYGCTSIVMLNQLNqSNSAWPCLQYWPEPGR--QQYGLMEVEFMSGTADEDLVARVFRVQNISrlQEG 1322
Cdd:smart00194   79 PSTVEDFWRMVWEQKVTVIVMLTELV-EKGREKCAQYWPDEEGepLTYGDITVTLKSVEKVDDYTIRTLEVTNTG--CSE 155
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404   1323 HLLVRHFQFLRWSaYRDTPDSKKAFLHLLAEVDKWQaESGDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAA 1402
Cdd:smart00194  156 TRTVTHYHYTNWP-DHGVPESPESILDLIRAVRKSQ-STSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIV 233
                           250       260
                    ....*....|....*....|....*.
gi 110735404   1403 KTLRNYKPNMVETMDQYHFCYDVALE 1428
Cdd:smart00194  234 KELRSQRPGMVQTEEQYIFLYRAILE 259
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
1222-1428 1.53e-82

PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350483 [Multi-domain]  Cd Length: 206  Bit Score: 269.25  E-value: 1.53e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1222 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNqsnSAWPCLQYWPEPGRQQYGLMEVEFMSGT 1301
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVD---PAQLCPQYWPENGVHRHGPIQVEFVSAD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1302 ADEDLVARVFRVQNISRLQEGHLLVRHFQFLRWSAYRDTPDSKKAFLHLLAEVDKWQAE--SGDGRTIVHCLNGGGRSGT 1379
Cdd:cd14635    78 LEEDIISRIFRIYNAARPQDGYRMVQQFQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEynGGEGRTVVHCLNGGGRSGT 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 110735404 1380 FCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1428
Cdd:cd14635   158 FCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
914-1136 9.52e-76

catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG has four splicing isoforms: three transmembrane isoforms, PTPRG-A, B, and C, and one secretory isoform, PTPRG-S, which are expressed in many tissues including the brain. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350505 [Multi-domain]  Cd Length: 274  Bit Score: 252.65  E-value: 9.52e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  914 AYDRHRVKLHPMLG--DPNADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRY 991
Cdd:cd17667    38 AYDHSRVKLRPLPGkdSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQY 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  992 WP-EDSDTYGDIKIMLVKTETLAEYVVRTFALER-----------RGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRR 1059
Cdd:cd17667   118 WPtENSEEYGNIIVTLKSTKIHACYTVRRFSIRNtkvkkgqkgnpKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRR 197
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110735404 1060 VKASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACL 1136
Cdd:cd17667   198 SSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
857-1142 8.73e-75

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1).


Pssm-ID: 350469 [Multi-domain]  Cd Length: 296  Bit Score: 250.71  E-value: 8.73e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  857 TGQLHPAVRVADLLQHINQMKTAEGYGFKQEYESF-----FEGWDATKKKDKVKGSRQEPMPAYDRHRVKLHPMLGDPNA 931
Cdd:cd14621     1 TNRKYPPLPVDKLEEEINRRMADDNKLFREEFNALpacpiQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  932 DYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPEDSD-TYGDIKIMLVKTE 1010
Cdd:cd14621    81 DYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCwTYGNIRVSVEDVT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1011 TLAEYVVRTFALERRG----YSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYI 1086
Cdd:cd14621   161 VLVDYTVRKFCIQQVGdvtnKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFI 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 110735404 1087 VLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLCGETTI 1142
Cdd:cd14621   241 VIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYLYGDTEL 296
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
915-1133 4.80e-73

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the first PTP domain (repeat 1).


Pssm-ID: 350468 [Multi-domain]  Cd Length: 229  Bit Score: 243.31  E-value: 4.80e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  915 YDRHRVKLHPMLGDPNADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPE 994
Cdd:cd14620     7 YDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKCYQYWPD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  995 DSD-TYGDIKIMLVKTETLAEYVVRTFALERR---GYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGP 1070
Cdd:cd14620    87 QGCwTYGNIRVAVEDCVVLVDYTIRKFCIQPQlpdGCKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKSVNPVHAGP 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110735404 1071 IVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1133
Cdd:cd14620   167 IVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
896-1128 3.80e-72

catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein phosphatase non-receptor type 9 (PTPN9), also called protein-tyrosine phosphatase MEG2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN9 plays an important role in promoting intracellular secretary vesicle fusion in hematopoietic cells and promotes the dephosphorylation of ErbB2 and EGFR in breast cancer cells, leading to impaired activation of STAT5 and STAT3. It also directly dephosphorylates STAT3 at the Tyr705 residue, resulting in its inactivation. PTPN9 has been found to be dysregulated in various human cancers, including breast, colorectal, and gastric cancer.


Pssm-ID: 350391 [Multi-domain]  Cd Length: 271  Bit Score: 242.27  E-value: 3.80e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  896 DATKKKDKVKGSRQEPMPAYDRHRVKLHPMLGDPNADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIV 975
Cdd:cd14543    22 LCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIV 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  976 MITKLVEVGRVKCSRYWPEDSDT---YGDIKIMLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATG 1052
Cdd:cd14543   102 MTTRVVERGRVKCGQYWPLEEGSslrYGDLTVTNLSVENKEHYKKTTLEIHNTETDESRQVTHFQFTSWPDFGVPSSAAA 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1053 LLAFI--------RRVKASTPPDAG-----PIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQ 1119
Cdd:cd14543   182 LLDFLgevrqqqaLAVKAMGDRWKGhppgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVRRMRTQRAFSIQ 261

                  ....*....
gi 110735404 1120 TEEQYIFIH 1128
Cdd:cd14543   262 TPDQYYFCY 270
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
915-1133 5.67e-72

catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type tyrosine-protein phosphatase J (PTPRJ or R-PTP-J), also known as receptor-type tyrosine-protein phosphatase eta (R-PTP-eta) or density-enhanced phosphatase 1 (DEP-1) OR CD148, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRJ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (eight in PTPRJ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed in various cell types including epithelial, hematopoietic, and endothelial cells. It plays a role in cell adhesion, migration, proliferation and differentiation. It dephosphorylates or contributes to the dephosphorylation of various substrates including protein kinases such as FLT3, PDGFRB, MET, RET (variant MEN2A), VEGFR-2, LYN, SRC, MAPK1, MAPK3, and EGFR, as well as PIK3R1 and PIK3R2.


Pssm-ID: 350463 [Multi-domain]  Cd Length: 229  Bit Score: 240.10  E-value: 5.67e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  915 YDRHRVKLhPMLGDPNADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPE 994
Cdd:cd14615     9 YDISRVKL-SVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPS 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  995 D-SDTYGDIKIMLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAF---IRRVKASTPPDaGP 1070
Cdd:cd14615    88 KqKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFrhlVREYMKQNPPN-SP 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110735404 1071 IVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1133
Cdd:cd14615   167 ILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1193-1428 2.52e-71

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 238.30  E-value: 2.52e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  1193 NRDKNRSMDVLPPDRCLPFLISTDGDSNnYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQS 1272
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGPSD-YINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  1273 NSAwPCLQYWPEP--GRQQYGLMEVEFMSGTADE-DLVARVFRVQNISRlQEGHLlVRHFQFLRWSAyRDTPDSKKAFLH 1349
Cdd:pfam00102   80 GRE-KCAQYWPEEegESLEYGDFTVTLKKEKEDEkDYTVRTLEVSNGGS-EETRT-VKHFHYTGWPD-HGVPESPNSLLD 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110735404  1350 LLAEVDKWQAESGDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1428
Cdd:pfam00102  156 LLRKVRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
933-1128 1.62e-69

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1).


Pssm-ID: 350399 [Multi-domain]  Cd Length: 202  Bit Score: 232.11  E-value: 1.62e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  933 YINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPEDSD-TYGDIKIMLVKTET 1011
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCwTYGNLRVRVEDTVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1012 LAEYVVRTFALERR----GYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIV 1087
Cdd:cd14551    81 LVDYTTRKFCIQKVnrgiGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTGTFIV 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 110735404 1088 LDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIH 1128
Cdd:cd14551   161 IDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
915-1128 3.52e-69

catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type tyrosine-protein phosphatase B (PTPRB), also known as receptor-type tyrosine-protein phosphatase beta (R-PTP-beta) or vascular endothelial protein tyrosine phosphatase(VE-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRB/VE-PTP is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed specifically in vascular endothelial cells and it plays an important role in blood vessel remodeling and angiogenesis.


Pssm-ID: 350465 [Multi-domain]  Cd Length: 228  Bit Score: 232.12  E-value: 3.52e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  915 YDRHRVKLHPMLGDPNADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPE 994
Cdd:cd14617     9 YDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPA 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  995 DSDT--YGDIKIMLVKTETLAEYVVRTFAL--ERRGYSARHeVRQFHFTAWPEHGVPYHATGLLAFIRRVK--ASTPPDA 1068
Cdd:cd14617    89 DQDSlyYGDLIVQMLSESVLPEWTIREFKIcsEEQLDAPRL-VRHFHYTVWPDHGVPETTQSLIQFVRTVRdyINRTPGS 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1069 GPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIH 1128
Cdd:cd14617   168 GPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
915-1133 5.60e-69

catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type tyrosine-protein phosphatase H (PTPRH or R-PTP-H), also known as stomach cancer-associated protein tyrosine phosphatase 1 (SAP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRH is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is localized specifically at microvilli of the brush border in gastrointestinal epithelial cells. It plays a role in intestinal immunity by regulating CEACAM20 through tyrosine dephosphorylation. It is also a negative regulator of integrin-mediated signaling and may contribute to contact inhibition of cell growth and motility.


Pssm-ID: 350467 [Multi-domain]  Cd Length: 233  Bit Score: 231.70  E-value: 5.60e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  915 YDRHRVKLHPMLGDPNADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPE 994
Cdd:cd14619     9 YDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRVKCEHYWPL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  995 DSD--TYGDIKIMLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKA--STPPDAGP 1070
Cdd:cd14619    89 DYTpcTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQwlDQTMSGGP 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110735404 1071 IVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1133
Cdd:cd14619   169 TVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILD 231
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
919-1128 3.07e-68

catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; The kinase interaction motif (KIM) family of protein-tyrosine phosphatases (PTPs) includes tyrosine-protein phosphatases non-receptor type 7 (PTPN7) and non-receptor type 5 (PTPN5), and protein-tyrosine phosphatase receptor type R (PTPRR). PTPN7 is also called hematopoietic protein-tyrosine phosphatase (HePTP) while PTPN5 is also called striatal-enriched protein-tyrosine phosphatase (STEP). They belong to the family of classical tyrosine-specific PTPs (EC 3.1.3.48) that catalyze the dephosphorylation of phosphotyrosine peptides. KIM-PTPs are characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. They are highly specific to the MAPKs ERK1/2 (extracellular-signal-regulated kinase 1/2) and p38, over JNK (c-Jun N-terminal kinase); they dephosphorylate these kinases and thereby critically modulate cell proliferation and differentiation.


Pssm-ID: 350395 [Multi-domain]  Cd Length: 224  Bit Score: 229.21  E-value: 3.07e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  919 RVKLHPMLGDPNADYINANYIDGY-HRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEvGRVKCSRYWPEDSD 997
Cdd:cd14547    13 RVCLPSVDDDPLSSYINANYIRGYdGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTE-AKEKCAQYWPEEEN 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  998 -TYGDIKIMLVKTETLAEYVVRTFALERRGysARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVK--ASTPPDAGPIVIH 1074
Cdd:cd14547    92 eTYGDFEVTVQSVKETDGYTVRKLTLKYGG--EKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEeaRQTEPHRGPIVVH 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 110735404 1075 CSAGTGRTGCYIVLDVMLDMAECEGVVDIyncVKTLCSRRVN---MIQTEEQYIFIH 1128
Cdd:cd14547   170 CSAGIGRTGCFIATSIGCQQLREEGVVDV---LGIVCQLRLDrggMVQTAEQYEFVH 223
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
933-1132 4.12e-68

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350506 [Multi-domain]  Cd Length: 209  Bit Score: 228.32  E-value: 4.12e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  933 YINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWP-EDSDTYGDIKIMLVKTET 1011
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPaDGSEEYGNFLVTQKSVQV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1012 LAEYVVRTFALE--------RRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTG 1083
Cdd:cd17668    81 LAYYTVRNFTLRntkikkgsQKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGRTG 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 110735404 1084 CYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAIL 1132
Cdd:cd17668   161 TYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
915-1132 1.05e-67

catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type tyrosine-protein phosphatase V (PTPRV or R-PTP-V), also known as embryonic stem cell protein-tyrosine phosphatase (ES cell phosphatase) or osteotesticular protein-tyrosine phosphatase (OST-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRV is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. In rodents, it may play a role in the maintenance of pluripotency and may function in signaling pathways during bone remodeling. It is the only PTP whose function has been lost between rodent and human. The human OST-PTP gene is a pseudogene.


Pssm-ID: 350466 [Multi-domain]  Cd Length: 230  Bit Score: 227.90  E-value: 1.05e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  915 YDRHRVKLHPMLGDPNADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPE 994
Cdd:cd14618     9 YDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRVLCDHYWPS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  995 DSD--TYGDIKIMLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKA--STPPDAGP 1070
Cdd:cd14618    89 ESTpvSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVREhvQATKGKGP 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110735404 1071 IVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAIL 1132
Cdd:cd14618   169 TLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
915-1128 7.35e-66

catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type tyrosine-protein phosphatase Q (PTPRQ or R-PTP-Q), also called phosphatidylinositol phosphatase PTPRQ, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRQ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (18 in PTPRQ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It displays low tyrosine-protein phosphatase activity; rather, it functions as a phosphatidylinositol phosphatase required for auditory processes. It regulates the levels of phosphatidylinositol 4,5-bisphosphate (PIP2) in the basal region of hair bundles. It can dephosphorylate a broad range of phosphatidylinositol phosphates, including phosphatidylinositol 3,4,5-trisphosphate and most phosphatidylinositol monophosphates and diphosphates.


Pssm-ID: 350464 [Multi-domain]  Cd Length: 224  Bit Score: 222.47  E-value: 7.35e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  915 YDRHRVKLHPMLGDPNADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPE 994
Cdd:cd14616     9 YNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRIRCHQYWPE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  995 DSD---TYGDIKIMLVKTETLAEYVVRTFALERRGYSARheVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPI 1071
Cdd:cd14616    89 DNKpvtVFGDIVITKLMEDVQIDWTIRDLKIERHGDYMM--VRQCNFTSWPEHGVPESSAPLIHFVKLVRASRAHDNTPM 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 110735404 1072 VIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIH 1128
Cdd:cd14616   167 IVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
915-1132 9.66e-66

PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2).


Pssm-ID: 350402 [Multi-domain]  Cd Length: 238  Bit Score: 222.40  E-value: 9.66e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  915 YDRHRVKLHPMLGDPNADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWP- 993
Cdd:cd14554    18 YESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLREMGREKCHQYWPa 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  994 EDSDTYGDIKIMLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPP--DAGPI 1071
Cdd:cd14554    98 ERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQfgQEGPI 177
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110735404 1072 VIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAIL 1132
Cdd:cd14554   178 TVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRAAL 238
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
933-1128 2.06e-65

catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 1.


Pssm-ID: 350405 [Multi-domain]  Cd Length: 201  Bit Score: 220.08  E-value: 2.06e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  933 YINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWP---EDSDTYGDIKIMLVKT 1009
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPsmeEGSRAFGDVVVKINEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1010 ETLAEYVVRTFAL--ERRGYSARhEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIV 1087
Cdd:cd14557    81 KICPDYIIRKLNInnKKEKGSGR-EVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYIG 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 110735404 1088 LDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIH 1128
Cdd:cd14557   160 IDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
933-1129 1.73e-64

fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae protein-tyrosine phosphatases 1 (PTP1) and 2 (PTP2), Schizosaccharomyces pombe PTP1, PTP2, and PTP3, and similar fungal proteins. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. PTP2, together with PTP3, is the major phosphatase that dephosphorylates and inactivates the MAP kinase HOG1 and also modulates its subcellular localization.


Pssm-ID: 350509 [Multi-domain]  Cd Length: 212  Bit Score: 217.89  E-value: 1.73e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  933 YINANYID-GYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPEDSDT--YGDIKIMLVKT 1009
Cdd:cd18533     1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEgeYGDLTVELVSE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1010 ETLAE--YVVRTFALeRRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKA--STPPDAGPIVIHCSAGTGRTGCY 1085
Cdd:cd18533    81 EENDDggFIVREFEL-SKEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRElnDSASLDPPIIVHCSAGVGRTGTF 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 110735404 1086 IVLDVMLDMAE--------CEGVVD-IYNCVKTLCSRRVNMIQTEEQYIFIHD 1129
Cdd:cd18533   160 IALDSLLDELKrglsdsqdLEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
915-1131 7.21e-64

catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) and type 6 (PTPN6) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 and PTPN6, are also called SH2 domain-containing tyrosine phosphatase 2 (SHP2) and 1 (SHP1), respectively. They contain two tandem SH2 domains: a catalytic PTP domain, and a C-terminal tail with regulatory properties. Although structurally similar, they have different localization and different roles in signal transduction. PTPN11/SHP2 is expressed ubiquitously and plays a positive role in cell signaling, leading to cell activation, while PTPN6/SHP1 expression is restricted mainly to hematopoietic and epithelial cells and functions as a negative regulator of signaling events.


Pssm-ID: 350392 [Multi-domain]  Cd Length: 251  Bit Score: 217.72  E-value: 7.21e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  915 YDRHRVKLHPmlGDPN---ADYINANYI-----DGYHRSNH--FIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVG 984
Cdd:cd14544    13 FDHTRVILKD--RDPNvpgSDYINANYIrneneGPTTDENAktYIATQGCLENTVSDFWSMVWQENSRVIVMTTKEVERG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  985 RVKCSRYWPEDSDT--YGDIKIMLVKTETLAEYVVRTFALER--RGYSARhEVRQFHFTAWPEHGVPYHATGLLAFIRRV 1060
Cdd:cd14544    91 KNKCVRYWPDEGMQkqYGPYRVQNVSEHDTTDYTLRELQVSKldQGDPIR-EIWHYQYLSWPDHGVPSDPGGVLNFLEDV 169
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110735404 1061 --KASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGV---VDIYNCVKTLCSRRVNMIQTEEQYIFIHDAI 1131
Cdd:cd14544   170 nqRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdcdIDIQKTIQMVRSQRSGMVQTEAQYKFIYVAV 245
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
915-1132 1.08e-63

catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type tyrosine-protein phosphatase O (PTPRO or R-PTP-O), also known as glomerular epithelial protein 1 or protein tyrosine phosphatase U2 (PTP-U2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRO is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is essential for sustaining the structure and function of foot processes by regulating tyrosine phosphorylation of podocyte proteins. It has been identified as a synaptic cell adhesion molecule (CAM) that serves as a potent initiator of synapse formation. It is also a tumor suppressor in several types of cancer, such as hepatocellular carcinoma, lung cancer, and breast cancer.


Pssm-ID: 350462 [Multi-domain]  Cd Length: 245  Bit Score: 217.06  E-value: 1.08e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  915 YDRHRVKLHPMLGDPNADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWP- 993
Cdd:cd14614    24 YDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWPf 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  994 -EDSDTYGDIKIMLVKTETLAEYVVRTFaleRRGYS-ARHEVRQFHFTAWPEHGVPY--HATGLLAFIRRVKASTPPDAG 1069
Cdd:cd14614   104 tEEPVAYGDITVEMLSEEEQPDWAIREF---RVSYAdEVQDVMHFNYTAWPDHGVPTanAAESILQFVQMVRQQAVKSKG 180
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110735404 1070 PIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAIL 1132
Cdd:cd14614   181 PMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCVQ 243
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
933-1134 2.62e-63

catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) and type 13 (PTPN13, also known as PTPL1) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization. Human PTPN13 is an important regulator of tumor aggressiveness.


Pssm-ID: 350386 [Multi-domain]  Cd Length: 207  Bit Score: 214.16  E-value: 2.62e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  933 YINANYI------DGYHrsnhFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPEDSDT----YGDI 1002
Cdd:cd14538     1 YINASHIripvggDTYH----YIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKplicGGRL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1003 KIMLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTppDAGPIVIHCSAGTGRT 1082
Cdd:cd14538    77 EVSLEKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIH--NSGPIVVHCSAGIGRT 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 110735404 1083 GCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEA 1134
Cdd:cd14538   155 GVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEV 206
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
933-1129 5.68e-61

PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 2.


Pssm-ID: 350406 [Multi-domain]  Cd Length: 203  Bit Score: 207.63  E-value: 5.68e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  933 YINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPEDSDTYGDIKIMLVKTETL 1012
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKTYGDIEVELKDTEKS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1013 AEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAG------PIVIHCSAGTGRTGCYI 1086
Cdd:cd14558    81 PTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNSkhgrsvPIVVHCSDGSSRTGIFC 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 110735404 1087 VLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHD 1129
Cdd:cd14558   161 ALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
932-1134 6.55e-61

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3) and type 4 (PTPN4) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 and PTPN4 are large modular proteins containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses.


Pssm-ID: 350389 [Multi-domain]  Cd Length: 212  Bit Score: 207.57  E-value: 6.55e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  932 DYINANYID----GYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPE--DSDTYGDIKIM 1005
Cdd:cd14541     1 DYINANYVNmeipGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDlgETMQFGNLQIT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1006 LVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCY 1085
Cdd:cd14541    81 CVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGIGRTGVL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 110735404 1086 IVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEA 1134
Cdd:cd14541   161 ITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRV 209
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
933-1131 1.63e-59

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350400 [Multi-domain]  Cd Length: 202  Bit Score: 203.27  E-value: 1.63e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  933 YINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPED-SDTYGDIKIMLVKTET 1011
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDgSVSSGDITVELKDQTD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1012 LAEYVVRTFALER-RGYSARhEVRQFHFTAWPEHGVPYHATGLLAFIRRV-KASTPPDAGPIVIHCSAGTGRTGCYIVLD 1089
Cdd:cd14552    81 YEDYTLRDFLVTKgKGGSTR-TVRQFHFHGWPEVGIPDNGKGMIDLIAAVqKQQQQSGNHPITVHCSAGAGRTGTFCALS 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 110735404 1090 VMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAI 1131
Cdd:cd14552   160 TVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
862-1133 3.86e-59

PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type tyrosine-protein phosphatase-like D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350476 [Multi-domain]  Cd Length: 292  Bit Score: 205.74  E-value: 3.86e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  862 PAVRVADLLQHINQMKTAEGY-GFKQEYESFFEGWDATKK-------KDKVKGSRQEPMPaYDRHRVKLHPMLGDPNADY 933
Cdd:cd14628     4 PARNLYAYIQKLTQIETGENVtGMELEFKRLASSKAHTSRfisanlpCNKFKNRLVNIMP-YESTRVCLQPIRGVEGSDY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  934 INANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWP-EDSDTYGDIKIMLVKTETL 1012
Cdd:cd14628    83 INASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPaERSARYQYFVVDPMAEYNM 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1013 AEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPP--DAGPIVIHCSAGTGRTGCYIVLDV 1090
Cdd:cd14628   163 PQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSI 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 110735404 1091 MLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1133
Cdd:cd14628   243 VLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALE 285
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
902-1133 5.98e-58

PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350475 [Multi-domain]  Cd Length: 290  Bit Score: 202.27  E-value: 5.98e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  902 DKVKGSRQEPMPaYDRHRVKLHPMLGDPNADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLV 981
Cdd:cd14627    53 NKFKNRLVNIMP-YETTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLR 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  982 EVGRVKCSRYWP-EDSDTYGDIKIMLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRV 1060
Cdd:cd14627   132 EMGREKCHQYWPaERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQV 211
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110735404 1061 KASTPP--DAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1133
Cdd:cd14627   212 HKTKEQfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALE 286
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
915-1133 5.47e-57

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350471 [Multi-domain]  Cd Length: 228  Bit Score: 197.19  E-value: 5.47e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  915 YDRHRVKLHPMLGDPNADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPE 994
Cdd:cd14623     8 YEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEKCAQYWPS 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  995 D-SDTYGDIKIMLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAG-PIV 1072
Cdd:cd14623    88 DgSVSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQQQSGNhPIT 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110735404 1073 IHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1133
Cdd:cd14623   168 VHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
932-1131 6.09e-57

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350470 [Multi-domain]  Cd Length: 205  Bit Score: 195.99  E-value: 6.09e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  932 DYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWP-EDSDTYGDIKIMLvKTE 1010
Cdd:cd14622     1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPsEGSVTHGEITIEI-KND 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1011 TLAEYV-VRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRV-KASTPPDAGPIVIHCSAGTGRTGCYIVL 1088
Cdd:cd14622    80 TLLETIsIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVqKQQQQTGNHPIVVHCSAGAGRTGTFIAL 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 110735404 1089 DVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAI 1131
Cdd:cd14622   160 SNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
22-186 7.08e-57

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 194.10  E-value: 7.08e-57
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404     22 TPAAGCTFEEASdpavPCEYSQAQYDDFQWEQVRIHPGTRAP---ADLPHGSYLMVNTSQHAPGQRAHVIFQSLSEN-DT 97
Cdd:smart00137    1 TSPGNCDFEEGS----TCGWHQDSNDDGHWERVSSATGIPGPnrdHTTGNGHFMFFETSSGAEGQTARLLSPPLYENrST 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404     98 HCVQFSYFLYsrdGHSPGTLGVYVRVNGGPLGSAVWNMTGSHGRQWHQAELAVSTfWPNEYQVLFEALISPDRRGYMGLD 177
Cdd:smart00137   77 HCLTFWYYMY---GSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALD 152

                    ....*....
gi 110735404    178 DILLLSYPC 186
Cdd:smart00137  153 DILLSNGPC 161
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
902-1133 7.21e-57

PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350477 [Multi-domain]  Cd Length: 291  Bit Score: 199.18  E-value: 7.21e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  902 DKVKGSRQEPMPaYDRHRVKLHPMLGDPNADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLV 981
Cdd:cd14629    53 NKFKNRLVNIMP-YELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLR 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  982 EVGRVKCSRYWP-EDSDTYGDIKIMLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRV 1060
Cdd:cd14629   132 EMGREKCHQYWPaERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQV 211
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110735404 1061 KASTPP--DAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1133
Cdd:cd14629   212 HKTKEQfgQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALE 286
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
901-1131 1.45e-56

catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11), also called SH2 domain-containing tyrosine phosphatase 2 (SHP-2 or SHP2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 promotes the activation of the RAS/Mitogen-Activated Protein Kinases (MAPK) Extracellular-Regulated Kinases 1/2 (ERK1/2) pathway, a canonical signaling cascade that plays key roles in various cellular processes, including proliferation, survival, differentiation, migration, or metabolism. It also regulates the phosphoinositide 3-kinase (PI3K)/AKT pathway, a fundamental cascade that functions in cell survival, proliferation, migration, morphogenesis, and metabolism. PTPN11 dysregulation is associated with several developmental diseases and malignancies, such as Noonan syndrome and juvenile myelomonocytic leukemia. It contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350453 [Multi-domain]  Cd Length: 253  Bit Score: 196.78  E-value: 1.45e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  901 KDKVKGSRQEPMPaYDRHRVKLHPmlGDPN---ADYINANYIDGYHRSN--------HFIATQGPKPEMVYDFWRMVWQE 969
Cdd:cd14605     1 ENKNKNRYKNILP-FDHTRVVLHD--GDPNepvSDYINANIIMPEFETKcnnskpkkSYIATQGCLQNTVNDFWRMVFQE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  970 HCSSIVMITKLVEVGRVKCSRYWPEDS--DTYGDIKIMLVKTETLAEYVVRTFALERRGY-SARHEVRQFHFTAWPEHGV 1046
Cdd:cd14605    78 NSRVIVMTTKEVERGKSKCVKYWPDEYalKEYGVMRVRNVKESAAHDYILRELKLSKVGQgNTERTVWQYHFRTWPDHGV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1047 PYHATGLLAFIRRV--KASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGV---VDIYNCVKTLCSRRVNMIQTE 1121
Cdd:cd14605   158 PSDPGGVLDFLEEVhhKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQTE 237
                         250
                  ....*....|
gi 110735404 1122 EQYIFIHDAI 1131
Cdd:cd14605   238 AQYRFIYMAV 247
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
919-1131 2.07e-55

catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein phosphatase non-receptor type 5 (PTPN5), also called striatum-enriched protein-tyrosine phosphatase (STEP) or neural-specific PTP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN5/STEP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. It is a CNS-enriched protein that regulates key signaling proteins required for synaptic strengthening, as well as NMDA and AMPA receptor trafficking. PTPN5 is implicated in multiple neurologic and neuropsychiatric disorders, such as Alzheimer's disease, Parkinson's disease, schizophrenia, and fragile X syndrome.


Pssm-ID: 350461 [Multi-domain]  Cd Length: 258  Bit Score: 193.54  E-value: 2.07e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  919 RVKL-HPMLGDPNADYINANYIDGY-HRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRvKCSRYWPEDS 996
Cdd:cd14613    41 RVCLtSPDQDDPLSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEMNE-KCTEYWPEEQ 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  997 DTYGDIKIMLVKTETLAEYVVRTFALERRGysARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKA---STPPDAGPIVI 1073
Cdd:cd14613   120 VTYEGIEITVKQVIHADDYRLRLITLKSGG--EERGLKHYWYTSWPDQKTPDNAPPLLQLVQEVEEarqQAEPNCGPVIV 197
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110735404 1074 HCSAGTGRTGCYIVLDVMLDMAECEGVVDIyncVKTLCSRRVN---MIQTEEQYIFIHDAI 1131
Cdd:cd14613   198 HCSAGIGRTGCFIATSICCKQLRNEGVVDI---LRTTCQLRLDrggMIQTCEQYQFVHHVL 255
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
932-1128 4.06e-55

catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein phosphatase non-receptor type 7 (PTPN7), also called hematopoietic protein-tyrosine phosphatase (HePTP) or LC-PTP. belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN7/HePTP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. PTPN7/HePTP is found exclusively in the white blood cells in bone marrow, thymus, spleen, lymph nodes and all myeloid and lymphoid cell lines. It negatively regulates T-cell activation and proliferation, and is often dysregulated in the preleukemic disorder myelodysplastic syndrome, as well as in acute myelogenous leukemia.


Pssm-ID: 350460 [Multi-domain]  Cd Length: 247  Bit Score: 192.36  E-value: 4.06e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  932 DYINANYIDGYH-RSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEvGRVKCSRYWPEDSDTYGDIKIMLVKTE 1010
Cdd:cd14612    45 SYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKE-KKEKCVHYWPEKEGTYGRFEIRVQDMK 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1011 TLAEYVVRTFALERRGysARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKAS--TPPDAGPIVIHCSAGTGRTGCYIVL 1088
Cdd:cd14612   124 ECDGYTIRDLTIQLEE--ESRSVKHYWFSSWPDHQTPESAGPLLRLVAEVEESrqTAASPGPIVVHCSAGIGRTGCFIAT 201
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 110735404 1089 DVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIH 1128
Cdd:cd14612   202 SIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLH 241
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
1222-1424 1.49e-54

catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr (pTyr) residues, instead of pSer or pThr. This family has a distinctive active site signature motif, HCSAGxGRxG, and are characterized as either transmembrane, receptor-like or non-transmembrane (soluble) PTPs. Receptor-like PTP domains tend to occur in two copies in the cytoplasmic region of the transmembrane proteins, only one copy may be active.


Pssm-ID: 350343 [Multi-domain]  Cd Length: 200  Bit Score: 189.03  E-value: 1.49e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1222 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGRQ--QYGLMEVEFMS 1299
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGRE-KCERYWPEEGGKplEYGDITVTLVS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1300 GTADEDLVARVFRVQNISrlQEGHLLVRHFQFLRWSAyRDTPDSKKAFLHLLAEVDKWQaESGDGRTIVHCLNGGGRSGT 1379
Cdd:cd00047    80 EEELSDYTIRTLELSPKG--CSESREVTHLHYTGWPD-HGVPSSPEDLLALVRRVRKEA-RKPNGPIVVHCSAGVGRTGT 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 110735404 1380 FCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCYD 1424
Cdd:cd00047   156 FIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
933-1128 3.15e-53

catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), type 18 (PTPN18) and type 12 (PTPN12) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. TPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling.


Pssm-ID: 350390 [Multi-domain]  Cd Length: 202  Bit Score: 185.32  E-value: 3.15e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  933 YINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPEDSD---TYGDIKIMLVKT 1009
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEeqlQFGPFKISLEKE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1010 ETLAE-YVVRTFALERRgySARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVL 1088
Cdd:cd14542    81 KRVGPdFLIRTLKVTFQ--KESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRTGTICAI 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 110735404 1089 DVMLDMAECEGVVD---IYNCVKTLCSRRVNMIQTEEQYIFIH 1128
Cdd:cd14542   159 DYVWNLLKTGKIPEefsLFDLVREMRKQRPAMVQTKEQYELVY 201
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
885-1133 4.69e-53

catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein phosphatase non-receptor type 6 (PTPN6), also called SH2 domain-containing protein-tyrosine phosphatase 1 (SHP1 or SHP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN6 expression is restricted mainly to hematopoietic and epithelial cells. It is an important regulator of hematopoietic cells, downregulating pathways that promote cell growth, survival, adhesion, and activation. It regulates glucose homeostasis by modulating insulin signalling in the liver and muscle, and it also negatively regulates bone resorption, affecting both the formation and the function of osteoclasts. PTPN6 contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350454 [Multi-domain]  Cd Length: 266  Bit Score: 187.39  E-value: 4.69e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  885 KQEYESFFEGWDATKKKDKVKGSRQEPMPaYDRHRVKLHPmlGDPN---ADYINANYIDGY-----HRSNHFIATQGPKP 956
Cdd:cd14606     1 KQEVKNLHQRLEGQRPENKSKNRYKNILP-FDHSRVILQG--RDSNipgSDYINANYVKNQllgpdENAKTYIASQGCLE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  957 EMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPEDSDT--YGDIKIMLVKTETLAEYVVRTFALE--RRGYSARhE 1032
Cdd:cd14606    78 ATVNDFWQMAWQENSRVIVMTTREVEKGRNKCVPYWPEVGMQraYGPYSVTNCGEHDTTEYKLRTLQVSplDNGELIR-E 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1033 VRQFHFTAWPEHGVPYHATGLLAFIRRV--KASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGV---VDIYNCV 1107
Cdd:cd14606   157 IWHYQYLSWPDHGVPSEPGGVLSFLDQInqRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTI 236
                         250       260
                  ....*....|....*....|....*.
gi 110735404 1108 KTLCSRRVNMIQTEEQYIFIHDAILE 1133
Cdd:cd14606   237 QMVRAQRSGMVQTEAQYKFIYVAIAQ 262
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
884-1133 7.16e-53

catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein phosphatase non-receptor type 18 (PTPN18), also called brain-derived phosphatase, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. The N-terminal catalytic PTP domain of PTPN18 blocks lysosomal routing and delays the degradation of HER2 by dephosphorylation, and its C-terminal PEST domain promotes K48-linked HER2 ubiquitination and its destruction via the proteasome pathway.


Pssm-ID: 350451 [Multi-domain]  Cd Length: 266  Bit Score: 186.57  E-value: 7.16e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  884 FKQEYESFFEgwdATKKKDKVKGSRQEPMPAYDRHRVKLHPMLGDPNADYINANYIDGYHRSNHFIATQGPKPEMVYDFW 963
Cdd:cd14603    14 FKADYVCSTV---AGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFW 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  964 RMVWQEHCSSIVMITKLVEVGRVKCSRYWPEDSDT--YGDIKIMLVKTETL-AEYVVRTFALERRGYSarHEVRQFHFTA 1040
Cdd:cd14603    91 RMIWQYGVKVILMACREIEMGKKKCERYWAQEQEPlqTGPFTITLVKEKRLnEEVILRTLKVTFQKES--RSVSHFQYMA 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1041 WPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVD---IYNCVKTLCSRRVNM 1117
Cdd:cd14603   169 WPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPdfsIFDVVLEMRKQRPAA 248
                         250
                  ....*....|....*.
gi 110735404 1118 IQTEEQYIFIHDAILE 1133
Cdd:cd14603   249 VQTEEQYEFLYHTVAQ 264
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
919-1128 9.31e-52

catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type tyrosine-protein phosphatase-like R (PTPRR or R-PTP-R), also called protein-tyrosine phosphatase PCPTP1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRR is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. The human and mouse PTPRR gene produces multiple neuronal protein isoforms of varying sizes (in human, PTPPBS-alpha, beta, gamma and delta). All isoforms contain the KIM motif and the catalytic PTP domain. PTPRR-deficient mice show significant defects in fine motor coordination and balance skills that are reminiscent of a mild ataxia.


Pssm-ID: 350459 [Multi-domain]  Cd Length: 226  Bit Score: 182.04  E-value: 9.31e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  919 RVKLHPM-LGDPNADYINANYIDGYH-RSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRvKCSRYWPEDS 996
Cdd:cd14611    15 RVCLKPKnSNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEKNE-KCVLYWPEKR 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  997 DTYGDIKIMLVKTETLAEYVVRTFALeRRGYSARHeVRQFHFTAWPEHGVPYHATGLLAFIRRVKAS--TPPDAGPIVIH 1074
Cdd:cd14611    94 GIYGKVEVLVNSVKECDNYTIRNLTL-KQGSQSRS-VKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDrlASPGRGPVVVH 171
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 110735404 1075 CSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIH 1128
Cdd:cd14611   172 CSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
901-1132 1.13e-51

catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein phosphatase non-receptor type 13 (PTPN13, also known as PTPL1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN13 is an important regulator of tumor aggressiveness. It regulates breast cancer cell aggressiveness through direct inactivation of Src kinase. In hepatocellular carcinoma, PTPN13 is a tumor suppressor. PTPN13 contains a FERM domain, five PDZ domains, and a C-terminal catalytic PTP domain. With its PDZ domains, PTPN13 has numerous interacting partners that can actively participate in the regulation of its phosphatase activity or can permit direct or indirect recruitment of tyrosine phosphorylated substrates. Its FERM domain is necessary for localization to the membrane.


Pssm-ID: 350445 [Multi-domain]  Cd Length: 234  Bit Score: 181.95  E-value: 1.13e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  901 KDKVKGSRQEPMPAYDRHRVklhpMLGDPNaDYINANYIDGYHRSNHF--IATQGPKPEMVYDFWRMVWQEHCSSIVMIT 978
Cdd:cd14597     1 KENRKKNRYKNILPYDTTRV----PLGDEG-GYINASFIKMPVGDEEFvyIACQGPLPTTVADFWQMVWEQKSTVIAMMT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  979 KLVEVGRVKCSRYWPE--DSDTYGD--IKIMLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLL 1054
Cdd:cd14597    76 QEVEGGKIKCQRYWPEilGKTTMVDnrLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1055 AFI---RRVKAStppdaGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAI 1131
Cdd:cd14597   156 TFIsymRHIHKS-----GPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVI 230

                  .
gi 110735404 1132 L 1132
Cdd:cd14597   231 L 231
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
1188-1427 2.81e-51

PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2).


Pssm-ID: 350402 [Multi-domain]  Cd Length: 238  Bit Score: 181.18  E-value: 2.81e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1188 ALLPRNRDKNRSMDVLPPDR---CLPFLISTDGdsNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIV 1264
Cdd:cd14554     1 ANLPCNKFKNRLVNILPYEStrvCLQPIRGVEG--SDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1265 MLNQLNQSNSAwPCLQYWPEPGRQQYGLMEVEFMSGTADEDLVARVFRVQNISRLQEGHllVRHFQFLRWSAyRDTPDSK 1344
Cdd:cd14554    79 MLTKLREMGRE-KCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRT--VRQFQFTDWPE-QGVPKSG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1345 KAFLHLLAEVDKWQAESG-DGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCY 1423
Cdd:cd14554   155 EGFIDFIGQVHKTKEQFGqEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCY 234

                  ....
gi 110735404 1424 DVAL 1427
Cdd:cd14554   235 RAAL 238
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
899-1131 8.99e-51

catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein phosphatase non-receptor type 12 (PTPN12), also called PTP-PEST or protein-tyrosine phosphatase G1 (PTPG1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling. It regulates various physiological processes, including cell migration, immune response, and neuronal activity, by dephosphorylating multiple substrates including HER2, FAK, PYK2, PSTPIP, WASP, p130Cas, paxillin, Shc, catenin, c-Abl, ArgBP2, p190RhoGAP, RhoGDI, cell adhesion kinase beta, and Rho GTPase.


Pssm-ID: 350452 [Multi-domain]  Cd Length: 297  Bit Score: 181.67  E-value: 8.99e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  899 KKKDKVKGSRQEPMPAYDRHRVKLHPMLGDPNADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMIT 978
Cdd:cd14604    53 EKEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMAC 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  979 KLVEVGRVKCSRYWP---EDSDTYGDIKIMLVKTETLAEYVVRTFALERRGYSarHEVRQFHFTAWPEHGVPYHATGLLA 1055
Cdd:cd14604   133 REFEMGRKKCERYWPlygEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQNET--RRLYQFHYVNWPDHDVPSSFDSILD 210
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110735404 1056 FIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLDV---MLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAI 1131
Cdd:cd14604   211 MISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYtwnLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 289
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
27-187 9.29e-51

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 176.40  E-value: 9.29e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404    27 CTFEEASDpavpCEYSQAQYDDFQWEQVRIHPGTRAPA-----DLPHGSYLMVNTSQHAPGQRAHVIFQSLSENDT-HCV 100
Cdd:pfam00629    1 CDFEDGNL----CGWTQDSSDDFDWERVSGPSVKTGPSsdhtqGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSpQCL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404   101 QFSYFLYsrdGHSPGTLGVYVRVNGGPLGSAVWNMTGSHGRQWHQAELAVSTFwPNEYQVLFEALISPDRRGYMGLDDIL 180
Cdd:pfam00629   77 RFWYHMS---GSGVGTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSS-TQPFQVVFEGIRGGGSRGGIALDDIS 152

                   ....*..
gi 110735404   181 LLSYPCA 187
Cdd:pfam00629  153 LSSGPCP 159
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
932-1133 6.84e-50

catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein phosphatase non-receptor type 4 (PTPN4), also called protein-tyrosine phosphatase MEG1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses. It specifically inhibits the TRIF-dependent TLR4 pathway by suppressing tyrosine phosphorylation of TRAM. It is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain; the PDZ domain regulates the catalytic activity of PTPN4.


Pssm-ID: 350449 [Multi-domain]  Cd Length: 212  Bit Score: 175.90  E-value: 6.84e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  932 DYINANYIDGYHRS----NHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPE--DSDTYGDIKIM 1005
Cdd:cd14601     1 DYINANYINMEIPSssiiNRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEpsGSSSYGGFQVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1006 LVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCY 1085
Cdd:cd14601    81 CHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTGVL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 110735404 1086 IVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1133
Cdd:cd14601   161 ITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 208
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
1222-1425 7.01e-50

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350400 [Multi-domain]  Cd Length: 202  Bit Score: 175.54  E-value: 7.01e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1222 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLnQSNSAWPCLQYWPEPGRQQYGLMEVEFMSGT 1301
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEI-KERSQNKCAQYWPEDGSVSSGDITVELKDQT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1302 ADEDLVARVFRVQNIsrlQEGHL-LVRHFQFLRWSAYrDTPDSKKAFLHLLAEVDKWQAESGDGRTIVHCLNGGGRSGTF 1380
Cdd:cd14552    80 DYEDYTLRDFLVTKG---KGGSTrTVRQFHFHGWPEV-GIPDNGKGMIDLIAAVQKQQQQSGNHPITVHCSAGAGRTGTF 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 110735404 1381 CACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCYDV 1425
Cdd:cd14552   156 CALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKV 200
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
933-1133 1.75e-49

PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type tyrosine-protein phosphatase-like N (PTPRN) and N2 (PTPRN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). They consist of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. They are mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells, and are involved in involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. They also are major autoantigens in type 1 diabetes and are involved in the regulation of insulin secretion.


Pssm-ID: 350394 [Multi-domain]  Cd Length: 208  Bit Score: 174.55  E-value: 1.75e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  933 YINANYI-DGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPED-SDTYGDIKIMLVKTE 1010
Cdd:cd14546     1 YINASTIyDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEgSEVYHIYEVHLVSEH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1011 TLAE-YVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLD 1089
Cdd:cd14546    81 IWCDdYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRTGTYILID 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 110735404 1090 VMLD-MAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1133
Cdd:cd14546   161 MVLNrMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
915-1133 2.49e-49

catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), also called lymphoid phosphatase (LyP), PEST-domain phosphatase (PEP), or hematopoietic cell protein-tyrosine phosphatase 70Z-PEP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. Mutations in the PTPN22 gene are associated with multiple connective tissue and autoimmune diseases including type 1 diabetes mellitus, rheumatoid arthritis, and systemic lupus erythematosus. PTPN22 contains an N-terminal catalytic PTP domain and four proline-rich regions at the C-terminus.


Pssm-ID: 350450 [Multi-domain]  Cd Length: 234  Bit Score: 175.41  E-value: 2.49e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  915 YDRHRVKLHPMLGDPNADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPE 994
Cdd:cd14602    10 YDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGKKKCERYWAE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  995 DSDT---YGDIKIMLVKTETLAEYVVRTfaLERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPI 1071
Cdd:cd14602    90 PGEMqleFGPFSVTCEAEKRKSDYIIRT--LKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPI 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110735404 1072 VIHCSAGTGRTGCYIVLDVMLDMAEcEGVV----DIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1133
Cdd:cd14602   168 CIHCSAGCGRTGVICAIDYTWMLLK-DGIIpenfSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIE 232
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
896-1133 7.60e-49

PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type tyrosine-protein phosphatase-like N (PTPRN or R-PTP-N), also called islet cell antigen 512 (ICA512) or PTP IA-2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. PTPRN is located in secretory granules of neuroendocrine cells and is involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. It is a major autoantigen in type 1 diabetes and is involved in the regulation of insulin secretion.


Pssm-ID: 350457 [Multi-domain]  Cd Length: 281  Bit Score: 175.61  E-value: 7.60e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  896 DATKKKDKVKGSRQEPMPAYDRHRVKLHPMLGDPNADYINAN-YIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSI 974
Cdd:cd14609    35 STAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWENGCTVI 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  975 VMITKLVEVGRVKCSRYWP-EDSDTYGDIKIMLVKTETLAE-YVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATG 1052
Cdd:cd14609   115 VMLTPLVEDGVKQCDRYWPdEGSSLYHIYEVNLVSEHIWCEdFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGIPSSTRP 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1053 LLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLD-MAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAI 1131
Cdd:cd14609   195 LLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNrMAKGVKEIDIAATLEHVRDQRPGMVRTKDQFEFALTAV 274

                  ..
gi 110735404 1132 LE 1133
Cdd:cd14609   275 AE 276
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
933-1134 1.30e-48

catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization.


Pssm-ID: 350444 [Multi-domain]  Cd Length: 207  Bit Score: 172.24  E-value: 1.30e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  933 YINANYI-----DGYHRsnhFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPEDSDTYGDIK---I 1004
Cdd:cd14596     1 YINASYItmpvgEEELF---YIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELEnyqL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1005 MLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTppDAGPIVIHCSAGTGRTGC 1084
Cdd:cd14596    78 RLENYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVH--NTGPIVVHCSAGIGRAGV 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 110735404 1085 YIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEA 1134
Cdd:cd14596   156 LICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEV 205
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
899-1133 4.65e-48

PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type tyrosine-protein phosphatase N2 (PTPRN2 or R-PTP-N2), also called islet cell autoantigen-related protein (IAR), ICAAR, phogrin, or IA-2beta, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. It is mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells. It may function as a phosphatidylinositol phosphatase to regulate insulin secretion. It is also required for normal accumulation of the neurotransmitters norepinephrine, dopamine and serotonin in the brain.


Pssm-ID: 350458 [Multi-domain]  Cd Length: 283  Bit Score: 173.32  E-value: 4.65e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  899 KKKDKVKGSRQEPMPAYDRHRVKLHPMLGDPNADYINANYI-DGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMI 977
Cdd:cd14610    40 QREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPImDHDPRNPAYIATQGPLPATVADFWQMVWESGCVVIVML 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  978 TKLVEVGRVKCSRYWP-EDSDTYGDIKIMLVKTETLAE-YVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLA 1055
Cdd:cd14610   120 TPLAENGVKQCYHYWPdEGSNLYHIYEVNLVSEHIWCEdFLVRSFYLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLLD 199
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110735404 1056 FIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLD-MAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1133
Cdd:cd14610   200 FRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNkMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 278
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
914-1126 6.65e-48

catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1) type 2 (PTPN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases, (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1 (or PTP-1B) is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor. PTPN2 (or TCPTP), a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner.


Pssm-ID: 350393 [Multi-domain]  Cd Length: 231  Bit Score: 171.04  E-value: 6.65e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  914 AYDRHRVKLHpmlgDPNADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWP 993
Cdd:cd14545    11 DHDRSRVKLK----QGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQIKCAQYWP 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  994 EDSDTYGD-----IKIMLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVK--ASTPP 1066
Cdd:cd14545    87 QGEGNAMIfedtgLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQKVResGSLSS 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110735404 1067 DAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGV--VDIYNCVKTLCSRRVNMIQTEEQYIF 1126
Cdd:cd14545   167 DVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRF 228
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
27-186 8.26e-48

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 167.94  E-value: 8.26e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404   27 CTFEEAsdpavPCEYSQAQYDDFQWEQVRIHPGTRAPADL-----PHGSYLMVNTSQHAPGQRAHVIFQSLSEN-DTHCV 100
Cdd:cd06263     1 CDFEDG-----LCGWTQDSTDDFDWTRVSGSTPSPGTPPDhthgtGSGHYLYVESSSGREGQKARLLSPLLPPPrSSHCL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  101 QFSYFLYsrdGHSPGTLGVYVRVNGGPLGSAVWNMTGSHGRQWHQAELAVSTFWpNEYQVLFEALISPDRRGYMGLDDIL 180
Cdd:cd06263    76 SFWYHMY---GSGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASS-KPFQVVFEGVRGSGSRGDIALDDIS 151

                  ....*.
gi 110735404  181 LLSYPC 186
Cdd:cd06263   152 LSPGPC 157
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
933-1129 1.25e-47

PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The type IIb (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350404 [Multi-domain]  Cd Length: 201  Bit Score: 169.12  E-value: 1.25e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  933 YINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRvKCSRYWPED-SDTYGDIKIMLVkTET 1011
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQ-SCPQYWPDEgSGTYGPIQVEFV-STT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1012 LAEYVV-RTFALER--RGYSARHEVRQFHFTAWPEHG-VPYHATGLLAFIRRV-KASTPPDAGPIVIHCSAGTGRTGCYI 1086
Cdd:cd14556    79 IDEDVIsRIFRLQNttRPQEGYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVeKWQEQSGEGPIVVHCLNGVGRSGVFC 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 110735404 1087 VLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHD 1129
Cdd:cd14556   159 AISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
1222-1424 1.97e-46

PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 2.


Pssm-ID: 350406 [Multi-domain]  Cd Length: 203  Bit Score: 165.64  E-value: 1.97e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1222 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAWpCLQYWPEpGRQQYGLMEVEFMSGT 1301
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQ-CAQYWGD-EKKTYGDIEVELKDTE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1302 ADEDLVARVFRVQNISRLQegHLLVRHFQFLRWSAyRDTPDSKKAFLHLLAEVDKWQAE--SGDGRT---IVHCLNGGGR 1376
Cdd:cd14558    79 KSPTYTVRVFEITHLKRKD--SRTVYQYQYHKWKG-EELPEKPKDLVDMIKSIKQKLPYknSKHGRSvpiVVHCSDGSSR 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 110735404 1377 SGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCYD 1424
Cdd:cd14558   156 TGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
PHA02738 PHA02738
hypothetical protein; Provisional
895-1131 2.10e-46

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 170.11  E-value: 2.10e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  895 WDATKKKDKVkgSRQEPMPAYDRHRVKLhPMLGDpNADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSI 974
Cdd:PHA02738   43 FNAEKKNRKL--NRYLDAVCFDHSRVIL-PAERN-RGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQII 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  975 VMITKLVEVGRVKCSRYWP--EDSD-TYGDIKIMLVKTETLAEYVVRTFALErRGYSARHEVRQFHFTAWPEHGVPYHAT 1051
Cdd:PHA02738  119 VMLCKKKENGREKCFPYWSdvEQGSiRFGKFKITTTQVETHPHYVKSTLLLT-DGTSATQTVTHFNFTAWPDHDVPKNTS 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1052 GLLAFIRRVKA----------------STPPdagPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRV 1115
Cdd:PHA02738  198 EFLNFVLEVRQcqkelaqeslqighnrLQPP---PIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRY 274
                         250
                  ....*....|....*.
gi 110735404 1116 NMIQTEEQYIFIHDAI 1131
Cdd:PHA02738  275 YSLFIPFQYFFCYRAV 290
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
1221-1429 6.02e-46

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350470 [Multi-domain]  Cd Length: 205  Bit Score: 164.41  E-value: 6.02e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1221 NYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLnQSNSAWPCLQYWPEPGRQQYGLMEVEFMSG 1300
Cdd:cd14622     1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTEL-QEREQEKCVQYWPSEGSVTHGEITIEIKND 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1301 TADEDLVARVFRVQNISRLQEghLLVRHFQFLRWSAYrDTPDSKKAFLHLLAEVDKWQAESGDGRTIVHCLNGGGRSGTF 1380
Cdd:cd14622    80 TLLETISIRDFLVTYNQEKQT--RLVRQFHFHGWPEI-GIPAEGKGMIDLIAAVQKQQQQTGNHPIVVHCSAGAGRTGTF 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 110735404 1381 CACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEY 1429
Cdd:cd14622   157 IALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
1140-1430 2.44e-45

PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350475 [Multi-domain]  Cd Length: 290  Bit Score: 166.06  E-value: 2.44e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1140 TTIPVSEFKATYKEMIRIDPQSNSSQLREEFQTLnsVTPPLDVEECSIALLPRNRDKNRSMDVLPPDR---CLPFLISTD 1216
Cdd:cd14627     2 TEVPARNLYSYIQKLAQVEVGEHVTGMELEFKRL--ANSKAHTSRFISANLPCNKFKNRLVNIMPYETtrvCLQPIRGVE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1217 GdsNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGRQQYGLMEVE 1296
Cdd:cd14627    80 G--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGRE-KCHQYWPAERSARYQYFVVD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1297 FMSGTADEDLVARVFRVQNISRLQEghLLVRHFQFLRWSAyRDTPDSKKAFLHLLAEVDKWQAESG-DGRTIVHCLNGGG 1375
Cdd:cd14627   157 PMAEYNMPQYILREFKVTDARDGQS--RTVRQFQFTDWPE-QGVPKSGEGFIDFIGQVHKTKEQFGqDGPISVHCSAGVG 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 110735404 1376 RSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEYL 1430
Cdd:cd14627   234 RTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYL 288
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
1217-1428 3.60e-45

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350471 [Multi-domain]  Cd Length: 228  Bit Score: 163.29  E-value: 3.60e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1217 GDSN-NYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGRQQYGLMEV 1295
Cdd:cd14623    20 GEENtDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQE-KCAQYWPSDGSVSYGDITI 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1296 EFMSGTADEDLVARVFRVQNISRLQEGHllVRHFQFLRWSAYrDTPDSKKAFLHLLAEVDKWQAESGDGRTIVHCLNGGG 1375
Cdd:cd14623    99 ELKKEEECESYTVRDLLVTNTRENKSRQ--IRQFHFHGWPEV-GIPSDGKGMINIIAAVQKQQQQSGNHPITVHCSAGAG 175
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 110735404 1376 RSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1428
Cdd:cd14623   176 RTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
933-1133 4.96e-45

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21) and type 14 (PTPN14) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Both PTPN21 and PTPN14 contain an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350388 [Multi-domain]  Cd Length: 219  Bit Score: 162.24  E-value: 4.96e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  933 YINANYIDGY--HRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWP-----EDSDTYGDIKIM 1005
Cdd:cd14540     1 YINASHITATvgGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPtlggeHDALTFGEYKVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1006 LVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKA------------STPPdagPIVI 1073
Cdd:cd14540    81 TKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSvrrhtnqdvaghNRNP---PTLV 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1074 HCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1133
Cdd:cd14540   158 HCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQ 217
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
1140-1430 5.29e-45

PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type tyrosine-protein phosphatase-like D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350476 [Multi-domain]  Cd Length: 292  Bit Score: 164.90  E-value: 5.29e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1140 TTIPVSEFKATYKEMIRIDPQSNSSQLREEFQTLNSVTPplDVEECSIALLPRNRDKNRSMDVLPPDR---CLPFLISTD 1216
Cdd:cd14628     1 TEVPARNLYAYIQKLTQIETGENVTGMELEFKRLASSKA--HTSRFISANLPCNKFKNRLVNIMPYEStrvCLQPIRGVE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1217 GdsNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGRQQYGLMEVE 1296
Cdd:cd14628    79 G--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGRE-KCHQYWPAERSARYQYFVVD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1297 FMSGTADEDLVARVFRVQNISRLQEghLLVRHFQFLRWSAyRDTPDSKKAFLHLLAEVDKWQAESG-DGRTIVHCLNGGG 1375
Cdd:cd14628   156 PMAEYNMPQYILREFKVTDARDGQS--RTVRQFQFTDWPE-QGVPKSGEGFIDFIGQVHKTKEQFGqDGPISVHCSAGVG 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 110735404 1376 RSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEYL 1430
Cdd:cd14628   233 RTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYL 287
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
1140-1430 2.08e-44

PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350477 [Multi-domain]  Cd Length: 291  Bit Score: 163.36  E-value: 2.08e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1140 TTIPVSEFKATYKEMIRIDPQSNSSQLREEFQTLNSVTPplDVEECSIALLPRNRDKNRSMDVLPPDR---CLPFLISTD 1216
Cdd:cd14629     2 TEVPARNLYAHIQKLTQVPPGESVTAMELEFKLLANSKA--HTSRFISANLPCNKFKNRLVNIMPYELtrvCLQPIRGVE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1217 GdsNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGRQQYGLMEVE 1296
Cdd:cd14629    80 G--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGRE-KCHQYWPAERSARYQYFVVD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1297 FMSGTADEDLVARVFRVQNISRLQEghLLVRHFQFLRWSAyRDTPDSKKAFLHLLAEVDKWQAESG-DGRTIVHCLNGGG 1375
Cdd:cd14629   157 PMAEYNMPQYILREFKVTDARDGQS--RTIRQFQFTDWPE-QGVPKTGEGFIDFIGQVHKTKEQFGqDGPITVHCSAGVG 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 110735404 1376 RSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEYL 1430
Cdd:cd14629   234 RTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEYL 288
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
915-1132 2.63e-44

catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3), also called protein-tyrosine phosphatase H1 (PTP-H1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN3 and p38gamma cooperate to promote Ras-induced oncogenesis. PTPN3 is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. Its PDZ domain binds with the PDZ-binding motif of p38gamma and enables efficient tyrosine dephosphorylation.


Pssm-ID: 350448 [Multi-domain]  Cd Length: 274  Bit Score: 162.33  E-value: 2.63e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  915 YDRHRVKLhpmlgDPNADYINANYID----GYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSR 990
Cdd:cd14600    52 YDATRVVL-----QGNEDYINASYVNmeipSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQ 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  991 YWPEDSDT--YGDIKIMLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKaSTPPDA 1068
Cdd:cd14600   127 YWPDPPDVmeYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTVTHLQYVAWPDHGVPDDSSDFLEFVNYVR-SKRVEN 205
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110735404 1069 GPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAIL 1132
Cdd:cd14600   206 EPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAIL 269
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
933-1129 1.20e-43

PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein phosphatase non-receptor type 23 (PTPN23), also called His domain-containing protein tyrosine phosphatase (HD-PTP) or protein tyrosine phosphatase TD14 (PTP-TD14), is a catalytically inactive member of the tyrosine-specific protein tyrosine phosphatase (PTP) family. Human PTPN23 may be involved in the regulation of small nuclear ribonucleoprotein assembly and pre-mRNA splicing by modifying the survival motor neuron (SMN) complex. It plays a role in ciliogenesis and is part of endosomal sorting complex required for transport (ESCRT) pathways. PTPN23 contains five domains: a BRO1-like domain that plays a role in endosomal sorting; a V-domain that interacts with Lys63-linked polyubiquitinated substrates; a central proline-rich region that might recruit SH3-containing proteins; a PTP-like domain; and a proteolytic degradation-targeting motif, also known as a PEST sequence.


Pssm-ID: 350387 [Multi-domain]  Cd Length: 205  Bit Score: 157.93  E-value: 1.20e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  933 YINANYIDGY-HRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPED---SDTYGDIKIMLVK 1008
Cdd:cd14539     1 YINASLIEDLtPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErgqALVYGAITVSLQS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1009 TETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKA---STPPDAGPIVIHCSAGTGRTGCY 1085
Cdd:cd14539    81 VRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHShylQQRSLQTPIVVHCSSGVGRTGAF 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 110735404 1086 -IVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHD 1129
Cdd:cd14539   161 cLLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
907-1142 1.40e-43

catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1), also called protein-tyrosine phosphatase 1B (PTP-1B), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1/PTP-1B is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It contains an N-terminal catalytic PTP domain, followed by two tandem proline-rich motifs that mediate interaction with SH3-domain-containing proteins, and a small hydrophobic stretch that localizes the enzyme to the endoplasmic reticulum (ER). It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor.


Pssm-ID: 350456 [Multi-domain]  Cd Length: 277  Bit Score: 160.19  E-value: 1.40e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  907 SRQEPMPAYDRHRVKLHpmlgDPNADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRV 986
Cdd:cd14608    29 NRYRDVSPFDHSRIKLH----QEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  987 KCSRYWPEDSDTY-----GDIKIMLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVK 1061
Cdd:cd14608   105 KCAQYWPQKEEKEmifedTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVR 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1062 --ASTPPDAGPIVIHCSAGTGRTGCYIVLD---VMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEAC- 1135
Cdd:cd14608   185 esGSLSPEHGPVVVHCSAGIGRSGTFCLADtclLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEGAk 264

                  ....*...
gi 110735404 1136 -LCGETTI 1142
Cdd:cd14608   265 fIMGDSSV 272
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
933-1128 6.93e-43

protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis thaliana protein tyrosine phosphatase 1 (AtPTP1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. AtPTP1 dephosphorylates and inhibits MAP kinase 6 (MPK6) in non-oxidative stress conditions. Together with MAP kinase phosphatase 1 (MKP1) it expresses salicylic acid (SA) and camalexin biosynthesis, and therefore, modulating defense response.


Pssm-ID: 350496 [Multi-domain]  Cd Length: 206  Bit Score: 155.70  E-value: 6.93e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  933 YINANYIDGYHRSNH--FIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVE-VGRVKCSRYWP---EDSDTYGDIKImL 1006
Cdd:cd17658     1 YINASLVETPASESLpkFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDnYSTAKCADYFPaeeNESREFGRISV-T 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1007 VKTETLAEYVvrtfaLERRGYSARH--------EVRQFHFTAWPEHGVPYHATGLLAFIRRVkASTPPDAGPIVIHCSAG 1078
Cdd:cd17658    80 NKKLKHSQHS-----ITLRVLEVQYieseepplSVLHIQYPEWPDHGVPKDTRSVRELLKRL-YGIPPSAGPIVVHCSAG 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 110735404 1079 TGRTGCYIVLDVML------DMAecegVVDIYNCVKTLCSRRVNMIQTEEQYIFIH 1128
Cdd:cd17658   154 IGRTGAYCTIHNTIrrilegDMS----AVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
1164-1423 9.49e-43

catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein phosphatase non-receptor type 9 (PTPN9), also called protein-tyrosine phosphatase MEG2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN9 plays an important role in promoting intracellular secretary vesicle fusion in hematopoietic cells and promotes the dephosphorylation of ErbB2 and EGFR in breast cancer cells, leading to impaired activation of STAT5 and STAT3. It also directly dephosphorylates STAT3 at the Tyr705 residue, resulting in its inactivation. PTPN9 has been found to be dysregulated in various human cancers, including breast, colorectal, and gastric cancer.


Pssm-ID: 350391 [Multi-domain]  Cd Length: 271  Bit Score: 157.53  E-value: 9.49e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1164 SQLREEFQTLnSVTPPLDVEECSiaLLPRNRDKNRSMDVLPPDRCLPFLISTDGDSN-NYINAALTDSYTRSAAFIVTLH 1242
Cdd:cd14543     3 RGIYEEYEDI-RREPPAGTFLCS--LAPANQEKNRYGDVLCLDQSRVKLPKRNGDERtDYINANFMDGYKQKNAYIATQG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1243 PLQSTTPDFWRLVYDYGCTSIVMLNQLNQsNSAWPCLQYWP--EPGRQQYGLMEVEFMSGTADEDLVARVFRVQNISRLQ 1320
Cdd:cd14543    80 PLPKTYSDFWRMVWEQKVLVIVMTTRVVE-RGRVKCGQYWPleEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1321 EghLLVRHFQFLRWSAYrDTPDSKKAFLHLLAEV------------DKWQAESGDGRTIVHCLNGGGRSGTFCA---CAT 1385
Cdd:cd14543   159 S--RQVTHFQFTSWPDF-GVPSSAAALLDFLGEVrqqqalavkamgDRWKGHPPGPPIVVHCSAGIGRTGTFCTldiCLS 235
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 110735404 1386 VLEMIRchnLVDVFFAAKTLRNYKPNMVETMDQYHFCY 1423
Cdd:cd14543   236 QLEDVG---TLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
907-1131 4.62e-40

catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein phosphatase non-receptor type 2 (PTPN2), also called T-cell protein-tyrosine phosphatase (TCPTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN2, a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner. It is deleted in 6% of all T-cell acute lymphoblastic leukemias and is associated with constitutive JAK1/STAT5 signaling and tumorigenesis.


Pssm-ID: 350455 [Multi-domain]  Cd Length: 257  Bit Score: 149.35  E-value: 4.62e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  907 SRQEPMPAYDRHRVKLHPMlgdpNADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRV 986
Cdd:cd14607    28 NRYRDVSPYDHSRVKLQNT----ENDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKDSV 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  987 KCSRYWPEDSD---TYGD--IKIMLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVK 1061
Cdd:cd14607   104 KCAQYWPTDEEevlSFKEtgFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVR 183
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110735404 1062 --ASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEG--VVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAI 1131
Cdd:cd14607   184 esGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKYRMGLIQTPDQLRFSYMAV 257
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
884-1133 1.11e-39

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 149.77  E-value: 1.11e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  884 FKQEYESFFEG------WDATKKKDkVKGSRQEPMPAYDRHRVKLHpmLGDPNADYINANYIDGYHRSNHFIATQGPKPE 957
Cdd:PHA02742   28 LKEEHEHIMQEivafscNESLELKN-MKKCRYPDAPCFDRNRVILK--IEDGGDDFINASYVDGHNAKGRFICTQAPLEE 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  958 MVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYW---PEDSDTYGDIKIMLVKTETLAEYVVRTFALERRGYSARHEVR 1034
Cdd:PHA02742  105 TALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYWmphERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIK 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1035 QFHFTAWPEHGVPYHATGLLAFIRRV-----------KASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDI 1103
Cdd:PHA02742  185 HFAYEDWPHGGLPRDPNKFLDFVLAVreadlkadvdiKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPL 264
                         250       260       270
                  ....*....|....*....|....*....|
gi 110735404 1104 YNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1133
Cdd:PHA02742  265 LSIVRDLRKQRHNCLSLPQQYIFCYFIVLI 294
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
915-1133 6.95e-38

catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein phosphatase non-receptor type 14 (PTPN14), also called protein-tyrosine phosphatase pez, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN14 is a potential tumor suppressor and plays a regulatory role in the Hippo and Wnt/beta-catenin signaling pathways. It contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350447 [Multi-domain]  Cd Length: 287  Bit Score: 144.37  E-value: 6.95e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  915 YDRHRVKLHPMlGDPNADYINANYIDGYHRSN--HFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYW 992
Cdd:cd14599    50 YEENRVELVPT-KENNTGYINASHIKVTVGGEewHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYW 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  993 PE-----DSDTYGDIKIML-VKTETLAeYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAF---IRRVKAS 1063
Cdd:cd14599   129 PKlgskhSSATYGKFKVTTkFRTDSGC-YATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEEVQGFLSYleeIQSVRRH 207
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110735404 1064 TPP--DAG-----PIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1133
Cdd:cd14599   208 TNSmlDSTkncnpPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQ 284
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
895-1128 8.66e-38

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 144.76  E-value: 8.66e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  895 WDATKKKDKVKGSRQEPMPAYDRHRVKLHPMLGDpNADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSI 974
Cdd:PHA02747   43 IANFEKPENQPKNRYWDIPCWDHNRVILDSGGGS-TSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSII 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  975 VMITKLVEV-GRVKCSRYW--PEDSD-TYGDIKIMLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHA 1050
Cdd:PHA02747  122 VMLTPTKGTnGEEKCYQYWclNEDGNiDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKISHFQCSEWFEDETPSDH 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1051 TGLLAFI------RRVKAS--TPPDA--GPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQT 1120
Cdd:PHA02747  202 PDFIKFIkiidinRKKSGKlfNPKDAllCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMN 281

                  ....*...
gi 110735404 1121 EEQYIFIH 1128
Cdd:PHA02747  282 FDDYLFIQ 289
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
1158-1421 8.90e-38

PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type tyrosine-protein phosphatase N2 (PTPRN2 or R-PTP-N2), also called islet cell autoantigen-related protein (IAR), ICAAR, phogrin, or IA-2beta, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. It is mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells. It may function as a phosphatidylinositol phosphatase to regulate insulin secretion. It is also required for normal accumulation of the neurotransmitters norepinephrine, dopamine and serotonin in the brain.


Pssm-ID: 350458 [Multi-domain]  Cd Length: 283  Bit Score: 143.66  E-value: 8.90e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1158 DPQSNSSQLREEFQTLNSVTPPLDVeeCSIALLPRNRDKNRSMDVLPPDRCLPFL-ISTDGDSNNYINAA-LTDSYTRSA 1235
Cdd:cd14610    11 DHLKNKNRLEKEWEALCAYQAEPNA--TNVAQREENVQKNRSLAVLPYDHSRIILkAENSHSHSDYINASpIMDHDPRNP 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1236 AFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQsNSAWPCLQYWPEPGRQQYGLMEVEFMSGTA-DEDLVARVFRVQ 1314
Cdd:cd14610    89 AYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAE-NGVKQCYHYWPDEGSNLYHIYEVNLVSEHIwCEDFLVRSFYLK 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1315 NISRLQEghLLVRHFQFLRWSAyRDTPDSKKAFLHLLAEVDKWQAesgdGRT---IVHCLNGGGRSGTFCACATVL-EMI 1390
Cdd:cd14610   168 NLQTNET--RTVTQFHFLSWND-QGVPASTRSLLDFRRKVNKCYR----GRScpiIVHCSDGAGRSGTYILIDMVLnKMA 240
                         250       260       270
                  ....*....|....*....|....*....|.
gi 110735404 1391 RCHNLVDVFFAAKTLRNYKPNMVETMDQYHF 1421
Cdd:cd14610   241 KGAKEIDIAATLEHLRDQRPGMVQTKEQFEF 271
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
1193-1428 2.15e-37

catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350401 [Multi-domain]  Cd Length: 238  Bit Score: 140.99  E-value: 2.15e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1193 NRDKNRSMDVLPPDRCLPFLISTDG-DSNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLnQ 1271
Cdd:cd14553     3 NKPKNRYANVIAYDHSRVILQPIEGvPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKL-E 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1272 SNSAWPCLQYWPEPGRQQYGLMEVEFMSGTADEDLVARVFRV--QNISRLQEghllVRHFQFLRWSAYrDTPDSKKAFLH 1349
Cdd:cd14553    82 ERSRVKCDQYWPTRGTETYGLIQVTLLDTVELATYTVRTFALhkNGSSEKRE----VRQFQFTAWPDH-GVPEHPTPFLA 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110735404 1350 LLAEVdKWQAESGDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1428
Cdd:cd14553   157 FLRRV-KACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLE 234
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
1198-1421 2.84e-37

catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar proteins; R3 subfamily receptor-type phosphotyrosine phosphatases (RPTP) are characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. Vertebrate members include receptor-type tyrosine-protein phosphatase-like O (PTPRO), J (PTPRJ), Q (PTPRQ), B (PTPRB), V (PTPRV) and H (PTPRH). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Most members are PTPs, except for PTPRQ, which dephosphorylates phosphatidylinositide substrates. PTPRV is characterized only in rodents; its function has been lost in humans. Both vertebrate and invertebrate R3 subfamily RPTPs are involved in the control of a variety of cellular processes, including cell growth, differentiation, mitotic cycle and oncogenic transformation.


Pssm-ID: 350396 [Multi-domain]  Cd Length: 222  Bit Score: 140.18  E-value: 2.84e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1198 RSMDVLPPDRCLPFLISTDGDS-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQsNSAW 1276
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINEEEgSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCME-KGRV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1277 PCLQYWPEPGRQQ-YGLMEVEFMSGTADEDLVARVFRVQNISRlqegHLLVRHFQFLRWSAYR--DTPDSKKAFLHLLAE 1353
Cdd:cd14548    80 KCDHYWPFDQDPVyYGDITVTMLSESVLPDWTIREFKLERGDE----VRSVRQFHFTAWPDHGvpEAPDSLLRFVRLVRD 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110735404 1354 vdkwQAESGDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHF 1421
Cdd:cd14548   156 ----YIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIF 219
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
1222-1423 4.40e-36

PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350398 [Multi-domain]  Cd Length: 200  Bit Score: 135.91  E-value: 4.40e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1222 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQlNQSNSAWPClqYWPEPGRQQYG------LMEV 1295
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTD-NELNEDEPI--YWPTKEKPLECetfkvtLSGE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1296 EFMSGTADEDLVARVFRVQNIsrlQEGHLL-VRHFQFLRWSAyRDTPDSKkaFLHLLAEVDKWqAESGDGRTIVHCLNGG 1374
Cdd:cd14550    78 DHSCLSNEIRLIVRDFILEST---QDDYVLeVRQFQCPSWPN-PCSPIHT--VFELINTVQEW-AQQRDGPIVVHDRYGG 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 110735404 1375 GRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCY 1423
Cdd:cd14550   151 VQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLY 199
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
1188-1421 1.42e-35

catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type tyrosine-protein phosphatase O (PTPRO or R-PTP-O), also known as glomerular epithelial protein 1 or protein tyrosine phosphatase U2 (PTP-U2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRO is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is essential for sustaining the structure and function of foot processes by regulating tyrosine phosphorylation of podocyte proteins. It has been identified as a synaptic cell adhesion molecule (CAM) that serves as a potent initiator of synapse formation. It is also a tumor suppressor in several types of cancer, such as hepatocellular carcinoma, lung cancer, and breast cancer.


Pssm-ID: 350462 [Multi-domain]  Cd Length: 245  Bit Score: 136.17  E-value: 1.42e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1188 ALLPRNRDKNRSMDVLPPDRCLPFLISTDGDS-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVML 1266
Cdd:cd14614     7 ADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEgSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVML 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1267 NQLNQSNSAwPCLQYWP---EPgrQQYGLMEVEFMSGTADEDLVARVFRVQNISRLQEghllVRHFQFLRWSAYR-DTPD 1342
Cdd:cd14614    87 TQCNEKRRV-KCDHYWPfteEP--VAYGDITVEMLSEEEQPDWAIREFRVSYADEVQD----VMHFNYTAWPDHGvPTAN 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110735404 1343 SKKAFLHLLAEVdKWQAESGDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHF 1421
Cdd:cd14614   160 AAESILQFVQMV-RQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIF 237
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
933-1127 1.67e-35

PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350398 [Multi-domain]  Cd Length: 200  Bit Score: 134.37  E-value: 1.67e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  933 YINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCsrYWPEDSDT--YGDIKIMLVKTE 1010
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDEPI--YWPTKEKPleCETFKVTLSGED 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1011 TL-----AEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATglLAFIRRVKASTPPDAGPIVIH-----CSAGTg 1080
Cdd:cd14550    79 HSclsneIRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTV--FELINTVQEWAQQRDGPIVVHdryggVQAAT- 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 110735404 1081 rtgcYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFI 1127
Cdd:cd14550   156 ----FCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFL 198
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
1222-1424 1.90e-35

catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350397 [Multi-domain]  Cd Length: 204  Bit Score: 134.40  E-value: 1.90e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1222 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGRQQYGLMEVEFMSGT 1301
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRR-KCDQYWPKEGTETYGNIQVTLLSTE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1302 ADEDLVARVFRVQNI----SRLQEGHLLVRHFQFLRWSAYrDTPDSKkafLHLLAEVDKWQAES--GDGRTIVHCLNGGG 1375
Cdd:cd14549    80 VLATYTVRTFSLKNLklkkVKGRSSERVVYQYHYTQWPDH-GVPDYT---LPVLSFVRKSSAANppGAGPIVVHCSAGVG 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 110735404 1376 RSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCYD 1424
Cdd:cd14549   156 RTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1032-1133 6.42e-35

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 129.02  E-value: 6.42e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404   1032 EVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTP--PDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECE-GVVDIYNCVK 1108
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNqsESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80
                            90       100
                    ....*....|....*....|....*
gi 110735404   1109 TLCSRRVNMIQTEEQYIFIHDAILE 1133
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
1032-1133 6.42e-35

Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine phosphatases. Homologues detected by this profile and not by those of "PTPc" or "DSPc" are predicted to be protein phosphatases with a similar fold to DSPs and PTPs, yet with unpredicted specificities.


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 129.02  E-value: 6.42e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404   1032 EVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTP--PDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECE-GVVDIYNCVK 1108
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNqsESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80
                            90       100
                    ....*....|....*....|....*
gi 110735404   1109 TLCSRRVNMIQTEEQYIFIHDAILE 1133
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
1197-1428 9.01e-35

catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type tyrosine-protein phosphatase J (PTPRJ or R-PTP-J), also known as receptor-type tyrosine-protein phosphatase eta (R-PTP-eta) or density-enhanced phosphatase 1 (DEP-1) OR CD148, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRJ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (eight in PTPRJ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed in various cell types including epithelial, hematopoietic, and endothelial cells. It plays a role in cell adhesion, migration, proliferation and differentiation. It dephosphorylates or contributes to the dephosphorylation of various substrates including protein kinases such as FLT3, PDGFRB, MET, RET (variant MEN2A), VEGFR-2, LYN, SRC, MAPK1, MAPK3, and EGFR, as well as PIK3R1 and PIK3R2.


Pssm-ID: 350463 [Multi-domain]  Cd Length: 229  Bit Score: 133.40  E-value: 9.01e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1197 NRSMDVLPPDRCLPFLISTDGDSNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAw 1276
Cdd:cd14615     1 NRYNNVLPYDISRVKLSVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1277 PCLQYWPEPGRQQYGLMEVEFMSGTADEDLVARVFRVQNISRLQEGHllVRHFQFLRWSAYR--DTPDSKKAFLHLLAEV 1354
Cdd:cd14615    80 KCEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRT--VRHFHFTSWPDHGvpETTDLLINFRHLVREY 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110735404 1355 DKwqAESGDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1428
Cdd:cd14615   158 MK--QNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
1158-1421 3.33e-34

PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type tyrosine-protein phosphatase-like N (PTPRN or R-PTP-N), also called islet cell antigen 512 (ICA512) or PTP IA-2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. PTPRN is located in secretory granules of neuroendocrine cells and is involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. It is a major autoantigen in type 1 diabetes and is involved in the regulation of insulin secretion.


Pssm-ID: 350457 [Multi-domain]  Cd Length: 281  Bit Score: 133.24  E-value: 3.33e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1158 DPQSNSSQLREEFQTLNSVTPplDVEECSIALLPRNRDKNRSMDVLPPDRC-LPFLISTDGDSNNYINAA-LTDSYTRSA 1235
Cdd:cd14609     9 DHLRNRDRLAKEWQALCAYQA--EPNTCSTAQGEANVKKNRNPDFVPYDHArIKLKAESNPSRSDYINASpIIEHDPRMP 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1236 AFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQsNSAWPCLQYWPEPGRQQYGLMEVEFMSGTA-DEDLVARVFRVQ 1314
Cdd:cd14609    87 AYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVE-DGVKQCDRYWPDEGSSLYHIYEVNLVSEHIwCEDFLVRSFYLK 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1315 NIsRLQEGHLLVRhFQFLRWSAyRDTPDSKKAFLHLLAEVDKwqaeSGDGRT---IVHCLNGGGRSGTFCACATVL-EMI 1390
Cdd:cd14609   166 NV-QTQETRTLTQ-FHFLSWPA-EGIPSSTRPLLDFRRKVNK----CYRGRScpiIVHCSDGAGRTGTYILIDMVLnRMA 238
                         250       260       270
                  ....*....|....*....|....*....|.
gi 110735404 1391 RCHNLVDVFFAAKTLRNYKPNMVETMDQYHF 1421
Cdd:cd14609   239 KGVKEIDIAATLEHVRDQRPGMVRTKDQFEF 269
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
929-1127 3.83e-34

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 133.29  E-value: 3.83e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  929 PNADYINANYIDGYhRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVG--RVKCSRYWPEDSDtYG--DIKI 1004
Cdd:COG5599    61 ANLGYLNANYIQVI-GNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISkpKVKMPVYFRQDGE-YGkyEVSS 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1005 MLVKTETLAEYV-VRTFALERRGYSAR-HEVRQFHFTAWPEHGVPyHATGLLAFIRRVKAS---TPPDAGPIVIHCSAGT 1079
Cdd:COG5599   139 ELTESIQLRDGIeARTYVLTIKGTGQKkIEIPVLHVKNWPDHGAI-SAEALKNLADLIDKKekiKDPDKLLPVVHCRAGV 217
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 110735404 1080 GRTGCYIVLDVMLDM--AECEGVVDIYNCVKTL-CSRRVNMIQTEEQYIFI 1127
Cdd:COG5599   218 GRTGTLIACLALSKSinALVQITLSVEEIVIDMrTSRNGGMVQTSEQLDVL 268
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
1222-1423 8.94e-34

PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type tyrosine-protein phosphatase-like N (PTPRN) and N2 (PTPRN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). They consist of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. They are mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells, and are involved in involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. They also are major autoantigens in type 1 diabetes and are involved in the regulation of insulin secretion.


Pssm-ID: 350394 [Multi-domain]  Cd Length: 208  Bit Score: 129.49  E-value: 8.94e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1222 YINAA-LTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLnQSNSAWPCLQYWPEPGRQQYGLMEVEFMSG 1300
Cdd:cd14546     1 YINAStIYDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRL-QENGVKQCARYWPEEGSEVYHIYEVHLVSE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1301 TA-DEDLVARVFRVQNIsRLQEGHlLVRHFQFLRWSAyRDTPDSKKAFLHLLAEVDKwqaeSGDGRT---IVHCLNGGGR 1376
Cdd:cd14546    80 HIwCDDYLVRSFYLKNL-QTSETR-TVTQFHFLSWPD-EGIPASAKPLLEFRRKVNK----SYRGRScpiVVHCSDGAGR 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 110735404 1377 SGTFCACATVLE-MIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCY 1423
Cdd:cd14546   153 TGTYILIDMVLNrMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVL 200
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
933-1133 9.00e-34

PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350482 [Multi-domain]  Cd Length: 206  Bit Score: 129.76  E-value: 9.00e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  933 YINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLvEVGRVkCSRYWPEDSD-TYGDIKIMLVKTET 1011
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM-DAAQL-CMQYWPEKTScCYGPIQVEFVSADI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1012 LAEYVVRTF-----ALERRGYSArheVRQFHFTAWPEH-GVPYHATGLLAFIRRV-KASTPPDA--GPIVIHCSAGTGRT 1082
Cdd:cd14634    79 DEDIISRIFricnmARPQDGYRI---VQHLQYIGWPAYrDTPPSKRSILKVVRRLeKWQEQYDGreGRTVVHCLNGGGRS 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 110735404 1083 GCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1133
Cdd:cd14634   156 GTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
933-1133 1.21e-33

catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21), also called protein-tyrosine phosphatase D1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN21 is a component of a multivalent scaffold complex nucleated by focal adhesion kinase (FAK) at specific intracellular sites. It promotes cytoskeleton events that induce cell adhesion and migration by modulating Src-FAK signaling. It can also selectively associate with and stimulate Tec family kinases and modulate Stat3 activation. Human PTPN21 may also play a pathologic role in gastrointestinal tract tumorigenesis. PTPN21 contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350446 [Multi-domain]  Cd Length: 220  Bit Score: 129.71  E-value: 1.21e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  933 YINANYIDGYHRSNH--FIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWP-----EDSDTYGDIKIM 1005
Cdd:cd14598     1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrlgsrHNTVTYGRFKIT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1006 L-VKTETLAeYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFI-------RRVKASTPPDAG--PIVIHC 1075
Cdd:cd14598    81 TrFRTDSGC-YATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLeeiqsvrRHTNSTIDPKSPnpPVLVHC 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 110735404 1076 SAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1133
Cdd:cd14598   160 SAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQ 217
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
1193-1428 5.28e-33

catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350474 [Multi-domain]  Cd Length: 276  Bit Score: 129.77  E-value: 5.28e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1193 NRDKNRSMDVLPPDRCLPFLISTDG-DSNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLnQ 1271
Cdd:cd14626    41 NKPKNRYANVIAYDHSRVILTSVDGvPGSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRL-E 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1272 SNSAWPCLQYWPEPGRQQYGLMEVEFMSGTADEDLVARVFRVQNISRLQEGHllVRHFQFLRWSAYrDTPDSKKAFLHLL 1351
Cdd:cd14626   120 EKSRVKCDQYWPIRGTETYGMIQVTLLDTVELATYSVRTFALYKNGSSEKRE--VRQFQFMAWPDH-GVPEYPTPILAFL 196
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110735404 1352 AEVDKWQAESGdGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1428
Cdd:cd14626   197 RRVKACNPPDA-GPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLE 272
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
1194-1423 1.05e-32

catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1) type 2 (PTPN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases, (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1 (or PTP-1B) is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor. PTPN2 (or TCPTP), a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner.


Pssm-ID: 350393 [Multi-domain]  Cd Length: 231  Bit Score: 127.51  E-value: 1.05e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1194 RDKNRSMDVLPPDRCLpfLISTDGDsNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSN 1273
Cdd:cd14545     1 LNRYRDRDPYDHDRSR--VKLKQGD-NDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1274 SAwPCLQYWPEPGRQQYGL----MEVEFMSGTADEDLVARVFRVQNISRLQEghLLVRHFQFLRWSAYrDTPDSKKAFLH 1349
Cdd:cd14545    78 QI-KCAQYWPQGEGNAMIFedtgLKVTLLSEEDKSYYTVRTLELENLKTQET--REVLHFHYTTWPDF-GVPESPAAFLN 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110735404 1350 LLAEV-DKWQAESGDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNL--VDVFFAAKTLRNYKPNMVETMDQYHFCY 1423
Cdd:cd14545   154 FLQKVrESGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRFSY 230
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
1197-1427 1.25e-32

catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type tyrosine-protein phosphatase V (PTPRV or R-PTP-V), also known as embryonic stem cell protein-tyrosine phosphatase (ES cell phosphatase) or osteotesticular protein-tyrosine phosphatase (OST-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRV is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. In rodents, it may play a role in the maintenance of pluripotency and may function in signaling pathways during bone remodeling. It is the only PTP whose function has been lost between rodent and human. The human OST-PTP gene is a pseudogene.


Pssm-ID: 350466 [Multi-domain]  Cd Length: 230  Bit Score: 126.98  E-value: 1.25e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1197 NRSMDVLPPDRCLPFLISTDGDS-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNqLNQSNSA 1275
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEPhSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLT-VGMENGR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1276 WPCLQYWP-EPGRQQYGLMEVEFMSGTADEDLVARVFRVQNISRLQEGHllVRHFQFLRWSAYR--DTPDSKKAFLHLLA 1352
Cdd:cd14618    80 VLCDHYWPsESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERR--VKHLHYTAWPDHGipESTSSLMAFRELVR 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110735404 1353 EvdKWQAESGDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVAL 1427
Cdd:cd14618   158 E--HVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
1142-1428 1.70e-32

catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350473 [Multi-domain]  Cd Length: 282  Bit Score: 128.29  E-value: 1.70e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1142 IPVSEFkATYKEMIRIDpqsNSSQLREEFQTLNsvtpPLDVEECSIALLPRNRDKNRSMDVLPPDRCLPFLISTDG-DSN 1220
Cdd:cd14625     4 IPISEL-AEHTERLKAN---DNLKLSQEYESID----PGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGiMGS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1221 NYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLnQSNSAWPCLQYWPEPGRQQYGLMEVEFMSG 1300
Cdd:cd14625    76 DYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKL-EEKSRIKCDQYWPSRGTETYGMIQVTLLDT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1301 TADEDLVARVFRVQNISRLQEGHllVRHFQFLRWSAYrDTPDSKKAFLHLLAEVDKWQAESGdGRTIVHCLNGGGRSGTF 1380
Cdd:cd14625   155 IELATFCVRTFSLHKNGSSEKRE--VRQFQFTAWPDH-GVPEYPTPFLAFLRRVKTCNPPDA-GPIVVHCSAGVGRTGCF 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 110735404 1381 CACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1428
Cdd:cd14625   231 IVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLE 278
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
933-1133 4.08e-32

PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350484 [Multi-domain]  Cd Length: 206  Bit Score: 124.75  E-value: 4.08e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  933 YINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGrvKCSRYWPEDSD-TYGDIKIMLVKTET 1011
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQ--GCPQYWPEEGMlRYGPIQVECMSCSM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1012 LAEYVVRTFAL-----ERRGYSArheVRQFHFTAWPEH-GVPYHATGLLAFIRRV---KASTPPDAGPIVIHCSAGTGRT 1082
Cdd:cd14636    79 DCDVISRIFRIcnltrPQEGYLM---VQQFQYLGWASHrEVPGSKRSFLKLILQVekwQEECDEGEGRTIIHCLNGGGRS 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 110735404 1083 GCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1133
Cdd:cd14636   156 GMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
1193-1428 1.04e-31

catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350478 [Multi-domain]  Cd Length: 237  Bit Score: 124.75  E-value: 1.04e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1193 NRDKNRSMDVLPPDRCLPFLISTDGDS-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQ 1271
Cdd:cd14630     3 NRNKNRYGNIISYDHSRVRLQLLDGDPhSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1272 SNSAwPCLQYWPEPgRQQYGLMEVEFMSGTADEDLVARVFRVQnisrlQEGHLLVRHFQFLRWSAYRD--TPDSKKAFLH 1349
Cdd:cd14630    83 VGRV-KCVRYWPDD-TEVYGDIKVTLIETEPLAEYVIRTFTVQ-----KKGYHEIREIRQFHFTSWPDhgVPCYATGLLG 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110735404 1350 LLAEVdKWQAESGDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1428
Cdd:cd14630   156 FVRQV-KFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
933-1133 1.06e-31

PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350485 [Multi-domain]  Cd Length: 207  Bit Score: 123.48  E-value: 1.06e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  933 YINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRV-KCSRYWPEDS-DTYGDIKIMLVKTE 1010
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGlQQYGPMEVEFVSGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1011 TLAEYVVRTFALER--RGYSARHEVRQFHFTAW-PEHGVPYHATGLLAFIRRV-KASTPPDAGPIVIHCSAGTGRTGCYI 1086
Cdd:cd14637    81 ADEDIVTRLFRVQNitRLQEGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLASVeKWQRESGEGRTVVHCLNGGGRSGTYC 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 110735404 1087 VLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1133
Cdd:cd14637   161 ASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
1166-1432 2.13e-31

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1).


Pssm-ID: 350469 [Multi-domain]  Cd Length: 296  Bit Score: 125.52  E-value: 2.13e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1166 LREEFQTLNSVtpPLDVEeCSIALLPRNRDKNRSMDVLPPDRCLPFLISTDG-DSNNYINAALTDSYTRSAAFIVTLHPL 1244
Cdd:cd14621    28 FREEFNALPAC--PIQAT-CEAASKEENKEKNRYVNILPYDHSRVHLTPVEGvPDSDYINASFINGYQEKNKFIAAQGPK 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1245 QSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGRQQYGLMEVEFMSGTADEDLVARVFRVQNISRL--QEG 1322
Cdd:cd14621   105 EETVNDFWRMIWEQNTATIVMVTNLKERKEC-KCAQYWPDQGCWTYGNIRVSVEDVTVLVDYTVRKFCIQQVGDVtnKKP 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1323 HLLVRHFQFLRWSAYrDTPDSKKAFLHLLAEVDKWQAESGdGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAA 1402
Cdd:cd14621   184 QRLITQFHFTSWPDF-GVPFTPIGMLKFLKKVKNCNPQYA-GAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFV 261
                         250       260       270
                  ....*....|....*....|....*....|.
gi 110735404 1403 KTLRNYKPNMVETMDQYHFCYDVALE-YLEG 1432
Cdd:cd14621   262 SRIRAQRCQMVQTDMQYVFIYQALLEhYLYG 292
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
1185-1432 2.53e-31

catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1), also called protein-tyrosine phosphatase 1B (PTP-1B), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1/PTP-1B is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It contains an N-terminal catalytic PTP domain, followed by two tandem proline-rich motifs that mediate interaction with SH3-domain-containing proteins, and a small hydrophobic stretch that localizes the enzyme to the endoplasmic reticulum (ER). It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor.


Pssm-ID: 350456 [Multi-domain]  Cd Length: 277  Bit Score: 124.75  E-value: 2.53e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1185 CSIALLPRNRDKNRSMDVLPPDRCLpflISTDGDSNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIV 1264
Cdd:cd14608    17 CRVAKLPKNKNRNRYRDVSPFDHSR---IKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVV 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1265 MLNQLNQSNSAwPCLQYWPEPGRQQYGLMEVEFMSGTADEDL----VARVFRVQNISRLQEGHLLvrHFQFLRWSAYrDT 1340
Cdd:cd14608    94 MLNRVMEKGSL-KCAQYWPQKEEKEMIFEDTNLKLTLISEDIksyyTVRQLELENLTTQETREIL--HFHYTTWPDF-GV 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1341 PDSKKAFLHLLAEVdkwqAESGD-----GRTIVHCLNGGGRSGTFC---ACATVLEMIRCHNLVDVFFAAKTLRNYKPNM 1412
Cdd:cd14608   170 PESPASFLNFLFKV----RESGSlspehGPVVVHCSAGIGRSGTFCladTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGL 245
                         250       260
                  ....*....|....*....|
gi 110735404 1413 VETMDQYHFCYdvaLEYLEG 1432
Cdd:cd14608   246 IQTADQLRFSY---LAVIEG 262
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
1222-1423 6.51e-31

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1).


Pssm-ID: 350399 [Multi-domain]  Cd Length: 202  Bit Score: 121.17  E-value: 6.51e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1222 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQsNSAWPCLQYWPEPGRQQYGLMEVEFMSGT 1301
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKE-RKEKKCSQYWPDQGCWTYGNLRVRVEDTV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1302 ADEDLVARVFRVQNISRL--QEGHLLVRHFQFLRWSAYrDTPDSKKAFLHLLAEVdKWQAESGDGRTIVHCLNGGGRSGT 1379
Cdd:cd14551    80 VLVDYTTRKFCIQKVNRGigEKRVRLVTQFHFTSWPDF-GVPFTPIGMLKFLKKV-KSANPPRAGPIVVHCSAGVGRTGT 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 110735404 1380 FCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCY 1423
Cdd:cd14551   158 FIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
933-1133 7.24e-31

PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350483 [Multi-domain]  Cd Length: 206  Bit Score: 121.33  E-value: 7.24e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  933 YINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKlVEVGRVkCSRYWPEDS-DTYGDIKIMLVKTET 1011
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLND-VDPAQL-CPQYWPENGvHRHGPIQVEFVSADL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1012 LAEYVVRTFAL--ERRGYSARHEVRQFHFTAWPEH-GVPYHATGLLAFIRRV-KASTPPDAGP--IVIHCSAGTGRTGCY 1085
Cdd:cd14635    79 EEDIISRIFRIynAARPQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVdKWQEEYNGGEgrTVVHCLNGGGRSGTF 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 110735404 1086 IVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILE 1133
Cdd:cd14635   159 CAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
1201-1428 8.25e-31

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the first PTP domain (repeat 1).


Pssm-ID: 350468 [Multi-domain]  Cd Length: 229  Bit Score: 121.97  E-value: 8.25e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1201 DVLPPDRCLPFLISTDGD-SNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCL 1279
Cdd:cd14620     3 NILPYDHSRVILSQLDGIpCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEE-KCY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1280 QYWPEPGRQQYGLMEVEFMSGTADEDLVARVFRVQniSRLQEGH---LLVRHFQFLRWSAYrDTPDSKKAFLHLLAEVdK 1356
Cdd:cd14620    82 QYWPDQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQ--PQLPDGCkapRLVTQLHFTSWPDF-GVPFTPIGMLKFLKKV-K 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110735404 1357 WQAESGDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1428
Cdd:cd14620   158 SVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
1222-1428 1.11e-30

catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350480 [Multi-domain]  Cd Length: 205  Bit Score: 120.54  E-value: 1.11e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1222 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGrQQYGLMEVEFMSGT 1301
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRV-KCSKYWPDDS-DTYGDIKITLLKTE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1302 ADEDLVARVFRVQNisRLQEGHLLVRHFQFLRWSAYrDTPDSKKAFLHLLAEVdKWQAESGDGRTIVHCLNGGGRSGTFC 1381
Cdd:cd14632    79 TLAEYSVRTFALER--RGYSARHEVKQFHFTSWPEH-GVPYHATGLLAFIRRV-KASTPPDAGPVVVHCSAGAGRTGCYI 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 110735404 1382 ACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1428
Cdd:cd14632   155 VLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
1222-1423 2.81e-30

protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis thaliana protein tyrosine phosphatase 1 (AtPTP1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. AtPTP1 dephosphorylates and inhibits MAP kinase 6 (MPK6) in non-oxidative stress conditions. Together with MAP kinase phosphatase 1 (MKP1) it expresses salicylic acid (SA) and camalexin biosynthesis, and therefore, modulating defense response.


Pssm-ID: 350496 [Multi-domain]  Cd Length: 206  Bit Score: 119.49  E-value: 2.81e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1222 YINAAL--TDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAWPCLQYWPEPGRQQ--YGLMEVEF 1297
Cdd:cd17658     1 YINASLveTPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTAKCADYFPAEENESreFGRISVTN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1298 MS-GTADEDLVARVFRVQNIsRLQEGHLLVRHFQFLRWSAYrDTPDSKKAFLHLLAEVdkWQAESGDGRTIVHCLNGGGR 1376
Cdd:cd17658    81 KKlKHSQHSITLRVLEVQYI-ESEEPPLSVLHIQYPEWPDH-GVPKDTRSVRELLKRL--YGIPPSAGPIVVHCSAGIGR 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 110735404 1377 SGTFCACATVLEMIRCHNL--VDVFFAAKTLRNYKPNMVETMDQYHFCY 1423
Cdd:cd17658   157 TGAYCTIHNTIRRILEGDMsaVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
1222-1428 5.19e-30

catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The type II (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350403 [Multi-domain]  Cd Length: 204  Bit Score: 118.87  E-value: 5.19e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1222 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEpGRQQYGLMEVEFMSGT 1301
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRV-KCSRYWPD-DTEVYGDIKVTLVETE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1302 ADEDLVARVFRVQN--ISRLQEghllVRHFQFLRWSAYrDTPDSKKAFLHLLAEVdKWQAESGDGRTIVHCLNGGGRSGT 1379
Cdd:cd14555    79 PLAEYVVRTFALERrgYHEIRE----VRQFHFTGWPDH-GVPYHATGLLGFIRRV-KASNPPSAGPIVVHCSAGAGRTGC 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 110735404 1380 FCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1428
Cdd:cd14555   153 YIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
1222-1424 8.88e-30

fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae protein-tyrosine phosphatases 1 (PTP1) and 2 (PTP2), Schizosaccharomyces pombe PTP1, PTP2, and PTP3, and similar fungal proteins. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. PTP2, together with PTP3, is the major phosphatase that dephosphorylates and inactivates the MAP kinase HOG1 and also modulates its subcellular localization.


Pssm-ID: 350509 [Multi-domain]  Cd Length: 212  Bit Score: 118.12  E-value: 8.88e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1222 YINAA-LTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQsNSAWPCLQYWPEPGRQQ-YGLMEVEFMS 1299
Cdd:cd18533     1 YINASyITLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVE-NGREKCDQYWPSGEYEGeYGDLTVELVS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1300 GTADEDLVArVFRVQNISRLQEGHLLVRHFQFLRWSAYRdTPDSKKAFLHLLAEVDKW-QAESGDGRTIVHCLNGGGRSG 1378
Cdd:cd18533    80 EEENDDGGF-IVREFELSKEDGKVKKVYHIQYKSWPDFG-VPDSPEDLLTLIKLKRELnDSASLDPPIIVHCSAGVGRTG 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 110735404 1379 TFCACATVLEMI-RCHNLVD--------VFFAAKTLRNYKPNMVETMDQYHFCYD 1424
Cdd:cd18533   158 TFIALDSLLDELkRGLSDSQdledsedpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
1222-1424 1.16e-29

PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein phosphatase non-receptor type 23 (PTPN23), also called His domain-containing protein tyrosine phosphatase (HD-PTP) or protein tyrosine phosphatase TD14 (PTP-TD14), is a catalytically inactive member of the tyrosine-specific protein tyrosine phosphatase (PTP) family. Human PTPN23 may be involved in the regulation of small nuclear ribonucleoprotein assembly and pre-mRNA splicing by modifying the survival motor neuron (SMN) complex. It plays a role in ciliogenesis and is part of endosomal sorting complex required for transport (ESCRT) pathways. PTPN23 contains five domains: a BRO1-like domain that plays a role in endosomal sorting; a V-domain that interacts with Lys63-linked polyubiquitinated substrates; a central proline-rich region that might recruit SH3-containing proteins; a PTP-like domain; and a proteolytic degradation-targeting motif, also known as a PEST sequence.


Pssm-ID: 350387 [Multi-domain]  Cd Length: 205  Bit Score: 117.87  E-value: 1.16e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1222 YINAALTDSYTRSAA-FIVTLHPLQSTTPDFWRLVYDYGCTSIVMLnQLNQSNSAWPCLQYWPEPGRQQ--YGLMEVEFM 1298
Cdd:cd14539     1 YINASLIEDLTPYCPrFIATQAPLPGTAADFWLMVYEQQVSVIVML-VSEQENEKQKVHRYWPTERGQAlvYGAITVSLQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1299 SGTADEDLVARVFRVQNisRLQEGHLLVRHFQFLRWSAYRdTPDSKKAFLHLLAEVDKW--QAESGDGRTIVHCLNGGGR 1376
Cdd:cd14539    80 SVRTTPTHVERIISIQH--KDTRLSRSVVHLQFTTWPELG-LPDSPNPLLRFIEEVHSHylQQRSLQTPIVVHCSSGVGR 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 110735404 1377 SGTFCAC-ATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCYD 1424
Cdd:cd14539   157 TGAFCLLyAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
1187-1423 1.60e-29

catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein phosphatase non-receptor type 2 (PTPN2), also called T-cell protein-tyrosine phosphatase (TCPTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN2, a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner. It is deleted in 6% of all T-cell acute lymphoblastic leukemias and is associated with constitutive JAK1/STAT5 signaling and tumorigenesis.


Pssm-ID: 350455 [Multi-domain]  Cd Length: 257  Bit Score: 118.92  E-value: 1.60e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1187 IALLPRNRDKNRSMDVLPPDRCLPFLISTDgdsNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVML 1266
Cdd:cd14607    18 VAKYPENRNRNRYRDVSPYDHSRVKLQNTE---NDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVML 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1267 NQLNQSNSAwPCLQYWPEPGRQQYGLMEVEFMSGTADEDL----VARVFRVQNISRLQEghLLVRHFQFLRWSAYrDTPD 1342
Cdd:cd14607    95 NRIVEKDSV-KCAQYWPTDEEEVLSFKETGFSVKLLSEDVksyyTVHLLQLENINSGET--RTISHFHYTTWPDF-GVPE 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1343 SKKAFLHLLAEVdkwqAESG-----DGRTIVHCLNGGGRSGTFCACATVLEMIRCHN--LVDVFFAAKTLRNYKPNMVET 1415
Cdd:cd14607   171 SPASFLNFLFKV----RESGslspeHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKYRMGLIQT 246

                  ....*...
gi 110735404 1416 MDQYHFCY 1423
Cdd:cd14607   247 PDQLRFSY 254
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
1222-1427 2.11e-29

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350507 [Multi-domain]  Cd Length: 204  Bit Score: 117.02  E-value: 2.11e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1222 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNqlNQSNSAWPCLQYWP---EPGRQQ---YGLMEV 1295
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLP--DGQNMAEDEFVYWPnkdEPINCEtfkVTLIAE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1296 EFMSGTADEDLVARVFRVQnisRLQEGHLL-VRHFQFLRWSayrdTPDSKKAFLHLLAEVDKWQAESGDGRTIVHCLNGG 1374
Cdd:cd17669    79 EHKCLSNEEKLIIQDFILE---ATQDDYVLeVRHFQCPKWP----NPDSPISKTFELISIIKEEAANRDGPMIVHDEHGG 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 110735404 1375 GRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVAL 1427
Cdd:cd17669   152 VTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
900-1131 3.18e-29

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 120.13  E-value: 3.18e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  900 KKDKVKGSRQEPMPAYDRHRVKL--HPMLG-----------------DPNADYINANYIDGYHRSNHFIATQGPKPEMVY 960
Cdd:PHA02746   48 KKENLKKNRFHDIPCWDHSRVVInaHESLKmfdvgdsdgkkievtseDNAENYIHANFVDGFKEANKFICAQGPKEDTSE 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  961 DFWRMVWQEHCSSIVMITKlVEVGRVKCSRYW--PEDSD-TYGD--IKIMLVKTETlaEYVVRTFALERRGYSARHEVRQ 1035
Cdd:PHA02746  128 DFFKLISEHESQVIVSLTD-IDDDDEKCFELWtkEEDSElAFGRfvAKILDIIEEL--SFTKTRLMITDKISDTSREIHH 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1036 FHFTAWPEHGVPYHATGLLAFIRRVKA----------STPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYN 1105
Cdd:PHA02746  205 FWFPDWPDNGIPTGMAEFLELINKVNEeqaelikqadNDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGE 284
                         250       260
                  ....*....|....*....|....*.
gi 110735404 1106 CVKTLCSRRVNMIQTEEQYIFIHDAI 1131
Cdd:PHA02746  285 IVLKIRKQRHSSVFLPEQYAFCYKAL 310
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
1190-1428 3.70e-29

catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type tyrosine-protein phosphatase D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350472 [Multi-domain]  Cd Length: 284  Bit Score: 118.68  E-value: 3.70e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1190 LPRNRDKNRSMDVLPPDRCLPFLISTDG-DSNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQ 1268
Cdd:cd14624    44 LEVNKPKNRYANVIAYDHSRVLLSAIEGiPGSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTK 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1269 LnQSNSAWPCLQYWPEPGRQQYGLMEVEFMSGTADEDLVARVFRVQNISRLQEGHllVRHFQFLRWSAYrDTPDSKKAFL 1348
Cdd:cd14624   124 L-EERSRVKCDQYWPSRGTETYGLIQVTLLDTVELATYCVRTFALYKNGSSEKRE--VRQFQFTAWPDH-GVPEHPTPFL 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1349 HLLAEVDKWQAESGdGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1428
Cdd:cd14624   200 AFLRRVKTCNPPDA-GPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLE 278
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
1180-1425 4.58e-29

catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein phosphatase non-receptor type 5 (PTPN5), also called striatum-enriched protein-tyrosine phosphatase (STEP) or neural-specific PTP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN5/STEP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. It is a CNS-enriched protein that regulates key signaling proteins required for synaptic strengthening, as well as NMDA and AMPA receptor trafficking. PTPN5 is implicated in multiple neurologic and neuropsychiatric disorders, such as Alzheimer's disease, Parkinson's disease, schizophrenia, and fragile X syndrome.


Pssm-ID: 350461 [Multi-domain]  Cd Length: 258  Bit Score: 117.66  E-value: 4.58e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1180 LDVEECSIALLPRnrdKNRSMDVLPPDRCLPFLISTDGDS--NNYINAALTDSY-TRSAAFIVTLHPLQSTTPDFWRLVY 1256
Cdd:cd14613    15 VDPKEYDIPGLVR---KNRYKTILPNPHSRVCLTSPDQDDplSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVW 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1257 DYGCTSIVMLNQLNQSNSAwpCLQYWPEPgRQQYGLMEVEFMSGTADEDLVARVFRVQniSRLQEGHLlvRHFQFLRWSA 1336
Cdd:cd14613    92 QERSPIIVMITNIEEMNEK--CTEYWPEE-QVTYEGIEITVKQVIHADDYRLRLITLK--SGGEERGL--KHYWYTSWPD 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1337 YRdTPDSKKAFLHLLAEVD--KWQAESGDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVE 1414
Cdd:cd14613   165 QK-TPDNAPPLLQLVQEVEeaRQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQ 243
                         250
                  ....*....|.
gi 110735404 1415 TMDQYHFCYDV 1425
Cdd:cd14613   244 TCEQYQFVHHV 254
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
1197-1421 1.38e-28

catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; The kinase interaction motif (KIM) family of protein-tyrosine phosphatases (PTPs) includes tyrosine-protein phosphatases non-receptor type 7 (PTPN7) and non-receptor type 5 (PTPN5), and protein-tyrosine phosphatase receptor type R (PTPRR). PTPN7 is also called hematopoietic protein-tyrosine phosphatase (HePTP) while PTPN5 is also called striatal-enriched protein-tyrosine phosphatase (STEP). They belong to the family of classical tyrosine-specific PTPs (EC 3.1.3.48) that catalyze the dephosphorylation of phosphotyrosine peptides. KIM-PTPs are characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. They are highly specific to the MAPKs ERK1/2 (extracellular-signal-regulated kinase 1/2) and p38, over JNK (c-Jun N-terminal kinase); they dephosphorylate these kinases and thereby critically modulate cell proliferation and differentiation.


Pssm-ID: 350395 [Multi-domain]  Cd Length: 224  Bit Score: 115.19  E-value: 1.38e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1197 NRSMDVLPPDR---CLPflISTDGDSNNYINAaltdSYTR-----SAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQ 1268
Cdd:cd14547     1 NRYKTILPNEHsrvCLP--SVDDDPLSSYINA----NYIRgydgeEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1269 LNQSNSAwpCLQYWPEPGRQQYGLMEVEFMSGTADEDlvarvFRVQNISRLQEGHLL-VRHFQFLRWSAYRdTPDSKKAF 1347
Cdd:cd14547    75 LTEAKEK--CAQYWPEEENETYGDFEVTVQSVKETDG-----YTVRKLTLKYGGEKRyLKHYWYTSWPDHK-TPEAAQPL 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110735404 1348 LHLLAEVDKW-QAESGDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHF 1421
Cdd:cd14547   147 LSLVQEVEEArQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEF 221
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
1222-1427 3.57e-28

PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350508 [Multi-domain]  Cd Length: 205  Bit Score: 113.62  E-value: 3.57e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1222 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVML--NQ-LNQSNSAwpclqYWPEpgRQQ--------Y 1290
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdNQgLAEDEFV-----YWPS--REEsmnceaftV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1291 GLMEVEFMSGTADEDLVARVFRVQNIsrlQEGHLL-VRHFQFLRWSayrdTPDSKKAFLHLLAEVDKWQAESGDGRTIVH 1369
Cdd:cd17670    74 TLISKDRLCLSNEEQIIIHDFILEAT---QDDYVLeVRHFQCPKWP----NPDAPISSTFELINVIKEEALTRDGPTIVH 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 110735404 1370 CLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVAL 1427
Cdd:cd17670   147 DEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
1190-1423 1.36e-27

catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein phosphatase non-receptor type 7 (PTPN7), also called hematopoietic protein-tyrosine phosphatase (HePTP) or LC-PTP. belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN7/HePTP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. PTPN7/HePTP is found exclusively in the white blood cells in bone marrow, thymus, spleen, lymph nodes and all myeloid and lymphoid cell lines. It negatively regulates T-cell activation and proliferation, and is often dysregulated in the preleukemic disorder myelodysplastic syndrome, as well as in acute myelogenous leukemia.


Pssm-ID: 350460 [Multi-domain]  Cd Length: 247  Bit Score: 113.01  E-value: 1.36e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1190 LPRNRDKNRSMDVLP-PDR--CLPFLISTDgDSNNYINAALTDSYT-RSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVM 1265
Cdd:cd14612    12 IPGHASKDRYKTILPnPQSrvCLRRAGSQE-EEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVM 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1266 LNQLNQSNSAwpCLQYWPEPgRQQYGLMEVEFMSGTADEDLVARVFRVQnisrLQEGHLLVRHFQFLRWSAYRdTPDSKK 1345
Cdd:cd14612    91 ITKLKEKKEK--CVHYWPEK-EGTYGRFEIRVQDMKECDGYTIRDLTIQ----LEEESRSVKHYWFSSWPDHQ-TPESAG 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110735404 1346 AFLHLLAEVDKW-QAESGDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCY 1423
Cdd:cd14612   163 PLLRLVAEVEESrQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLH 241
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
1193-1431 3.10e-27

catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) and type 6 (PTPN6) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 and PTPN6, are also called SH2 domain-containing tyrosine phosphatase 2 (SHP2) and 1 (SHP1), respectively. They contain two tandem SH2 domains: a catalytic PTP domain, and a C-terminal tail with regulatory properties. Although structurally similar, they have different localization and different roles in signal transduction. PTPN11/SHP2 is expressed ubiquitously and plays a positive role in cell signaling, leading to cell activation, while PTPN6/SHP1 expression is restricted mainly to hematopoietic and epithelial cells and functions as a negative regulator of signaling events.


Pssm-ID: 350392 [Multi-domain]  Cd Length: 251  Bit Score: 112.17  E-value: 3.10e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1193 NRDKNRSMDVLPPDRCLpfLISTDGDSN----NYINAaltdSYTRSAA-----------FIVTLHPLQSTTPDFWRLVYD 1257
Cdd:cd14544     1 NKGKNRYKNILPFDHTR--VILKDRDPNvpgsDYINA----NYIRNENegpttdenaktYIATQGCLENTVSDFWSMVWQ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1258 YGCTSIVML-NQLNQSNSAwpCLQYWPEPGRQ-QYGLMEVEFMSGTADEDLVARVFrvqNISRLQEGHLL--VRHFQFLR 1333
Cdd:cd14544    75 ENSRVIVMTtKEVERGKNK--CVRYWPDEGMQkQYGPYRVQNVSEHDTTDYTLREL---QVSKLDQGDPIreIWHYQYLS 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1334 WSAYrDTPDSKKAFLHLLAEVDKWQAESGD-GRTIVHCLNGGGRSGTFCACATVLEMIRCHNL---VDVFFAAKTLRNYK 1409
Cdd:cd14544   150 WPDH-GVPSDPGGVLNFLEDVNQRQESLPHaGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdcdIDIQKTIQMVRSQR 228
                         250       260
                  ....*....|....*....|..
gi 110735404 1410 PNMVETMDQYHFCYDVALEYLE 1431
Cdd:cd14544   229 SGMVQTEAQYKFIYVAVAQYIE 250
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
1191-1428 3.84e-27

catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG has four splicing isoforms: three transmembrane isoforms, PTPRG-A, B, and C, and one secretory isoform, PTPRG-S, which are expressed in many tissues including the brain. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350505 [Multi-domain]  Cd Length: 274  Bit Score: 112.44  E-value: 3.84e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1191 PRNRDKNRSMDVLPPDRC---LPFLISTDGDSNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLN 1267
Cdd:cd17667    25 PDNKHKNRYINILAYDHSrvkLRPLPGKDSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMIT 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1268 QLNQSNSAwPCLQYWPEPGRQQYGLMEVEFMSGTADEDLVARVFRVQN--ISRLQEGHLLVRH-------FQFLRWsayr 1338
Cdd:cd17667   105 NLVEKGRR-KCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNtkVKKGQKGNPKGRQnertviqYHYTQW---- 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1339 dtPDS--KKAFLHLLAEVDKWQAE--SGDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVE 1414
Cdd:cd17667   180 --PDMgvPEYALPVLTFVRRSSAArtPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQ 257
                         250
                  ....*....|....
gi 110735404 1415 TMDQYHFCYDVALE 1428
Cdd:cd17667   258 TEEQYIFIHDALLE 271
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
1197-1423 7.23e-27

catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type tyrosine-protein phosphatase B (PTPRB), also known as receptor-type tyrosine-protein phosphatase beta (R-PTP-beta) or vascular endothelial protein tyrosine phosphatase(VE-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRB/VE-PTP is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed specifically in vascular endothelial cells and it plays an important role in blood vessel remodeling and angiogenesis.


Pssm-ID: 350465 [Multi-domain]  Cd Length: 228  Bit Score: 110.39  E-value: 7.23e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1197 NRSMDVLPPDRCLPFLISTDGDS-NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSA 1275
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDDDPcSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1276 wPCLQYWP-EPGRQQYGLMEVEFMSGTADEDLVARVFRVQNISRLqEGHLLVRHFQFLRWSAYrDTPDSKKAFLHLLAEV 1354
Cdd:cd14617    81 -KCDHYWPaDQDSLYYGDLIVQMLSESVLPEWTIREFKICSEEQL-DAPRLVRHFHYTVWPDH-GVPETTQSLIQFVRTV 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1355 -DKWQAESGDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCY 1423
Cdd:cd14617   158 rDYINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
1193-1428 8.39e-27

catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350481 [Multi-domain]  Cd Length: 273  Bit Score: 111.67  E-value: 8.39e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1193 NRDKNRSMDVLPPDRCLPFLISTDGDSN-NYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQ 1271
Cdd:cd14633    40 NRMKNRYGNIIAYDHSRVRLQPIEGETSsDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVE 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1272 SNSAwPCLQYWPEpGRQQYGLMEVEFMSGTADEDLVARVFRVQN--ISRLQEghllVRHFQFLRWSAYrDTPDSKKAFLH 1349
Cdd:cd14633   120 VGRV-KCCKYWPD-DTEIYKDIKVTLIETELLAEYVIRTFAVEKrgVHEIRE----IRQFHFTGWPDH-GVPYHATGLLG 192
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110735404 1350 LLAEVdKWQAESGDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1428
Cdd:cd14633   193 FVRQV-KSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 270
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
1191-1423 1.01e-26

catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein phosphatase non-receptor type 18 (PTPN18), also called brain-derived phosphatase, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. The N-terminal catalytic PTP domain of PTPN18 blocks lysosomal routing and delays the degradation of HER2 by dephosphorylation, and its C-terminal PEST domain promotes K48-linked HER2 ubiquitination and its destruction via the proteasome pathway.


Pssm-ID: 350451 [Multi-domain]  Cd Length: 266  Bit Score: 111.07  E-value: 1.01e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1191 PRNRDKNRSMDVLPPDR---CLPFLISTDGdsNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLN 1267
Cdd:cd14603    28 KENVKKNRYKDILPYDQtrvILSLLQEEGH--SDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMAC 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1268 QlNQSNSAWPCLQYWP-EPGRQQYGLMEVEFMSGT-ADEDLVARVFRV--QNISRlqeghlLVRHFQFLRWSAyRDTPDS 1343
Cdd:cd14603   106 R-EIEMGKKKCERYWAqEQEPLQTGPFTITLVKEKrLNEEVILRTLKVtfQKESR------SVSHFQYMAWPD-HGIPDS 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1344 KKAFLHLLAEVDKWQAESGDgRTIVHCLNGGGRSGTFCACATV-----LEMIRCHnlVDVFFAAKTLRNYKPNMVETMDQ 1418
Cdd:cd14603   178 PDCMLAMIELARRLQGSGPE-PLCVHCSAGCGRTGVICTVDYVrqlllTQRIPPD--FSIFDVVLEMRKQRPAAVQTEEQ 254

                  ....*
gi 110735404 1419 YHFCY 1423
Cdd:cd14603   255 YEFLY 259
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
1193-1431 1.02e-26

catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11), also called SH2 domain-containing tyrosine phosphatase 2 (SHP-2 or SHP2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 promotes the activation of the RAS/Mitogen-Activated Protein Kinases (MAPK) Extracellular-Regulated Kinases 1/2 (ERK1/2) pathway, a canonical signaling cascade that plays key roles in various cellular processes, including proliferation, survival, differentiation, migration, or metabolism. It also regulates the phosphoinositide 3-kinase (PI3K)/AKT pathway, a fundamental cascade that functions in cell survival, proliferation, migration, morphogenesis, and metabolism. PTPN11 dysregulation is associated with several developmental diseases and malignancies, such as Noonan syndrome and juvenile myelomonocytic leukemia. It contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350453 [Multi-domain]  Cd Length: 253  Bit Score: 110.88  E-value: 1.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1193 NRDKNRSMDVLPPDRCLpfLISTDGDSN----NYINA--ALTDSYTRS------AAFIVTLHPLQSTTPDFWRLVYDYGC 1260
Cdd:cd14605     2 NKNKNRYKNILPFDHTR--VVLHDGDPNepvsDYINAniIMPEFETKCnnskpkKSYIATQGCLQNTVNDFWRMVFQENS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1261 TSIVMLNQLNQSNSAwPCLQYWP-EPGRQQYGLMEVEFMSGTADEDLVARVFRvqnISRLQEGHL--LVRHFQFLRWSAY 1337
Cdd:cd14605    80 RVIVMTTKEVERGKS-KCVKYWPdEYALKEYGVMRVRNVKESAAHDYILRELK---LSKVGQGNTerTVWQYHFRTWPDH 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1338 rDTPDSKKAFLHLLAEVD-KWQAESGDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNL---VDVFFAAKTLRNYKPNMV 1413
Cdd:cd14605   156 -GVPSDPGGVLDFLEEVHhKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMV 234
                         250
                  ....*....|....*...
gi 110735404 1414 ETMDQYHFCYDVALEYLE 1431
Cdd:cd14605   235 QTEAQYRFIYMAVQHYIE 252
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
1197-1430 1.02e-26

catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type tyrosine-protein phosphatase H (PTPRH or R-PTP-H), also known as stomach cancer-associated protein tyrosine phosphatase 1 (SAP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRH is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is localized specifically at microvilli of the brush border in gastrointestinal epithelial cells. It plays a role in intestinal immunity by regulating CEACAM20 through tyrosine dephosphorylation. It is also a negative regulator of integrin-mediated signaling and may contribute to contact inhibition of cell growth and motility.


Pssm-ID: 350467 [Multi-domain]  Cd Length: 233  Bit Score: 109.98  E-value: 1.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1197 NRSMDVLPPD--RCLPFLISTDGDSNnYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQsNS 1274
Cdd:cd14619     1 NRFRNVLPYDwsRVPLKPIHEEPGSD-YINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCME-AG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1275 AWPCLQYWP-EPGRQQYGLMEVEFMSGTADEDLVARVFRVQNIsrLQEGHLLVRHFQFLRWSAY--RDTPDSKKAFLHLL 1351
Cdd:cd14619    79 RVKCEHYWPlDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQV--EEQKTLSVRHFHFTAWPDHgvPSSTDTLLAFRRLL 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110735404 1352 AEVDKWQAESGDgrTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEYL 1430
Cdd:cd14619   157 RQWLDQTMSGGP--TVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
933-1132 1.48e-26

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350507 [Multi-domain]  Cd Length: 204  Bit Score: 108.93  E-value: 1.48e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  933 YINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSrYWPEDSDTYG--DIKIMLVKTE 1010
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPNKDEPINceTFKVTLIAEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1011 TLA-----EYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATglLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCY 1085
Cdd:cd17669    80 HKClsneeKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISIIKEEAANRDGPMIVHDEHGGVTAGTF 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 110735404 1086 IVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAIL 1132
Cdd:cd17669   158 CALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
933-1132 1.49e-26

PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350508 [Multi-domain]  Cd Length: 205  Bit Score: 108.61  E-value: 1.49e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  933 YINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITK---LVEVGRVkcsrYWP--EDSDTYGDIKIMLV 1007
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDnqgLAEDEFV----YWPsrEESMNCEAFTVTLI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1008 KTETLA-----EYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATglLAFIRRVKASTPPDAGPIVIHCSAGTGRT 1082
Cdd:cd17670    77 SKDRLClsneeQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST--FELINVIKEEALTRDGPTIVHDEFGAVSA 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 110735404 1083 GCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAIL 1132
Cdd:cd17670   155 GTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
1196-1423 1.52e-26

catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type tyrosine-protein phosphatase-like R (PTPRR or R-PTP-R), also called protein-tyrosine phosphatase PCPTP1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRR is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. The human and mouse PTPRR gene produces multiple neuronal protein isoforms of varying sizes (in human, PTPPBS-alpha, beta, gamma and delta). All isoforms contain the KIM motif and the catalytic PTP domain. PTPRR-deficient mice show significant defects in fine motor coordination and balance skills that are reminiscent of a mild ataxia.


Pssm-ID: 350459 [Multi-domain]  Cd Length: 226  Bit Score: 109.24  E-value: 1.52e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1196 KNRSMDVLPPDR---CLPFLISTDGDSNnYINAALTDSYT-RSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQ 1271
Cdd:cd14611     2 KNRYKTILPNPHsrvCLKPKNSNDSLST-YINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1272 SNSAwpCLQYWPEPgRQQYGLMEVEFMSGTADEDLVARVFRVQNISRLQEghllVRHFQFLRWSAYRdTPDSKKAFLHLL 1351
Cdd:cd14611    81 KNEK--CVLYWPEK-RGIYGKVEVLVNSVKECDNYTIRNLTLKQGSQSRS----VKHYWYTSWPDHK-TPDSAQPLLQLM 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110735404 1352 AEVDKWQAES-GDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCY 1423
Cdd:cd14611   153 LDVEEDRLASpGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
1222-1421 4.50e-26

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3) and type 4 (PTPN4) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 and PTPN4 are large modular proteins containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses.


Pssm-ID: 350389 [Multi-domain]  Cd Length: 212  Bit Score: 107.42  E-value: 4.50e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1222 YINAALTDSYTRSAA----FIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPG-RQQYGLMEVE 1296
Cdd:cd14541     2 YINANYVNMEIPGSGivnrYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRV-KCHQYWPDLGeTMQFGNLQIT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1297 FMSGTADEDLVARVFRVQNISRLQEGHllVRHFQFLRWSAYrDTPDSKKAFLHLLAEVDKWQAESGDgRTIVHCLNGGGR 1376
Cdd:cd14541    81 CVSEEVTPSFAFREFILTNTNTGEERH--ITQMQYLAWPDH-GVPDDSSDFLDFVKRVRQNRVGMVE-PTVVHCSAGIGR 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 110735404 1377 SGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHF 1421
Cdd:cd14541   157 TGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRF 201
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
1216-1428 6.64e-26

catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350479 [Multi-domain]  Cd Length: 218  Bit Score: 107.41  E-value: 6.64e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1216 DGDSNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGrQQYGLMEV 1295
Cdd:cd14631     9 DDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRV-KCYKYWPDDT-EVYGDFKV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1296 EFMSGTADEDLVARVFRVQ--NISRLQEghllVRHFQFLRWSAYrDTPDSKKAFLHLLAEVdKWQAESGDGRTIVHCLNG 1373
Cdd:cd14631    87 TCVEMEPLAEYVVRTFTLErrGYNEIRE----VKQFHFTGWPDH-GVPYHATGLLSFIRRV-KLSNPPSAGPIVVHCSAG 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 110735404 1374 GGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1428
Cdd:cd14631   161 AGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
1222-1430 1.50e-25

catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) and type 13 (PTPN13, also known as PTPL1) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization. Human PTPN13 is an important regulator of tumor aggressiveness.


Pssm-ID: 350386 [Multi-domain]  Cd Length: 207  Bit Score: 105.92  E-value: 1.50e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1222 YINAaltdSYTR------SAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQlNQSNSAWPCLQYWPEPGRQQ---YGL 1292
Cdd:cd14538     1 YINA----SHIRipvggdTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQ-DVEGGKVKCHRYWPDSLNKPlicGGR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1293 MEVEFMSGTADEDLVARVFRVQNISRLQEGHllVRHFQFLRWSAYrDTPDSKKAFLHLLAEVDKWQAesgDGRTIVHCLN 1372
Cdd:cd14538    76 LEVSLEKYQSLQDFVIRRISLRDKETGEVHH--ITHLNFTTWPDH-GTPQSADPLLRFIRYMRRIHN---SGPIVVHCSA 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 110735404 1373 GGGRSGTFCACATVLEMIRcHNL-VDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEYL 1430
Cdd:cd14538   150 GIGRTGVLITIDVALGLIE-RDLpFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
1222-1424 2.52e-25

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350506 [Multi-domain]  Cd Length: 209  Bit Score: 105.45  E-value: 2.52e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1222 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGRQQYGLMEVEFMSGT 1301
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRR-KCDQYWPADGSEEYGNFLVTQKSVQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1302 ADEDLVARVFRVQNiSRLQEG-------HLLVRHFQFLRWsayrdtPDS--KKAFLHLLAEVDKWQA--ESGDGRTIVHC 1370
Cdd:cd17668    80 VLAYYTVRNFTLRN-TKIKKGsqkgrpsGRVVTQYHYTQW------PDMgvPEYTLPVLTFVRKASYakRHAVGPVVVHC 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 110735404 1371 LNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCYD 1424
Cdd:cd17668   153 SAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHD 206
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
1220-1421 1.85e-24

catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type tyrosine-protein phosphatase Q (PTPRQ or R-PTP-Q), also called phosphatidylinositol phosphatase PTPRQ, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRQ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (18 in PTPRQ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It displays low tyrosine-protein phosphatase activity; rather, it functions as a phosphatidylinositol phosphatase required for auditory processes. It regulates the levels of phosphatidylinositol 4,5-bisphosphate (PIP2) in the basal region of hair bundles. It can dephosphorylate a broad range of phosphatidylinositol phosphates, including phosphatidylinositol 3,4,5-trisphosphate and most phosphatidylinositol monophosphates and diphosphates.


Pssm-ID: 350464 [Multi-domain]  Cd Length: 224  Bit Score: 103.45  E-value: 1.85e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1220 NNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGR--QQYGLMEVEF 1297
Cdd:cd14616    25 SDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI-RCHQYWPEDNKpvTVFGDIVITK 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1298 MSGTADEDLVARVFRVQnisrlQEGH-LLVRHFQFLRWSAYrDTPDSKKAFLHLLAEVDKWQAESgDGRTIVHCLNGGGR 1376
Cdd:cd14616   104 LMEDVQIDWTIRDLKIE-----RHGDyMMVRQCNFTSWPEH-GVPESSAPLIHFVKLVRASRAHD-NTPMIVHCSAGVGR 176
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 110735404 1377 SGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHF 1421
Cdd:cd14616   177 TGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIF 221
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
1193-1430 2.18e-24

catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein phosphatase non-receptor type 13 (PTPN13, also known as PTPL1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN13 is an important regulator of tumor aggressiveness. It regulates breast cancer cell aggressiveness through direct inactivation of Src kinase. In hepatocellular carcinoma, PTPN13 is a tumor suppressor. PTPN13 contains a FERM domain, five PDZ domains, and a C-terminal catalytic PTP domain. With its PDZ domains, PTPN13 has numerous interacting partners that can actively participate in the regulation of its phosphatase activity or can permit direct or indirect recruitment of tyrosine phosphorylated substrates. Its FERM domain is necessary for localization to the membrane.


Pssm-ID: 350445 [Multi-domain]  Cd Length: 234  Bit Score: 103.37  E-value: 2.18e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1193 NRDKNRSMDVLPPDRCLPFListdGDSNNYINAALTDSYTRSAAF--IVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLN 1270
Cdd:cd14597     3 NRKKNRYKNILPYDTTRVPL----GDEGGYINASFIKMPVGDEEFvyIACQGPLPTTVADFWQMVWEQKSTVIAMMTQEV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1271 QSNSAwPCLQYWPEPGRQQYGLMEVEFMSGTADEDLVARVFRVQNISRLQEGHllVRHFQFLRWSAYRD--TPDSKKAFL 1348
Cdd:cd14597    79 EGGKI-KCQRYWPEILGKTTMVDNRLQLTLVRMQQLKNFVIRVLELEDIQTRE--VRHITHLNFTAWPDhdTPSQPEQLL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1349 HLLAEVDKWQAEsgdGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALE 1428
Cdd:cd14597   156 TFISYMRHIHKS---GPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVILY 232

                  ..
gi 110735404 1429 YL 1430
Cdd:cd14597   233 VL 234
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
1154-1421 6.10e-24

catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3), also called protein-tyrosine phosphatase H1 (PTP-H1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN3 and p38gamma cooperate to promote Ras-induced oncogenesis. PTPN3 is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. Its PDZ domain binds with the PDZ-binding motif of p38gamma and enables efficient tyrosine dephosphorylation.


Pssm-ID: 350448 [Multi-domain]  Cd Length: 274  Bit Score: 103.39  E-value: 6.10e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1154 MIRIDPQSNSSQLREEFQTLNSVTPPLDVeecSIALLPRNRDKNRSMDVLPPDRCLPFListDGDsNNYINAALTDSYTR 1233
Cdd:cd14600     4 MAQLKKGLESGTVLIQFEQLYRKKPGLAI---TCAKLPQNMDKNRYKDVLPYDATRVVL---QGN-EDYINASYVNMEIP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1234 SAA----FIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGR-QQYGLMEVEFMSgtadEDL-V 1307
Cdd:cd14600    77 SANivnkYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTERGRT-KCHQYWPDPPDvMEYGGFRVQCHS----EDCtI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1308 ARVFRVQNISRLQEG-HLLVRHFQFLRWSAYrDTPDSKKAFLHLLAEVDKWQAESGDgrTIVHCLNGGGRSGTFCACATV 1386
Cdd:cd14600   152 AYVFREMLLTNTQTGeERTVTHLQYVAWPDH-GVPDDSSDFLEFVNYVRSKRVENEP--VLVHCSAGIGRTGVLVTMETA 228
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 110735404 1387 LEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHF 1421
Cdd:cd14600   229 MCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKF 263
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
1222-1419 9.11e-24

catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 1.


Pssm-ID: 350405 [Multi-domain]  Cd Length: 201  Bit Score: 100.67  E-value: 9.11e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1222 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEP--GRQQYGLMEVEFMS 1299
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRN-KCAQYWPSMeeGSRAFGDVVVKINE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1300 GTADEDLVARVFRVQNiSRLQEGHLLVRHFQFLRWSAYrDTPDSKKAFLHLLAEVDKWQaESGDGRTIVHCLNGGGRSGT 1379
Cdd:cd14557    80 EKICPDYIIRKLNINN-KKEKGSGREVTHIQFTSWPDH-GVPEDPHLLLKLRRRVNAFN-NFFSGPIVVHCSAGVGRTGT 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 110735404 1380 FCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQY 1419
Cdd:cd14557   157 YIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQY 196
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
1222-1431 1.01e-23

catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization.


Pssm-ID: 350444 [Multi-domain]  Cd Length: 207  Bit Score: 100.59  E-value: 1.01e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1222 YINAaltdSYTRSAA------FIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEPGRQQyglMEV 1295
Cdd:cd14596     1 YINA----SYITMPVgeeelfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKV-KCHRYWPETLQEP---MEL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1296 EFMSGTADEDLVARVFRVQNISRLQ----EGHLlVRHFQFLRWSAYrDTPDSKKAFLHLLAEVDKWQAEsgdGRTIVHCL 1371
Cdd:cd14596    73 ENYQLRLENYQALQYFIIRIIKLVEketgENRL-IKHLQFTTWPDH-GTPQSSDQLVKFICYMRKVHNT---GPIVVHCS 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110735404 1372 NGGGRSGTFCACATVLEMIR---CHNLVDVffaAKTLRNYKPNMVETMDQYHFCYDVALEYLE 1431
Cdd:cd14596   148 AGIGRAGVLICVDVLLSLIEkdlSFNIKDI---VREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
1191-1430 2.09e-23

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 102.77  E-value: 2.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1191 PRNRDKNRSMDVLPPDRCLPFLISTDGDSNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLN 1270
Cdd:PHA02747   49 PENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPTK 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1271 QSNSAWPCLQYW--PEPGRQQYGLMEVEFMSGTADEDLVARVFRVQNisRLQEGHLLVRHFQFLRWSAYrDTPDSKKAFL 1348
Cdd:PHA02747  129 GTNGEEKCYQYWclNEDGNIDMEDFRIETLKTSVRAKYILTLIEITD--KILKDSRKISHFQCSEWFED-ETPSDHPDFI 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1349 HLLAEVDKWQAESGDGRT---------IVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQY 1419
Cdd:PHA02747  206 KFIKIIDINRKKSGKLFNpkdallcpiVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDY 285
                         250
                  ....*....|....
gi 110735404 1420 HF---CYDVALEYL 1430
Cdd:PHA02747  286 LFiqpGYEVLHYFL 299
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
1221-1430 2.49e-23

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21) and type 14 (PTPN14) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Both PTPN21 and PTPN14 contain an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350388 [Multi-domain]  Cd Length: 219  Bit Score: 99.84  E-value: 2.49e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1221 NYINAALTDSYTRsaaFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQlNQSNSAWPCLQYWP----EPGRQQYGLMEVE 1296
Cdd:cd14540     5 SHITATVGGKQRF---YIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTA-EEEGGREKCFRYWPtlggEHDALTFGEYKVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1297 FMSGTADEDLVARVFRVQNISRLQegHLLVRHFQFLRWsAYRDTPDSKKAFLHLLAEVDK-----WQAESGDGR---TIV 1368
Cdd:cd14540    81 TKFSVSSGCYTTTGLRVKHTLSGQ--SRTVWHLQYTDW-PDHGCPEDVSGFLDFLEEINSvrrhtNQDVAGHNRnppTLV 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110735404 1369 HCLNGGGRSGTFCACATVLEMIRcHNL-VDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEYL 1430
Cdd:cd14540   158 HCSAGVGRTGVVILADLMLYCLD-HNEeLDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
1222-1423 2.27e-22

catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), type 18 (PTPN18) and type 12 (PTPN12) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. TPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling.


Pssm-ID: 350390 [Multi-domain]  Cd Length: 202  Bit Score: 96.72  E-value: 2.27e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1222 YINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQlNQSNSAWPCLQYWPEPGRQ--QYGLMEVEFMS 1299
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACR-EFEMGKKKCERYWPEEGEEqlQFGPFKISLEK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1300 GTA-DEDLVARVFRVQnisRLQEGHlLVRHFQFLRWSAyRDTPDSKKAFLHLLAEVDKWQaESGDGRTIVHCLNGGGRSG 1378
Cdd:cd14542    80 EKRvGPDFLIRTLKVT---FQKESR-TVYQFHYTAWPD-HGVPSSVDPILDLVRLVRDYQ-GSEDVPICVHCSAGCGRTG 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 110735404 1379 TFCACATVLEMIRCHNLVD---VFFAAKTLRNYKPNMVETMDQYHFCY 1423
Cdd:cd14542   154 TICAIDYVWNLLKTGKIPEefsLFDLVREMRKQRPAMVQTKEQYELVY 201
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1326-1428 2.94e-22

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 92.81  E-value: 2.94e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404   1326 VRHFQFLRWSAyRDTPDSKKAFLHLLAEVDKWQ-AESGDGRTIVHCLNGGGRSGTFCACATVLEMIR-CHNLVDVFFAAK 1403
Cdd:smart00404    2 VKHYHYTGWPD-HGVPESPDSILELLRAVKKNLnQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEaEAGEVDIFDTVK 80
                            90       100
                    ....*....|....*....|....*
gi 110735404   1404 TLRNYKPNMVETMDQYHFCYDVALE 1428
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
1326-1428 2.94e-22

Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine phosphatases. Homologues detected by this profile and not by those of "PTPc" or "DSPc" are predicted to be protein phosphatases with a similar fold to DSPs and PTPs, yet with unpredicted specificities.


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 92.81  E-value: 2.94e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404   1326 VRHFQFLRWSAyRDTPDSKKAFLHLLAEVDKWQ-AESGDGRTIVHCLNGGGRSGTFCACATVLEMIR-CHNLVDVFFAAK 1403
Cdd:smart00012    2 VKHYHYTGWPD-HGVPESPDSILELLRAVKKNLnQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEaEAGEVDIFDTVK 80
                            90       100
                    ....*....|....*....|....*
gi 110735404   1404 TLRNYKPNMVETMDQYHFCYDVALE 1428
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
1196-1428 3.14e-22

catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), also called lymphoid phosphatase (LyP), PEST-domain phosphatase (PEP), or hematopoietic cell protein-tyrosine phosphatase 70Z-PEP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. Mutations in the PTPN22 gene are associated with multiple connective tissue and autoimmune diseases including type 1 diabetes mellitus, rheumatoid arthritis, and systemic lupus erythematosus. PTPN22 contains an N-terminal catalytic PTP domain and four proline-rich regions at the C-terminus.


Pssm-ID: 350450 [Multi-domain]  Cd Length: 234  Bit Score: 97.22  E-value: 3.14e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1196 KNRSMDVLPPDRCLP--FLISTDGDSNnYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSN 1273
Cdd:cd14602     1 KNRYKDILPYDHSRVelSLITSDEDSD-YINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1274 SAwPCLQYWPEPGRQ--QYGLMEVEFMSGTADEDLVARVFRVQnisrLQEGHLLVRHFQFLRWSAYrDTPDSKKAFLHLL 1351
Cdd:cd14602    80 KK-KCERYWAEPGEMqlEFGPFSVTCEAEKRKSDYIIRTLKVK----FNSETRTIYQFHYKNWPDH-DVPSSIDPILELI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1352 AEVDKWQAEsgDGRTI-VHCLNGGGRSGTFCACATVLEMIRcHNLVDVFFAAKTL----RNYKPNMVETMDQYHFCYDVA 1426
Cdd:cd14602   154 WDVRCYQED--DSVPIcIHCSAGCGRTGVICAIDYTWMLLK-DGIIPENFSVFSLiqemRTQRPSLVQTKEQYELVYNAV 230

                  ..
gi 110735404 1427 LE 1428
Cdd:cd14602   231 IE 232
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
1191-1431 1.12e-21

catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein phosphatase non-receptor type 6 (PTPN6), also called SH2 domain-containing protein-tyrosine phosphatase 1 (SHP1 or SHP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN6 expression is restricted mainly to hematopoietic and epithelial cells. It is an important regulator of hematopoietic cells, downregulating pathways that promote cell growth, survival, adhesion, and activation. It regulates glucose homeostasis by modulating insulin signalling in the liver and muscle, and it also negatively regulates bone resorption, affecting both the formation and the function of osteoclasts. PTPN6 contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350454 [Multi-domain]  Cd Length: 266  Bit Score: 96.49  E-value: 1.12e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1191 PRNRDKNRSMDVLPPDRCLpfLISTDGDSN---------NYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCT 1261
Cdd:cd14606    16 PENKSKNRYKNILPFDHSR--VILQGRDSNipgsdyinaNYVKNQLLGPDENAKTYIASQGCLEATVNDFWQMAWQENSR 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1262 SIVMLNQLNQSNSAwPCLQYWPEPGRQ-QYGLMEVEFMSGTADEDLVARVFRVQNISRlQEGHLLVRHFQFLRWSAYrDT 1340
Cdd:cd14606    94 VIVMTTREVEKGRN-KCVPYWPEVGMQrAYGPYSVTNCGEHDTTEYKLRTLQVSPLDN-GELIREIWHYQYLSWPDH-GV 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1341 PDSKKAFLHLLAEVDKWQAE-SGDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNL---VDVFFAAKTLRNYKPNMVETM 1416
Cdd:cd14606   171 PSEPGGVLSFLDQINQRQESlPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRSGMVQTE 250
                         250
                  ....*....|....*
gi 110735404 1417 DQYHFCYDVALEYLE 1431
Cdd:cd14606   251 AQYKFIYVAIAQFIE 265
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
1194-1429 5.66e-21

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 95.87  E-value: 5.66e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1194 RDKNRSMDVLPPDRCLPFLISTDGDSNnYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSN 1273
Cdd:PHA02746   73 HESLKMFDVGDSDGKKIEVTSEDNAEN-YIHANFVDGFKEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTDIDDDD 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1274 SAwpCLQYWPEPgrQQYGLMEVEFMSGTAD--EDLVARVFRVQNISRLQEGHLLVRHFQFLRWSAYrDTPDSKKAFLHLL 1351
Cdd:PHA02746  152 EK--CFELWTKE--EDSELAFGRFVAKILDiiEELSFTKTRLMITDKISDTSREIHHFWFPDWPDN-GIPTGMAEFLELI 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1352 AEVDKWQAE---------SGDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFC 1422
Cdd:PHA02746  227 NKVNEEQAElikqadndpQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFC 306

                  ....*..
gi 110735404 1423 YdVALEY 1429
Cdd:PHA02746  307 Y-KALKY 312
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
1221-1431 1.32e-20

catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein phosphatase non-receptor type 4 (PTPN4), also called protein-tyrosine phosphatase MEG1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses. It specifically inhibits the TRIF-dependent TLR4 pathway by suppressing tyrosine phosphorylation of TRAM. It is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain; the PDZ domain regulates the catalytic activity of PTPN4.


Pssm-ID: 350449 [Multi-domain]  Cd Length: 212  Bit Score: 91.93  E-value: 1.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1221 NYINAALTDSyTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAwPCLQYWPEP-GRQQYGLMEVEFMS 1299
Cdd:cd14601     6 NYINMEIPSS-SIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRV-KCHQYWPEPsGSSSYGGFQVTCHS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1300 GTADEDLVARVFRVQNISRLQEGHLLvrHFQFLRWSAYrDTPDSKKAFLHLLAEVDKWQAeSGDGRTIVHCLNGGGRSGT 1379
Cdd:cd14601    84 EEGNPAYVFREMTLTNLEKNESRPLT--QIQYIAWPDH-GVPDDSSDFLDFVCLVRNKRA-GKDEPVVVHCSAGIGRTGV 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 110735404 1380 FCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEYLE 1431
Cdd:cd14601   160 LITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVYE 211
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
1186-1431 1.81e-20

catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein phosphatase non-receptor type 14 (PTPN14), also called protein-tyrosine phosphatase pez, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN14 is a potential tumor suppressor and plays a regulatory role in the Hippo and Wnt/beta-catenin signaling pathways. It contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350447 [Multi-domain]  Cd Length: 287  Bit Score: 93.52  E-value: 1.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1186 SIALLPRNRDKNRSMDVLPPDRCLPFLISTDGDSNNYINAALTDSYTRSAA--FIVTLHPLQSTTPDFWRLVYDYGCTSI 1263
Cdd:cd14599    31 TTATLPENAERNRIREVVPYEENRVELVPTKENNTGYINASHIKVTVGGEEwhYIATQGPLPHTCHDFWQMVWEQGVNVI 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1264 VMLNQLNQSNSAwPCLQYWPEPGRQQyglmevefMSGTADEDLVARVFRVQN----ISRLQEGHLL------VRHFQFLR 1333
Cdd:cd14599   111 AMVTAEEEGGRS-KSHRYWPKLGSKH--------SSATYGKFKVTTKFRTDSgcyaTTGLKVKHLLsgqertVWHLQYTD 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1334 WSAYrDTPDSKKAFLHLLAEVDKWQ---------AESGDGRTIVHCLNGGGRSGTFCACATvleMIRC--HN-LVDVFFA 1401
Cdd:cd14599   182 WPDH-GCPEEVQGFLSYLEEIQSVRrhtnsmldsTKNCNPPIVVHCSAGVGRTGVVILTEL---MIGCleHNeKVEVPVM 257
                         250       260       270
                  ....*....|....*....|....*....|
gi 110735404 1402 AKTLRNYKPNMVETMDQYHFCYDVALEYLE 1431
Cdd:cd14599   258 LRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
PHA02738 PHA02738
hypothetical protein; Provisional
1192-1431 3.57e-19

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 90.37  E-value: 3.57e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1192 RNRDKNRSMDVLPPDRCLPFLiSTDGDSNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQlNQ 1271
Cdd:PHA02738   48 KNRKLNRYLDAVCFDHSRVIL-PAERNRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCK-KK 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1272 SNSAWPCLQYWP--EPGRQQYGLMEVEFMSGTADEDLVARVFRVQN-ISRLQEghllVRHFQFLRWSAYrDTPDSKKAFL 1348
Cdd:PHA02738  126 ENGREKCFPYWSdvEQGSIRFGKFKITTTQVETHPHYVKSTLLLTDgTSATQT----VTHFNFTAWPDH-DVPKNTSEFL 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1349 HLLAEVDKWQAE-------SGDGRT-----IVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETM 1416
Cdd:PHA02738  201 NFVLEVRQCQKElaqeslqIGHNRLqpppiVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIP 280
                         250
                  ....*....|....*
gi 110735404 1417 DQYHFCYDVALEYLE 1431
Cdd:PHA02738  281 FQYFFCYRAVKRYVN 295
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
1185-1429 1.27e-18

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 88.52  E-value: 1.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1185 CSIALLPRNRDKNRSMDVLPPDRCLPFLISTDGDSNnYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIV 1264
Cdd:PHA02742   44 CNESLELKNMKKCRYPDAPCFDRNRVILKIEDGGDD-FINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIV 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1265 MLNQLNQSNSAwPCLQYW--PEPGRQQYGLMEVefmsgtadEDLVARVFRVQNISRLQ-----EGHLL-VRHFQFLRWSa 1336
Cdd:PHA02742  123 MITKIMEDGKE-ACYPYWmpHERGKATHGEFKI--------KTKKIKSFRNYAVTNLCltdtnTGASLdIKHFAYEDWP- 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1337 YRDTPDSKKAFLHLLAEVDKWQAE-----SGDGRT-----IVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLR 1406
Cdd:PHA02742  193 HGGLPRDPNKFLDFVLAVREADLKadvdiKGENIVkeppiLVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLR 272
                         250       260
                  ....*....|....*....|...
gi 110735404 1407 NYKPNMVETMDQYHFCYDVALEY 1429
Cdd:PHA02742  273 KQRHNCLSLPQQYIFCYFIVLIF 295
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
1193-1419 1.91e-17

catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein phosphatase non-receptor type 12 (PTPN12), also called PTP-PEST or protein-tyrosine phosphatase G1 (PTPG1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling. It regulates various physiological processes, including cell migration, immune response, and neuronal activity, by dephosphorylating multiple substrates including HER2, FAK, PYK2, PSTPIP, WASP, p130Cas, paxillin, Shc, catenin, c-Abl, ArgBP2, p190RhoGAP, RhoGDI, cell adhesion kinase beta, and Rho GTPase.


Pssm-ID: 350452 [Multi-domain]  Cd Length: 297  Bit Score: 84.60  E-value: 1.91e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1193 NRDKNRSMDVLPPDRC-LPFLISTDGDSNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQ 1271
Cdd:cd14604    57 NVKKNRYKDILPFDHSrVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFE 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1272 SNSAwPCLQYWPEPGRQ--QYGLMEVEFMSGTADEDLVARVFRV--QNISRlqeghlLVRHFQFLRWSAYrDTPDSKKAF 1347
Cdd:cd14604   137 MGRK-KCERYWPLYGEEpmTFGPFRISCEAEQARTDYFIRTLLLefQNETR------RLYQFHYVNWPDH-DVPSSFDSI 208
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110735404 1348 LHLLAEVDKWQaESGDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNL---VDVFFAAKTLRNYKPNMVETMDQY 1419
Cdd:cd14604   209 LDMISLMRKYQ-EHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQY 282
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
1222-1431 1.90e-16

catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21), also called protein-tyrosine phosphatase D1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN21 is a component of a multivalent scaffold complex nucleated by focal adhesion kinase (FAK) at specific intracellular sites. It promotes cytoskeleton events that induce cell adhesion and migration by modulating Src-FAK signaling. It can also selectively associate with and stimulate Tec family kinases and modulate Stat3 activation. Human PTPN21 may also play a pathologic role in gastrointestinal tract tumorigenesis. PTPN21 contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350446 [Multi-domain]  Cd Length: 220  Bit Score: 80.02  E-value: 1.90e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1222 YINAALTDSYTRSAA--FIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNqLNQSNSAWPCLQYWPEPGRQQ----YGLMEV 1295
Cdd:cd14598     1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVT-AEEEGGREKSFRYWPRLGSRHntvtYGRFKI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1296 EFMSGTADEDLVARVFRVQNISRLQEghLLVRHFQFLRWSAYrDTPDSKKAFLHLLAEVDKWQ--------AESGDGRTI 1367
Cdd:cd14598    80 TTRFRTDSGCYATTGLKIKHLLTGQE--RTVWHLQYTDWPEH-GCPEDLKGFLSYLEEIQSVRrhtnstidPKSPNPPVL 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110735404 1368 VHCLNGGGRSGTFCACATvleMIRC--HN-LVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEYLE 1431
Cdd:cd14598   157 VHCSAGVGRTGVVILSEI---MIACleHNeMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
934-1124 2.01e-14

YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. YopH is an essential virulence determinant of the pathogenic bacterium by dephosphorylating several focal adhesion proteins including p130Cas in human epithelial cells, resulting in the disruption of focal adhesions and cell detachment from the extracellular matrix. It contains an N-terminal domain that contains signals required for TTSS-mediated delivery of YopH into host cells and a C-terminal catalytic PTP domain.


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 74.36  E-value: 2.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  934 INANY--IDGYHRsnhFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPEDSdTYGDIKImlVKTET 1011
Cdd:cd14559    18 LNANRvqIGNKNV---AIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYFRQSG-TYGSVTV--KSKKT 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1012 LAEYVVRTFA-----LERRGYSARHEVRQFHFTAWPEHG-VPYHATGLLAfiRRVKAST----------------PPDAG 1069
Cdd:cd14559    92 GKDELVDGLKadmynLKITDGNKTITIPVVHVTNWPDHTaISSEGLKELA--DLVNKSAeekrnfykskgssainDKNKL 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 110735404 1070 PIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTlcSRRVNMIQTEEQY 1124
Cdd:cd14559   170 LPVIHCRAGVGRTGQLAAAMELNKSPNNLSVEDIVSDMRT--SRNGKMVQKDEQL 222
fn3 pfam00041
Fibronectin type III domain;
494-577 3.85e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 68.98  E-value: 3.85e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404   494 LTFTPL-EDMIFLKWEEPQEPNGLITQYEISYQSIESSDPAVNVPGPRrtisklrNETYHVFSNLHPGTTYLFSVRARTG 572
Cdd:pfam00041    6 LTVTDVtSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPG-------TTTSVTLTGLKPGTEYEVRVQAVNG 78

                   ....*
gi 110735404   573 KGFGQ 577
Cdd:pfam00041   79 GGEGP 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
484-585 1.68e-13

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 67.52  E-value: 1.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  484 DVPSGIAAESLTftplEDMIFLKWEEPQEPNGLITQYEISYQSIESSDPA-VNVPGPrrtisklrNETYHVFSNLHPGTT 562
Cdd:cd00063     2 SPPTNLRVTDVT----STSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKeVEVTPG--------SETSYTLTGLKPGTE 69
                          90       100
                  ....*....|....*....|....
gi 110735404  563 YLFSVRARTGKGFGQAA-LTEITT 585
Cdd:cd00063    70 YEFRVRAVNGGGESPPSeSVTVTT 93
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
911-1131 1.01e-12

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 70.77  E-value: 1.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  911 PMPAYDRHRVKLHPmlgdpNADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEvgrVKC-S 989
Cdd:PHA02740   61 HITRLLHRRIKLFN-----DEKVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHAD---KKCfN 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  990 RYWPEDSD---TYGDIKIMLVKTETLAEYVVRTFALERRGYSARhEVRQFHFTAWPEHGVPYHATGLLAFIRRVKA---- 1062
Cdd:PHA02740  133 QFWSLKEGcviTSDKFQIETLEIIIKPHFNLTLLSLTDKFGQAQ-KISHFQYTAWPADGFSHDPDAFIDFFCNIDDlcad 211
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110735404 1063 ----STPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAI 1131
Cdd:PHA02740  212 lekhKADGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLI 284
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
347-624 1.37e-11

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 69.26  E-value: 1.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  347 LDPDTEYEISVLLTrpGDGGTGRPGPPlISRTKCAEPMRAPKGLAFAEIQARQLTLQWEP------LGYNVTRchtytvs 420
Cdd:COG3401   199 IEPGTTYYYRVAAT--DTGGESAPSNE-VSVTTPTTPPSAPTGLTATADTPGSVTLSWDPvtesdaTGYRVYR------- 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  421 lcyhytlGSSHNQTIREcVKTEQGVSrYTIKNLLPYRNVHVRLVLTNPEGRKEGK--EVTFQTDEDVPSgiAAESLTFTP 498
Cdd:COG3401   269 -------SNSGDGPFTK-VATVTTTS-YTDTGLTNGTTYYYRVTAVDAAGNESAPsnVVSVTTDLTPPA--APSGLTATA 337
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  499 LEDM-IFLKWEEPQEPNglITQYEIsYQSIESSdpavnvpGPRRTISKLRNETYHVFSNLHPGTTYLFSVRARTGKGfgq 577
Cdd:COG3401   338 VGSSsITLSWTASSDAD--VTGYNV-YRSTSGG-------GTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAG--- 404
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 110735404  578 aalteittNISAPSFDYADMPSPLGESENTITVLLRPAQGRGAPISV 624
Cdd:COG3401   405 --------NESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATA 443
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
486-576 1.55e-10

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 58.78  E-value: 1.55e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404    486 PSGIAAESLTftplEDMIFLKWEEPQEPNGL--ITQYEISYQSIESSDPAVNVPGprrtisklrNETYHVFSNLHPGTTY 563
Cdd:smart00060    4 PSNLRVTDVT----STSVTLSWEPPPDDGITgyIVGYRVEYREEGSEWKEVNVTP---------SSTSYTLTGLKPGTEY 70
                            90
                    ....*....|...
gi 110735404    564 LFSVRARTGKGFG 576
Cdd:smart00060   71 EFRVRAVNGAGEG 83
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
1223-1431 1.52e-07

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 54.97  E-value: 1.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1223 INAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAWpclQYWpepgrqqyglmevefmSGTA 1302
Cdd:PHA02740   79 LDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHADKKCFN---QFW----------------SLKE 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1303 DEDLVARVFRVQNISRLQEGH----LLV-----------RHFQFLRWSA--YRDTPDskkAFL-------HLLAEVDKWQ 1358
Cdd:PHA02740  140 GCVITSDKFQIETLEIIIKPHfnltLLSltdkfgqaqkiSHFQYTAWPAdgFSHDPD---AFIdffcnidDLCADLEKHK 216
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110735404 1359 AESGDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEYLE 1431
Cdd:PHA02740  217 ADGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLIAAYLK 289
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
1029-1129 3.06e-07

protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine phosphatase domain-containing protein 1 (PTPDC1) is an uncharacterized non-receptor class protein-tyrosine phosphatase (PTP). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Small interfering RNA (siRNA) knockdown of the ptpdc1 gene is associated with elongated cilia.


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 52.74  E-value: 3.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1029 ARHEVRQFHFtAWPEHGVPyhATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTG----CYIVLdvMLDMAECEgvvdiy 1104
Cdd:cd14506    73 MRAGIYFYNF-GWKDYGVP--SLTTILDIVKVMAFALQEGGKVAVHCHAGLGRTGvliaCYLVY--ALRMSADQ------ 141
                          90       100
                  ....*....|....*....|....*
gi 110735404 1105 nCVKTLCSRRVNMIQTEEQYIFIHD 1129
Cdd:cd14506   142 -AIRLVRSKRPNSIQTRGQVLCVRE 165
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
386-481 4.77e-07

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 49.03  E-value: 4.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404  386 APKGLAFAEIQARQLTLQWEPLGYNVTRCHTYTVSLCyhytlgSSHNQTIRECVKTEQGVSRYTIKNLLPYRNVHVRLVL 465
Cdd:cd00063     3 PPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYR------EKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRA 76
                          90
                  ....*....|....*..
gi 110735404  466 TNPEGR-KEGKEVTFQT 481
Cdd:cd00063    77 VNGGGEsPPSESVTVTT 93
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
1328-1424 1.92e-06

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This superfamily is composed of cys-based phosphatases, which includes classical protein tyrosine phosphatases (PTPs) as well as dual-specificity phosphatases (DUSPs or DSPs). They are characterized by a CxxxxxR conserved catalytic loop (where C is the catalytic cysteine, x is any amino acid, and R is an arginine). PTPs are part of the tyrosine phosphorylation/dephosphorylation regulatory mechanism, and are important in the response of the cells to physiologic and pathologic changes in their environment. DUSPs show more substrate diversity (including RNA and lipids) and include pTyr, pSer, and pThr phosphatases.


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 48.11  E-value: 1.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1328 HFQFLRWSAYRDTPDSKKAFLHLLAEVDKwQAESGDGRTIVHCLNGGGRSGTFCACATVlemirCHNLVDVFFAAKTLR- 1406
Cdd:cd14494    22 DSRFLKQLGVTTIVDLTLAMVDRFLEVLD-QAEKPGEPVLVHCKAGVGRTGTLVACYLV-----LLGGMSAEEAVRIVRl 95
                          90
                  ....*....|....*...
gi 110735404 1407 NYKPNMVETMDQYHFCYD 1424
Cdd:cd14494    96 IRPGGIPQTIEQLDFLIK 113
fn3 pfam00041
Fibronectin type III domain;
291-365 2.92e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 46.64  E-value: 2.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404   291 PPQLLRA---GPTYLIIQLNTNSIiGDGPIVRKEIEYRMARGPWAEVHAV---SLQTYKLWHLDPDTEYEISVlLTRPGD 364
Cdd:pfam00041    2 APSNLTVtdvTSTSLTVSWTPPPD-GNGPITGYEVEYRPKNSGEPWNEITvpgTTTSVTLTGLKPGTEYEVRV-QAVNGG 79

                   .
gi 110735404   365 G 365
Cdd:pfam00041   80 G 80
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
1332-1424 7.78e-05

cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of eukaryotic cyclin-dependent kinase inhibitor 3 (CDKN3) and related archaeal and bacterial proteins. CDKN3 is also known as kinase-associated phosphatase (KAP), CDK2-associated dual-specificity phosphatase, cyclin-dependent kinase interactor 1 (CDI1), or cyclin-dependent kinase-interacting protein 2 (CIP2). It has been characterized as dual-specificity phosphatase, which function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and protein-tyrosine-phosphatase (EC 3.1.3.48). It dephosphorylates CDK2 at a threonine residue in a cyclin-dependent manner, resulting in the inhibition of G1/S cell cycle progression. It also interacts with CDK1 and controls progression through mitosis by dephosphorylating CDC2. CDKN3 may also function as a tumor suppressor; its loss of function was found in a variety of cancers including glioblastoma and hepatocellular carcinoma. However, it has also been found over-expressed in many cancers such as breast, cervical, lung and prostate cancers, and may also have an oncogenic function.


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 44.56  E-value: 7.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1332 LRWSAY--RD--TPDSKKAFLHLLAEVDkwQAESGDGRTIVHCLNGGGRSGTFCACAtvleMIRCHNLVDVFFAAKTLRN 1407
Cdd:cd14505    73 ITWHHLpiPDggVPSDIAQWQELLEELL--SALENGKKVLIHCKGGLGRTGLIAACL----LLELGDTLDPEQAIAAVRA 146
                          90
                  ....*....|....*..
gi 110735404 1408 YKPNMVETMDQYHFCYD 1424
Cdd:cd14505   147 LRPGAIQTPKQENFLHQ 163
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
386-471 1.25e-04

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 42.22  E-value: 1.25e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404    386 APKGLAFAEIQARQLTLQWEPLGYNVTRChtYTVslcyHYTLGSSHNQTIRECVKTEQGVSRYTIKNLLPYRNVHVRLVL 465
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDGITG--YIV----GYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRA 76

                    ....*.
gi 110735404    466 TNPEGR 471
Cdd:smart00060   77 VNGAGE 82
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
286-357 1.58e-04

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 41.83  E-value: 1.58e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110735404    286 PTPIAPPQLLRAGPTYLIIQ-LNTNSIIGDGPIVRKEIEYRMARGPWAEVHAVSLQT-YKLWHLDPDTEYEISV 357
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSwEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTsYTLTGLKPGTEYEFRV 74
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
1053-1129 3.44e-04

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This superfamily is composed of cys-based phosphatases, which includes classical protein tyrosine phosphatases (PTPs) as well as dual-specificity phosphatases (DUSPs or DSPs). They are characterized by a CxxxxxR conserved catalytic loop (where C is the catalytic cysteine, x is any amino acid, and R is an arginine). PTPs are part of the tyrosine phosphorylation/dephosphorylation regulatory mechanism, and are important in the response of the cells to physiologic and pathologic changes in their environment. DUSPs show more substrate diversity (including RNA and lipids) and include pTyr, pSer, and pThr phosphatases.


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 41.57  E-value: 3.44e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110735404 1053 LLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAEC-EGVVDIYNcvktlCSRRVNMIQTEEQYIFIHD 1129
Cdd:cd14494    41 MVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLGGMSaEEAVRIVR-----LIRPGGIPQTIEQLDFLIK 113
fn3 pfam00041
Fibronectin type III domain;
386-467 9.30e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 39.71  E-value: 9.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404   386 APKGLAFAEIQARQLTLQWEP--------LGYNVTRCHTYTVSLCYHYTLGSSHNqtirecvkteqgvsRYTIKNLLPYR 457
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPppdgngpiTGYEVEYRPKNSGEPWNEITVPGTTT--------------SVTLTGLKPGT 67
                           90
                   ....*....|
gi 110735404   458 NVHVRLVLTN 467
Cdd:pfam00041   68 EYEVRVQAVN 77
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1029-1129 2.49e-03

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 39.95  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735404 1029 ARHEVRQFHFtAWPEHGVPyHATGLLAFIRRVKASTPPDaGPIVIHCSAGTGRTGCyiVLdVMLDMAECEGVVDIYNCVK 1108
Cdd:COG2453    44 EEAGLEYLHL-PIPDFGAP-DDEQLQEAVDFIDEALREG-KKVLVHCRGGIGRTGT--VA-AAYLVLLGLSAEEALARVR 117
                          90       100
                  ....*....|....*....|.
gi 110735404 1109 tlcSRRVNMIQTEEQYIFIHD 1129
Cdd:COG2453   118 ---AARPGAVETPAQRAFLER 135
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
1348-1383 6.05e-03

protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar proteins; Phosphatase and tensin homolog (PTEN) is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It dephosphorylates phosphoinositide trisphosphate. In addition to PTEN, this family includes tensins, voltage-sensitive phosphatases (VSPs), and auxilins. They all contain a protein tyrosine phosphatase-like domain although not all are active phosphatases. Tensins are intracellular proteins that act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility, and they may or may not have phosphatase activity. VSPs are phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. Auxilins are J domain-containing proteins that facilitate Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles, and they do not exhibit phosphatase activity.


Pssm-ID: 350347 [Multi-domain]  Cd Length: 160  Bit Score: 39.10  E-value: 6.05e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 110735404 1348 LHLLAEVDKWQAESGDGRTIVHCLNGGGRSGTFCAC 1383
Cdd:cd14497    80 LEIVDDIDSWLSEDPNNVAVVHCKAGKGRTGTVICA 115
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
1071-1129 7.61e-03

cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of eukaryotic cyclin-dependent kinase inhibitor 3 (CDKN3) and related archaeal and bacterial proteins. CDKN3 is also known as kinase-associated phosphatase (KAP), CDK2-associated dual-specificity phosphatase, cyclin-dependent kinase interactor 1 (CDI1), or cyclin-dependent kinase-interacting protein 2 (CIP2). It has been characterized as dual-specificity phosphatase, which function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and protein-tyrosine-phosphatase (EC 3.1.3.48). It dephosphorylates CDK2 at a threonine residue in a cyclin-dependent manner, resulting in the inhibition of G1/S cell cycle progression. It also interacts with CDK1 and controls progression through mitosis by dephosphorylating CDC2. CDKN3 may also function as a tumor suppressor; its loss of function was found in a variety of cancers including glioblastoma and hepatocellular carcinoma. However, it has also been found over-expressed in many cancers such as breast, cervical, lung and prostate cancers, and may also have an oncogenic function.


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 38.78  E-value: 7.61e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110735404 1071 IVIHCSAGTGRTG----CyivldVMLDMAECEGVVDIYNCVKTLcsrRVNMIQTEEQYIFIHD 1129
Cdd:cd14505   109 VLIHCKGGLGRTGliaaC-----LLLELGDTLDPEQAIAAVRAL---RPGAIQTPKQENFLHQ 163
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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