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Conserved domains on  [gi|333108235|ref|NP_001193942|]
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tyrosine-protein phosphatase non-receptor type 2 isoform 4 [Homo sapiens]

Protein Classification

protein-tyrosine phosphatase family protein( domain architecture ID 1000023)

cys-based protein-tyrosine phosphatase (PTP) family protein may be a PTP or a dual-specificity phosphatase (DUSP or DSP), and may catalyze the dephosphorylation of target phosphoproteins at tyrosine or tyrosine and serine/threonine residues, respectively

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 19-295 0e+00

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.


The actual alignment was detected with superfamily member cd14607:

Pssm-ID: 475123 [Multi-domain]  Cd Length: 257  Bit Score: 536.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  19 QPLYLEIRNESHDYPHRVAKFPENRNRNRYRDVSPYDHSRVKLQNAENDYINASLVDIEEAQRSYILTQGPLPNTCCHFW 98
Cdd:cd14607    1 QPLYLEIRNESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  99 LMVWQQKTKAVVMLNRIVEKESVKCAQYWPTDDQEML-FKETGFSVKLLSEDVKSYYTVHLLQLENINyienlwitlylk 177
Cdd:cd14607   81 LMVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVLsFKETGFSVKLLSEDVKSYYTVHLLQLENIN------------ 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 178 llmldvkrslkSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLV 257
Cdd:cd14607  149 -----------SGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLV 217

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 333108235 258 LMEK--GDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAI 295
Cdd:cd14607  218 LMEKkdPDSVDIKQVLLDMRKYRMGLIQTPDQLRFSYMAV 257
 
Name Accession Description Interval E-value
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 19-295 0e+00

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: 536.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  19 QPLYLEIRNESHDYPHRVAKFPENRNRNRYRDVSPYDHSRVKLQNAENDYINASLVDIEEAQRSYILTQGPLPNTCCHFW 98
Cdd:cd14607    1 QPLYLEIRNESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  99 LMVWQQKTKAVVMLNRIVEKESVKCAQYWPTDDQEML-FKETGFSVKLLSEDVKSYYTVHLLQLENINyienlwitlylk 177
Cdd:cd14607   81 LMVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVLsFKETGFSVKLLSEDVKSYYTVHLLQLENIN------------ 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 178 llmldvkrslkSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLV 257
Cdd:cd14607  149 -----------SGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLV 217

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 333108235 258 LMEK--GDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAI 295
Cdd:cd14607  218 LMEKkdPDSVDIKQVLLDMRKYRMGLIQTPDQLRFSYMAV 257
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
42-297 1.43e-106

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 313.79  E-value: 1.43e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235   42 NRNRNRYRDVSPYDHSRVKLQNAE--NDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKE 119
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGDPgpSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  120 SVKCAQYWPTDDQEMLfKETGFSVKLLSE-DVKSYYTVHLLQLENINyienlwitlylkllmldvkrslkSGETRTISHF 198
Cdd:pfam00102  81 REKCAQYWPEEEGESL-EYGDFTVTLKKEkEDEKDYTVRTLEVSNGG-----------------------SEETRTVKHF 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  199 HYTTWPDFGVPESPASFLNFLFKVRESgSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYR 278
Cdd:pfam00102 137 HYTGWPDHGVPESPNSLLDLLRKVRKS-SLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQR 215

                         250
                  ....*....|....*....
gi 333108235  279 MGLIQTPDQLRFSYMAIIE 297
Cdd:pfam00102 216 PGMVQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
5-297 2.37e-104

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 309.20  E-value: 2.37e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235     5 IEREFEELDtqrrwqplyleiRNESHDYPHRVAKFPENRNRNRYRDVSPYDHSRVKLQN---AENDYINASLVDIEEAQR 81
Cdd:smart00194   2 LEEEFEKLD------------RLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPppgEGSDYINASYIDGPNGPK 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235    82 SYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKESVKCAQYWPTD-DQEMLFKetGFSVKLLSEDVKSYYTVHLLQ 160
Cdd:smart00194  70 AYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEeGEPLTYG--DITVTLKSVEKVDDYTIRTLE 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235   161 LENINyienlwitlylkllmldvkrslkSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLNpdHGPAVIHCS 240
Cdd:smart00194 148 VTNTG-----------------------CSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTS--TGPIVVHCS 202

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 333108235   241 AGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIE 297
Cdd:smart00194 203 AGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 41-302 4.19e-45

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 158.24  E-value: 4.19e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  41 ENRNRNRYRDVSPYDHSRV--KLQNAENDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEK 118
Cdd:PHA02742  51 KNMKKCRYPDAPCFDRNRVilKIEDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIMED 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 119 ESVKCAQYWPTDDQEmlfKETGFSVKLLSEDVKS--YYTVHLLQLENINyienlwitlylkllmldvkrslkSGETRTIS 196
Cdd:PHA02742 131 GKEACYPYWMPHERG---KATHGEFKIKTKKIKSfrNYAVTNLCLTDTN-----------------------TGASLDIK 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 197 HFHYTTWPDFGVPESPASFLNFLFKVRE---------SGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINI 267
Cdd:PHA02742 185 HFAYEDWPHGGLPRDPNKFLDFVLAVREadlkadvdiKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPL 264

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 333108235 268 KQVLLNMRKYRMGLIQTPDQLRFSYMAIIEGAKCI 302
Cdd:PHA02742 265 LSIVRDLRKQRHNCLSLPQQYIFCYFIVLIFAKLM 299
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
40-288 2.02e-38

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 139.84  E-value: 2.02e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  40 PENRNRNRYRDVSPYDHSRVklqNAENDYINASLVDIEEAQRsYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVE-- 117
Cdd:COG5599   40 INGSPLNRFRDIQPYKETAL---RANLGYLNANYIQVIGNHR-YIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEis 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 118 KESVKCAQYWPTDDQEMLfketgfsvkllsedvksyYTVHLLQLENINYIENLWITLYLkllmldVKRSLKSGETRTISH 197
Cdd:COG5599  116 KPKVKMPVYFRQDGEYGK------------------YEVSSELTESIQLRDGIEARTYV------LTIKGTGQKKIEIPV 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 198 FHYTTWPDFGVPESPAsFLNFLFKVRES-GSLNPDHGPAVIHCSAGIGRSGTFSLvdtCLVLMEKGD-----DINIKQVL 271
Cdd:COG5599  172 LHVKNWPDHGAISAEA-LKNLADLIDKKeKIKDPDKLLPVVHCRAGVGRTGTLIA---CLALSKSINalvqiTLSVEEIV 247

                        250
                 ....*....|....*...
gi 333108235 272 LNMRKYR-MGLIQTPDQL 288
Cdd:COG5599  248 IDMRTSRnGGMVQTSEQL 265
 
Name Accession Description Interval E-value
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 19-295 0e+00

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: 536.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  19 QPLYLEIRNESHDYPHRVAKFPENRNRNRYRDVSPYDHSRVKLQNAENDYINASLVDIEEAQRSYILTQGPLPNTCCHFW 98
Cdd:cd14607    1 QPLYLEIRNESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  99 LMVWQQKTKAVVMLNRIVEKESVKCAQYWPTDDQEML-FKETGFSVKLLSEDVKSYYTVHLLQLENINyienlwitlylk 177
Cdd:cd14607   81 LMVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVLsFKETGFSVKLLSEDVKSYYTVHLLQLENIN------------ 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 178 llmldvkrslkSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLV 257
Cdd:cd14607  149 -----------SGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLV 217

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 333108235 258 LMEK--GDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAI 295
Cdd:cd14607  218 LMEKkdPDSVDIKQVLLDMRKYRMGLIQTPDQLRFSYMAV 257
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 18-313 5.96e-170

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: 476.44  E-value: 5.96e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  18 WQPLYLEIRNESHDYPHRVAKFPENRNRNRYRDVSPYDHSRVKLQNAENDYINASLVDIEEAQRSYILTQGPLPNTCCHF 97
Cdd:cd14608    1 WAAIYQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  98 WLMVWQQKTKAVVMLNRIVEKESVKCAQYWP-TDDQEMLFKETGFSVKLLSEDVKSYYTVHLLQLENinyienlwitlyl 176
Cdd:cd14608   81 WEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPqKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELEN------------- 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 177 kllmldvkrsLKSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCL 256
Cdd:cd14608  148 ----------LTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCL 217

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 257 VLMEKGDD---INIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIEGAKCIKGDSSIQKRWK 313
Cdd:cd14608  218 LLMDKRKDpssVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEGAKFIMGDSSVQDQWK 277
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 43-293 5.37e-157

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: 441.83  E-value: 5.37e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  43 RNRNRYRDVSPYDHSRVKLQNAENDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKESVK 122
Cdd:cd14545    1 LNRYRDRDPYDHDRSRVKLKQGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 123 CAQYWPT-DDQEMLFKETGFSVKLLSEDVKSYYTVHLLQLENinyienlwitlylkllmldvkrsLKSGETRTISHFHYT 201
Cdd:cd14545   81 CAQYWPQgEGNAMIFEDTGLKVTLLSEEDKSYYTVRTLELEN-----------------------LKTQETREVLHFHYT 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 202 TWPDFGVPESPASFLNFLFKVRESGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGD--DINIKQVLLNMRKYRM 279
Cdd:cd14545  138 TWPDFGVPESPAAFLNFLQKVRESGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNpsSVDVKKVLLEMRKYRM 217

                        250
                 ....*....|....
gi 333108235 280 GLIQTPDQLRFSYM 293
Cdd:cd14545  218 GLIQTPDQLRFSYL 231
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
42-297 1.43e-106

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 313.79  E-value: 1.43e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235   42 NRNRNRYRDVSPYDHSRVKLQNAE--NDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKE 119
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGDPgpSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  120 SVKCAQYWPTDDQEMLfKETGFSVKLLSE-DVKSYYTVHLLQLENINyienlwitlylkllmldvkrslkSGETRTISHF 198
Cdd:pfam00102  81 REKCAQYWPEEEGESL-EYGDFTVTLKKEkEDEKDYTVRTLEVSNGG-----------------------SEETRTVKHF 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  199 HYTTWPDFGVPESPASFLNFLFKVRESgSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYR 278
Cdd:pfam00102 137 HYTGWPDHGVPESPNSLLDLLRKVRKS-SLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQR 215

                         250
                  ....*....|....*....
gi 333108235  279 MGLIQTPDQLRFSYMAIIE 297
Cdd:pfam00102 216 PGMVQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
5-297 2.37e-104

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 309.20  E-value: 2.37e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235     5 IEREFEELDtqrrwqplyleiRNESHDYPHRVAKFPENRNRNRYRDVSPYDHSRVKLQN---AENDYINASLVDIEEAQR 81
Cdd:smart00194   2 LEEEFEKLD------------RLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPppgEGSDYINASYIDGPNGPK 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235    82 SYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKESVKCAQYWPTD-DQEMLFKetGFSVKLLSEDVKSYYTVHLLQ 160
Cdd:smart00194  70 AYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEeGEPLTYG--DITVTLKSVEKVDDYTIRTLE 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235   161 LENINyienlwitlylkllmldvkrslkSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLNpdHGPAVIHCS 240
Cdd:smart00194 148 VTNTG-----------------------CSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTS--TGPIVVHCS 202

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 333108235   241 AGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIE 297
Cdd:smart00194 203 AGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 68-293 1.34e-81

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: 248.74  E-value: 1.34e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKESVKCAQYWPTD-DQEMLFKEtgFSVKLL 146
Cdd:cd00047    1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEgGKPLEYGD--ITVTLV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 147 SEDVKSYYTVHLLQLENINyienlwitlylkllmldvkrslkSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVREsg 226
Cdd:cd00047   79 SEEELSDYTIRTLELSPKG-----------------------CSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRK-- 133

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 333108235 227 SLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYM 293
Cdd:cd00047  134 EARKPNGPIVVHCSAGVGRTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 22-293 7.31e-79

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: 244.58  E-value: 7.31e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  22 YLEIRNESHDYPHRVAKFPENRNRNRYRDVSPYDHSRVKL----QNAENDYINASLVDIEEAQRSYILTQGPLPNTCCHF 97
Cdd:cd14543    9 YEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLpkrnGDERTDYINANFMDGYKQKNAYIATQGPLPKTYSDF 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  98 WLMVWQQKTKAVVMLNRIVEKESVKCAQYWPtDDQEMLFKETGFSVKLLSEDVKSYYTVHLLQLENInyienlwitlylk 177
Cdd:cd14543   89 WRMVWEQKVLVIVMTTRVVERGRVKCGQYWP-LEEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNT------------- 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 178 llmldvkrslKSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLN-----------PDHGPAVIHCSAGIGRS 246
Cdd:cd14543  155 ----------ETDESRQVTHFQFTSWPDFGVPSSAAALLDFLGEVRQQQALAvkamgdrwkghPPGPPIVVHCSAGIGRT 224

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 333108235 247 GTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYM 293
Cdd:cd14543  225 GTFCTLDICLSQLEDVGTLNVMQTVRRMRTQRAFSIQTPDQYYFCYK 271
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 42-301 6.22e-74

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: 230.75  E-value: 6.22e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  42 NRNRNRYRDVSPYDHSRVKLQNAE----NDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVE 117
Cdd:cd14553    3 NKPKNRYANVIAYDHSRVILQPIEgvpgSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 118 KESVKCAQYWPTDDQEmlfKETGFSVKLLSEDVKSYYTVHLLQLENinyienlwitlylkllmldvkrsLKSGETRTISH 197
Cdd:cd14553   83 RSRVKCDQYWPTRGTE---TYGLIQVTLLDTVELATYTVRTFALHK-----------------------NGSSEKREVRQ 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 198 FHYTTWPDFGVPESPASFLNFLFKVRESGslNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKY 277
Cdd:cd14553  137 FQFTAWPDHGVPEHPTPFLAFLRRVKACN--PPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQ 214

                        250       260
                 ....*....|....*....|....
gi 333108235 278 RMGLIQTPDQLRFSYMAIIEGAKC 301
Cdd:cd14553  215 RNYMVQTEDQYIFIHDALLEAVTC 238
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 47-290 4.03e-69

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: 217.61  E-value: 4.03e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  47 RYRDVSPYDHSRVKL--QNAE--NDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKESVK 122
Cdd:cd14548    1 RYTNILPYDHSRVKLipINEEegSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 123 CAQYWPTDDQEMLFKEtgFSVKLLSEDVKSYYTVHLLQLENInyienlwitlylkllmldvkrslksGETRTISHFHYTT 202
Cdd:cd14548   81 CDHYWPFDQDPVYYGD--ITVTMLSESVLPDWTIREFKLERG-------------------------DEVRSVRQFHFTA 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 203 WPDFGVPESPASFLNFLFKVREsgSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLI 282
Cdd:cd14548  134 WPDHGVPEAPDSLLRFVRLVRD--YIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMV 211


                 ....*...
gi 333108235 283 QTPDQLRF 290
Cdd:cd14548  212 QTEAQYIF 219
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 68-290 6.58e-66

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: 208.74  E-value: 6.58e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKESVKCAQYWPTDDQEmlfkETG-FSVKLL 146
Cdd:cd14549    1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTE----TYGnIQVTLL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 147 SEDVKSYYTVHLLQLENINyienlwitlylkllmldVKRSLKSGETRTISHFHYTTWPDFGVPESPASFLNFlfkVRESG 226
Cdd:cd14549   77 STEVLATYTVRTFSLKNLK-----------------LKKVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSF---VRKSS 136

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333108235 227 SLNPDH-GPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRF 290
Cdd:cd14549  137 AANPPGaGPIVVHCSAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIF 201
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 42-295 2.73e-65

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: 208.86  E-value: 2.73e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  42 NRNRNRYRDVSPYDHSRVKLQNAEN-----DYINASLVDIEEAQR-------SYILTQGPLPNTCCHFWLMVWQQKTKAV 109
Cdd:cd14544    1 NKGKNRYKNILPFDHTRVILKDRDPnvpgsDYINANYIRNENEGPttdenakTYIATQGCLENTVSDFWSMVWQENSRVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 110 VMLNRIVEKESVKCAQYWPtdDQEMLFKETGFSVKLLSEDVKSYYTvhllqleninyienlwitlylkLLMLDVKRSLKS 189
Cdd:cd14544   81 VMTTKEVERGKNKCVRYWP--DEGMQKQYGPYRVQNVSEHDTTDYT----------------------LRELQVSKLDQG 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 190 GETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCL-VLMEKGDD--IN 266
Cdd:cd14544  137 DPIREIWHYQYLSWPDHGVPSDPGGVLNFLEDVNQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLdQIKRKGLDcdID 216

                        250       260
                 ....*....|....*....|....*....
gi 333108235 267 IKQVLLNMRKYRMGLIQTPDQLRFSYMAI 295
Cdd:cd14544  217 IQKTIQMVRSQRSGMVQTEAQYKFIYVAV 245
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 37-296 3.10e-64

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: 207.01  E-value: 3.10e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  37 AKFPENRNRNRYRDVSPYDHSRVKLQNAEnDYINASLVDIEEAQRS----YILTQGPLPNTCCHFWLMVWQQKTKAVVML 112
Cdd:cd14600   35 AKLPQNMDKNRYKDVLPYDATRVVLQGNE-DYINASYVNMEIPSANivnkYIATQGPLPHTCAQFWQVVWEQKLSLIVML 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 113 NRIVEKESVKCAQYWPtDDQEMLfKETGFSVKLLSEDVKSYYTVHLLQLENInyienlwitlylkllmldvkrslKSGET 192
Cdd:cd14600  114 TTLTERGRTKCHQYWP-DPPDVM-EYGGFRVQCHSEDCTIAYVFREMLLTNT-----------------------QTGEE 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 193 RTISHFHYTTWPDFGVPESPASFLNFLFKVResgSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLL 272
Cdd:cd14600  169 RTVTHLQYVAWPDHGVPDDSSDFLEFVNYVR---SKRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVR 245

                        250       260
                 ....*....|....*....|....
gi 333108235 273 NMRKYRMGLIQTPDQLRFSYMAII 296
Cdd:cd14600  246 KMRDQRAMMVQTSSQYKFVCEAIL 269
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 68-297 1.86e-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: 202.60  E-value: 1.86e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  68 YINASLV--DIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKESVKCAQYWPTDDQEMLFKETGFSVKL 145
Cdd:cd14538    1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKPLICGGRLEVSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 146 LSedvksyytvhllqLENINYIENLWITLylkllmldvkRSLKSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRES 225
Cdd:cd14538   81 EK-------------YQSLQDFVIRRISL----------RDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRI 137

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333108235 226 GslnpDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIE 297
Cdd:cd14538  138 H----NSGPIVVHCSAGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLE 205
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 46-290 1.91e-61

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: 198.12  E-value: 1.91e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  46 NRYRDVSPYDHSRVKLQN---AENDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKESVK 122
Cdd:cd14615    1 NRYNNVLPYDISRVKLSVqshSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRTK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 123 CAQYWPTDdQEMLFkeTGFSVKLLSEDVKSYYTVHLLQLENInyienlwitlylkllmldvkrslKSGETRTISHFHYTT 202
Cdd:cd14615   81 CEEYWPSK-QKKDY--GDITVTMTSEIVLPEWTIRDFTVKNA-----------------------QTNESRTVRHFHFTS 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 203 WPDFGVPESPASFLNFLFKVRESGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLI 282
Cdd:cd14615  135 WPDHGVPETTDLLINFRHLVREYMKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMV 214


                 ....*...
gi 333108235 283 QTPDQLRF 290
Cdd:cd14615  215 QTEDQYVF 222
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 46-293 7.44e-60

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: 193.98  E-value: 7.44e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  46 NRYRDVSPYDHSRVKLQNAEN----DYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKESV 121
Cdd:cd14617    1 NRYNNILPYDSTRVKLSNVDDdpcsDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 122 KCAQYWPTDDQEMLFKEtgFSVKLLSEDVKSYYTVHLLQLENINyienlwitlylkllMLDVKrslksgetRTISHFHYT 201
Cdd:cd14617   81 KCDHYWPADQDSLYYGD--LIVQMLSESVLPEWTIREFKICSEE--------------QLDAP--------RLVRHFHYT 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 202 TWPDFGVPESPASFLNFLFKVRESGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGL 281
Cdd:cd14617  137 VWPDHGVPETTQSLIQFVRTVRDYINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHM 216

                        250
                 ....*....|..
gi 333108235 282 IQTPDQlrFSYM 293
Cdd:cd14617  217 VQTECQ--YVYL 226
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 67-296 2.24e-59

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: 192.16  E-value: 2.24e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  67 DYINASLVDIE----EAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKESVKCAQYWPTDDQEMLFKetGFS 142
Cdd:cd14541    1 DYINANYVNMEipgsGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGETMQFG--NLQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 143 VKLLSEDvksyytvhllqlENINYIenlwitlYLKLLMLDVkrslKSGETRTISHFHYTTWPDFGVPESPASFLNFLFKV 222
Cdd:cd14541   79 ITCVSEE------------VTPSFA-------FREFILTNT----NTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRV 135

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 333108235 223 R--ESGSLNpdhgPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAII 296
Cdd:cd14541  136 RqnRVGMVE----PTVVHCSAGIGRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAIL 207
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 41-295 1.15e-58

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: 191.77  E-value: 1.15e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  41 ENRNRNRYRDVSPYDHSRVKLQNAE-----NDYINASLVDIE--------EAQRSYILTQGPLPNTCCHFWLMVWQQKTK 107
Cdd:cd14605    1 ENKNKNRYKNILPFDHTRVVLHDGDpnepvSDYINANIIMPEfetkcnnsKPKKSYIATQGCLQNTVNDFWRMVFQENSR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 108 AVVMLNRIVEKESVKCAQYWPtddQEMLFKETG-FSVKLLSEDVKSYYTVHLLQLENINyienlwitlylkllmldvkrs 186
Cdd:cd14605   81 VIVMTTKEVERGKSKCVKYWP---DEYALKEYGvMRVRNVKESAAHDYILRELKLSKVG--------------------- 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 187 lkSGET-RTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCL-VLMEKGD- 263
Cdd:cd14605  137 --QGNTeRTVWQYHFRTWPDHGVPSDPGGVLDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIdIIREKGVd 214

                        250       260       270
                 ....*....|....*....|....*....|...
gi 333108235 264 -DINIKQVLLNMRKYRMGLIQTPDQLRFSYMAI 295
Cdd:cd14605  215 cDIDVPKTIQMVRSQRSGMVQTEAQYRFIYMAV 247
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 46-290 1.45e-58

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: 190.69  E-value: 1.45e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  46 NRYRDVSPYDHSRVKLQNAEND----YINASLV---DIEEaqRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEK 118
Cdd:cd14547    1 NRYKTILPNEHSRVCLPSVDDDplssYINANYIrgyDGEE--KAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 119 EsVKCAQYWPTDDQEmlfKETGFSVKLLSEDVKSYYTVHLLQLENinyienlwitlylkllmldvkrslkSGETRTISHF 198
Cdd:cd14547   79 K-EKCAQYWPEEENE---TYGDFEVTVQSVKETDGYTVRKLTLKY-------------------------GGEKRYLKHY 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 199 HYTTWPDFGVPESPASFLNFLFKVRESGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYR 278
Cdd:cd14547  130 WYTSWPDHKTPEAAQPLLSLVQEVEEARQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDR 209

                        250
                 ....*....|..
gi 333108235 279 MGLIQTPDQLRF 290
Cdd:cd14547  210 GGMVQTAEQYEF 221
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 40-297 9.39e-58

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: 190.09  E-value: 9.39e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  40 PENRNRNRYRDVSPYDHSRVKLQNAEN-----DYINAS-----LVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAV 109
Cdd:cd14606   16 PENKSKNRYKNILPFDHSRVILQGRDSnipgsDYINANyvknqLLGPDENAKTYIASQGCLEATVNDFWQMAWQENSRVI 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 110 VMLNRIVEKESVKCAQYWPTDDQEmlfKETG-FSVKLLSEDVKSYYTVHLLQLENINyienlwitlylkllmldvkrslK 188
Cdd:cd14606   96 VMTTREVEKGRNKCVPYWPEVGMQ---RAYGpYSVTNCGEHDTTEYKLRTLQVSPLD----------------------N 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 189 SGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLME-KG--DDI 265
Cdd:cd14606  151 GELIREIWHYQYLSWPDHGVPSEPGGVLSFLDQINQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENIStKGldCDI 230

                        250       260       270
                 ....*....|....*....|....*....|..
gi 333108235 266 NIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIE 297
Cdd:cd14606  231 DIQKTIQMVRAQRSGMVQTEAQYKFIYVAIAQ 262
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 40-297 1.08e-57

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: 190.25  E-value: 1.08e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  40 PENRNRNRYRDVSPYDHSRVKLQ------NAENDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLN 113
Cdd:cd17667   25 PDNKHKNRYINILAYDHSRVKLRplpgkdSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMIT 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 114 RIVEKESVKCAQYWPTDDQEmlfkETG-FSVKLLSEDVKSYYTVHLLQLENINyienlwitlylkllmldVKRSLKSG-- 190
Cdd:cd17667  105 NLVEKGRRKCDQYWPTENSE----EYGnIIVTLKSTKIHACYTVRRFSIRNTK-----------------VKKGQKGNpk 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 191 ---ETRTISHFHYTTWPDFGVPESPASFLNFLfkVRESGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINI 267
Cdd:cd17667  164 grqNERTVIQYHYTQWPDMGVPEYALPVLTFV--RRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNV 241

                        250       260       270
                 ....*....|....*....|....*....|
gi 333108235 268 KQVLLNMRKYRMGLIQTPDQLRFSYMAIIE 297
Cdd:cd17667  242 LGFLKHIRTQRNYLVQTEEQYIFIHDALLE 271
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 41-296 1.58e-57

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: 188.12  E-value: 1.58e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  41 ENRNRNRYRDVSPYDHSRVKLQNaENDYINASLVDIEEAQRS--YILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEK 118
Cdd:cd14597    2 ENRKKNRYKNILPYDTTRVPLGD-EGGYINASFIKMPVGDEEfvYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQEVEG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 119 ESVKCAQYWPtddqEMLFKETgfsvkLLSEDVKsyytvhlLQLENINYIENLWItlylKLLMLDvkrSLKSGETRTISHF 198
Cdd:cd14597   81 GKIKCQRYWP----EILGKTT-----MVDNRLQ-------LTLVRMQQLKNFVI----RVLELE---DIQTREVRHITHL 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 199 HYTTWPDFGVPESPASFLNFLFKVRESGSLnpdhGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYR 278
Cdd:cd14597  138 NFTAWPDHDTPSQPEQLLTFISYMRHIHKS----GPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQR 213

                        250
                 ....*....|....*...
gi 333108235 279 MGLIQTPDQLRFSYMAII 296
Cdd:cd14597  214 HGMVQTEDQYIFCYQVIL 231
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 7-301 7.02e-57

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: 187.94  E-value: 7.02e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235   7 REFEELD--TQRRWQPLYLEIrneshdyphrvakfpeNRNRNRYRDVSPYDHSRVKLQNAE----NDYINASLVDIEEAQ 80
Cdd:cd14626   20 QEYESIDpgQQFTWENSNLEV----------------NKPKNRYANVIAYDHSRVILTSVDgvpgSDYINANYIDGYRKQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  81 RSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKESVKCAQYWPTDDQEMLfkeTGFSVKLLSEDVKSYYTVHLLq 160
Cdd:cd14626   84 NAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTETY---GMIQVTLLDTVELATYSVRTF- 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 161 leninyienlwiTLYLKllmldvkrslKSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSlnPDHGPAVIHCS 240
Cdd:cd14626  160 ------------ALYKN----------GSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNP--PDAGPMVVHCS 215

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 333108235 241 AGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIEGAKC 301
Cdd:cd14626  216 AGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAATC 276
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 40-297 1.42e-56

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: 186.95  E-value: 1.42e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  40 PENRNRNRYRDVSPYDHSRVKL----QNAENDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRI 115
Cdd:cd14603   28 KENVKKNRYKDILPYDQTRVILsllqEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMACRE 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 116 VEKESVKCAQYWPTDDQEMlfkETG-FSVKLLSEDvksyytvhllqleninyienlWITLYLKLLMLDVKRslkSGETRT 194
Cdd:cd14603  108 IEMGKKKCERYWAQEQEPL---QTGpFTITLVKEK---------------------RLNEEVILRTLKVTF---QKESRS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 195 ISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLNPDhgPAVIHCSAGIGRSGTFSLVDTC--LVLMEK-GDDINIKQVL 271
Cdd:cd14603  161 VSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPE--PLCVHCSAGCGRTGVICTVDYVrqLLLTQRiPPDFSIFDVV 238

                        250       260
                 ....*....|....*....|....*.
gi 333108235 272 LNMRKYRMGLIQTPDQLRFSYMAIIE 297
Cdd:cd14603  239 LEMRKQRPAAVQTEEQYEFLYHTVAQ 264
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 31-290 3.84e-55

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: 182.40  E-value: 3.84e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  31 DYPHRVAKFPENRNRNRYRDVSPYDHSRVKLQNAEN----DYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKT 106
Cdd:cd14614    1 DIPHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEeegsDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 107 KAVVMLNRIVEKESVKCAQYWPTDDQEMLFKEtgFSVKLLSEDVKSYYTVHLLqleNINYIEnlwitlylkllmldvkrs 186
Cdd:cd14614   81 QIIVMLTQCNEKRRVKCDHYWPFTEEPVAYGD--ITVEMLSEEEQPDWAIREF---RVSYAD------------------ 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 187 lksgETRTISHFHYTTWPDFGVPESPA--SFLNFLFKVRESGSLNPdhGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDD 264
Cdd:cd14614  138 ----EVQDVMHFNYTAWPDHGVPTANAaeSILQFVQMVRQQAVKSK--GPMIIHCSAGVGRTGTFIALDRLLQHIRDHEF 211

                        250       260
                 ....*....|....*....|....*.
gi 333108235 265 INIKQVLLNMRKYRMGLIQTPDQLRF 290
Cdd:cd14614  212 VDILGLVSEMRSYRMSMVQTEEQYIF 237
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 46-297 2.34e-54

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: 180.08  E-value: 2.34e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  46 NRYRDVSPYDHSRVKL----QNAENDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKESV 121
Cdd:cd14619    1 NRFRNVLPYDWSRVPLkpihEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 122 KCAQYWPTDDQEMLFKEtgFSVKLLSEDVKSYYTVHLLQLENInyienlwitlylkllmldvkrslKSGETRTISHFHYT 201
Cdd:cd14619   81 KCEHYWPLDYTPCTYGH--LRVTVVSEEVMENWTVREFLLKQV-----------------------EEQKTLSVRHFHFT 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 202 TWPDFGVPESPASFLNFLFKVRESGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGL 281
Cdd:cd14619  136 AWPDHGVPSSTDTLLAFRRLLRQWLDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLM 215

                        250
                 ....*....|....*.
gi 333108235 282 IQTPDQLRFSYMAIIE 297
Cdd:cd14619  216 VQTESQYVFLHQCILD 231
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 5-301 3.91e-54

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: 181.06  E-value: 3.91e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235   5 IEREFEELD--TQRRWQPLYLEIrneshdyphrvakfpeNRNRNRYRDVSPYDHSRVKLQNAE----NDYINASLVDIEE 78
Cdd:cd14625   24 LSQEYESIDpgQQFTWEHSNLEV----------------NKPKNRYANVIAYDHSRVILQPIEgimgSDYINANYIDGYR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  79 AQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKESVKCAQYWPTDDQEmlfketgfsvkllsedvksyyTVHL 158
Cdd:cd14625   88 KQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTE---------------------TYGM 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 159 LQLENINYIEnlWITLYLKLLMLDVKrslKSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSlnPDHGPAVIH 238
Cdd:cd14625  147 IQVTLLDTIE--LATFCVRTFSLHKN---GSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNP--PDAGPIVVH 219

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 333108235 239 CSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIEGAKC 301
Cdd:cd14625  220 CSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAVAC 282
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 68-292 7.74e-54

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: 177.83  E-value: 7.74e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  68 YINASLVDIEEA-QRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKESVKCAQYWPTDDQEMLFKetGFSVKLL 146
Cdd:cd18533    1 YINASYITLPGTsSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEYG--DLTVELV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 147 SEDV--KSYYTVHLLQLeninyienlwitlylkllmldvkrSLKSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRE 224
Cdd:cd18533   79 SEEEndDGGFIVREFEL------------------------SKEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRE 134

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 333108235 225 SGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDIN---------IKQVLLNMRKYRMGLIQTPDQLRFSY 292
Cdd:cd18533  135 LNDSASLDPPIIVHCSAGVGRTGTFIALDSLLDELKRGLSDSqdledsedpVYEIVNQLRKQRMSMVQTLRQYIFLY 211
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 36-302 1.97e-53

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: 179.48  E-value: 1.97e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  36 VAKFPENRNRNRYRDVSPYDHSRV--KLQNAEN--DYINAS-LVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVV 110
Cdd:cd14610   38 VAQREENVQKNRSLAVLPYDHSRIilKAENSHShsDYINASpIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCVVIV 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 111 MLNRIVEKESVKCAQYWPtDDQEMLFKEtgFSVKLLSEDVksyytvhllqleninYIENLWI-TLYLKllmldvkrSLKS 189
Cdd:cd14610  118 MLTPLAENGVKQCYHYWP-DEGSNLYHI--YEVNLVSEHI---------------WCEDFLVrSFYLK--------NLQT 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 190 GETRTISHFHYTTWPDFGVPESPASFLNFLFKVREsgSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKG-DDINIK 268
Cdd:cd14610  172 NETRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNK--CYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMAKGaKEIDIA 249

                        250       260       270
                 ....*....|....*....|....*....|....
gi 333108235 269 QVLLNMRKYRMGLIQTPDQLRFSYMAIIEGAKCI 302
Cdd:cd14610  250 ATLEHLRDQRPGMVQTKEQFEFALTAVAEEVNAI 283
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 68-297 1.10e-52

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: 174.94  E-value: 1.10e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  68 YINASLVDIE--EAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKESVKCAQYWPTDDQEMLfKETGFSVKL 145
Cdd:cd14596    1 YINASYITMPvgEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPM-ELENYQLRL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 146 LSEDVKSYYTVHLLQLeninyIENlwitlylkllmldvkrslKSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRES 225
Cdd:cd14596   80 ENYQALQYFIIRIIKL-----VEK------------------ETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKV 136

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333108235 226 GSLnpdhGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIE 297
Cdd:cd14596  137 HNT----GPIVVHCSAGIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLE 204
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 68-297 3.72e-52

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: 173.40  E-value: 3.72e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  68 YINASLV-DIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKESVKCAQYWPTDDQEmlfketgfsvkll 146
Cdd:cd14546    1 YINASTIyDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSE------------- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 147 sedVKSYYTVHLLQlENINYIENLWITLYLKllmldvkrSLKSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVREsg 226
Cdd:cd14546   68 ---VYHIYEVHLVS-EHIWCDDYLVRSFYLK--------NLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNK-- 133

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333108235 227 SLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKG-DDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIE 297
Cdd:cd14546  134 SYRGRSCPIVVHCSDGAGRTGTYILIDMVLNRMAKGaKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 41-301 6.20e-52

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: 174.06  E-value: 6.20e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  41 ENRNRNRYRDVSPYDHSRVKLQNAE----NDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIV 116
Cdd:cd14630    2 ENRNKNRYGNIISYDHSRVRLQLLDgdphSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 117 EKESVKCAQYWPtDDQEML--FKETGFSVKLLSEDVKSYYTVHllqleninyienlwitlylkllmldvkrslKSG--ET 192
Cdd:cd14630   82 EVGRVKCVRYWP-DDTEVYgdIKVTLIETEPLAEYVIRTFTVQ------------------------------KKGyhEI 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 193 RTISHFHYTTWPDFGVPESPASFLNFlfkVRESGSLN-PDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVL 271
Cdd:cd14630  131 REIRQFHFTSWPDHGVPCYATGLLGF---VRQVKFLNpPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCV 207

                        250       260       270
                 ....*....|....*....|....*....|
gi 333108235 272 LNMRKYRMGLIQTPDQLRFSYMAIIEGAKC 301
Cdd:cd14630  208 RELRAQRVNMVQTEEQYVFVHDAILEACLC 237
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 36-302 1.57e-51

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: 174.46  E-value: 1.57e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  36 VAKFPENRNRNRYRDVSPYDHSRVKLQNAEN----DYINAS-LVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVV 110
Cdd:cd14609   36 TAQGEANVKKNRNPDFVPYDHARIKLKAESNpsrsDYINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWENGCTVIV 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 111 MLNRIVEKESVKCAQYWPtDDQEMLFKEtgFSVKLLSEDVksyytvhllqleninYIENLWI-TLYLKllmldvkrSLKS 189
Cdd:cd14609  116 MLTPLVEDGVKQCDRYWP-DEGSSLYHI--YEVNLVSEHI---------------WCEDFLVrSFYLK--------NVQT 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 190 GETRTISHFHYTTWPDFGVPESPASFLNFLFKVREsgSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKG-DDINIK 268
Cdd:cd14609  170 QETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNK--CYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGvKEIDIA 247

                        250       260       270
                 ....*....|....*....|....*....|....
gi 333108235 269 QVLLNMRKYRMGLIQTPDQLRFSYMAIIEGAKCI 302
Cdd:cd14609  248 ATLEHVRDQRPGMVRTKDQFEFALTAVAEEVNAI 281
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 7-301 2.31e-51

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: 174.15  E-value: 2.31e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235   7 REFEELD--TQRRWQPLYLEIrneshdyphrvakfpeNRNRNRYRDVSPYDHSRVKLQNAE----NDYINASLVDIEEAQ 80
Cdd:cd14624   26 QEYESIDpgQQFTWEHSNLEV----------------NKPKNRYANVIAYDHSRVLLSAIEgipgSDYINANYIDGYRKQ 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  81 RSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKESVKCAQYWPTDDQEmlfketgfsvkllsedvksyyTVHLLQ 160
Cdd:cd14624   90 NAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTE---------------------TYGLIQ 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 161 LENINYIEnlwITLYLKLLMLDVKRSlkSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSlnPDHGPAVIHCS 240
Cdd:cd14624  149 VTLLDTVE---LATYCVRTFALYKNG--SSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNP--PDAGPMVVHCS 221

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 333108235 241 AGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIEGAKC 301
Cdd:cd14624  222 AGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAVTC 282
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 67-297 9.80e-51

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: 170.13  E-value: 9.80e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  67 DYINASLVDIEEAQRS----YILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKESVKCAQYWPTDDQEMLFKetGFS 142
Cdd:cd14601    1 DYINANYINMEIPSSSiinrYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSSSYG--GFQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 143 VKLLSEDVKSYYTVHLLQLENinyienlwitlylkllmldvkrsLKSGETRTISHFHYTTWPDFGVPESPASFLNFLFKV 222
Cdd:cd14601   79 VTCHSEEGNPAYVFREMTLTN-----------------------LEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLV 135

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333108235 223 RESGSLNPDhgPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIE 297
Cdd:cd14601  136 RNKRAGKDE--PVVVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 208
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 48-297 2.90e-50

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: 169.35  E-value: 2.90e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  48 YRDVSPYDHSRVKLQNAE----NDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKESVKC 123
Cdd:cd14620    1 YPNILPYDHSRVILSQLDgipcSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 124 AQYWPtdDQEMLfkeTGFSVKLLSED--VKSYYTVhllqleninyienlwitlylKLLMLDVKRSLKSGETRTISHFHYT 201
Cdd:cd14620   81 YQYWP--DQGCW---TYGNIRVAVEDcvVLVDYTI--------------------RKFCIQPQLPDGCKAPRLVTQLHFT 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 202 TWPDFGVPESPASFLNFLFKVResgSLNPDH-GPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMG 280
Cdd:cd14620  136 SWPDFGVPFTPIGMLKFLKKVK---SVNPVHaGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQ 212

                        250
                 ....*....|....*..
gi 333108235 281 LIQTPDQLRFSYMAIIE 297
Cdd:cd14620  213 MVQTDMQYSFIYQALLE 229
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 46-296 4.87e-50

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: 168.58  E-value: 4.87e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  46 NRYRDVSPYDHSRVKL----QNAENDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKESV 121
Cdd:cd14618    1 NRYPHVLPYDHSRVRLsqlgGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 122 KCAQYWPTDdqemlfketgfsvklLSEDVKSYYTVHLLQLENinyiENLWITLYLKLLMLDVKrslksgETRTISHFHYT 201
Cdd:cd14618   81 LCDHYWPSE---------------STPVSYGHITVHLLAQSS----EDEWTRREFKLWHEDLR------KERRVKHLHYT 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 202 TWPDFGVPESPASFLNFLFKVRESGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGL 281
Cdd:cd14618  136 AWPDHGIPESTSSLMAFRELVREHVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLM 215

                        250
                 ....*....|....*
gi 333108235 282 IQTPDQLRFSYMAII 296
Cdd:cd14618  216 IQTLSQYIFLHSCIL 230
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 68-297 4.64e-49

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: 165.71  E-value: 4.64e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  68 YINASLVDIEE--AQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKESVKCAQYWPTDDQEMLFKETG-FSVK 144
Cdd:cd14540    1 YINASHITATVggKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEHDALTFGeYKVS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 145 LLSEDVKSYYTVHLLQLENinyienlwitlylkllmldvkrsLKSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVR- 223
Cdd:cd14540   81 TKFSVSSGCYTTTGLRVKH-----------------------TLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINs 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 224 -------ESGSLNPdHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAII 296
Cdd:cd14540  138 vrrhtnqDVAGHNR-NPPTLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLI 216


                 .
gi 333108235 297 E 297
Cdd:cd14540  217 Q 217
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 37-294 5.27e-49

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: 166.16  E-value: 5.27e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  37 AKFPENRNRNRYRDVSPYDHSRVKLQ---NAE-NDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVML 112
Cdd:cd14554    1 ANLPCNKFKNRLVNILPYESTRVCLQpirGVEgSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 113 NRIVEKESVKCAQYWPTDDQEmlfKETGFSVKLLSEDVKSYYTVHLLQLENINyienlwitlylkllmldvkrslkSGET 192
Cdd:cd14554   81 TKLREMGREKCHQYWPAERSA---RYQYFVVDPMAEYNMPQYILREFKVTDAR-----------------------DGQS 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 193 RTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLL 272
Cdd:cd14554  135 RTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVK 214

                        250       260
                 ....*....|....*....|..
gi 333108235 273 NMRKYRMGLIQTPDQLRFSYMA 294
Cdd:cd14554  215 LLRTQRPAMVQTEDQYQFCYRA 236
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 28-298 8.12e-49

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: 167.14  E-value: 8.12e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  28 ESHDYPHRVAKFPENRNRNRYRDVSPYDHSRVKLQNAE----NDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQ 103
Cdd:cd14633   26 EGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEgetsSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWH 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 104 QKTKAVVMLNRIVEKESVKCAQYWPTDDQemLFKEtgFSVKLLSEDVKSYYTVHLLQLEninyienlwitlylkllmldv 183
Cdd:cd14633  106 ENTASIIMVTNLVEVGRVKCCKYWPDDTE--IYKD--IKVTLIETELLAEYVIRTFAVE--------------------- 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 184 KRSLKsgETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSlnPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGD 263
Cdd:cd14633  161 KRGVH--EIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSP--PNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREG 236

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 333108235 264 DINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIEG 298
Cdd:cd14633  237 VVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEA 271
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 41-297 1.34e-48

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: 167.12  E-value: 1.34e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  41 ENRNRNRYRDVSPYDHSRVKLQNAE----NDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIV 116
Cdd:cd14621   51 ENKEKNRYVNILPYDHSRVHLTPVEgvpdSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLK 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 117 EKESVKCAQYWPtdDQEMLfkeTGFSVKLLSEDVKSY--YTVHLLQLENINYIENlwitlylkllmldvkrslkSGETRT 194
Cdd:cd14621  131 ERKECKCAQYWP--DQGCW---TYGNIRVSVEDVTVLvdYTVRKFCIQQVGDVTN-------------------KKPQRL 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 195 ISHFHYTTWPDFGVPESPASFLNFLFKVResgSLNPDH-GPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLN 273
Cdd:cd14621  187 ITQFHFTSWPDFGVPFTPIGMLKFLKKVK---NCNPQYaGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSR 263

                        250       260
                 ....*....|....*....|....
gi 333108235 274 MRKYRMGLIQTPDQLRFSYMAIIE 297
Cdd:cd14621  264 IRAQRCQMVQTDMQYVFIYQALLE 287
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 32-295 1.48e-48

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: 167.03  E-value: 1.48e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  32 YPHRVAKFPENRNRNRYRDVSPYDHSRVKL----QNAENDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTK 107
Cdd:cd14604   47 YPTATGEKEENVKKNRYKDILPFDHSRVKLtlktSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVA 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 108 AVVMLNRIVEKESVKCAQYWPT-DDQEMLFKEtgFSVKLLSEDVKSYYTVHLLQLENINyienlwitlylkllmldvkrs 186
Cdd:cd14604  127 IIVMACREFEMGRKKCERYWPLyGEEPMTFGP--FRISCEAEQARTDYFIRTLLLEFQN--------------------- 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 187 lksgETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSlnPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKG---D 263
Cdd:cd14604  184 ----ETRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQE--HEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGkipE 257

                        250       260       270
                 ....*....|....*....|....*....|..
gi 333108235 264 DINIKQVLLNMRKYRMGLIQTPDQLRFSYMAI 295
Cdd:cd14604  258 EFNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 289
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 68-296 4.70e-48

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: 162.84  E-value: 4.70e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKESVKCAQYWPTDDQEmlfkETG-FSVKLL 146
Cdd:cd17668    1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSE----EYGnFLVTQK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 147 SEDVKSYYTVHLLQLENINyienlwitlylkllmldVKRSLKSGET--RTISHFHYTTWPDFGVPESPASFLNFLFKvrE 224
Cdd:cd17668   77 SVQVLAYYTVRNFTLRNTK-----------------IKKGSQKGRPsgRVVTQYHYTQWPDMGVPEYTLPVLTFVRK--A 137

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333108235 225 SGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAII 296
Cdd:cd17668  138 SYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 22-297 3.65e-47

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: 162.86  E-value: 3.65e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  22 YLEIRNESHDYPHRVAKFPENRNRNRYRDVSPYDHSRVKL-QNAEND--YINAS--LVDIEEAQRSYILTQGPLPNTCCH 96
Cdd:cd14599   18 YEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELvPTKENNtgYINAShiKVTVGGEEWHYIATQGPLPHTCHD 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  97 FWLMVWQQKTKAVVMLNRIVEKESVKCAQYWPtddqemlfketgfsvKLLSEDVKSYYTVHLLQlENINYIENLWITLYL 176
Cdd:cd14599   98 FWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWP---------------KLGSKHSSATYGKFKVT-TKFRTDSGCYATTGL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 177 KLlmldvkRSLKSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRE-----------SGSLNPdhgPAVIHCSAGIGR 245
Cdd:cd14599  162 KV------KHLLSGQERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSvrrhtnsmldsTKNCNP---PIVVHCSAGVGR 232

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 333108235 246 SGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIE 297
Cdd:cd14599  233 TGVVILTELMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQ 284
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 46-290 5.90e-47

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: 160.46  E-value: 5.90e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  46 NRYRDVSPYDHSRVKLQN----AENDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKESV 121
Cdd:cd14616    1 NRFPNIKPYNNNRVKLIAdagvPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 122 KCAQYWPTDDQEMlfkeTGFS---VKLLSEDVKSYYTVHLLQLEninyienlwitlylkllmldvkrslKSGETRTISHF 198
Cdd:cd14616   81 RCHQYWPEDNKPV----TVFGdivITKLMEDVQIDWTIRDLKIE-------------------------RHGDYMMVRQC 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 199 HYTTWPDFGVPESPASFLNFLFKVRESGSlnPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYR 278
Cdd:cd14616  132 NFTSWPEHGVPESSAPLIHFVKLVRASRA--HDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSER 209

                        250
                 ....*....|..
gi 333108235 279 MGLIQTPDQLRF 290
Cdd:cd14616  210 MCMVQNLAQYIF 221
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 68-292 7.01e-47

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: 159.47  E-value: 7.01e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  68 YINASLV-DIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKESVKCAQYWPTD-DQEMLFKetGFSVKL 145
Cdd:cd14539    1 YINASLIeDLTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErGQALVYG--AITVSL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 146 LSEDVKSYYTVHLLQLENinyienlwitlylkllmLDVKrslksgETRTISHFHYTTWPDFGVPESPASFLNFLFKVRES 225
Cdd:cd14539   79 QSVRTTPTHVERIISIQH-----------------KDTR------LSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSH 135

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 333108235 226 GSL-NPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDI-NIKQVLLNMRKYRMGLIQTPDQLRFSY 292
Cdd:cd14539  136 YLQqRSLQTPIVVHCSSGVGRTGAFCLLYAAVQEIEAGNGIpDLPQLVRKMRQQRKYMLQEKEHLKFCY 204
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 45-297 2.80e-45

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: 156.54  E-value: 2.80e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  45 RNRYRDVSPYDHSRVKLQ----NAENDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKES 120
Cdd:cd14602    1 KNRYKDILPYDHSRVELSlitsDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 121 VKCAQYWpTDDQEMLFKETGFSVKLLSEDVKSYYTVHLLQLENINyienlwitlylkllmldvkrslksgETRTISHFHY 200
Cdd:cd14602   81 KKCERYW-AEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNS-------------------------ETRTIYQFHY 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 201 TTWPDFGVPESPASFLNFLFKVResgSLNPDHG-PAVIHCSAGIGRSGTFSLVDTCLVLMEKG---DDINIKQVLLNMRK 276
Cdd:cd14602  135 KNWPDHDVPSSIDPILELIWDVR---CYQEDDSvPICIHCSAGCGRTGVICAIDYTWMLLKDGiipENFSVFSLIQEMRT 211

                        250       260
                 ....*....|....*....|.
gi 333108235 277 YRMGLIQTPDQLRFSYMAIIE 297
Cdd:cd14602  212 QRPSLVQTKEQYELVYNAVIE 232
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 41-302 4.19e-45

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 158.24  E-value: 4.19e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  41 ENRNRNRYRDVSPYDHSRV--KLQNAENDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEK 118
Cdd:PHA02742  51 KNMKKCRYPDAPCFDRNRVilKIEDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIMED 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 119 ESVKCAQYWPTDDQEmlfKETGFSVKLLSEDVKS--YYTVHLLQLENINyienlwitlylkllmldvkrslkSGETRTIS 196
Cdd:PHA02742 131 GKEACYPYWMPHERG---KATHGEFKIKTKKIKSfrNYAVTNLCLTDTN-----------------------TGASLDIK 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 197 HFHYTTWPDFGVPESPASFLNFLFKVRE---------SGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINI 267
Cdd:PHA02742 185 HFAYEDWPHGGLPRDPNKFLDFVLAVREadlkadvdiKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPL 264

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 333108235 268 KQVLLNMRKYRMGLIQTPDQLRFSYMAIIEGAKCI 302
Cdd:PHA02742 265 LSIVRDLRKQRHNCLSLPQQYIFCYFIVLIFAKLM 299
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 40-292 6.18e-45

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: 155.76  E-value: 6.18e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  40 PENRNRNRYRDVSPYDHSRVKLQNA-----ENDYINASLV-DIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLN 113
Cdd:cd14612   13 PGHASKDRYKTILPNPQSRVCLRRAgsqeeEGSYINANYIrGYDGKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMIT 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 114 RIVEKESvKCAQYWPTddqemlfKETGFS-VKLLSEDVKSY--YTVHLLQLENinyienlwitlylkllmldvkrslkSG 190
Cdd:cd14612   93 KLKEKKE-KCVHYWPE-------KEGTYGrFEIRVQDMKECdgYTIRDLTIQL-------------------------EE 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 191 ETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLNPDHGPAVIHCSAGIGRSGTFSLVDT-CLVLMEKGdDINIKQ 269
Cdd:cd14612  140 ESRSVKHYWFSSWPDHQTPESAGPLLRLVAEVEESRQTAASPGPIVVHCSAGIGRTGCFIATSIgCQQLKDTG-KVDILG 218

                        250       260
                 ....*....|....*....|...
gi 333108235 270 VLLNMRKYRMGLIQTPDQLRFSY 292
Cdd:cd14612  219 IVCQLRLDRGGMIQTSEQYQFLH 241
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 3-297 6.61e-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: 157.20  E-value: 6.61e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235   3 TTIEREFEELDTQRrwqplyleirneSHDYPHRVAKFPENRNRNRYRDVSPYDHSRVKLQNAE----NDYINASLVDIEE 78
Cdd:cd14628   25 TGMELEFKRLASSK------------AHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRgvegSDYINASFIDGYR 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  79 AQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKESVKCAQYWPTDDQEmlfKETGFSVKLLSEDVKSYYTVHL 158
Cdd:cd14628   93 QQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSA---RYQYFVVDPMAEYNMPQYILRE 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 159 LQLENInyienlwitlylkllmldvkrslKSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLNPDHGPAVIH 238
Cdd:cd14628  170 FKVTDA-----------------------RDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPISVH 226

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 333108235 239 CSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIE 297
Cdd:cd14628  227 CSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALE 285
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 37-297 7.81e-44

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: 154.51  E-value: 7.81e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  37 AKFPENRNRNRYRDVSPYDHSRVKLQNAE----NDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVML 112
Cdd:cd14627   48 ANLPCNKFKNRLVNIMPYETTRVCLQPIRgvegSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVML 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 113 NRIVEKESVKCAQYWPTDDQEmlfKETGFSVKLLSEDVKSYYTVHLLQLENInyienlwitlylkllmldvkrslKSGET 192
Cdd:cd14627  128 TKLREMGREKCHQYWPAERSA---RYQYFVVDPMAEYNMPQYILREFKVTDA-----------------------RDGQS 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 193 RTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLL 272
Cdd:cd14627  182 RTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVK 261

                        250       260
                 ....*....|....*....|....*
gi 333108235 273 NMRKYRMGLIQTPDQLRFSYMAIIE 297
Cdd:cd14627  262 MLRTQRPAMVQTEDEYQFCYQAALE 286
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 68-292 1.02e-43

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: 151.22  E-value: 1.02e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKESVKCAQYWPTDDQEmlfkeTGFSVKLLS 147
Cdd:cd14551    1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCW-----TYGNLRVRV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 148 EDVKSY--YTVHllqleninyienlwitlylKLLMLDVKRSLKSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRes 225
Cdd:cd14551   76 EDTVVLvdYTTR-------------------KFCIQKVNRGIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVK-- 134

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 333108235 226 gSLNPDH-GPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSY 292
Cdd:cd14551  135 -SANPPRaGPIVVHCSAGVGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 68-297 1.38e-43

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: 150.84  E-value: 1.38e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKESVKCAQYWPtDDQEML--FKETGFSVKL 145
Cdd:cd14555    1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWP-DDTEVYgdIKVTLVETEP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 146 LSEdvksyYTVHLLQLENINYienlwitlylkllmldvkrslksGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRES 225
Cdd:cd14555   80 LAE-----YVVRTFALERRGY-----------------------HEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKAS 131

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333108235 226 GSlnPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIE 297
Cdd:cd14555  132 NP--PSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 58-298 1.01e-42

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: 149.02  E-value: 1.01e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  58 RVKLQNAEND----YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKESVKCAQYWPtDDQE 133
Cdd:cd14631    1 RVILQPVEDDpssdYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP-DDTE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 134 ML--FKETGFSVKLLSEdvksyYTVHLLQLENINYienlwitlylkllmldvkrslksGETRTISHFHYTTWPDFGVPES 211
Cdd:cd14631   80 VYgdFKVTCVEMEPLAE-----YVVRTFTLERRGY-----------------------NEIREVKQFHFTGWPDHGVPYH 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 212 PASFLNFLFKVRESGSlnPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFS 291
Cdd:cd14631  132 ATGLLSFIRRVKLSNP--PSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFI 209


                 ....*..
gi 333108235 292 YMAIIEG 298
Cdd:cd14631  210 HDAILEA 216
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 68-292 1.31e-42

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: 148.31  E-value: 1.31e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKESVKCAQYWPTDDQEmlFKETGfsVKLLS 147
Cdd:cd14558    1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKT--YGDIE--VELKD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 148 EDVKSYYTVHLLQLeninyienlwitlylkllmldvkRSLKSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESG- 226
Cdd:cd14558   77 TEKSPTYTVRVFEI-----------------------THLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLp 133

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 333108235 227 ---SLNPDHGPAVIHCSAGIGRSGTFslvdtC--LVLMEKGDD---INIKQVLLNMRKYRMGLIQTPDQLRFSY 292
Cdd:cd14558  134 yknSKHGRSVPIVVHCSDGSSRTGIF-----CalWNLLESAETekvVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 40-290 2.54e-42

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 150.92  E-value: 2.54e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  40 PENRNRNRYRDVSPYDHSRVKLQN---AENDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVML--NR 114
Cdd:PHA02747  49 PENQPKNRYWDIPCWDHNRVILDSgggSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLtpTK 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 115 IVEKESvKCAQYWPTDDQEMLFKEtGFSVKLLSEDVKSYYTVHLLQLENinyienlwitlylkllmldvkRSLKSgeTRT 194
Cdd:PHA02747 129 GTNGEE-KCYQYWCLNEDGNIDME-DFRIETLKTSVRAKYILTLIEITD---------------------KILKD--SRK 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 195 ISHFHYTTWPDFGVPESPASFLNFLFKV----RESGSL-NPDHG---PAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDIN 266
Cdd:PHA02747 184 ISHFQCSEWFEDETPSDHPDFIKFIKIIdinrKKSGKLfNPKDAllcPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAIC 263

                        250       260
                 ....*....|....*....|....
gi 333108235 267 IKQVLLNMRKYRMGLIQTPDQLRF 290
Cdd:PHA02747 264 LAKTAEKIREQRHAGIMNFDDYLF 287
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 37-297 5.17e-42

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: 149.49  E-value: 5.17e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  37 AKFPENRNRNRYRDVSPYDHSRVKLQNAE----NDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVML 112
Cdd:cd14629   48 ANLPCNKFKNRLVNIMPYELTRVCLQPIRgvegSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVML 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 113 NRIVEKESVKCAQYWPTDDQEmlfKETGFSVKLLSEDVKSYYTVHLLQLENInyienlwitlylkllmldvkrslKSGET 192
Cdd:cd14629  128 TKLREMGREKCHQYWPAERSA---RYQYFVVDPMAEYNMPQYILREFKVTDA-----------------------RDGQS 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 193 RTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLL 272
Cdd:cd14629  182 RTIRQFQFTDWPEQGVPKTGEGFIDFIGQVHKTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVK 261

                        250       260
                 ....*....|....*....|....*
gi 333108235 273 NMRKYRMGLIQTPDQLRFSYMAIIE 297
Cdd:cd14629  262 TLRTQRPAMVQTEDQYQLCYRAALE 286
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 68-301 3.55e-41

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: 144.81  E-value: 3.55e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKESVKCAQYWPtDDQEMLfkeTGFSVKLLS 147
Cdd:cd14632    1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWP-DDSDTY---GDIKITLLK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 148 EDVKSYYTVHLLQLENINYienlwitlylkllmlDVKRSLKsgetrtisHFHYTTWPDFGVPESPASFLNFLFKVRESGS 227
Cdd:cd14632   77 TETLAEYSVRTFALERRGY---------------SARHEVK--------QFHFTSWPEHGVPYHATGLLAFIRRVKASTP 133

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 333108235 228 lnPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIEGAKC 301
Cdd:cd14632  134 --PDAGPVVVHCSAGAGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACLC 205
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 68-295 5.34e-41

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: 143.95  E-value: 5.34e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKESVKCAQYWPTDDqemLFKETGFSVKLLS 147
Cdd:cd14552    1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDG---SVSSGDITVELKD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 148 EDVKSYYTVHLLQLENInyienlwitlylkllmldvkrslKSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGS 227
Cdd:cd14552   78 QTDYEDYTLRDFLVTKG-----------------------KGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQ 134

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 333108235 228 LNPDHgPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAI 295
Cdd:cd14552  135 QSGNH-PITVHCSAGAGRTGTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 45-290 6.25e-41

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: 145.78  E-value: 6.25e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  45 RNRYRDVSPYDHSRVKLQNAEND-----YINASLV-DIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEK 118
Cdd:cd14613   28 KNRYKTILPNPHSRVCLTSPDQDdplssYINANYIrGYGGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 119 ESvKCAQYWPtdDQEMLFKETGFSVK--LLSEDvksyYTVHLLQLEninyienlwitlylkllmldvkrslKSGETRTIS 196
Cdd:cd14613  108 NE-KCTEYWP--EEQVTYEGIEITVKqvIHADD----YRLRLITLK-------------------------SGGEERGLK 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 197 HFHYTTWPDFGVPESPASFLNFLFKVRES-GSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMR 275
Cdd:cd14613  156 HYWYTSWPDQKTPDNAPPLLQLVQEVEEArQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLR 235

                        250
                 ....*....|....*
gi 333108235 276 KYRMGLIQTPDQLRF 290
Cdd:cd14613  236 LDRGGMIQTCEQYQF 250
PHA02738 PHA02738
hypothetical protein; Provisional
 42-295 1.07e-40

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 146.99  E-value: 1.07e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  42 NRNRNRYRDVSPYDHSRVKLQNAEN--DYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKE 119
Cdd:PHA02738  49 NRKLNRYLDAVCFDHSRVILPAERNrgDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENG 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 120 SVKCAQYWPTDDQEML----FKETGFSVKLLSEDVKSyytvhllqleninyienlwitlylKLLMLDvkrslKSGETRTI 195
Cdd:PHA02738 129 REKCFPYWSDVEQGSIrfgkFKITTTQVETHPHYVKS------------------------TLLLTD-----GTSATQTV 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 196 SHFHYTTWPDFGVPESPASFLNFLFKVRE------SGSLNPDHG-----PAVIHCSAGIGRSGTFSLVDTCLVLMEKGDD 264
Cdd:PHA02738 180 THFNFTAWPDHDVPKNTSEFLNFVLEVRQcqkelaQESLQIGHNrlqppPIVVHCNAGLGRTPCYCVVDISISRFDACAT 259

                        250       260       270
                 ....*....|....*....|....*....|.
gi 333108235 265 INIKQVLLNMRKYRMGLIQTPDQLRFSYMAI 295
Cdd:PHA02738 260 VSIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 40-300 2.68e-40

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 145.94  E-value: 2.68e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  40 PENRNRNRYRDVSPYDHSRVKL-----------------------QNAENDYINASLVDIEEAQRSYILTQGPLPNTCCH 96
Cdd:PHA02746  49 KENLKKNRFHDIPCWDHSRVVInaheslkmfdvgdsdgkkievtsEDNAENYIHANFVDGFKEANKFICAQGPKEDTSED 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  97 FWLMVWQQKTKAVVMLNRIvEKESVKCAQYWPT-DDQEMLFKEtgFSVKLLSEDVKSYYTVHLLQLENinyienlwitly 175
Cdd:PHA02746 129 FFKLISEHESQVIVSLTDI-DDDDEKCFELWTKeEDSELAFGR--FVAKILDIIEELSFTKTRLMITD------------ 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 176 lkllmldvkrslKSGET-RTISHFHYTTWPDFGVPESPASFLNFLFKVRE--------SGSLNPDHGPAVIHCSAGIGRS 246
Cdd:PHA02746 194 ------------KISDTsREIHHFWFPDWPDNGIPTGMAEFLELINKVNEeqaelikqADNDPQTLGPIVVHCSAGIGRA 261

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 333108235 247 GTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYM----AIIEGAK 300
Cdd:PHA02746 262 GTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKalkyAIIEEAK 319
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 68-292 1.74e-39

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: 140.25  E-value: 1.74e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKESVKCAQYWPtDDQEMLFKETGFSVKLLS 147
Cdd:cd14542    1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWP-EEGEEQLQFGPFKISLEK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 148 EDVKSY-YTVHLLQLENINyienlwitlylkllmldvkrslksgETRTISHFHYTTWPDFGVPESPASFLNFLFKVR--- 223
Cdd:cd14542   80 EKRVGPdFLIRTLKVTFQK-------------------------ESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRdyq 134

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333108235 224 ESGSLnpdhgPAVIHCSAGIGRSGTFSLVDTCLVLMEKG---DDINIKQVLLNMRKYRMGLIQTPDQLRFSY 292
Cdd:cd14542  135 GSEDV-----PICVHCSAGCGRTGTICAIDYVWNLLKTGkipEEFSLFDLVREMRKQRPAMVQTKEQYELVY 201
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
194-297 4.27e-39

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 135.56  E-value: 4.27e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235   194 TISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDD-INIKQVLL 272
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDTVK 80

                           90       100
                   ....*....|....*....|....*
gi 333108235   273 NMRKYRMGLIQTPDQLRFSYMAIIE 297
Cdd:smart00404  81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 194-297 4.27e-39

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: 135.56  E-value: 4.27e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235   194 TISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDD-INIKQVLL 272
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDTVK 80

                           90       100
                   ....*....|....*....|....*
gi 333108235   273 NMRKYRMGLIQTPDQLRFSYMAIIE 297
Cdd:smart00012  81 ELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 47-297 1.51e-38

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: 138.64  E-value: 1.51e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  47 RYRDVSPYDHSRVKL---QNAEN-DYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKESVK 122
Cdd:cd14623    1 RVLQIIPYEFNRVIIpvkRGEENtDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 123 CAQYWPTDDqemLFKETGFSVKLLSEDVKSYYTVHLLQLENInyienlwitlylkllmldvkrslKSGETRTISHFHYTT 202
Cdd:cd14623   81 CAQYWPSDG---SVSYGDITIELKKEEECESYTVRDLLVTNT-----------------------RENKSRQIRQFHFHG 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 203 WPDFGVPESPASFLNFLFKVRESGSLNPDHgPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLI 282
Cdd:cd14623  135 WPEVGIPSDGKGMINIIAAVQKQQQQSGNH-PITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMV 213

                        250
                 ....*....|....*
gi 333108235 283 QTPDQLRFSYMAIIE 297
Cdd:cd14623  214 QTLEQYEFCYKVVQE 228
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 68-292 1.68e-38

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: 137.60  E-value: 1.68e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  68 YINASLV--DIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKES-VKCAQYWPTDDQEMlfKETG-FSV 143
Cdd:cd17658    1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYStAKCADYFPAEENES--REFGrISV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 144 KLLSEDVKSyytvHLLQLENinyienlwitlylkllmLDVKRSLKSGETRTISHFHYTTWPDFGVPESPASFLNFLfkvR 223
Cdd:cd17658   79 TNKKLKHSQ----HSITLRV-----------------LEVQYIESEEPPLSVLHIQYPEWPDHGVPKDTRSVRELL---K 134

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 333108235 224 ESGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGD--DINIKQVLLNMRKYRMGLIQTPDQLRFSY 292
Cdd:cd17658  135 RLYGIPPSAGPIVVHCSAGIGRTGAYCTIHNTIRRILEGDmsAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 45-290 1.93e-38

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: 138.13  E-value: 1.93e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  45 RNRYRDVSPYDHSRVKLQ-----NAENDYINASLV-DIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEK 118
Cdd:cd14611    2 KNRYKTILPNPHSRVCLKpknsnDSLSTYINANYIrGYGGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 119 ESvKCAQYWPtdDQEMLFKETGFSVKLLSEdvKSYYTVHLLQLENinyienlwitlylkllmldvkrslkSGETRTISHF 198
Cdd:cd14611   82 NE-KCVLYWP--EKRGIYGKVEVLVNSVKE--CDNYTIRNLTLKQ-------------------------GSQSRSVKHY 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 199 HYTTWPDFGVPESPASFLNFLFKVRESGSLNPDHGPAVIHCSAGIGRSGTF-SLVDTCLVLMEKGdDINIKQVLLNMRKY 277
Cdd:cd14611  132 WYTSWPDHKTPDSAQPLLQLMLDVEEDRLASPGRGPVVVHCSAGIGRTGCFiATTIGCQQLKEEG-VVDVLSIVCQLRVD 210

                        250
                 ....*....|...
gi 333108235 278 RMGLIQTPDQLRF 290
Cdd:cd14611  211 RGGMVQTSEQYEF 223
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
40-288 2.02e-38

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 139.84  E-value: 2.02e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  40 PENRNRNRYRDVSPYDHSRVklqNAENDYINASLVDIEEAQRsYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVE-- 117
Cdd:COG5599   40 INGSPLNRFRDIQPYKETAL---RANLGYLNANYIQVIGNHR-YIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEis 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 118 KESVKCAQYWPTDDQEMLfketgfsvkllsedvksyYTVHLLQLENINYIENLWITLYLkllmldVKRSLKSGETRTISH 197
Cdd:COG5599  116 KPKVKMPVYFRQDGEYGK------------------YEVSSELTESIQLRDGIEARTYV------LTIKGTGQKKIEIPV 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 198 FHYTTWPDFGVPESPAsFLNFLFKVRES-GSLNPDHGPAVIHCSAGIGRSGTFSLvdtCLVLMEKGD-----DINIKQVL 271
Cdd:COG5599  172 LHVKNWPDHGAISAEA-LKNLADLIDKKeKIKDPDKLLPVVHCRAGVGRTGTLIA---CLALSKSINalvqiTLSVEEIV 247

                        250
                 ....*....|....*...
gi 333108235 272 LNMRKYR-MGLIQTPDQL 288
Cdd:COG5599  248 IDMRTSRnGGMVQTSEQL 265
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 68-287 1.74e-37

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: 134.95  E-value: 1.74e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKESVKCAQYWPT-DDQEMLFKEtgFSVKLL 146
Cdd:cd14557    1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSmEEGSRAFGD--VVVKIN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 147 SEDVKSYYTVHLLQLENinyienlwitlylkllmldvkrSLKSGETRTISHFHYTTWPDFGVPESPasflNFLFKVRE-- 224
Cdd:cd14557   79 EEKICPDYIIRKLNINN----------------------KKEKGSGREVTHIQFTSWPDHGVPEDP----HLLLKLRRrv 132

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 333108235 225 SGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQ 287
Cdd:cd14557  133 NAFNNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQ 195
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 68-297 2.26e-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: 124.32  E-value: 2.26e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  68 YINAS--LVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKESVKCAQYWP---TDDQEMLFKETGFS 142
Cdd:cd14598    1 YINAShiKVTVGGKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrlgSRHNTVTYGRFKIT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 143 VKLLSEDVksyytvhllqleninyienLWITLYLKLlmldvkRSLKSGETRTISHFHYTTWPDFGVPESPASFLNFLFKV 222
Cdd:cd14598   81 TRFRTDSG-------------------CYATTGLKI------KHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEI 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 223 RE-----SGSLNPD--HGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAI 295
Cdd:cd14598  136 QSvrrhtNSTIDPKspNPPVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVL 215


                 ..
gi 333108235 296 IE 297
Cdd:cd14598  216 IQ 217
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 67-295 2.47e-33

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: 123.96  E-value: 2.47e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  67 DYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKESVKCAQYWPTDDqemlfketgfSVKll 146
Cdd:cd14622    1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEG----------SVT-- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 147 sedvksyYTVHLLQLENINYIENLWITlylkllmlDVKRSLKSGE-TRTISHFHYTTWPDFGVPESPASFLNFLFKVRES 225
Cdd:cd14622   69 -------HGEITIEIKNDTLLETISIR--------DFLVTYNQEKqTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQ 133

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 226 GSLNPDHgPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAI 295
Cdd:cd14622  134 QQQTGNH-PIVVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 68-292 4.18e-32

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: 120.59  E-value: 4.18e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIvEKESVKCAQYWPtdDQEMlfKETG-FSVKLL 146
Cdd:cd14556    1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQL-DPKDQSCPQYWP--DEGS--GTYGpIQVEFV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 147 SEDVKSYYTVHLLQLENInyienlwitlylkllmldvkrSLKSGETRTISHFHYTTWPDFG-VPESPASFLNFLFKV--- 222
Cdd:cd14556   76 STTIDEDVISRIFRLQNT---------------------TRPQEGYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVekw 134

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 333108235 223 -RESGSlnpdhGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSY 292
Cdd:cd14556  135 qEQSGE-----GPIVVHCLNGVGRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 68-292 2.35e-27

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: 107.41  E-value: 2.35e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKEsvKCAQYWPTDDQEMLFKetGFSVKLLS 147
Cdd:cd14550    1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTKEKPLECE--TFKVTLSG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 148 EDVKSY-----YTVHLLQLENI--NYIenlwitlylkllmLDVKrslksgetrtisHFHYTTWPDfgvPESPAS-FLNFL 219
Cdd:cd14550   77 EDHSCLsneirLIVRDFILESTqdDYV-------------LEVR------------QFQCPSWPN---PCSPIHtVFELI 128

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333108235 220 FKVRESGSLNpdHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQV--LLNMRkyRMGLIQTPDQLRFSY 292
Cdd:cd14550  129 NTVQEWAQQR--DGPIVVHDRYGGVQAATFCALTTLHQQLEHESSVDVYQVakLYHLM--RPGVFTSKEDYQFLY 199
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 42-295 3.63e-24

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 101.20  E-value: 3.63e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  42 NRNRNRYRD------VSPYDHSRVKLQNAENdYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRI 115
Cdd:PHA02740  47 AQAENKAKDenlalhITRLLHRRIKLFNDEK-VLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRH 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 116 VEKESVKcaQYWPTDDQEMLFKETgFSVKLLSEDVKSYYTVHLLQLENinyienlwitlylkllmldvkrslKSGETRTI 195
Cdd:PHA02740 126 ADKKCFN--QFWSLKEGCVITSDK-FQIETLEIIIKPHFNLTLLSLTD------------------------KFGQAQKI 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 196 SHFHYTTWPDFGVPESPASFLNFLFKVR------ESGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQ 269
Cdd:PHA02740 179 SHFQYTAWPADGFSHDPDAFIDFFCNIDdlcadlEKHKADGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIAN 258

                        250       260
                 ....*....|....*....|....*.
gi 333108235 270 VLLNMRKYRMGLIQTPDQLRFSYMAI 295
Cdd:PHA02740 259 ALKKVRQKKYGCMNCLDDYVFCYHLI 284
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 68-297 1.36e-22

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: 94.70  E-value: 1.36e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNrivEKESVK-CAQYWPTddqemlfKETG----FS 142
Cdd:cd14634    1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLN---EMDAAQlCMQYWPE-------KTSCcygpIQ 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 143 VKLLSEDVKSYYTVHLLQLENINYIENLWitlylkllmldvkrslksgetRTISHFHYTTWPDF-GVPESPASFLNFLFK 221
Cdd:cd14634   71 VEFVSADIDEDIISRIFRICNMARPQDGY---------------------RIVQHLQYIGWPAYrDTPPSKRSILKVVRR 129

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 333108235 222 VRE-SGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIE 297
Cdd:cd14634  130 LEKwQEQYDGREGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 68-297 5.19e-22

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: 93.05  E-value: 5.19e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKESV-KCAQYWPtddqEMLFKETG-FSVKL 145
Cdd:cd14637    1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWP----EPGLQQYGpMEVEF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 146 LSEDVKSYYTVHLLQLENINYIENlwitlylkllmldvkrslksgETRTISHFHYTTWPDF-GVPESPASFLNFLFKV-- 222
Cdd:cd14637   77 VSGSADEDIVTRLFRVQNITRLQE---------------------GHLMVRHFQFLRWSAYrDTPDSKKAFLHLLASVek 135

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 333108235 223 --RESGSlnpdhGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIE 297
Cdd:cd14637  136 wqRESGE-----GRTVVHCLNGGGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 68-297 1.47e-20

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: 88.93  E-value: 1.47e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKESvkCAQYWPtddQEMLFKETGFSVKLLS 147
Cdd:cd14636    1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQG--CPQYWP---EEGMLRYGPIQVECMS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 148 EDVKSYYTVHLLQLENINYIENLWItlylkllmldvkrslksgetrTISHFHYTTWPDF-GVPESPASFLNFLFKVRE-S 225
Cdd:cd14636   76 CSMDCDVISRIFRICNLTRPQEGYL---------------------MVQQFQYLGWASHrEVPGSKRSFLKLILQVEKwQ 134

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333108235 226 GSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIE 297
Cdd:cd14636  135 EECDEGEGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 68-296 1.18e-19

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: 86.59  E-value: 1.18e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVML---NRIVEKESVkcaqYWPTDDQEMLFKetGFSVK 144
Cdd:cd17669    1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLpdgQNMAEDEFV----YWPNKDEPINCE--TFKVT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 145 LLSEDVKSyytvhLLQLENInYIENLWITLYLKLLMLDVKrslksgetrtisHFHYTTWPDfgvPESPASFLNFLFKVRE 224
Cdd:cd17669   75 LIAEEHKC-----LSNEEKL-IIQDFILEATQDDYVLEVR------------HFQCPKWPN---PDSPISKTFELISIIK 133

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333108235 225 SGSLNPDhGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAII 296
Cdd:cd17669  134 EEAANRD-GPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 68-297 1.23e-19

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: 86.67  E-value: 1.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIveKESVKCAQYWPTDDqemLFKETGFSVKLLS 147
Cdd:cd14635    1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDV--DPAQLCPQYWPENG---VHRHGPIQVEFVS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 148 EDVKSYYTVHLLQLENINYIENLWitlylkllmldvkrslksgetRTISHFHYTTWPDF-GVPESPASFLNFLFKV-RES 225
Cdd:cd14635   76 ADLEEDIISRIFRIYNAARPQDGY---------------------RMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVdKWQ 134

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333108235 226 GSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIE 297
Cdd:cd14635  135 EEYNGGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 68-296 6.41e-18

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: 81.65  E-value: 6.41e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVML---NRIVEKESVkcaqYWPTDDQEMlfKETGFSVK 144
Cdd:cd17670    1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdnQGLAEDEFV----YWPSREESM--NCEAFTVT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 145 LLSEDvksyytvhLLQLENINYIenlwitlYLKLLMLDVKRSLKSGETRtisHFHYTTWPDfgvPESPASFLNFLFKVRE 224
Cdd:cd17670   75 LISKD--------RLCLSNEEQI-------IIHDFILEATQDDYVLEVR---HFQCPKWPN---PDAPISSTFELINVIK 133

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 333108235 225 SGSLNPDhGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAII 296
Cdd:cd17670  134 EEALTRD-GPTIVHDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
179-290 2.39e-11

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 61.14  E-value: 2.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 179 LMLDVKRSLKSGETRTISHFHYTtWPDFGVPEsPASFLNFLFKVREsgsLNPDHGPAVIHCSAGIGRSGTFslvdTCLVL 258
Cdd:COG2453   32 LTEEEELLLGLLEEAGLEYLHLP-IPDFGAPD-DEQLQEAVDFIDE---ALREGKKVLVHCRGGIGRTGTV----AAAYL 102

                         90       100       110
                 ....*....|....*....|....*....|....
gi 333108235 259 MEKGDDIN--IKQVllnmRKYRMGLIQTPDQLRF 290
Cdd:COG2453  103 VLLGLSAEeaLARV----RAARPGAVETPAQRAF 132
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 178-290 4.70e-11

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: 60.74  E-value: 4.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 178 LLMLDVKRSLKSGETRTISHFHYTTwPDFGVPESPASFLNFLfkvRESGSLNPDHGPAVIHCSAGIGRSGtfsLVDTCLv 257
Cdd:cd14505   56 LEELGVPDLLEQYQQAGITWHHLPI-PDGGVPSDIAQWQELL---EELLSALENGKKVLIHCKGGLGRTG---LIAACL- 127

                         90       100       110
                 ....*....|....*....|....*....|...
gi 333108235 258 LMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRF 290
Cdd:cd14505  128 LLELGDTLDPEQAIAAVRALRPGAIQTPKQENF 160
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 46-288 6.56e-10

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: 58.95  E-value: 6.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235  46 NRYRDVSpydhSRVKLQNAENdyINASLVDIEEaQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKESVKCAQ 125
Cdd:cd14559    1 NRFTNIQ----TRVSTPVGKN--LNANRVQIGN-KNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPP 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 126 YWPTDDQemlfkeTGfSVKLLSEDVKSYYTVHLLQLENinYieNLWITlylkllmldvkrslKSGETRTISHFHYTTWPD 205
Cdd:cd14559   74 YFRQSGT------YG-SVTVKSKKTGKDELVDGLKADM--Y--NLKIT--------------DGNKTITIPVVHVTNWPD 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 206 FG-------------VPESPASFLNFLFKVRESGSLNPDHGPAVIHCSAGIGRSGTFSlvdTCLVLMEKGDDINIKQVLL 272
Cdd:cd14559  129 HTaisseglkeladlVNKSAEEKRNFYKSKGSSAINDKNKLLPVIHCRAGVGRTGQLA---AAMELNKSPNNLSVEDIVS 205

                        250
                 ....*....|....*..
gi 333108235 273 NMRKYRMG-LIQTPDQL 288
Cdd:cd14559  206 DMRTSRNGkMVQKDEQL 222
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 212-290 1.98e-05

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: 43.49  E-value: 1.98e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 333108235 212 PASFLNFLFKVRESGSLNPdhgPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDInIKQVllnMRKYRMGLIQTPDQLRF 290
Cdd:cd14494   39 LAMVDRFLEVLDQAEKPGE---PVLVHCKAGVGRTGTLVACYLVLLGGMSAEEA-VRIV---RLIRPGGIPQTIEQLDF 110
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 195-290 3.15e-04

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: 41.57  E-value: 3.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 195 ISHFHYTtWPDFGVPeSPASFLN----FLFKVRESGSLnpdhgpaVIHCSAGIGRSGtfsLVDTC-LVLMEKgddINIKQ 269
Cdd:cd14506   77 IYFYNFG-WKDYGVP-SLTTILDivkvMAFALQEGGKV-------AVHCHAGLGRTG---VLIACyLVYALR---MSADQ 141

                         90       100
                 ....*....|....*....|.
gi 333108235 270 VLLNMRKYRMGLIQTPDQLRF 290
Cdd:cd14506  142 AIRLVRSKRPNSIQTRGQVLC 162
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 204-290 3.58e-04

dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as VH1-like phosphatase Z (VHZ) or low molecular mass dual specificity phosphatase 3 (LDP-3), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP23 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. It is able to enhance activation of JNK and p38 MAPK, and has been shown to dephosphorylate p44-ERK1 (MAPK3) in vitro. It has been associated with cell growth and human primary cancers. It has also been identified as a cell-cell adhesion regulatory protein; it promotes the dephosphorylation of beta-catenin at Tyr 142 and enhances the interaction between alpha- and beta-catenin.


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 40.34  E-value: 3.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 204 PDFGVP--ESPASFLNFLFKVRESGslnpdhGPAVIHCSAGIGRSGTFSlvdTC-LVLMEK--GDDInIKQVllnmRKYR 278
Cdd:cd14504   58 EDYTPPtlEQIDEFLDIVEEANAKN------EAVLVHCLAGKGRTGTML---ACyLVKTGKisAVDA-INEI----RRIR 123

                         90
                 ....*....|..
gi 333108235 279 MGLIQTPDQLRF 290
Cdd:cd14504  124 PGSIETSEQEKF 135
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 187-292 1.92e-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: 38.72  E-value: 1.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 187 LKSGETRTISHFHyTTWPDFGVPESPASFLNFLFKVRESG----SLNPDHgPAVIHCSAGIGRSGTFslvdTCLVLMEKG 262
Cdd:cd14497   48 LSEEEYDDDSKFE-GRVLHYGFPDHHPPPLGLLLEIVDDIdswlSEDPNN-VAVVHCKAGKGRTGTV----ICAYLLYYG 121

                         90       100       110
                 ....*....|....*....|....*....|....
gi 333108235 263 DDINIKQVL--LNMRKYRMGL--IQTPDQLRFSY 292
Cdd:cd14497  122 QYSTADEALeyFAKKRFKEGLpgVTIPSQLRYLQ 155
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 196-290 7.80e-03

protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase/transmembrane phosphatase with tensin homology; Voltage-sensitive phosphatase (VSP) proteins comprise a family of phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. This family is conserved in deuterostomes; VSP was first identified as a sperm flagellar plasma membrane protein in Ciona intestinalis. Gene duplication events in primates resulted in the presence of paralogs, transmembrane phosphatase with tensin homology (TPTE) and TPTE2, that retain protein domain architecture but, in the case of TPTE, have lost catalytic activity. TPTE, also called cancer/testis antigen 44 (CT44), may play a role in the signal transduction pathways of the endocrine or spermatogenic function of the testis. TPTE2, also called TPTE and PTEN homologous inositol lipid phosphatase (TPIP), occurs in several differentially spliced forms; TPIP alpha displays phosphoinositide 3-phosphatase activity and is localized on the endoplasmic reticulum, while TPIP beta is cytosolic and lacks detectable phosphatase activity. VSP/TPTE proteins contain an N-terminal voltage sensor consisting of four transmembrane segments, a protein tyrosine phosphatase (PTP)-like phosphoinositide phosphatase catalytic domain, followed by a regulatory C2 domain.


Pssm-ID: 350360 [Multi-domain]  Cd Length: 177  Bit Score: 36.96  E-value: 7.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333108235 196 SHFHYTT----WPDFGVPESPaSFLNFLFKVRESGSLNPDHGPAvIHCSAGIGRSGTFslvdTCLVLMEKGDDINIKQVL 271
Cdd:cd14510   70 KYFHNRVervpIDDHNVPTLD-EMLSFTAEVREWMAADPKNVVA-IHCKGGKGRTGTM----VCAWLIYSGQFESAKEAL 143

                         90       100
                 ....*....|....*....|....*..
gi 333108235 272 --LNMRKYRMGL------IQTPDQLRF 290
Cdd:cd14510  144 eyFGERRTDKSVsskfqgVETPSQSRY 170
 
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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