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Conserved domains on  [gi|315113878|ref|NP_001186692|]
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receptor-type tyrosine-protein phosphatase-like N isoform 2 precursor [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 664-944 0e+00

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: 659.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 664 HMILAYMEDHLRNRDRLAKEWQALCAYQAEPNTCATAQGEGNIKKNRHPDFLPYDHARIKLKVESSPSRSDYINASPIIE 743
Cdd:cd14609    1 HMILAYMEDHLRNRDRLAKEWQALCAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 744 HDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGASLYHVYEVNLVSEHIWCEDFLVR 823
Cdd:cd14609   81 HDPRMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHIYEVNLVSEHIWCEDFLVR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 824 SFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKG 903
Cdd:cd14609  161 SFYLKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKG 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 315113878 904 VKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAEEVNAI 944
Cdd:cd14609  241 VKEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAEEVNAI 281
RESP18 super family cl20829
RESP18 domain; This domain is found in the glucocorticoid-responsive protein regulated ...
 60-160 2.57e-28

RESP18 domain; This domain is found in the glucocorticoid-responsive protein regulated endocrine-specific protein 18 (RESP18) and in the N-terminal extracellular region of receptor-type tyrosine-protein phosphatases containing the protein-tyrosine phosphatase receptor IA-2 domain (pfam11548).


The actual alignment was detected with superfamily member pfam14948:

Pssm-ID: 464394  Cd Length: 103  Bit Score: 109.53  E-value: 2.57e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878   60 GQCQVGVGQARPLLQVTSPVLQRLQGVLRQLMSQGLSWHDDLTQYVISQEMERIPRLRPPEPRPRDRSGLAPKRPGPAG- 138
Cdd:pfam14948   1 GQGQVGVGQLWPLQGFTAPVFQHLQVVLHQIVPQGLFWKDDLTQDVMTQKMEHISRLHPQDPCLKDGKAVFPTRTTGVRg 80

                          90       100
                  ....*....|....*....|....
gi 315113878  139 --ELLLQDIPTGSaPAAQHRLPQP 160
Cdd:pfam14948  81 kqEEKLRLLFPKS-PAVKVNRDQC 103
Receptor_IA-2 super family cl13063
Protein-tyrosine phosphatase receptor IA-2; IA-2 is a protein-tyrosine phosphatase receptor ...
 469-528 5.31e-22

Protein-tyrosine phosphatase receptor IA-2; IA-2 is a protein-tyrosine phosphatase receptor that upon exocytosis, the cytoplasmic domain is cleaved and moves to the nucleus where it enhances transcription of the insulin gene. The mature exodomain of IA-2 participates in adhesion to the extracellular matrix and is self-proteolyzed in vitro by reactive oxygen species which may be a new shedding mechanism.


The actual alignment was detected with superfamily member pfam11548:

Pssm-ID: 463293  Cd Length: 89  Bit Score: 91.14  E-value: 5.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878  469 EEYGYIVTDQ-----------------------------NVVGPALTFRIRHNEQNLSLADVTQQAGLVKSELEAQTGLQ 519
Cdd:pfam11548   1 EEYGYIVTDNdplsweeglrlmekvaellhlpmssfadiRVLGPAVTFKVRANNKNLTAADVAKAAVDIKDKLEKETGLK 80


                  ....*....
gi 315113878  520 ILQTGVGQR 528
Cdd:pfam11548  81 ILQAGVGDK 89
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 234-479 4.94e-05

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.63  E-value: 4.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878  234 PLPKAEAPALFSRTASKGIFGDHPGHSYGDLPGPSPAQLFQDSGLLYLAQEL-----PAPSRARVPRLPEQGSSSRAEDS 308
Cdd:PHA03247 2710 PAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPttagpPAPAPPAAPAAGPPRRLTRPAVA 2789

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878  309 PEGYEKEGLgdrgEKPASPAVQPDAALQRLAAVLAGYGVELRQLTPEQLSTLLTLLQLLPKGAGRNPGGVVNVGadikkt 388
Cdd:PHA03247 2790 SLSESRESL----PSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPG------ 2859

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878  389 meGPVEGRDTAELPARTSPMPGHPTAS---------PTSSEVQQVPSPVSSEPPKAARPPVTPVLLEKKS-------PLG 452
Cdd:PHA03247 2860 --GDVRRRPPSRSPAAKPAAPARPPVRrlarpavsrSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPqpqppppPPP 2937

                         250       260
                  ....*....|....*....|....*..
gi 315113878  453 QSQPTVAGQPSARPAAEEYGYIVTDQN 479
Cdd:PHA03247 2938 RPQPPLAPTTDPAGAGEPSGAVPQPWL 2964
 
Name Accession Description Interval E-value
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 664-944 0e+00

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: 659.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 664 HMILAYMEDHLRNRDRLAKEWQALCAYQAEPNTCATAQGEGNIKKNRHPDFLPYDHARIKLKVESSPSRSDYINASPIIE 743
Cdd:cd14609    1 HMILAYMEDHLRNRDRLAKEWQALCAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 744 HDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGASLYHVYEVNLVSEHIWCEDFLVR 823
Cdd:cd14609   81 HDPRMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHIYEVNLVSEHIWCEDFLVR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 824 SFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKG 903
Cdd:cd14609  161 SFYLKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKG 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 315113878 904 VKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAEEVNAI 944
Cdd:cd14609  241 VKEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAEEVNAI 281
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
680-939 1.08e-103

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 323.07  E-value: 1.08e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878   680 LAKEWQALCAYQAEPNTCATAQGEGNIKKNRHPDFLPYDHARIKLKVESSPSrSDYINASPI-IEHDPRmpAYIATQGPL 758
Cdd:smart00194   2 LEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEG-SDYINASYIdGPNGPK--AYIATQGPL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878   759 SHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEG--ASLYHVYEVNLVSEHIwCEDFLVRSFYLKNVQTQETR 836
Cdd:smart00194  79 PSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEgePLTYGDITVTLKSVEK-VDDYTIRTLEVTNTGCSETR 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878   837 TLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGvKEIDIAATLEHV 916
Cdd:smart00194 158 TVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAG-KEVDIFEIVKEL 236

                          250       260
                   ....*....|....*....|...
gi 315113878   917 RDQRPGLVRSKDQFEFALTAVAE 939
Cdd:smart00194 237 RSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
705-939 6.45e-102

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 317.65  E-value: 6.45e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878  705 NIKKNRHPDFLPYDHARIKLKveSSPSRSDYINASPIIEHdPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLV 784
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGY-KKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878  785 EDGVKQCDRYWPDE-GASL-YHVYEVNLVSEHIWCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFR 862
Cdd:pfam00102  78 EKGREKCAQYWPEEeGESLeYGDFTVTLKKEKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 315113878  863 RKVNKCY-RGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGvKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAE 939
Cdd:pfam00102 158 RKVRKSSlDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAE-GEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 705-932 9.54e-39

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 146.69  E-value: 9.54e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 705 NIKKNRHPDFLPYDHARIKLKVESSpSRSDYINASPI--IEHDPRmpaYIATQGPLSHTIADFWQMVWESGCTVIVMLTP 782
Cdd:PHA02747  51 NQPKNRYWDIPCWDHNRVILDSGGG-STSDYIHANWIdgFEDDKK---FIATQGPFAETCADFWKAVWQEHCSIIVMLTP 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 783 L-VEDGVKQCDRYW-PDEGASL----YHVYEVNLVsehiwcedflVRSFYLK------NVQTQETRTLTQFHFLSWPAEG 850
Cdd:PHA02747 127 TkGTNGEEKCYQYWcLNEDGNIdmedFRIETLKTS----------VRAKYILtlieitDKILKDSRKISHFQCSEWFEDE 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 851 TPASTRPLLDF-------RRKVNKCYRGRS---CPIIVHCSDGAGRTGTYILIDMVLNRMAKgVKEIDIAATLEHVRDQR 920
Cdd:PHA02747 197 TPSDHPDFIKFikiidinRKKSGKLFNPKDallCPIVVHCSDGVGKTGIFCAVDICLNQLVK-RKAICLAKTAEKIREQR 275

                        250
                 ....*....|..
gi 315113878 921 PGLVRSKDQFEF 932
Cdd:PHA02747 276 HAGIMNFDDYLF 287
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
663-945 8.16e-33

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 128.67  E-value: 8.16e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 663 GHMILAYMEDHLRNRdrLAKEWQALcAYQAEPNtcataQGEGNI---KKNRHPDFLPYDHARIklkvesspsRSD--YIN 737
Cdd:COG5599    5 NPIAIKSEEEKINSR--LSTLTNEL-APSHNDP-----QYLQNIngsPLNRFRDIQPYKETAL---------RANlgYLN 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 738 ASPIIEHDPRMpaYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGV--KQCDRYWPDEG-ASLYHVyEVNLVSEH 814
Cdd:COG5599   68 ANYIQVIGNHR--YIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISKpkVKMPVYFRQDGeYGKYEV-SSELTESI 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 815 IWCEDFLVRSFYLKNVQT-QETRTLTQFHFLSWPAEGTPAST--RPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYI 891
Cdd:COG5599  145 QLRDGIEARTYVLTIKGTgQKKIEIPVLHVKNWPDHGAISAEalKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLI 224

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 315113878 892 LIdMVLNRMAKGVKEIDIAA--TLEHVRDQR-PGLVRSKDQFEFaLTAVAEEVNAIL 945
Cdd:COG5599  225 AC-LALSKSINALVQITLSVeeIVIDMRTSRnGGMVQTSEQLDV-LVKLAEQQIRPL 279
RESP18 pfam14948
RESP18 domain; This domain is found in the glucocorticoid-responsive protein regulated ...
 60-160 2.57e-28

RESP18 domain; This domain is found in the glucocorticoid-responsive protein regulated endocrine-specific protein 18 (RESP18) and in the N-terminal extracellular region of receptor-type tyrosine-protein phosphatases containing the protein-tyrosine phosphatase receptor IA-2 domain (pfam11548).


Pssm-ID: 464394  Cd Length: 103  Bit Score: 109.53  E-value: 2.57e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878   60 GQCQVGVGQARPLLQVTSPVLQRLQGVLRQLMSQGLSWHDDLTQYVISQEMERIPRLRPPEPRPRDRSGLAPKRPGPAG- 138
Cdd:pfam14948   1 GQGQVGVGQLWPLQGFTAPVFQHLQVVLHQIVPQGLFWKDDLTQDVMTQKMEHISRLHPQDPCLKDGKAVFPTRTTGVRg 80

                          90       100
                  ....*....|....*....|....
gi 315113878  139 --ELLLQDIPTGSaPAAQHRLPQP 160
Cdd:pfam14948  81 kqEEKLRLLFPKS-PAVKVNRDQC 103
Receptor_IA-2 pfam11548
Protein-tyrosine phosphatase receptor IA-2; IA-2 is a protein-tyrosine phosphatase receptor ...
 469-528 5.31e-22

Protein-tyrosine phosphatase receptor IA-2; IA-2 is a protein-tyrosine phosphatase receptor that upon exocytosis, the cytoplasmic domain is cleaved and moves to the nucleus where it enhances transcription of the insulin gene. The mature exodomain of IA-2 participates in adhesion to the extracellular matrix and is self-proteolyzed in vitro by reactive oxygen species which may be a new shedding mechanism.


Pssm-ID: 463293  Cd Length: 89  Bit Score: 91.14  E-value: 5.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878  469 EEYGYIVTDQ-----------------------------NVVGPALTFRIRHNEQNLSLADVTQQAGLVKSELEAQTGLQ 519
Cdd:pfam11548   1 EEYGYIVTDNdplsweeglrlmekvaellhlpmssfadiRVLGPAVTFKVRANNKNLTAADVAKAAVDIKDKLEKETGLK 80


                  ....*....
gi 315113878  520 ILQTGVGQR 528
Cdd:pfam11548  81 ILQAGVGDK 89
PHA03247 PHA03247
large tegument protein UL36; Provisional
 234-479 4.94e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.63  E-value: 4.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878  234 PLPKAEAPALFSRTASKGIFGDHPGHSYGDLPGPSPAQLFQDSGLLYLAQEL-----PAPSRARVPRLPEQGSSSRAEDS 308
Cdd:PHA03247 2710 PAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPttagpPAPAPPAAPAAGPPRRLTRPAVA 2789

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878  309 PEGYEKEGLgdrgEKPASPAVQPDAALQRLAAVLAGYGVELRQLTPEQLSTLLTLLQLLPKGAGRNPGGVVNVGadikkt 388
Cdd:PHA03247 2790 SLSESRESL----PSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPG------ 2859

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878  389 meGPVEGRDTAELPARTSPMPGHPTAS---------PTSSEVQQVPSPVSSEPPKAARPPVTPVLLEKKS-------PLG 452
Cdd:PHA03247 2860 --GDVRRRPPSRSPAAKPAAPARPPVRrlarpavsrSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPqpqppppPPP 2937

                         250       260
                  ....*....|....*....|....*..
gi 315113878  453 QSQPTVAGQPSARPAAEEYGYIVTDQN 479
Cdd:PHA03247 2938 RPQPPLAPTTDPAGAGEPSGAVPQPWL 2964
 
Name Accession Description Interval E-value
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 664-944 0e+00

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: 659.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 664 HMILAYMEDHLRNRDRLAKEWQALCAYQAEPNTCATAQGEGNIKKNRHPDFLPYDHARIKLKVESSPSRSDYINASPIIE 743
Cdd:cd14609    1 HMILAYMEDHLRNRDRLAKEWQALCAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 744 HDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGASLYHVYEVNLVSEHIWCEDFLVR 823
Cdd:cd14609   81 HDPRMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHIYEVNLVSEHIWCEDFLVR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 824 SFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKG 903
Cdd:cd14609  161 SFYLKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKG 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 315113878 904 VKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAEEVNAI 944
Cdd:cd14609  241 VKEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAEEVNAI 281
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 662-944 0e+00

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: 565.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 662 TGHMILAYMEDHLRNRDRLAKEWQALCAYQAEPNTCATAQGEGNIKKNRHPDFLPYDHARIKLKVESSPSRSDYINASPI 741
Cdd:cd14610    1 TGHMILSYMEDHLKNKNRLEKEWEALCAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 742 IEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGASLYHVYEVNLVSEHIWCEDFL 821
Cdd:cd14610   81 MDHDPRNPAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYHIYEVNLVSEHIWCEDFL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 822 VRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMA 901
Cdd:cd14610  161 VRSFYLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMA 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 315113878 902 KGVKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAEEVNAI 944
Cdd:cd14610  241 KGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEVNAI 283
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 735-942 4.68e-158

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: 462.68  E-value: 4.68e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 735 YINASPIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGASLYHVYEVNLVSEH 814
Cdd:cd14546    1 YINASTIYDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVYHIYEVHLVSEH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 815 IWCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILID 894
Cdd:cd14546   81 IWCDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRTGTYILID 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 315113878 895 MVLNRMAKGVKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAEEVN 942
Cdd:cd14546  161 MVLNRMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAEEVN 208
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
680-939 1.08e-103

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 323.07  E-value: 1.08e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878   680 LAKEWQALCAYQAEPNTCATAQGEGNIKKNRHPDFLPYDHARIKLKVESSPSrSDYINASPI-IEHDPRmpAYIATQGPL 758
Cdd:smart00194   2 LEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEG-SDYINASYIdGPNGPK--AYIATQGPL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878   759 SHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEG--ASLYHVYEVNLVSEHIwCEDFLVRSFYLKNVQTQETR 836
Cdd:smart00194  79 PSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEgePLTYGDITVTLKSVEK-VDDYTIRTLEVTNTGCSETR 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878   837 TLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGvKEIDIAATLEHV 916
Cdd:smart00194 158 TVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAG-KEVDIFEIVKEL 236

                          250       260
                   ....*....|....*....|...
gi 315113878   917 RDQRPGLVRSKDQFEFALTAVAE 939
Cdd:smart00194 237 RSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
705-939 6.45e-102

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 317.65  E-value: 6.45e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878  705 NIKKNRHPDFLPYDHARIKLKveSSPSRSDYINASPIIEHdPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLV 784
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGY-KKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878  785 EDGVKQCDRYWPDE-GASL-YHVYEVNLVSEHIWCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFR 862
Cdd:pfam00102  78 EKGREKCAQYWPEEeGESLeYGDFTVTLKKEKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 315113878  863 RKVNKCY-RGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGvKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAE 939
Cdd:pfam00102 158 RKVRKSSlDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAE-GEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 735-932 6.51e-82

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: 262.99  E-value: 6.51e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 735 YINASPIIEHDPRmPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGAS--LYHVYEVNLVS 812
Cdd:cd00047    1 YINASYIDGYRGP-KEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKplEYGDITVTLVS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 813 EHIwCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYIL 892
Cdd:cd00047   80 EEE-LSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTFIA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 315113878 893 IDMVLNRMAKGvKEIDIAATLEHVRDQRPGLVRSKDQFEF 932
Cdd:cd00047  159 IDILLERLEAE-GEVDVFEIVKALRKQRPGMVQTLEQYEF 197
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 703-943 1.21e-66

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: 223.04  E-value: 1.21e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 703 EGNIKKNRHPDFLPYDHARIKLK-VESSPSrSDYINASPIIEHDpRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLT 781
Cdd:cd14553    1 EVNKPKNRYANVIAYDHSRVILQpIEGVPG-SDYINANYCDGYR-KQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 782 PLVEDGVKQCDRYWPDEGASLYHVYEVNLVsEHIWCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDF 861
Cdd:cd14553   79 KLEERSRVKCDQYWPTRGTETYGLIQVTLL-DTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAF 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 862 RRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAEEV 941
Cdd:cd14553  158 LRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERI-KHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLEAV 236


                 ..
gi 315113878 942 NA 943
Cdd:cd14553  237 TC 238
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 705-938 6.21e-66

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: 221.57  E-value: 6.21e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 705 NIKKNRHPDFLPYDHARIKLK-VESSPSRSDYINASPII------EHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVI 777
Cdd:cd14544    1 NKGKNRYKNILPFDHTRVILKdRDPNVPGSDYINANYIRnenegpTTDENAKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 778 VMLTPLVEDGVKQCDRYWPDEGAS-LYHVYEVNLVSEHIwCEDFLVRSFYLKNV-QTQETRTLTQFHFLSWPAEGTPAST 855
Cdd:cd14544   81 VMTTKEVERGKNKCVRYWPDEGMQkQYGPYRVQNVSEHD-TTDYTLRELQVSKLdQGDPIREIWHYQYLSWPDHGVPSDP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 856 RPLLDFRRKVNKCYRGR--SCPIIVHCSDGAGRTGTYILIDMVLNRMAK-GVK-EIDIAATLEHVRDQRPGLVRSKDQFE 931
Cdd:cd14544  160 GGVLNFLEDVNQRQESLphAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRkGLDcDIDIQKTIQMVRSQRSGMVQTEAQYK 239


                 ....*..
gi 315113878 932 FALTAVA 938
Cdd:cd14544  240 FIYVAVA 246
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 677-932 6.74e-66

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: 222.24  E-value: 6.74e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 677 RDRLAKEWQALCAyQAEPNTCATAQGEGNIKKNRHPDFLPYDHARIKLKVESSPSRSDYINASpIIEHDPRMPAYIATQG 756
Cdd:cd14543    2 KRGIYEEYEDIRR-EPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINAN-FMDGYKQKNAYIATQG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 757 PLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGASLYHVYEVNLVSEHIWC-EDFLVRSFYLKNVQTQET 835
Cdd:cd14543   80 PLPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENkEHYKKTTLEIHNTETDES 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 836 RTLTQFHFLSWPAEGTPASTRPLLDFRRKVnKCYRGRSC--------------PIIVHCSDGAGRTGTYILIDMVLNRMA 901
Cdd:cd14543  160 RQVTHFQFTSWPDFGVPSSAAALLDFLGEV-RQQQALAVkamgdrwkghppgpPIVVHCSAGIGRTGTFCTLDICLSQLE 238

                        250       260       270
                 ....*....|....*....|....*....|.
gi 315113878 902 KgVKEIDIAATLEHVRDQRPGLVRSKDQFEF 932
Cdd:cd14543  239 D-VGTLNVMQTVRRMRTQRAFSIQTPDQYYF 268
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 710-932 1.97e-62

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: 210.67  E-value: 1.97e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 710 RHPDFLPYDHARIKLKVESSPSRSDYINASPII-EHDPRmpAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGV 788
Cdd:cd14548    1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPgYNSPR--EFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 789 KQCDRYWPDEGASLYHVY-EVNLVSEHIwCEDFLVRSFYLKNVqtQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVnK 867
Cdd:cd14548   79 VKCDHYWPFDQDPVYYGDiTVTMLSESV-LPDWTIREFKLERG--DEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLV-R 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 315113878 868 CYRGRSC-PIIVHCSDGAGRTGTYILIDMVLNRMAKGvKEIDIAATLEHVRDQRPGLVRSKDQFEF 932
Cdd:cd14548  155 DYIKQEKgPTIVHCSAGVGRTGTFIALDRLLQQIESE-DYVDIFGIVYDLRKHRPLMVQTEAQYIF 219
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 705-936 2.29e-62

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: 211.23  E-value: 2.29e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 705 NIKKNRHPDFLPYDHARIKLKVESSPSRSDYINASPIIEHDPRmPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLV 784
Cdd:cd14554    6 NKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQR-GAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 785 EDGVKQCDRYWPDEGASLYHVYEVNLVSEHIWcEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRK 864
Cdd:cd14554   85 EMGREKCHQYWPAERSARYQYFVVDPMAEYNM-PQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQ 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 315113878 865 VNKCYR--GRSCPIIVHCSDGAGRTGTYILIDMVLNRM-AKGVkeIDIAATLEHVRDQRPGLVRSKDQFEFALTA 936
Cdd:cd14554  164 VHKTKEqfGQEGPITVHCSAGVGRTGVFITLSIVLERMrYEGV--VDVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 735-932 3.54e-62

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: 209.51  E-value: 3.54e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 735 YINASPIIE-HDPRmpAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGASLYHVYEVNLVSE 813
Cdd:cd14549    1 YINANYVDGyNKAR--AYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGNIQVTLLST 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 814 HIWCEdFLVRSFYLKNVQ------TQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRT 887
Cdd:cd14549   79 EVLAT-YTVRTFSLKNLKlkkvkgRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRT 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 315113878 888 GTYILIDMVLNRMAKgVKEIDIAATLEHVRDQRPGLVRSKDQFEF 932
Cdd:cd14549  158 GTYIVIDSMLQQIQD-KGTVNVFGFLKHIRTQRNYLVQTEEQYIF 201
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 735-932 9.22e-62

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: 208.64  E-value: 9.22e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 735 YINASPI-IEHDPRMpAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGA-SLYHVYEVNLVS 812
Cdd:cd18533    1 YINASYItLPGTSSK-RYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYeGEYGDLTVELVS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 813 EH-IWCEDFLVRSFYLKnVQTQETRTLTQFHFLSWPAEGTPASTRPLL---DFRRKVNKCYRGRScPIIVHCSDGAGRTG 888
Cdd:cd18533   80 EEeNDDGGFIVREFELS-KEDGKVKKVYHIQYKSWPDFGVPDSPEDLLtliKLKRELNDSASLDP-PIIVHCSAGVGRTG 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 315113878 889 TYILIDMVLNRMAKGV-------KEID-IAATLEHVRDQRPGLVRSKDQFEF 932
Cdd:cd18533  158 TFIALDSLLDELKRGLsdsqdleDSEDpVYEIVNQLRKQRMSMVQTLRQYIF 209
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 709-932 3.13e-60

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: 205.05  E-value: 3.13e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 709 NRHPDFLPYDHARIKLKVESSPSrSDYINASpiiehdpRMPAY------IATQGPLSHTIADFWQMVWESGCTVIVMLTP 782
Cdd:cd14615    1 NRYNNVLPYDISRVKLSVQSHST-DDYINAN-------YMPGYnskkefIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTK 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 783 LVEDGVKQCDRYWPDEGASLYHVYEVNLVSEhIWCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFR 862
Cdd:cd14615   73 CVEQGRTKCEEYWPSKQKKDYGDITVTMTSE-IVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFR 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 315113878 863 RKVNKCYRG--RSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGvKEIDIAATLEHVRDQRPGLVRSKDQFEF 932
Cdd:cd14615  152 HLVREYMKQnpPNSPILVHCSAGVGRTGTFIAIDRLIYQIENE-NVVDVYGIVYDLRMHRPLMVQTEDQYVF 222
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 734-947 5.57e-58

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: 197.94  E-value: 5.57e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 734 DYINASPIIEHDPRMPA---YIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGASLYH-VYEVN 809
Cdd:cd14541    1 DYINANYVNMEIPGSGIvnrYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGETMQFgNLQIT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 810 LVSEHIwCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGT 889
Cdd:cd14541   81 CVSEEV-TPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGIGRTGV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 890 YILID--MVLNRMAKGVKEIDIAATLehvRDQRPGLVRSKDQFEFaltaVAEevnAILKA 947
Cdd:cd14541  160 LITMEtaMCLIEANEPVYPLDIVRTM---RDQRAMLIQTPSQYRF----VCE---AILRV 209
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 708-932 3.38e-57

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: 196.46  E-value: 3.38e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 708 KNRHPDFLPYDHARIKLKVESSpsRSDYINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDG 787
Cdd:cd14545    1 LNRYRDRDPYDHDRSRVKLKQG--DNDYINAS-LVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 788 VKQCDRYWP---DEGASLYHV-YEVNLVSEHIWcEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRR 863
Cdd:cd14545   78 QIKCAQYWPqgeGNAMIFEDTgLKVTLLSEEDK-SYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQ 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 315113878 864 KVNK--CYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKG-VKEIDIAATLEHVRDQRPGLVRSKDQFEF 932
Cdd:cd14545  157 KVREsgSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGnPSSVDVKKVLLEMRKYRMGLIQTPDQLRF 228
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 669-939 5.27e-57

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: 198.62  E-value: 5.27e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 669 YMEDHLRNRdRLAKEWQALCAYQAepntcATAQGEGNIKKNRHPDFLPYDHARIKLKVESSPSRSDYINASPIIE-HDPR 747
Cdd:cd14604   27 FASDFMRLR-RLSTKYRTEKIYPT-----ATGEKEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGvYGPK 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 748 mpAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPdegasLYHVYEVNLVSEHIWCE------DFL 821
Cdd:cd14604  101 --AYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWP-----LYGEEPMTFGPFRISCEaeqartDYF 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 822 VRSFYLKNvqTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMA 901
Cdd:cd14604  174 IRTLLLEF--QNETRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLK 251

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 315113878 902 KGV--KEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAE 939
Cdd:cd14604  252 AGKipEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQ 291
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 735-939 1.68e-56

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: 193.74  E-value: 1.68e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 735 YINASPIiehdpRMPA------YIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPD---EGASLYHV 805
Cdd:cd14538    1 YINASHI-----RIPVggdtyhYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDslnKPLICGGR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 806 YEVNLVSEHIWcEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYrgRSCPIIVHCSDGAG 885
Cdd:cd14538   76 LEVSLEKYQSL-QDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIH--NSGPIVVHCSAGIG 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 315113878 886 RTGTYILIDMVLNRMAKGvKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAE 939
Cdd:cd14538  153 RTGVLITIDVALGLIERD-LPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLE 205
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 703-941 7.21e-56

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: 194.48  E-value: 7.21e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 703 EGNIKKNRHPDFLPYDHARIKL-KVESSPSrSDYINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLT 781
Cdd:cd14626   39 EVNKPKNRYANVIAYDHSRVILtSVDGVPG-SDYINAN-YIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMT 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 782 PLVEDGVKQCDRYWPDEGASLYHVYEVNLVsEHIWCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDF 861
Cdd:cd14626  117 RLEEKSRVKCDQYWPIRGTETYGMIQVTLL-DTVELATYSVRTFALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAF 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 862 RRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAEEV 941
Cdd:cd14626  196 LRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERM-KHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAA 274
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 705-941 1.77e-55

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: 193.33  E-value: 1.77e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 705 NIKKNRHPDFLPYDHARIKLK--VESSPSRSDYINASPIIEHDpRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTP 782
Cdd:cd17667   27 NKHKNRYINILAYDHSRVKLRplPGKDSKHSDYINANYVDGYN-KAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITN 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 783 LVEDGVKQCDRYWPDEGASLYHVYEVNLVSEHIW-CedFLVRSFYLKNVQT-----------QETRTLTQFHFLSWPAEG 850
Cdd:cd17667  106 LVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHaC--YTVRRFSIRNTKVkkgqkgnpkgrQNERTVIQYHYTQWPDMG 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 851 TPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLEHVRDQRPGLVRSKDQF 930
Cdd:cd17667  184 VPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQI-KDKSTVNVLGFLKHIRTQRNYLVQTEEQY 262

                        250
                 ....*....|.
gi 315113878 931 EFALTAVAEEV 941
Cdd:cd17667  263 IFIHDALLEAI 273
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 709-932 2.61e-55

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: 191.26  E-value: 2.61e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 709 NRHPDFLPYDHARIKLKVESSPSRSDYINASpiiehdpRMPAY------IATQGPLSHTIADFWQMVWESGCTVIVMLTP 782
Cdd:cd14619    1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINAN-------YMPGYwssqefIATQGPLPQTVGDFWRMIWEQQSSTIVMLTN 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 783 LVEDGVKQCDRYWP-DEGASLYHVYEVNLVSEHIwCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDF 861
Cdd:cd14619   74 CMEAGRVKCEHYWPlDYTPCTYGHLRVTVVSEEV-MENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAF 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 315113878 862 RRKVNKCYRGR--SCPIIVHCSDGAGRTGTYILIDMVLNRMAKGvKEIDIAATLEHVRDQRPGLVRSKDQFEF 932
Cdd:cd14619  153 RRLLRQWLDQTmsGGPTVVHCSAGVGRTGTLIALDVLLQQLQSE-GLLGPFSFVQKMRENRPLMVQTESQYVF 224
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 705-932 6.55e-55

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: 190.43  E-value: 6.55e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 705 NIKKNRHPDFLPYDHARIKLKVESspsrsDYINASPIiehdpRMPA------YIATQGPLSHTIADFWQMVWESGCTVIV 778
Cdd:cd14597    3 NRKKNRYKNILPYDTTRVPLGDEG-----GYINASFI-----KMPVgdeefvYIACQGPLPTTVADFWQMVWEQKSTVIA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 779 MLTPLVEDGVKQCDRYWPDEGASLYHVYE---VNLVS-EHIwcEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPAS 854
Cdd:cd14597   73 MMTQEVEGGKIKCQRYWPEILGKTTMVDNrlqLTLVRmQQL--KNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQ 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 315113878 855 TRPLLDFRRKVNKCYrgRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGVkEIDIAATLEHVRDQRPGLVRSKDQFEF 932
Cdd:cd14597  151 PEQLLTFISYMRHIH--KSGPIITHCSAGIGRSGTLICIDVVLGLISKDL-DFDISDIVRTMRLQRHGMVQTEDQYIF 225
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 683-939 9.30e-55

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: 191.19  E-value: 9.30e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 683 EWQALCAYQAEPNTCATAQG--EGNIKKNRHPDFLPYDHARIKLKVESSPSRSDYINASPIIEHDpRMPAYIATQGPLSH 760
Cdd:cd14603    6 EIRACSAAFKADYVCSTVAGgrKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVD-GSRAYIATQGPLSH 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 761 TIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGASL-YHVYEVNLVSEHIWCEDFLVRSfyLKNVQTQETRTLT 839
Cdd:cd14603   85 TVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAQEQEPLqTGPFTITLVKEKRLNEEVILRT--LKVTFQKESRSVS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 840 QFHFLSWPAEGTPASTRPLLDFRRKVNKcYRGRS-CPIIVHCSDGAGRTGTYILIDMVLNRMAKGVKEIDIA---ATLEh 915
Cdd:cd14603  163 HFQYMAWPDHGIPDSPDCMLAMIELARR-LQGSGpEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSifdVVLE- 240

                        250       260
                 ....*....|....*....|....
gi 315113878 916 VRDQRPGLVRSKDQFEFALTAVAE 939
Cdd:cd14603  241 MRKQRPAAVQTEEQYEFLYHTVAQ 264
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 683-939 1.94e-54

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: 191.10  E-value: 1.94e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 683 EWQALCAYQAEPNTCATAQGEGNIKKNRHPDFLPYDHARIKLKVESSPSRSDYINASpIIEHDPRMPAYIATQGPLSHTI 762
Cdd:cd14628   30 EFKRLASSKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINAS-FIDGYRQQKAYIATQGPLAETT 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 763 ADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGASLYHVYEVNLVSEHIWCEdFLVRSFYLKNVQTQETRTLTQFH 842
Cdd:cd14628  109 EDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQ-YILREFKVTDARDGQSRTVRQFQ 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 843 FLSWPAEGTPASTRPLLDFRRKVNKCYR--GRSCPIIVHCSDGAGRTGTYILIDMVLNRMA-KGVkeIDIAATLEHVRDQ 919
Cdd:cd14628  188 FTDWPEQGVPKSGEGFIDFIGQVHKTKEqfGQDGPISVHCSAGVGRTGVFITLSIVLERMRyEGV--VDIFQTVKMLRTQ 265

                        250       260
                 ....*....|....*....|
gi 315113878 920 RPGLVRSKDQFEFALTAVAE 939
Cdd:cd14628  266 RPAMVQTEDQYQFCYRAALE 285
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 709-932 2.59e-54

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: 188.37  E-value: 2.59e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 709 NRHPDFLPYDHARIKLKVESSPSRSDYINASPIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGV 788
Cdd:cd14547    1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 789 KqCDRYWPDEGASLYHVYEVnLVSEHIWCEDFLVRSFYLKNVqtQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKC 868
Cdd:cd14547   81 K-CAQYWPEEENETYGDFEV-TVQSVKETDGYTVRKLTLKYG--GEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEEA 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 315113878 869 -YRGRSC-PIIVHCSDGAGRTGTYILIDMVLNRMAKGVKeIDIAATLEHVRDQRPGLVRSKDQFEF 932
Cdd:cd14547  157 rQTEPHRgPIVVHCSAGIGRTGCFIATSIGCQQLREEGV-VDVLGIVCQLRLDRGGMVQTAEQYEF 221
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 667-941 3.28e-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: 190.30  E-value: 3.28e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 667 LAYMEDHLRNRD--RLAKEWQALCAYQAepNTCATAQGEGNIKKNRHPDFLPYDHARIKLKVESSPSRSDYINASpIIEH 744
Cdd:cd14625    9 LAEHTERLKANDnlKLSQEYESIDPGQQ--FTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINAN-YIDG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 745 DPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGASLYHVYEVNLVsEHIWCEDFLVRS 824
Cdd:cd14625   86 YRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTETYGMIQVTLL-DTIELATFCVRT 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 825 FYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMaKGV 904
Cdd:cd14625  165 FSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERI-KHE 243

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 315113878 905 KEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAEEV 941
Cdd:cd14625  244 KTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAV 280
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 705-937 6.71e-54

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: 188.30  E-value: 6.71e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 705 NIKKNRHPDFLPYDHARIKLKvESSPSR--SDYINASPI-----IEHDPRMP--AYIATQGPLSHTIADFWQMVWESGCT 775
Cdd:cd14605    2 NKNKNRYKNILPFDHTRVVLH-DGDPNEpvSDYINANIImpefeTKCNNSKPkkSYIATQGCLQNTVNDFWRMVFQENSR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 776 VIVMLTPLVEDGVKQCDRYWPDEGA-SLYHVYEVNLVSEHIwCEDFLVRSFYLKNV-QTQETRTLTQFHFLSWPAEGTPA 853
Cdd:cd14605   81 VIVMTTKEVERGKSKCVKYWPDEYAlKEYGVMRVRNVKESA-AHDYILRELKLSKVgQGNTERTVWQYHFRTWPDHGVPS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 854 STRPLLDFRRKVNKCYRG--RSCPIIVHCSDGAGRTGTYILIDMVLNRM-AKGVK-EIDIAATLEHVRDQRPGLVRSKDQ 929
Cdd:cd14605  160 DPGGVLDFLEEVHHKQESimDAGPVVVHCSAGIGRTGTFIVIDILIDIIrEKGVDcDIDVPKTIQMVRSQRSGMVQTEAQ 239


                 ....*...
gi 315113878 930 FEFALTAV 937
Cdd:cd14605  240 YRFIYMAV 247
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 705-939 1.78e-53

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: 186.38  E-value: 1.78e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 705 NIKKNRHPDFLPYDHARIKLKVESSPSRSDYINASPII-EHDPRMpaYIATQGPLSHTIADFWQMVWESGCTVIVMLTPL 783
Cdd:cd14630    3 NRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDgYHRPRH--YIATQGPMQETVKDFWRMIWQENSASVVMVTNL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 784 VEDGVKQCDRYWPDEgASLYHVYEVNLVSEHIWCEdFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRR 863
Cdd:cd14630   81 VEVGRVKCVRYWPDD-TEVYGDIKVTLIETEPLAE-YVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVR 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 315113878 864 KVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNrMAKGVKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAE 939
Cdd:cd14630  159 QVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLD-MAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 683-939 3.54e-53

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: 187.63  E-value: 3.54e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 683 EWQALCAYQAEPNTCATAQGEGNIKKNRHPDFLPYDHARIKLKVESSPSRSDYINASpIIEHDPRMPAYIATQGPLSHTI 762
Cdd:cd14627   31 EFKRLANSKAHTSRFISANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINAS-FIDGYRQQKAYIATQGPLAETT 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 763 ADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGASLYHVYEVNLVSEHIWCEdFLVRSFYLKNVQTQETRTLTQFH 842
Cdd:cd14627  110 EDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQ-YILREFKVTDARDGQSRTVRQFQ 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 843 FLSWPAEGTPASTRPLLDFRRKVNKCYR--GRSCPIIVHCSDGAGRTGTYILIDMVLNRMA-KGVkeIDIAATLEHVRDQ 919
Cdd:cd14627  189 FTDWPEQGVPKSGEGFIDFIGQVHKTKEqfGQDGPISVHCSAGVGRTGVFITLSIVLERMRyEGV--VDIFQTVKMLRTQ 266

                        250       260
                 ....*....|....*....|
gi 315113878 920 RPGLVRSKDQFEFALTAVAE 939
Cdd:cd14627  267 RPAMVQTEDEYQFCYQAALE 286
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 708-939 5.48e-53

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: 185.04  E-value: 5.48e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 708 KNRHPDFLPYDHARIKLKVESSPSRSDYINASPIIE-HDPRmpAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVED 786
Cdd:cd14602    1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGvYGPR--AYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEM 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 787 GVKQCDRYWPDEGASLYHVYEVNLVsehiwCE------DFLVRSfyLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLD 860
Cdd:cd14602   79 GKKKCERYWAEPGEMQLEFGPFSVT-----CEaekrksDYIIRT--LKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILE 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 861 FRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGV--KEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVA 938
Cdd:cd14602  152 LIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIipENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVI 231


                 .
gi 315113878 939 E 939
Cdd:cd14602  232 E 232
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 735-932 2.91e-52

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: 181.47  E-value: 2.91e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 735 YINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGASL--YHVYEVNLVS 812
Cdd:cd14542    1 YINAN-FIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQlqFGPFKISLEK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 813 EHIWCEDFLVRSfyLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYIL 892
Cdd:cd14542   80 EKRVGPDFLIRT--LKVTFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRTGTICA 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 315113878 893 IDMVLNRMAKGV--KEIDIAATLEHVRDQRPGLVRSKDQFEF 932
Cdd:cd14542  158 IDYVWNLLKTGKipEEFSLFDLVREMRKQRPAMVQTKEQYEL 199
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 705-939 4.21e-52

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: 183.54  E-value: 4.21e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 705 NIKKNRHPDFLPYDHARIKLK-VESSPSRSDYINASPIIEH--DPRMPA--YIATQGPLSHTIADFWQMVWESGCTVIVM 779
Cdd:cd14606   18 NKSKNRYKNILPFDHSRVILQgRDSNIPGSDYINANYVKNQllGPDENAktYIASQGCLEATVNDFWQMAWQENSRVIVM 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 780 LTPLVEDGVKQCDRYWPD-EGASLYHVYEVNLVSEHIwCEDFLVRSFYLKNVQTQET-RTLTQFHFLSWPAEGTPASTRP 857
Cdd:cd14606   98 TTREVEKGRNKCVPYWPEvGMQRAYGPYSVTNCGEHD-TTEYKLRTLQVSPLDNGELiREIWHYQYLSWPDHGVPSEPGG 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 858 LLDFRRKVNKCYRG--RSCPIIVHCSDGAGRTGTYILIDMVLNRM-AKGVK-EIDIAATLEHVRDQRPGLVRSKDQFEFA 933
Cdd:cd14606  177 VLSFLDQINQRQESlpHAGPIIVHCSAGIGRTGTIIVIDMLMENIsTKGLDcDIDIQKTIQMVRAQRSGMVQTEAQYKFI 256


                 ....*.
gi 315113878 934 LTAVAE 939
Cdd:cd14606  257 YVAIAQ 262
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 690-945 8.13e-52

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: 183.30  E-value: 8.13e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 690 YQAEPNTCATAQGEGNIKKNRHPDFLPYDHARIKLKVESSpsrsDYINASpIIEHDPRMPAYIATQGPLSHTIADFWQMV 769
Cdd:cd14608   10 HEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDN----DYINAS-LIKMEEAQRSYILTQGPLPNTCGHFWEMV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 770 WESGCTVIVMLTPLVEDGVKQCDRYWP--DEGASLYH--VYEVNLVSEHIWCEdFLVRSFYLKNVQTQETRTLTQFHFLS 845
Cdd:cd14608   85 WEQKSRGVVMLNRVMEKGSLKCAQYWPqkEEKEMIFEdtNLKLTLISEDIKSY-YTVRQLELENLTTQETREILHFHYTT 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 846 WPAEGTPASTRPLLDFRRKVNK--CYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMA--KGVKEIDIAATLEHVRDQRP 921
Cdd:cd14608  164 WPDFGVPESPASFLNFLFKVREsgSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDkrKDPSSVDIKKVLLEMRKFRM 243

                        250       260
                 ....*....|....*....|....
gi 315113878 922 GLVRSKDQFEFALTAVAEEVNAIL 945
Cdd:cd14608  244 GLIQTADQLRFSYLAVIEGAKFIM 267
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 682-939 3.44e-51

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: 182.15  E-value: 3.44e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 682 KEWQAL--CAYQAepnTCATAQGEGNIKKNRHPDFLPYDHARIKLK-VESSPSrSDYINASPIIEHDPRmPAYIATQGPL 758
Cdd:cd14621   30 EEFNALpaCPIQA---TCEAASKEENKEKNRYVNILPYDHSRVHLTpVEGVPD-SDYINASFINGYQEK-NKFIAAQGPK 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 759 SHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGASLYHVYEVNlVSEHIWCEDFLVRSFYLKNV----QTQE 834
Cdd:cd14621  105 EETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCWTYGNIRVS-VEDVTVLVDYTVRKFCIQQVgdvtNKKP 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 835 TRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNrMAKGVKEIDIAATLE 914
Cdd:cd14621  184 QRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLD-MMHAERKVDVYGFVS 262

                        250       260
                 ....*....|....*....|....*
gi 315113878 915 HVRDQRPGLVRSKDQFEFALTAVAE 939
Cdd:cd14621  263 RIRAQRCQMVQTDMQYVFIYQALLE 287
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 735-932 3.53e-51

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: 179.02  E-value: 3.53e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 735 YINASPIIEHDpRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGASLYHVYEVNLVSEH 814
Cdd:cd17668    1 YINANYVDGYN-KPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 815 IWCEdFLVRSFYLKNVQT--------QETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGR 886
Cdd:cd17668   80 VLAY-YTVRNFTLRNTKIkkgsqkgrPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGR 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 315113878 887 TGTYILIDMVLNRMaKGVKEIDIAATLEHVRDQRPGLVRSKDQFEF 932
Cdd:cd17668  159 TGTYIVLDSMLQQI-QHEGTVNIFGFLKHIRSQRNYLVQTEEQYVF 203
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 683-939 4.90e-51

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: 181.46  E-value: 4.90e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 683 EWQALCAYQAEPNTCATAQGEGNIKKNRHPDFLPYDHARIKLKVESSPSRSDYINASpIIEHDPRMPAYIATQGPLSHTI 762
Cdd:cd14629   31 EFKLLANSKAHTSRFISANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINAS-FIDGYRQQKAYIATQGPLAETT 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 763 ADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGASLYHVYEVNLVSEHIWCEdFLVRSFYLKNVQTQETRTLTQFH 842
Cdd:cd14629  110 EDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQ-YILREFKVTDARDGQSRTIRQFQ 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 843 FLSWPAEGTPASTRPLLDFRRKVNKCYR--GRSCPIIVHCSDGAGRTGTYILIDMVLNRMA-KGVkeIDIAATLEHVRDQ 919
Cdd:cd14629  189 FTDWPEQGVPKTGEGFIDFIGQVHKTKEqfGQDGPITVHCSAGVGRTGVFITLSIVLERMRyEGV--VDMFQTVKTLRTQ 266

                        250       260
                 ....*....|....*....|
gi 315113878 920 RPGLVRSKDQFEFALTAVAE 939
Cdd:cd14629  267 RPAMVQTEDQYQLCYRAALE 286
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 735-937 7.65e-51

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: 177.85  E-value: 7.65e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 735 YINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGASLYHVYEVNLVSEH 814
Cdd:cd14552    1 YINAS-FIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVSSGDITVELKDQT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 815 IwCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGR-SCPIIVHCSDGAGRTGTYILI 893
Cdd:cd14552   80 D-YEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSgNHPITVHCSAGAGRTGTFCAL 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 315113878 894 DMVLNRM-AKGVkeIDIAATLEHVRDQRPGLVRSKDQFEFALTAV 937
Cdd:cd14552  159 STVLERVkAEGV--LDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 711-939 1.43e-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: 177.83  E-value: 1.43e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 711 HPDFLPYDHARIKL-KVESSPSrSDYINASPIIEHDPRmPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVK 789
Cdd:cd14620    1 YPNILPYDHSRVILsQLDGIPC-SDYINASYIDGYKEK-NKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 790 QCDRYWPDEGASLYHVYEVNlVSEHIWCEDFLVRSFYLKNVQT---QETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVN 866
Cdd:cd14620   79 KCYQYWPDQGCWTYGNIRVA-VEDCVVLVDYTIRKFCIQPQLPdgcKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVK 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 315113878 867 KCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNrMAKGVKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAE 939
Cdd:cd14620  158 SVNPVHAGPIVVHCSAGVGRTGTFIVIDAMID-MMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 682-939 4.76e-50

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: 177.93  E-value: 4.76e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 682 KEWQALCAYQAEPntCATAQGEGNIKKNRHPDFLPYDHARIKLKVESSPSRSDYINASpIIEHDPRMPAYIATQGPLSHT 761
Cdd:cd14633   19 EEYESFFEGQSAP--WDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGN-YIDGYHRPNHYIATQGPMQET 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 762 IADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEgASLYHVYEVNLVSEHIWCEdFLVRSFYLKNVQTQETRTLTQF 841
Cdd:cd14633   96 IYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDD-TEIYKDIKVTLIETELLAE-YVIRTFAVEKRGVHEIREIRQF 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 842 HFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNrMAKGVKEIDIAATLEHVRDQRP 921
Cdd:cd14633  174 HFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLD-MAEREGVVDIYNCVRELRSRRV 252

                        250
                 ....*....|....*...
gi 315113878 922 GLVRSKDQFEFALTAVAE 939
Cdd:cd14633  253 NMVQTEEQYVFIHDAILE 270
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 735-939 6.58e-50

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: 175.32  E-value: 6.58e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 735 YINASPIiehdpRMPA------YIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGASLYHV--Y 806
Cdd:cd14596    1 YINASYI-----TMPVgeeelfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELenY 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 807 EVNLVSEHIwCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYrgRSCPIIVHCSDGAGR 886
Cdd:cd14596   76 QLRLENYQA-LQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVH--NTGPIVVHCSAGIGR 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 315113878 887 TGTYILIDMVLNRMAKGVkEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAE 939
Cdd:cd14596  153 AGVLICVDVLLSLIEKDL-SFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLE 204
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 735-932 7.52e-50

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: 174.89  E-value: 7.52e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 735 YINASPIIE-HDPRmpAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGASlYHVYEVNLVSE 813
Cdd:cd14558    1 YINASFIDGyWGPK--SLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKT-YGDIEVELKDT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 814 HIwCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKV------NKCYRGRSCPIIVHCSDGAGRT 887
Cdd:cd14558   78 EK-SPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIkqklpyKNSKHGRSVPIVVHCSDGSSRT 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 315113878 888 GTYILIdmvLNRMAKGVKE--IDIAATLEHVRDQRPGLVRSKDQFEF 932
Cdd:cd14558  157 GIFCAL---WNLLESAETEkvVDVFQVVKALRKQRPGMVSTLEQYQF 200
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 703-941 1.67e-49

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: 176.85  E-value: 1.67e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 703 EGNIKKNRHPDFLPYDHARIKLKVESSPSRSDYINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTP 782
Cdd:cd14624   45 EVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINAN-YIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTK 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 783 LVEDGVKQCDRYWPDEGASLYHVYEVNLVsEHIWCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFR 862
Cdd:cd14624  124 LEERSRVKCDQYWPSRGTETYGLIQVTLL-DTVELATYCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFL 202

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 315113878 863 RKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAEEV 941
Cdd:cd14624  203 RRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERI-KHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAV 280
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 715-939 2.70e-49

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: 174.08  E-value: 2.70e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 715 LPYDHARIKLKVESSPSRSDYINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRY 794
Cdd:cd14623    6 IPYEFNRVIIPVKRGEENTDYVNAS-FIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEKCAQY 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 795 WPDEGASLYHVYEVNLVSEHiWCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGR-S 873
Cdd:cd14623   85 WPSDGSVSYGDITIELKKEE-ECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQQQSgN 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 315113878 874 CPIIVHCSDGAGRTGTYILIDMVLNRM-AKGVkeIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAE 939
Cdd:cd14623  164 HPITVHCSAGAGRTGTFCALSTVLERVkAEGI--LDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 734-939 1.82e-48

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: 170.96  E-value: 1.82e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 734 DYINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGASLYHVYEVNLVSE 813
Cdd:cd14622    1 DYINAS-FIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVTHGEITIEIKND 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 814 HIwCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGR-SCPIIVHCSDGAGRTGTYIL 892
Cdd:cd14622   80 TL-LETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTgNHPIVVHCSAGAGRTGTFIA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 315113878 893 IDMVLNRM-AKGVkeIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAE 939
Cdd:cd14622  159 LSNILERVkAEGL--LDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQD 204
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 705-937 7.42e-48

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: 171.30  E-value: 7.42e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 705 NIKKNRHPDFLPYDHARIKLKvessPSRSDYINASPI-IEHDPRmpAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPL 783
Cdd:cd14607   24 NRNRNRYRDVSPYDHSRVKLQ----NTENDYINASLVvIEEAQR--SYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRI 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 784 VEDGVKQCDRYWPDEGASLYHVYE----VNLVSEHIWCEdFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLL 859
Cdd:cd14607   98 VEKDSVKCAQYWPTDEEEVLSFKEtgfsVKLLSEDVKSY-YTVHLLQLENINSGETRTISHFHYTTWPDFGVPESPASFL 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 860 DFRRKV--NKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGVK-EIDIAATLEHVRDQRPGLVRSKDQFEFALTA 936
Cdd:cd14607  177 NFLFKVreSGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDPdSVDIKQVLLDMRKYRMGLIQTPDQLRFSYMA 256


                 .
gi 315113878 937 V 937
Cdd:cd14607  257 V 257
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 709-932 1.07e-47

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: 169.74  E-value: 1.07e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 709 NRHPDFLPYDHARIKLKVESSPSRSDYINASpiiehdpRMPAY------IATQGPLSHTIADFWQMVWESGCTVIVMLTP 782
Cdd:cd14618    1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINAN-------FIPGYtspqefIATQGPLKKTIEDFWRLVWEQQVCNIIMLTV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 783 LVEDGVKQCDRYWPDEGASLYHVY-EVNLVSEHIwCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDF 861
Cdd:cd14618   74 GMENGRVLCDHYWPSESTPVSYGHiTVHLLAQSS-EDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAF 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 315113878 862 RRKVN---KCYRGRScPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLEHVRDQRPGLVRSKDQFEF 932
Cdd:cd14618  153 RELVRehvQATKGKG-PTLVHCSAGVGRSGTFIALDRLLRQL-KEEKVVDVFNTVYILRMHRYLMIQTLSQYIF 224
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 690-937 1.15e-47

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: 171.19  E-value: 1.15e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 690 YQAEPN---TCATaQGEgNIKKNRHPDFLPYDHARIKLKVESspsrsDYINASPIIEHDPRMP---AYIATQGPLSHTIA 763
Cdd:cd14600   24 YRKKPGlaiTCAK-LPQ-NMDKNRYKDVLPYDATRVVLQGNE-----DYINASYVNMEIPSANivnKYIATQGPLPHTCA 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 764 DFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGASL-YHVYEVNLVSEHiwCE-DFLVRSFYLKNVQTQETRTLTQF 841
Cdd:cd14600   97 QFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPDVMeYGGFRVQCHSED--CTiAYVFREMLLTNTQTGEERTVTHL 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 842 HFLSWPAEGTPASTRPLLDFRRKVnKCYRGRSCPIIVHCSDGAGRTGTYILID--MVLNRMAKGVKEIDIAATLehvRDQ 919
Cdd:cd14600  175 QYVAWPDHGVPDDSSDFLEFVNYV-RSKRVENEPVLVHCSAGIGRTGVLVTMEtaMCLTERNQPVYPLDIVRKM---RDQ 250

                        250
                 ....*....|....*...
gi 315113878 920 RPGLVRSKDQFEFALTAV 937
Cdd:cd14600  251 RAMMVQTSSQYKFVCEAI 268
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 709-932 7.78e-47

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: 167.40  E-value: 7.78e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 709 NRHPDFLPYDHARIKLKVESSPSRSDYINASPIIEHDPRMpAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGV 788
Cdd:cd14617    1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRR-EYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 789 KQCDRYWPDEGASLYHV-YEVNLVSEHIWCEdFLVRSFYLKNV-QTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVN 866
Cdd:cd14617   80 VKCDHYWPADQDSLYYGdLIVQMLSESVLPE-WTIREFKICSEeQLDAPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVR 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 315113878 867 KcYRGRS---CPIIVHCSDGAGRTGTYILIDMVLNRMAKgVKEIDIAATLEHVRDQRPGLVRSKDQFEF 932
Cdd:cd14617  159 D-YINRTpgsGPTVVHCSAGVGRTGTFIALDRILQQLDS-KDSVDIYGAVHDLRLHRVHMVQTECQYVY 225
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 735-939 1.66e-46

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: 165.48  E-value: 1.66e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 735 YINASPII-EHDPRMpaYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEgASLYHVYEVNLVSE 813
Cdd:cd14555    1 YINANYIDgYHRPNH--YIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDD-TEVYGDIKVTLVET 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 814 HIWCEdFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILI 893
Cdd:cd14555   78 EPLAE-YVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYIVI 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 315113878 894 DMVLNrMAKGVKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAE 939
Cdd:cd14555  157 DIMLD-MAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 735-932 6.72e-46

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: 163.54  E-value: 6.72e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 735 YINASPIIEHDPRmPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGASLYHVYEVNlVSEH 814
Cdd:cd14551    1 YINASYIDGYQEK-NKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTYGNLRVR-VEDT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 815 IWCEDFLVRSFYLKNVQ----TQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTY 890
Cdd:cd14551   79 VVLVDYTTRKFCIQKVNrgigEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTGTF 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 315113878 891 ILIDMVLNrMAKGVKEIDIAATLEHVRDQRPGLVRSKDQFEF 932
Cdd:cd14551  159 IVIDAMLD-MMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVF 199
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 726-939 8.64e-46

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: 164.04  E-value: 8.64e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 726 VESSPSrSDYINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEgASLYHV 805
Cdd:cd14631    7 VEDDPS-SDYINAN-YIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDD-TEVYGD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 806 YEVNLVS-EHIwcEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGA 884
Cdd:cd14631   84 FKVTCVEmEPL--AEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAGA 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 315113878 885 GRTGTYILIDMVLNrMAKGVKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAE 939
Cdd:cd14631  162 GRTGCYIVIDIMLD-MAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 734-937 4.41e-45

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: 161.65  E-value: 4.41e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 734 DYINASPI---IEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPD-EGASLYHVYEVN 809
Cdd:cd14601    1 DYINANYInmeIPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEpSGSSSYGGFQVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 810 LVSEHiWCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGT 889
Cdd:cd14601   81 CHSEE-GNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTGV 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 315113878 890 YILID--MVLNRMAKGVKEIDIAATLehvRDQRPGLVRSKDQFEFALTAV 937
Cdd:cd14601  160 LITMEtaMCLIECNQPVYPLDIVRTM---RDQRAMMIQTPSQYRFVCEAI 206
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 704-932 1.25e-43

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: 158.85  E-value: 1.25e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 704 GNIKKNRHPDFLPYDHARIKLKVE-SSPSRSDYINASPIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTP 782
Cdd:cd14612   14 GHASKDRYKTILPNPQSRVCLRRAgSQEEEGSYINANYIRGYDGKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITK 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 783 LVEdGVKQCDRYWPDEGASlYHVYE--VNLVSEhiwCEDFLVRSFYLKnvQTQETRTLTQFHFLSWPAEGTPASTRPLLD 860
Cdd:cd14612   94 LKE-KKEKCVHYWPEKEGT-YGRFEirVQDMKE---CDGYTIRDLTIQ--LEEESRSVKHYWFSSWPDHQTPESAGPLLR 166

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 315113878 861 FRRKVNKCYR--GRSCPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLEHVRDQRPGLVRSKDQFEF 932
Cdd:cd14612  167 LVAEVEESRQtaASPGPIVVHCSAGIGRTGCFIATSIGCQQL-KDTGKVDILGIVCQLRLDRGGMIQTSEQYQF 239
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 704-932 2.80e-43

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: 158.10  E-value: 2.80e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 704 GNIKKNRHPDFLPYDHARIKLKVESSPS-RSDYINASPIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTP 782
Cdd:cd14613   24 GLVRKNRYKTILPNPHSRVCLTSPDQDDpLSSYINANYIRGYGGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITN 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 783 LVEDGVKqCDRYWPDEGAsLYHVYEVNlVSEHIWCEDFLVRSFYLKNvqTQETRTLTQFHFLSWPAEGTPASTRPLLDFR 862
Cdd:cd14613  104 IEEMNEK-CTEYWPEEQV-TYEGIEIT-VKQVIHADDYRLRLITLKS--GGEERGLKHYWYTSWPDQKTPDNAPPLLQLV 178

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 315113878 863 RKVN---KCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGVKeIDIAATLEHVRDQRPGLVRSKDQFEF 932
Cdd:cd14613  179 QEVEearQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGV-VDILRTTCQLRLDRGGMIQTCEQYQF 250
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 735-932 3.09e-43

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: 156.46  E-value: 3.09e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 735 YINASPI-IEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEG----ASLYHVYEVN 809
Cdd:cd14540    1 YINASHItATVGGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGgehdALTFGEYKVS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 810 LVSEHIwCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDF-------RRKVNKCYRGRS--CPIIVHC 880
Cdd:cd14540   81 TKFSVS-SGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFleeinsvRRHTNQDVAGHNrnPPTLVHC 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 315113878 881 SDGAGRTGTYILIDMVLNRMAKGVkEIDIAATLEHVRDQRPGLVRSKDQFEF 932
Cdd:cd14540  160 SAGVGRTGVVILADLMLYCLDHNE-ELDIPRVLALLRHQRMLLVQTLAQYKF 210
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 735-932 7.56e-43

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


Pssm-ID: 350496 [Multi-domain]  Cd Length: 206  Bit Score: 154.93  E-value: 7.56e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 735 YINASPIIEHD-PRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVeDGVK--QCDRYWPDEGASLYHVYEVNLV 811
Cdd:cd17658    1 YINASLVETPAsESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLV-DNYStaKCADYFPAEENESREFGRISVT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 812 SEHIWCED--FLVRSFYLKNVQTQET-RTLTQFHFLSWPAEGTPASTRPLldfrRKVNKCYRG---RSCPIIVHCSDGAG 885
Cdd:cd17658   80 NKKLKHSQhsITLRVLEVQYIESEEPpLSVLHIQYPEWPDHGVPKDTRSV----RELLKRLYGippSAGPIVVHCSAGIG 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 315113878 886 RTGTYILIDMVLNRMAKG-VKEIDIAATLEHVRDQRPGLVRSKDQFEF 932
Cdd:cd17658  156 RTGAYCTIHNTIRRILEGdMSAVDLSKTVRKFRSQRIGMVQTQDQYIF 203
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 735-939 1.00e-42

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: 154.82  E-value: 1.00e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 735 YINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEgASLYHVYEVNLVSEH 814
Cdd:cd14632    1 YINAN-YIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDD-SDTYGDIKITLLKTE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 815 IWCEdFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILID 894
Cdd:cd14632   79 TLAE-YSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYIVLD 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 315113878 895 MVLNrMAKGVKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAE 939
Cdd:cd14632  158 VMLD-MAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 735-933 2.23e-42

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: 153.69  E-value: 2.23e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 735 YINASPIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDE-GASL-YHVYEVNLVS 812
Cdd:cd14539    1 YINASLIEDLTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErGQALvYGAITVSLQS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 813 EH---IWCEdflvRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCY---RGRSCPIIVHCSDGAGR 886
Cdd:cd14539   81 VRttpTHVE----RIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYlqqRSLQTPIVVHCSSGVGR 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 315113878 887 TGTYILIDMVLNRMAKGVKEIDIAATLEHVRDQRPGLVRSKDQFEFA 933
Cdd:cd14539  157 TGAFCLLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFC 203
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 735-930 4.61e-42

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: 152.67  E-value: 4.61e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 735 YINASPIIEH-DPRmpAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWP--DEGASLYHVYEVNLV 811
Cdd:cd14557    1 YINASYIDGFkEPR--KYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPsmEEGSRAFGDVVVKIN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 812 SEHIwCEDFLVRSFYLKNVQTQET-RTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTY 890
Cdd:cd14557   79 EEKI-CPDYIIRKLNINNKKEKGSgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTY 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 315113878 891 ILIDMVLNRM-AKGVkeIDIAATLEHVRDQRPGLVRSKDQF 930
Cdd:cd14557  158 IGIDAMLEGLeAEGR--VDVYGYVVKLRRQRCLMVQVEAQY 196
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 708-932 8.93e-42

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: 152.76  E-value: 8.93e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 708 KNRHPDFLPYDHARIKLKVE-SSPSRSDYINASPIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVED 786
Cdd:cd14611    2 KNRYKTILPNPHSRVCLKPKnSNDSLSTYINANYIRGYGGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 787 GVKqCDRYWPdEGASLYHVYE--VNLVSEhiwCEDFLVRSFYLKnvQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRK 864
Cdd:cd14611   82 NEK-CVLYWP-EKRGIYGKVEvlVNSVKE---CDNYTIRNLTLK--QGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLD 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 315113878 865 VN---KCYRGRScPIIVHCSDGAGRTGTYILIDMVLNRMA-KGVkeIDIAATLEHVRDQRPGLVRSKDQFEF 932
Cdd:cd14611  155 VEedrLASPGRG-PVVVHCSAGIGRTGCFIATTIGCQQLKeEGV--VDVLSIVCQLRVDRGGMVQTSEQYEF 223
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 735-932 1.38e-40

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: 148.32  E-value: 1.38e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 735 YINASPIIEHDPRmPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLvEDGVKQCDRYWPDEGASLYHVYEVNLVSEH 814
Cdd:cd14556    1 YINAALLDSYKQP-AAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQL-DPKDQSCPQYWPDEGSGTYGPIQVEFVSTT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 815 IwCEDFLVRSFYLKNV-QTQE-TRTLTQFHFLSWPAEG-TPASTRPLLDFRRKVNK----CYRGrscPIIVHCSDGAGRT 887
Cdd:cd14556   79 I-DEDVISRIFRLQNTtRPQEgYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKwqeqSGEG---PIVVHCLNGVGRS 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 315113878 888 GTYILIDMVLNRMaKGVKEIDIAATLEHVRDQRPGLVRSKDQFEF 932
Cdd:cd14556  155 GVFCAISSVCERI-KVENVVDVFQAVKTLRNHRPNMVETEEQYKF 198
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 709-932 4.16e-40

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: 147.75  E-value: 4.16e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 709 NRHPDFLPYDHARIKLKVESSPSRSDYINASPIIEHdpRMP-AYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDG 787
Cdd:cd14616    1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGY--LCPnEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 788 VKQCDRYWPDEG--ASLYHVYEVNLVSEHIWcEDFLVRSfyLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKV 865
Cdd:cd14616   79 RIRCHQYWPEDNkpVTVFGDIVITKLMEDVQ-IDWTIRD--LKIERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLV 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 315113878 866 NKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLEHVRDQRPGLVRSKDQFEF 932
Cdd:cd14616  156 RASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHI-NDHDFVDIYGLVAELRSERMCMVQNLAQYIF 221
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 705-932 1.19e-39

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: 147.34  E-value: 1.19e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 705 NIKKNRHPDFLPYDHARIKLKVESSPSRSDYINASPIIEHD-PRmpAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPL 783
Cdd:cd14614   12 NRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNsPQ--EYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQC 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 784 VEDGVKQCDRYWP-DEGASLYHVYEVNLVSEHiWCEDFLVRSFYLKnvQTQETRTLTQFHFLSWPAEGTPA--STRPLLD 860
Cdd:cd14614   90 NEKRRVKCDHYWPfTEEPVAYGDITVEMLSEE-EQPDWAIREFRVS--YADEVQDVMHFNYTAWPDHGVPTanAAESILQ 166

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 315113878 861 F----RRKVNKcyrgRSCPIIVHCSDGAGRTGTYILIDmvlnRMAKGVKE---IDIAATLEHVRDQRPGLVRSKDQFEF 932
Cdd:cd14614  167 FvqmvRQQAVK----SKGPMIIHCSAGVGRTGTFIALD----RLLQHIRDhefVDILGLVSEMRSYRMSMVQTEEQYIF 237
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 705-932 9.54e-39

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 146.69  E-value: 9.54e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 705 NIKKNRHPDFLPYDHARIKLKVESSpSRSDYINASPI--IEHDPRmpaYIATQGPLSHTIADFWQMVWESGCTVIVMLTP 782
Cdd:PHA02747  51 NQPKNRYWDIPCWDHNRVILDSGGG-STSDYIHANWIdgFEDDKK---FIATQGPFAETCADFWKAVWQEHCSIIVMLTP 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 783 L-VEDGVKQCDRYW-PDEGASL----YHVYEVNLVsehiwcedflVRSFYLK------NVQTQETRTLTQFHFLSWPAEG 850
Cdd:PHA02747 127 TkGTNGEEKCYQYWcLNEDGNIdmedFRIETLKTS----------VRAKYILtlieitDKILKDSRKISHFQCSEWFEDE 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 851 TPASTRPLLDF-------RRKVNKCYRGRS---CPIIVHCSDGAGRTGTYILIDMVLNRMAKgVKEIDIAATLEHVRDQR 920
Cdd:PHA02747 197 TPSDHPDFIKFikiidinRKKSGKLFNPKDallCPIVVHCSDGVGKTGIFCAVDICLNQLVK-RKAICLAKTAEKIREQR 275

                        250
                 ....*....|..
gi 315113878 921 PGLVRSKDQFEF 932
Cdd:PHA02747 276 HAGIMNFDDYLF 287
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 699-932 2.40e-37

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: 142.06  E-value: 2.40e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 699 TAQGEGNIKKNRHPDFLPYDHARIKLkVESSPSRSDYINASPI-IEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVI 777
Cdd:cd14599   32 TATLPENAERNRIREVVPYEENRVEL-VPTKENNTGYINASHIkVTVGGEEWHYIATQGPLPHTCHDFWQMVWEQGVNVI 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 778 VMLTPLVEDGVKQCDRYWPDEG----ASLYHVYEVNL-VSEHIWCedFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTP 852
Cdd:cd14599  111 AMVTAEEEGGRSKSHRYWPKLGskhsSATYGKFKVTTkFRTDSGC--YATTGLKVKHLLSGQERTVWHLQYTDWPDHGCP 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 853 ASTRPLLDF-------RRKVNKCYRG-RSC--PIIVHCSDGAGRTGTYILIDMVLNRMAKGVKeIDIAATLEHVRDQRPG 922
Cdd:cd14599  189 EEVQGFLSYleeiqsvRRHTNSMLDStKNCnpPIVVHCSAGVGRTGVVILTELMIGCLEHNEK-VEVPVMLRHLREQRMF 267

                        250
                 ....*....|
gi 315113878 923 LVRSKDQFEF 932
Cdd:cd14599  268 MIQTIAQYKF 277
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
837-939 8.13e-34

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 125.16  E-value: 8.13e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878   837 TLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSC--PIIVHCSDGAGRTGTYILIDMVLNRMAKGVKEIDIAATLE 914
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESsgPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|....*
gi 315113878   915 HVRDQRPGLVRSKDQFEFALTAVAE 939
Cdd:smart00404  81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 837-939 8.13e-34

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: 125.16  E-value: 8.13e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878   837 TLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSC--PIIVHCSDGAGRTGTYILIDMVLNRMAKGVKEIDIAATLE 914
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESsgPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|....*
gi 315113878   915 HVRDQRPGLVRSKDQFEFALTAVAE 939
Cdd:smart00012  81 ELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 735-932 7.97e-33

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: 126.29  E-value: 7.97e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 735 YINASPIIEHdpRMPA-YIATQGPLSHTIADFWQMVWESGCTVIVMLTPLveDGVKQCDRYWPDEGASLYHVYEVNLVSE 813
Cdd:cd14634    1 YINAALMDSH--KQPAaFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM--DAAQLCMQYWPEKTSCCYGPIQVEFVSA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 814 HIwCEDFLVRSFYLKNVQTQET--RTLTQFHFLSWPA-EGTPASTRPLLDFRRKVNKC---YRGRSCPIIVHCSDGAGRT 887
Cdd:cd14634   77 DI-DEDIISRIFRICNMARPQDgyRIVQHLQYIGWPAyRDTPPSKRSILKVVRRLEKWqeqYDGREGRTVVHCLNGGGRS 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 315113878 888 GTYILIDMVlNRMAKGVKEIDIAATLEHVRDQRPGLVRSKDQFEF 932
Cdd:cd14634  156 GTFCAICSV-CEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKF 199
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
663-945 8.16e-33

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 128.67  E-value: 8.16e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 663 GHMILAYMEDHLRNRdrLAKEWQALcAYQAEPNtcataQGEGNI---KKNRHPDFLPYDHARIklkvesspsRSD--YIN 737
Cdd:COG5599    5 NPIAIKSEEEKINSR--LSTLTNEL-APSHNDP-----QYLQNIngsPLNRFRDIQPYKETAL---------RANlgYLN 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 738 ASPIIEHDPRMpaYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGV--KQCDRYWPDEG-ASLYHVyEVNLVSEH 814
Cdd:COG5599   68 ANYIQVIGNHR--YIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISKpkVKMPVYFRQDGeYGKYEV-SSELTESI 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 815 IWCEDFLVRSFYLKNVQT-QETRTLTQFHFLSWPAEGTPAST--RPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYI 891
Cdd:COG5599  145 QLRDGIEARTYVLTIKGTgQKKIEIPVLHVKNWPDHGAISAEalKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLI 224

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 315113878 892 LIdMVLNRMAKGVKEIDIAA--TLEHVRDQR-PGLVRSKDQFEFaLTAVAEEVNAIL 945
Cdd:COG5599  225 AC-LALSKSINALVQITLSVeeIVIDMRTSRnGGMVQTSEQLDV-LVKLAEQQIRPL 279
PHA02738 PHA02738
hypothetical protein; Provisional
 705-942 8.41e-33

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 129.66  E-value: 8.41e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 705 NIKKNRHPDFLPYDHARIKLKVESSpsRSDYINASPI--IEHDPRmpaYIATQGPLSHTIADFWQMVWESGCTVIVMLTP 782
Cdd:PHA02738  49 NRKLNRYLDAVCFDHSRVILPAERN--RGDYINANYVdgFEYKKK---FICGQAPTRQTCYDFYRMLWMEHVQIIVMLCK 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 783 LVEDGVKQCDRYWPD-EGASL-YHVYEVNLVSehiwCEDFL--VRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPL 858
Cdd:PHA02738 124 KKENGREKCFPYWSDvEQGSIrFGKFKITTTQ----VETHPhyVKSTLLLTDGTSATQTVTHFNFTAWPDHDVPKNTSEF 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 859 LDFRRKVNKCY-------------RGRSCPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLEHVRDQRPGLVR 925
Cdd:PHA02738 200 LNFVLEVRQCQkelaqeslqighnRLQPPPIVVHCNAGLGRTPCYCVVDISISRF-DACATVSIPSIVSSIRNQRYYSLF 278

                        250
                 ....*....|....*..
gi 315113878 926 SKDQFEFALTAVAEEVN 942
Cdd:PHA02738 279 IPFQYFFCYRAVKRYVN 295
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 735-932 3.87e-32

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: 123.97  E-value: 3.87e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 735 YINASPIIEHDpRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGvkQCDRYWPDEGASLYHV-YEVNLVSE 813
Cdd:cd14550    1 YINASYLQGYR-RSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTKEKPLECEtFKVTLSGE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 814 HIWC----EDFLVRSFYLKNvqTQETRTLT--QFHFLSWPAEGTPASTrpLLDFRRKVNKCYRGRSCPIIVHCSDGAGRT 887
Cdd:cd14550   78 DHSClsneIRLIVRDFILES--TQDDYVLEvrQFQCPSWPNPCSPIHT--VFELINTVQEWAQQRDGPIVVHDRYGGVQA 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 315113878 888 GTYILIdMVLNRMAKGVKEIDI--AATLEHVRdqRPGLVRSKDQFEF 932
Cdd:cd14550  154 ATFCAL-TTLHQQLEHESSVDVyqVAKLYHLM--RPGVFTSKEDYQF 197
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 735-932 4.44e-30

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: 118.92  E-value: 4.44e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 735 YINASPI------IEHDprmpaYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGASLYHV-YE 807
Cdd:cd14598    1 YINASHIkvtvggKEWD-----YIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSRHNTVtYG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 808 VNLVSEHIWCED--FLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDF-------RRKVNKCY--RGRSCPI 876
Cdd:cd14598   76 RFKITTRFRTDSgcYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYleeiqsvRRHTNSTIdpKSPNPPV 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 315113878 877 IVHCSDGAGRTGTYILIDMVL-----NRMakgvkeIDIAATLEHVRDQRPGLVRSKDQFEF 932
Cdd:cd14598  156 LVHCSAGVGRTGVVILSEIMIaclehNEM------LDIPRVLDMLRQQRMMMVQTLSQYTF 210
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 694-932 7.12e-30

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 120.88  E-value: 7.12e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 694 PNTCATAQGEGNIKKNRHPDFLPYDHARIKLKVESSpsRSDYINASPIIEHDPRMpAYIATQGPLSHTIADFWQMVWESG 773
Cdd:PHA02742  41 AFSCNESLELKNMKKCRYPDAPCFDRNRVILKIEDG--GDDFINASYVDGHNAKG-RFICTQAPLEETALDFWQAIFQDQ 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 774 CTVIVMLTPLVEDGVKQCDRYW-PDEGASLYHvYEVNLVSEHIWC-EDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGT 851
Cdd:PHA02742 118 VRVIVMITKIMEDGKEACYPYWmPHERGKATH-GEFKIKTKKIKSfRNYAVTNLCLTDTNTGASLDIKHFAYEDWPHGGL 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 852 PASTRPLLDFRRKVNKC-----------YRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGVKeIDIAATLEHVRDQR 920
Cdd:PHA02742 197 PRDPNKFLDFVLAVREAdlkadvdikgeNIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAI-IPLLSIVRDLRKQR 275

                        250
                 ....*....|..
gi 315113878 921 PGLVRSKDQFEF 932
Cdd:PHA02742 276 HNCLSLPQQYIF 287
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 735-939 1.35e-29

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: 116.93  E-value: 1.35e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 735 YINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVE-DGVKQCDRYWPDEGASLYHVYEVNLVSE 813
Cdd:cd14637    1 YINAA-LTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQsNSAWPCLQYWPEPGLQQYGPMEVEFVSG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 814 HIwCEDFLVRSFYLKNV-QTQETRTLT-QFHFLSWPA-EGTPASTRPLLDFRRKVNK----CYRGRScpiIVHCSDGAGR 886
Cdd:cd14637   80 SA-DEDIVTRLFRVQNItRLQEGHLMVrHFQFLRWSAyRDTPDSKKAFLHLLASVEKwqreSGEGRT---VVHCLNGGGR 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 315113878 887 TGTYILIDMVLNrMAKGVKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAE 939
Cdd:cd14637  156 SGTYCASAMILE-MIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 735-939 1.73e-29

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: 116.71  E-value: 1.73e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 735 YINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLveDGVKQCDRYWPDEGASLYHVYEVNLVSEH 814
Cdd:cd14635    1 YINAA-LMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDV--DPAQLCPQYWPENGVHRHGPIQVEFVSAD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 815 IWcEDFLVRSFYLKNVQTQET--RTLTQFHFLSWPA-EGTPASTRPLLDFRRKVNKC---YRGRSCPIIVHCSDGAGRTG 888
Cdd:cd14635   78 LE-EDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMyRDTPVSKRSFLKLIRQVDKWqeeYNGGEGRTVVHCLNGGGRSG 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 315113878 889 TYILIDMVLnRMAKGVKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAE 939
Cdd:cd14635  157 TFCAISIVC-EMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 735-939 3.09e-29

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: 115.89  E-value: 3.09e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 735 YINASPIIEHdpRMPA-YIATQGPLSHTIADFWQMVWESGCTVIVMLTPLveDGVKQCDRYWPDEGASLYHVYEVNLVSE 813
Cdd:cd14636    1 YINAALMDSY--RQPAaFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEV--DLAQGCPQYWPEEGMLRYGPIQVECMSC 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 814 HIWCeDFLVRSFYLKNV-QTQETRTLT-QFHFLSWPA-EGTPASTRPLLDFRRKVNK----CYRGRSCPIIvHCSDGAGR 886
Cdd:cd14636   77 SMDC-DVISRIFRICNLtRPQEGYLMVqQFQYLGWAShREVPGSKRSFLKLILQVEKwqeeCDEGEGRTII-HCLNGGGR 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 315113878 887 TGTYILIDMVLnRMAKGVKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAE 939
Cdd:cd14636  155 SGMFCAISIVC-EMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 705-937 2.16e-28

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 117.05  E-value: 2.16e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 705 NIKKNRHPDFLPYDHARI-------------------KLKVESSPSRSDYINASpIIEHDPRMPAYIATQGPLSHTIADF 765
Cdd:PHA02746  51 NLKKNRFHDIPCWDHSRVvinaheslkmfdvgdsdgkKIEVTSEDNAENYIHAN-FVDGFKEANKFICAQGPKEDTSEDF 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 766 WQMVWESGCTVIVMLTPlVEDGVKQCDRYW-PDEGASLYHVYEVNLVSEHIWCEDFLVRSFYLKNVQTQETRTLTQFHFL 844
Cdd:PHA02746 130 FKLISEHESQVIVSLTD-IDDDDEKCFELWtKEEDSELAFGRFVAKILDIIEELSFTKTRLMITDKISDTSREIHHFWFP 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 845 SWPAEGTPASTRPLLDFRRKVNKcYRGR-----------SCPIIVHCSDGAGRTGTYILIDMVLNRMAKGvKEIDIAATL 913
Cdd:PHA02746 209 DWPDNGIPTGMAEFLELINKVNE-EQAElikqadndpqtLGPIVVHCSAGIGRAGTFCAIDNALEQLEKE-KEVCLGEIV 286

                        250       260
                 ....*....|....*....|....
gi 315113878 914 EHVRDQRPGLVRSKDQFEFALTAV 937
Cdd:PHA02746 287 LKIRKQRHSSVFLPEQYAFCYKAL 310
RESP18 pfam14948
RESP18 domain; This domain is found in the glucocorticoid-responsive protein regulated ...
 60-160 2.57e-28

RESP18 domain; This domain is found in the glucocorticoid-responsive protein regulated endocrine-specific protein 18 (RESP18) and in the N-terminal extracellular region of receptor-type tyrosine-protein phosphatases containing the protein-tyrosine phosphatase receptor IA-2 domain (pfam11548).


Pssm-ID: 464394  Cd Length: 103  Bit Score: 109.53  E-value: 2.57e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878   60 GQCQVGVGQARPLLQVTSPVLQRLQGVLRQLMSQGLSWHDDLTQYVISQEMERIPRLRPPEPRPRDRSGLAPKRPGPAG- 138
Cdd:pfam14948   1 GQGQVGVGQLWPLQGFTAPVFQHLQVVLHQIVPQGLFWKDDLTQDVMTQKMEHISRLHPQDPCLKDGKAVFPTRTTGVRg 80

                          90       100
                  ....*....|....*....|....
gi 315113878  139 --ELLLQDIPTGSaPAAQHRLPQP 160
Cdd:pfam14948  81 kqEEKLRLLFPKS-PAVKVNRDQC 103
Receptor_IA-2 pfam11548
Protein-tyrosine phosphatase receptor IA-2; IA-2 is a protein-tyrosine phosphatase receptor ...
 469-528 5.31e-22

Protein-tyrosine phosphatase receptor IA-2; IA-2 is a protein-tyrosine phosphatase receptor that upon exocytosis, the cytoplasmic domain is cleaved and moves to the nucleus where it enhances transcription of the insulin gene. The mature exodomain of IA-2 participates in adhesion to the extracellular matrix and is self-proteolyzed in vitro by reactive oxygen species which may be a new shedding mechanism.


Pssm-ID: 463293  Cd Length: 89  Bit Score: 91.14  E-value: 5.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878  469 EEYGYIVTDQ-----------------------------NVVGPALTFRIRHNEQNLSLADVTQQAGLVKSELEAQTGLQ 519
Cdd:pfam11548   1 EEYGYIVTDNdplsweeglrlmekvaellhlpmssfadiRVLGPAVTFKVRANNKNLTAADVAKAAVDIKDKLEKETGLK 80


                  ....*....
gi 315113878  520 ILQTGVGQR 528
Cdd:pfam11548  81 ILQAGVGDK 89
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 735-937 2.22e-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: 87.36  E-value: 2.22e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 735 YINASPIIEHDpRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCdRYWPDEGASLY-HVYEVNLVSE 813
Cdd:cd17669    1 YINASYIMGYY-QSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWPNKDEPINcETFKVTLIAE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 814 HIWC----EDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPAS-TRPLLDFrrkVNKCYRGRSCPIIVHCSDGAGRTG 888
Cdd:cd17669   79 EHKClsneEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISkTFELISI---IKEEAANRDGPMIVHDEHGGVTAG 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 315113878 889 TYILIDMVLNRMAKGvKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAV 937
Cdd:cd17669  156 TFCALTTLMHQLEKE-NSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 735-937 5.15e-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: 83.57  E-value: 5.15e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 735 YINASPIIEHdPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVML---TPLVEDGVKqcdrYWPDEGASLY-HVYEVNL 810
Cdd:cd17670    1 YINASYIMGY-YRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdnQGLAEDEFV----YWPSREESMNcEAFTVTL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 811 VSEHIWC----EDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTP-ASTRPLLDFrrkVNKCYRGRSCPIIVHCSDGAG 885
Cdd:cd17670   76 ISKDRLClsneEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPiSSTFELINV---IKEEALTRDGPTIVHDEFGAV 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 315113878 886 RTGTYILIdMVLNRMAKGVKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAV 937
Cdd:cd17670  153 SAGTLCAL-TTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAM 203
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 679-949 6.18e-14

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 73.46  E-value: 6.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 679 RLAKEWQALCAYQAEPNTCATAQGEGNIKK-NRHPDFLPYDHARIKLKVESSPSRSDYINAspiIEHDPRmpaYIATQGP 757
Cdd:PHA02740  26 CIIKEYRAIVPEHEDEANKACAQAENKAKDeNLALHITRLLHRRIKLFNDEKVLDARFVDG---YDFEQK---FICIINL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 758 LSHTIADFWQMVWESGCTVIVMLTPLVEdgvKQC-DRYWP-DEG-ASLYHVYEVNLVsEHIWCEDFLVRSFYLKNVQTQE 834
Cdd:PHA02740 100 CEDACDKFLQALSDNKVQIIVLISRHAD---KKCfNQFWSlKEGcVITSDKFQIETL-EIIIKPHFNLTLLSLTDKFGQA 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 835 tRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYR--------GRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKgVKE 906
Cdd:PHA02740 176 -QKISHFQYTAWPADGFSHDPDAFIDFFCNIDDLCAdlekhkadGKIAPIIIDCIDGISSSAVFCVFDICATEFDK-TGM 253

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 315113878 907 IDIAATLEHVRDQRPGLVRSKDQFEFALTAVAEEVNAILKALP 949
Cdd:PHA02740 254 LSIANALKKVRQKKYGCMNCLDDYVFCYHLIAAYLKEKFDILK 296
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 875-932 1.96e-06

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: 48.43  E-value: 1.96e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 315113878 875 PIIVHCSDGAGRTGTYILIDMVLNRMAKGVKEIDIaatlehVRDQRPGLVRSKDQFEF 932
Cdd:cd14504   84 AVLVHCLAGKGRTGTMLACYLVKTGKISAVDAINE------IRRIRPGSIETSEQEKF 135
PHA03247 PHA03247
large tegument protein UL36; Provisional
 234-479 4.94e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.63  E-value: 4.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878  234 PLPKAEAPALFSRTASKGIFGDHPGHSYGDLPGPSPAQLFQDSGLLYLAQEL-----PAPSRARVPRLPEQGSSSRAEDS 308
Cdd:PHA03247 2710 PAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPttagpPAPAPPAAPAAGPPRRLTRPAVA 2789

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878  309 PEGYEKEGLgdrgEKPASPAVQPDAALQRLAAVLAGYGVELRQLTPEQLSTLLTLLQLLPKGAGRNPGGVVNVGadikkt 388
Cdd:PHA03247 2790 SLSESRESL----PSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPG------ 2859

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878  389 meGPVEGRDTAELPARTSPMPGHPTAS---------PTSSEVQQVPSPVSSEPPKAARPPVTPVLLEKKS-------PLG 452
Cdd:PHA03247 2860 --GDVRRRPPSRSPAAKPAAPARPPVRrlarpavsrSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPqpqppppPPP 2937

                         250       260
                  ....*....|....*....|....*..
gi 315113878  453 QSQPTVAGQPSARPAAEEYGYIVTDQN 479
Cdd:PHA03247 2938 RPQPPLAPTTDPAGAGEPSGAVPQPWL 2964
PHA03247 PHA03247
large tegument protein UL36; Provisional
 265-470 1.44e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 1.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878  265 PGPSPAQLFQDSGLLYLAQE------LPAPSRARVPR-LPEQGSSSRAEDSPEGYEKEG----------LGDRGEKPASP 327
Cdd:PHA03247 2629 PSPSPAANEPDPHPPPTVPPperprdDPAPGRVSRPRrARRLGRAAQASSPPQRPRRRAarptvgsltsLADPPPPPPTP 2708

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878  328 AVQPDAALQRLAAVLAGYGVelRQLTPeqlSTLLTLLQLLPKGAGRNPGGVVNVGA-DIKKTMEGPVEGRDTAELPARTS 406
Cdd:PHA03247 2709 EPAPHALVSATPLPPGPAAA--RQASP---ALPAAPAPPAVPAGPATPGGPARPARpPTTAGPPAPAPPAAPAAGPPRRL 2783

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 315113878  407 PMPGhptASPTSSEVQQVPSPVSSEPPKAARPPVTPVLLEKKSPLGQSQPTVAGQPSARPAAEE 470
Cdd:PHA03247 2784 TRPA---VASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPG 2844
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 851-922 3.65e-04

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


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 41.18  E-value: 3.65e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 315113878 851 TPASTRPLLDFRRKVNKCYrgrsCPIIVHCSDGAGRTGTYILIDMVLnRMAKGVKEIdiaatLEHVRDQRPG 922
Cdd:cd14494   38 TLAMVDRFLEVLDQAEKPG----EPVLVHCKAGVGRTGTLVACYLVL-LGGMSAEEA-----VRIVRLIRPG 99
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 374-465 4.82e-04

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 43.52  E-value: 4.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 374 NPGGVVNVGADIKKTMEGPVEGRDTAELPARTSPMPGHPTASPTSSEVQQVPSPVSSEPPKAARPPvTPVLLEKKSPlgq 453
Cdd:PTZ00144 104 EEGDTVEVGAPLSEIDTGGAPPAAAPAAAAAAKAEKTTPEKPKAAAPTPEPPAASKPTPPAAAKPP-EPAPAAKPPP--- 179

                         90
                 ....*....|..
gi 315113878 454 sQPTVAGQPSAR 465
Cdd:PTZ00144 180 -TPVARADPRET 190
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 749-804 1.46e-03

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: 39.26  E-value: 1.46e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 315113878 749 PAYIATQGPLSHtIADFWQMVWESGCTVIVMLT-PLVEDGVKQCDRYWPDEGASLYH 804
Cdd:cd14494    7 LRLIAGALPLSP-LEADSRFLKQLGVTTIVDLTlAMVDRFLEVLDQAEKPGEPVLVH 62
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 127-468 1.64e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.47  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878  127 SGLAPKRPGPAGELLLQDIPTGSAPAAQHRLPQPPVGKGGAG---ASSSLSPLQAELLPPLLEHLLLPPQPPHPSLSYEP 203
Cdd:PHA03307   75 PGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPpppTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPA 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878  204 ALLQPylfhqfgsRDGSRVSEGSPGMVSVGPLPKAEAPALFSRTASKGIFGDHPGHSYGDLPGPSPAQLFQDSgllylaq 283
Cdd:PHA03307  155 AGASP--------AAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASS------- 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878  284 elPAPSRARVPRLPEQGSSSRAeDSPEGYEKeGLGDRGEKPASPAVQPDAALQRLAAVLAGYGVELRQLTPEQLSTLLTL 363
Cdd:PHA03307  220 --PAPAPGRSAADDAGASSSDS-SSSESSGC-GWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERS 295

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878  364 LQLLPKGAGrnpGGVVNVGADIKKTMEGPVEGRD--TAELPARTSPMPGHPTASPTSSEVQQVPSPVSSEPPKAARPPvt 441
Cdd:PHA03307  296 PSPSPSSPG---SGPAPSSPRASSSSSSSRESSSssTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPR-- 370

                         330       340
                  ....*....|....*....|....*..
gi 315113878  442 pvllekKSPLGQSQPTVAGQPSARPAA 468
Cdd:PHA03307  371 ------PSRAPSSPAASAGRPTRRRAR 391
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
875-932 3.24e-03

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 38.80  E-value: 3.24e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 315113878 875 PIIVHCSDGAGRTGTyILIdMVLnrMAKGVkeiDIAATLEHVRDQRPGLVRSKDQFEF 932
Cdd:COG2453   82 KVLVHCRGGIGRTGT-VAA-AYL--VLLGL---SAEEALARVRAARPGAVETPAQRAF 132
PRK06975 PRK06975
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed
 397-529 8.78e-03

bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed


Pssm-ID: 235899 [Multi-domain]  Cd Length: 656  Bit Score: 39.70  E-value: 8.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315113878 397 DTAELPARTSPMPGHPTASPTSSEVQQVPSPVSSEPPKAARPPVTPvllekksplgqsqPTVAGQPSARPAAEEYGYIVT 476
Cdd:PRK06975 267 DAAAQPATAAPAPSRMTDTNDSKSVTSQPAAAAAAPAPPPNPPATP-------------PEPPARRGRGSAALWFVVVVL 333

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 315113878 477 DQNVV--GPALTFRIRHNEQNLS----LADVTQQAGLVKSElEAQTGLQILQTGVGQRE 529
Cdd:PRK06975 334 ACAAAvgGYALNRKVDRLDQELVqrqqANDAQTAELRVKTE-QAQASVHQLDSQFAQLD 391
 
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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