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Conserved domains on  [gi|392894211|ref|NP_497484|]
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WSN domain-containing protein [Caenorhabditis elegans]

Protein Classification

protein tyrosine phosphatase family protein( domain architecture ID 12032608)

cys-based protein tyrosine phosphatase (PTP) family protein, such as tyrosine-protein phosphatase that catalyzes the dephosphorylation of phosphotyrosine groups in phosphoproteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
868-1151 8.98e-57

Protein tyrosine phosphatase, catalytic domain;


:

Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 197.50  E-value: 8.98e-57
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211    868 FMKFFKTSYENKVaNMQSPEVSDLVKKHEMDLRVANPLIEKTRVILKGYKKQfNDNFLHANYVTCPDG-MRFILMQSPQc 946
Cdd:smart00194    2 LEEEFEKLDRLKP-DDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGE-GSDYINASYIDGPNGpKAYIATQGPL- 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211    947 eilepkpakekekytemtprrNSTIEKFWWMIRQEKVEQVVMTCDFLERNRetglffENCSKYYPMKVDTELTFKGITVK 1026
Cdd:smart00194   79 ---------------------PSTVEDFWRMVWEQKVTVIVMLTELVEKGR------EKCAQYWPDEEGEPLTYGDITVT 131

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211   1027 CTNMVKVDGIERRTLCITF-GDGVQLTVTHNLMSSWTYLNTQKTTISIISLIQYLNKCKG---APIVIHDHDGISRSATI 1102
Cdd:smart00194  132 LKSVEKVDDYTIRTLEVTNtGCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQStstGPIVVHCSAGVGRTGTF 211

                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....*....
gi 392894211   1103 PASIIGYQKIaETSGAFVLTDVIDYIREHRALAISTPGELSYIDAVIVR 1151
Cdd:smart00194  212 IAIDILLQQL-EAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
WSN pfam02206
Domain of unknown function;
47-112 2.33e-21

Domain of unknown function;


:

Pssm-ID: 426657  Cd Length: 66  Bit Score: 88.66  E-value: 2.33e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392894211    47 EFKSSLIQMQMISRVTNGIYLQHGLSNGSIKSDDLIPELLHFGTITPTQISAINTDKLSKIVEGIN 112
Cdd:pfam02206    1 NLSLIVEKLSILARITNAISLQAGLIDGSIPVDDVISELLNLGSVTLSDIIKIDVDKLKELLEKLK 66
 
Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
868-1151 8.98e-57

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 197.50  E-value: 8.98e-57
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211    868 FMKFFKTSYENKVaNMQSPEVSDLVKKHEMDLRVANPLIEKTRVILKGYKKQfNDNFLHANYVTCPDG-MRFILMQSPQc 946
Cdd:smart00194    2 LEEEFEKLDRLKP-DDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGE-GSDYINASYIDGPNGpKAYIATQGPL- 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211    947 eilepkpakekekytemtprrNSTIEKFWWMIRQEKVEQVVMTCDFLERNRetglffENCSKYYPMKVDTELTFKGITVK 1026
Cdd:smart00194   79 ---------------------PSTVEDFWRMVWEQKVTVIVMLTELVEKGR------EKCAQYWPDEEGEPLTYGDITVT 131

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211   1027 CTNMVKVDGIERRTLCITF-GDGVQLTVTHNLMSSWTYLNTQKTTISIISLIQYLNKCKG---APIVIHDHDGISRSATI 1102
Cdd:smart00194  132 LKSVEKVDDYTIRTLEVTNtGCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQStstGPIVVHCSAGVGRTGTF 211

                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....*....
gi 392894211   1103 PASIIGYQKIaETSGAFVLTDVIDYIREHRALAISTPGELSYIDAVIVR 1151
Cdd:smart00194  212 IAIDILLQQL-EAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
904-1150 8.71e-40

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 147.77  E-value: 8.71e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211   904 PLIEKTRVILKGYKKqfNDNFLHANYVTCPDGMR-FILMQSPQceilepkpakekekytemtprrNSTIEKFWWMIRQEK 982
Cdd:pfam00102   11 LPYDHTRVKLTGDPG--PSDYINASYIDGYKKPKkYIATQGPL----------------------PNTVEDFWRMVWEEK 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211   983 VEQVVMTCDFLERNRETglffenCSKYYPMKVDTELTFKGITVKCTNMVKV-DGIERRTLCITF-GDGVQLTVTHNLMSS 1060
Cdd:pfam00102   67 VTIIVMLTELEEKGREK------CAQYWPEEEGESLEYGDFTVTLKKEKEDeKDYTVRTLEVSNgGSEETRTVKHFHYTG 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  1061 WTYLNTQKTTISIISLIQYLNKCKG----APIVIHDHDGISRSATIPASIIGYQKIaETSGAFVLTDVIDYIREHRALAI 1136
Cdd:pfam00102  141 WPDHGVPESPNSLLDLLRKVRKSSLdgrsGPIVVHCSAGIGRTGTFIAIDIALQQL-EAEGEVDIFQIVKELRSQRPGMV 219

                          250
                   ....*....|....
gi 392894211  1137 STPGELSYIDAVIV 1150
Cdd:pfam00102  220 QTLEQYIFLYDAIL 233
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 924-1145 1.17e-28

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: 114.30  E-value: 1.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  924 FLHANYVTCPDG-MRFILMQSPQceilepkpakekekytemtprrNSTIEKFWWMIRQEKVEQVVMTCDFLERNRETglf 1002
Cdd:cd00047     1 YINASYIDGYRGpKEYIATQGPL----------------------PNTVEDFWRMVWEQKVSVIVMLTNLVEKGREK--- 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211 1003 fenCSKYYPMKVDTELTFKGITVKCTNMVKVDGIERRTLCITFGDGVQ-LTVTHNLMSSWTYLNTQKTTISIISLIQYLN 1081
Cdd:cd00047    56 ---CERYWPEEGGKPLEYGDITVTLVSEEELSDYTIRTLELSPKGCSEsREVTHLHYTGWPDHGVPSSPEDLLALVRRVR 132

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392894211 1082 KCKGA---PIVIHDHDGISRSATIPASIIGYQKIaETSGAFVLTDVIDYIREHRALAISTPGELSYI 1145
Cdd:cd00047   133 KEARKpngPIVVHCSAGVGRTGTFIAIDILLERL-EAEGEVDVFEIVKALRKQRPGMVQTLEQYEFI 198
WSN pfam02206
Domain of unknown function;
47-112 2.33e-21

Domain of unknown function;


Pssm-ID: 426657  Cd Length: 66  Bit Score: 88.66  E-value: 2.33e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392894211    47 EFKSSLIQMQMISRVTNGIYLQHGLSNGSIKSDDLIPELLHFGTITPTQISAINTDKLSKIVEGIN 112
Cdd:pfam02206    1 NLSLIVEKLSILARITNAISLQAGLIDGSIPVDDVISELLNLGSVTLSDIIKIDVDKLKELLEKLK 66
WSN smart00453
Worm-specific (usually) N-terminal domain;
47-115 6.98e-21

Worm-specific (usually) N-terminal domain;


Pssm-ID: 197734  Cd Length: 69  Bit Score: 87.64  E-value: 6.98e-21
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392894211     47 EFKSSLIQMQMISRVTNGIYLQHGLSNGSIKSDDLIPELLHfgtITPTQISAINTDKLSKIVEGINGLK 115
Cdd:smart00453    2 KLQTVIERLSMLARVTNAISLQAGLINGSIPIDDVIAELLN---IDSSKLSDIINVDLTKIDEGLNKLK 67
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 850-1156 1.77e-10

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 63.87  E-value: 1.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  850 CDRDRRYSDFRRNESTFDFMKFFKTSYENKV--------ANMQSPEvsDLVKKHEMDLrvanPLIEKTRVILKGyKKQFN 921
Cdd:PHA02747    5 CFAECRAIDFLKRRNQLNCFGIIRDEHHQIIlkpfdgliANFEKPE--NQPKNRYWDI----PCWDHNRVILDS-GGGST 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  922 DNFLHANYVtcpDGM----RFILMQSPQCEilepkpakekekytemtprrnsTIEKFWWMIRQEKVEQVVMTCDFLERNR 997
Cdd:PHA02747   78 SDYIHANWI---DGFeddkKFIATQGPFAE----------------------TCADFWKAVWQEHCSIIVMLTPTKGTNG 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  998 EtglffENCSKYYPMKVDTELTFKGITVKCTNMVKVDGIERRTLCITfgDGVQLT---VTHNLMSSWTYLNTQKTTISII 1074
Cdd:PHA02747  133 E-----EKCYQYWCLNEDGNIDMEDFRIETLKTSVRAKYILTLIEIT--DKILKDsrkISHFQCSEWFEDETPSDHPDFI 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211 1075 SLIQYLNKCKG-------------APIVIHDHDGISRSATIPASIIGYQKIAETSgAFVLTDVIDYIREHRALAISTPGE 1141
Cdd:PHA02747  206 KFIKIIDINRKksgklfnpkdallCPIVVHCSDGVGKTGIFCAVDICLNQLVKRK-AICLAKTAEKIREQRHAGIMNFDD 284

                         330
                  ....*....|....*...
gi 392894211 1142 LSYIDA---VIVRLLAIQ 1156
Cdd:PHA02747  285 YLFIQPgyeVLHYFLSKI 302
 
Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
868-1151 8.98e-57

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 197.50  E-value: 8.98e-57
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211    868 FMKFFKTSYENKVaNMQSPEVSDLVKKHEMDLRVANPLIEKTRVILKGYKKQfNDNFLHANYVTCPDG-MRFILMQSPQc 946
Cdd:smart00194    2 LEEEFEKLDRLKP-DDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGE-GSDYINASYIDGPNGpKAYIATQGPL- 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211    947 eilepkpakekekytemtprrNSTIEKFWWMIRQEKVEQVVMTCDFLERNRetglffENCSKYYPMKVDTELTFKGITVK 1026
Cdd:smart00194   79 ---------------------PSTVEDFWRMVWEQKVTVIVMLTELVEKGR------EKCAQYWPDEEGEPLTYGDITVT 131

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211   1027 CTNMVKVDGIERRTLCITF-GDGVQLTVTHNLMSSWTYLNTQKTTISIISLIQYLNKCKG---APIVIHDHDGISRSATI 1102
Cdd:smart00194  132 LKSVEKVDDYTIRTLEVTNtGCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQStstGPIVVHCSAGVGRTGTF 211

                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....*....
gi 392894211   1103 PASIIGYQKIaETSGAFVLTDVIDYIREHRALAISTPGELSYIDAVIVR 1151
Cdd:smart00194  212 IAIDILLQQL-EAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
904-1150 8.71e-40

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 147.77  E-value: 8.71e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211   904 PLIEKTRVILKGYKKqfNDNFLHANYVTCPDGMR-FILMQSPQceilepkpakekekytemtprrNSTIEKFWWMIRQEK 982
Cdd:pfam00102   11 LPYDHTRVKLTGDPG--PSDYINASYIDGYKKPKkYIATQGPL----------------------PNTVEDFWRMVWEEK 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211   983 VEQVVMTCDFLERNRETglffenCSKYYPMKVDTELTFKGITVKCTNMVKV-DGIERRTLCITF-GDGVQLTVTHNLMSS 1060
Cdd:pfam00102   67 VTIIVMLTELEEKGREK------CAQYWPEEEGESLEYGDFTVTLKKEKEDeKDYTVRTLEVSNgGSEETRTVKHFHYTG 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  1061 WTYLNTQKTTISIISLIQYLNKCKG----APIVIHDHDGISRSATIPASIIGYQKIaETSGAFVLTDVIDYIREHRALAI 1136
Cdd:pfam00102  141 WPDHGVPESPNSLLDLLRKVRKSSLdgrsGPIVVHCSAGIGRTGTFIAIDIALQQL-EAEGEVDIFQIVKELRSQRPGMV 219

                          250
                   ....*....|....
gi 392894211  1137 STPGELSYIDAVIV 1150
Cdd:pfam00102  220 QTLEQYIFLYDAIL 233
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 924-1145 1.17e-28

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: 114.30  E-value: 1.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  924 FLHANYVTCPDG-MRFILMQSPQceilepkpakekekytemtprrNSTIEKFWWMIRQEKVEQVVMTCDFLERNRETglf 1002
Cdd:cd00047     1 YINASYIDGYRGpKEYIATQGPL----------------------PNTVEDFWRMVWEQKVSVIVMLTNLVEKGREK--- 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211 1003 fenCSKYYPMKVDTELTFKGITVKCTNMVKVDGIERRTLCITFGDGVQ-LTVTHNLMSSWTYLNTQKTTISIISLIQYLN 1081
Cdd:cd00047    56 ---CERYWPEEGGKPLEYGDITVTLVSEEELSDYTIRTLELSPKGCSEsREVTHLHYTGWPDHGVPSSPEDLLALVRRVR 132

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392894211 1082 KCKGA---PIVIHDHDGISRSATIPASIIGYQKIaETSGAFVLTDVIDYIREHRALAISTPGELSYI 1145
Cdd:cd00047   133 KEARKpngPIVVHCSAGVGRTGTFIAIDILLERL-EAEGEVDVFEIVKALRKQRPGMVQTLEQYEFI 198
WSN pfam02206
Domain of unknown function;
47-112 2.33e-21

Domain of unknown function;


Pssm-ID: 426657  Cd Length: 66  Bit Score: 88.66  E-value: 2.33e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392894211    47 EFKSSLIQMQMISRVTNGIYLQHGLSNGSIKSDDLIPELLHFGTITPTQISAINTDKLSKIVEGIN 112
Cdd:pfam02206    1 NLSLIVEKLSILARITNAISLQAGLIDGSIPVDDVISELLNLGSVTLSDIIKIDVDKLKELLEKLK 66
WSN smart00453
Worm-specific (usually) N-terminal domain;
47-115 6.98e-21

Worm-specific (usually) N-terminal domain;


Pssm-ID: 197734  Cd Length: 69  Bit Score: 87.64  E-value: 6.98e-21
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392894211     47 EFKSSLIQMQMISRVTNGIYLQHGLSNGSIKSDDLIPELLHfgtITPTQISAINTDKLSKIVEGINGLK 115
Cdd:smart00453    2 KLQTVIERLSMLARVTNAISLQAGLINGSIPIDDVIAELLN---IDSSKLSDIINVDLTKIDEGLNKLK 67
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 907-1114 2.14e-18

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: 85.53  E-value: 2.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  907 EKTRVILKGYKKQFNDNFLHANYVTCPDGMR--FILMQSPQceilepkpakekekytemtprrNSTIEKFWWMIRQEKVE 984
Cdd:cd14547    10 EHSRVCLPSVDDDPLSSYINANYIRGYDGEEkaYIATQGPL----------------------PNTVADFWRMVWQEKTP 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  985 QVVMTCDFLERNretglffENCSKYYPMKVDteLTFKGITVKCTNMVKVDGIERRTLCITFGDGVQlTVTHNLMSSWTYL 1064
Cdd:cd14547    68 IIVMITNLTEAK-------EKCAQYWPEEEN--ETYGDFEVTVQSVKETDGYTVRKLTLKYGGEKR-YLKHYWYTSWPDH 137

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392894211 1065 NTQKTTISIISLIQYLNKCK-----GAPIVIHDHDGISRSATIPASIIGYQKIAE 1114
Cdd:cd14547   138 KTPEAAQPLLSLVQEVEEARqtephRGPIVVHCSAGIGRTGCFIATSIGCQQLRE 192
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1052-1149 7.18e-17

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 77.40  E-value: 7.18e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211   1052 TVTHNLMSSWTYLNTQKTTISIISLIQYLNKCK-----GAPIVIHDHDGISRSATIPASIIGYQKIAETSGAFVLTDVID 1126
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLnqsesSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|...
gi 392894211   1127 YIREHRALAISTPGELSYIDAVI 1149
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRAL 103
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1052-1149 7.18e-17

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: 77.40  E-value: 7.18e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211   1052 TVTHNLMSSWTYLNTQKTTISIISLIQYLNKCK-----GAPIVIHDHDGISRSATIPASIIGYQKIAETSGAFVLTDVID 1126
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLnqsesSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|...
gi 392894211   1127 YIREHRALAISTPGELSYIDAVI 1149
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRAL 103
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 903-1121 2.17e-14

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: 74.49  E-value: 2.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  903 NPlieKTRVILKGYKKQFND-NFLHANYVTCPDGmrfilmqspqceilepkpaKEKEKYTEMTPRRNsTIEKFWWMIRQE 981
Cdd:cd14612    27 NP---QSRVCLRRAGSQEEEgSYINANYIRGYDG-------------------KEKAYIATQGPMLN-TVSDFWEMVWQE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  982 KVEQVVMTCDFLERNretglffENCSKYYPMKvdtELTFKGITVKCTNMVKVDGIERRTLCITFGdGVQLTVTHNLMSSW 1061
Cdd:cd14612    84 ECPIIVMITKLKEKK-------EKCVHYWPEK---EGTYGRFEIRVQDMKECDGYTIRDLTIQLE-EESRSVKHYWFSSW 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392894211 1062 TYLNTQKTTISIISLIQYLNKCKGA-----PIVIHDHDGISRSATIPASIIGYQKIAETSGAFVL 1121
Cdd:cd14612   153 PDHQTPESAGPLLRLVAEVEESRQTaaspgPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDIL 217
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 927-1101 2.25e-12

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: 67.66  E-value: 2.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  927 ANYVT--CPDGMRFILMQspqceilEPKPAkekekytemtprrnsTIEKFWWMIRQEKVEQVVMTCDFLERNRetglffE 1004
Cdd:cd18533     4 ASYITlpGTSSKRYIATQ-------GPLPA---------------TIGDFWKMIWQNNVGVIVMLTPLVENGR------E 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211 1005 NCSKYYPMKVDTELTfKGITVKCTNMVKVD--GIERRTLCITFGDGVQLTVTHNLMSSWTYLNTQKTTISIISLIQYLNK 1082
Cdd:cd18533    56 KCDQYWPSGEYEGEY-GDLTVELVSEEENDdgGFIVREFELSKEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRE 134

                         170       180
                  ....*....|....*....|....
gi 392894211 1083 CK-----GAPIVIHDHDGISRSAT 1101
Cdd:cd18533   135 LNdsaslDPPIIVHCSAGVGRTGT 158
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 904-1139 4.30e-11

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: 65.08  E-value: 4.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  904 PLIEKTRVILKGYKKQFNDNFLHANYVtcpDGMR----FILMQSPQceilePKpakekekytemtprrnsTIEKFWWMIR 979
Cdd:cd14543    39 LCLDQSRVKLPKRNGDERTDYINANFM---DGYKqknaYIATQGPL-----PK-----------------TYSDFWRMVW 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  980 QEKVEQVVMTCDFLERNRetglffENCSKYYPMKVDTELTFKGITVkcTNMvkvdGIE------RRTLCITFGDGVQL-T 1052
Cdd:cd14543    94 EQKVLVIVMTTRVVERGR------VKCGQYWPLEEGSSLRYGDLTV--TNL----SVEnkehykKTTLEIHNTETDESrQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211 1053 VTHNLMSSWTYLNTQKTTISII----SLIQYLNKC------------KGAPIVIHDHDGISRSATIPASIIGYQKIAETS 1116
Cdd:cd14543   162 VTHFQFTSWPDFGVPSSAAALLdflgEVRQQQALAvkamgdrwkghpPGPPIVVHCSAGIGRTGTFCTLDICLSQLEDVG 241

                         250       260
                  ....*....|....*....|...
gi 392894211 1117 GAFVLTDViDYIREHRALAISTP 1139
Cdd:cd14543   242 TLNVMQTV-RRMRTQRAFSIQTP 263
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 850-1156 1.77e-10

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 63.87  E-value: 1.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  850 CDRDRRYSDFRRNESTFDFMKFFKTSYENKV--------ANMQSPEvsDLVKKHEMDLrvanPLIEKTRVILKGyKKQFN 921
Cdd:PHA02747    5 CFAECRAIDFLKRRNQLNCFGIIRDEHHQIIlkpfdgliANFEKPE--NQPKNRYWDI----PCWDHNRVILDS-GGGST 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  922 DNFLHANYVtcpDGM----RFILMQSPQCEilepkpakekekytemtprrnsTIEKFWWMIRQEKVEQVVMTCDFLERNR 997
Cdd:PHA02747   78 SDYIHANWI---DGFeddkKFIATQGPFAE----------------------TCADFWKAVWQEHCSIIVMLTPTKGTNG 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  998 EtglffENCSKYYPMKVDTELTFKGITVKCTNMVKVDGIERRTLCITfgDGVQLT---VTHNLMSSWTYLNTQKTTISII 1074
Cdd:PHA02747  133 E-----EKCYQYWCLNEDGNIDMEDFRIETLKTSVRAKYILTLIEIT--DKILKDsrkISHFQCSEWFEDETPSDHPDFI 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211 1075 SLIQYLNKCKG-------------APIVIHDHDGISRSATIPASIIGYQKIAETSgAFVLTDVIDYIREHRALAISTPGE 1141
Cdd:PHA02747  206 KFIKIIDINRKksgklfnpkdallCPIVVHCSDGVGKTGIFCAVDICLNQLVKRK-AICLAKTAEKIREQRHAGIMNFDD 284

                         330
                  ....*....|....*...
gi 392894211 1142 LSYIDA---VIVRLLAIQ 1156
Cdd:PHA02747  285 YLFIQPgyeVLHYFLSKI 302
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 955-1145 1.70e-09

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: 59.16  E-value: 1.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  955 KEKEKYTEMTPRRNSTIEKFWWMIRQEKVEQVVMTCDFLERNRetglffENCSKYYPMKvdTELTFKGITVKCTNMVKVD 1034
Cdd:cd14551    11 QEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKE------KKCSQYWPDQ--GCWTYGNLRVRVEDTVVLV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211 1035 GIERRTLCIT-----FGDGVQLTVTHNLMSSWTYLNTQKTTISIISL---IQYLNKCKGAPIVIHDHDGISRSATIpASI 1106
Cdd:cd14551    83 DYTTRKFCIQkvnrgIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFlkkVKSANPPRAGPIVVHCSAGVGRTGTF-IVI 161

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 392894211 1107 IGYQKIAETSGAFVLTDVIDYIREHRALAISTPGELSYI 1145
Cdd:cd14551   162 DAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFI 200
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 970-1138 1.87e-09

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: 58.97  E-value: 1.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  970 TIEKFWWMIRQEKVEQVVMTCDFLERNRetglffENCSKYYPMKVDTELTFKGITVKCTNMVKV-DGIERRTLCITFGDG 1048
Cdd:cd14542    26 TVLDFWRMIWEYNVQVIVMACREFEMGK------KKCERYWPEEGEEQLQFGPFKISLEKEKRVgPDFLIRTLKVTFQKE 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211 1049 VQlTVTHNLMSSWTYLNTQKTTISIISLIQYLNKCKGA---PIVIHDHDGISRSATIPAsiIGY-------QKIAEtsgA 1118
Cdd:cd14542   100 SR-TVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSedvPICVHCSAGCGRTGTICA--IDYvwnllktGKIPE---E 173

                         170       180
                  ....*....|....*....|
gi 392894211 1119 FVLTDVIDYIREHRALAIST 1138
Cdd:cd14542   174 FSLFDLVREMRKQRPAMVQT 193
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 909-1145 6.44e-09

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: 57.75  E-value: 6.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  909 TRVILKGYKKQFNDNFLHANYV---TCPDgmRFILMQSPQceilepkpakekekytemtprrNSTIEKFWWMIRQEKVEQ 985
Cdd:cd14548    11 SRVKLIPINEEEGSDYINANYIpgyNSPR--EFIATQGPL----------------------PGTKDDFWRMVWEQNSHT 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  986 VVMTCDFLERNRetglffENCSKYYPMKvDTELTFKGITVKCTNMVKVDGIERRTLCITFGDGVQlTVTHNLMSSWTYLN 1065
Cdd:cd14548    67 IVMLTQCMEKGR------VKCDHYWPFD-QDPVYYGDITVTMLSESVLPDWTIREFKLERGDEVR-SVRQFHFTAWPDHG 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211 1066 TQKTTISIISLI----QYLNKCKGaPIVIHDHDGISRSATIPASIIGYQKIAETSGAFVLTDVIDyIREHRALAISTpgE 1141
Cdd:cd14548   139 VPEAPDSLLRFVrlvrDYIKQEKG-PTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYD-LRKHRPLMVQT--E 214


                  ....
gi 392894211 1142 LSYI 1145
Cdd:cd14548   215 AQYI 218
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 907-1138 6.97e-09

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: 58.30  E-value: 6.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  907 EKTRVILKGYKKQFNDNFLHANYVTCPDGMR-FILMQSPQceilepkpakekekytemtprrNSTIEKFWWMIRQEKVEQ 985
Cdd:cd14603    43 DQTRVILSLLQEEGHSDYINANFIKGVDGSRaYIATQGPL----------------------SHTVLDFWRMIWQYGVKV 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  986 VVMTCdflernRETGLFFENCSKYYPMKVDTeLTFKGITVKCTNMVKVDG-IERRTLCITFGDgVQLTVTHNLMSSWTYL 1064
Cdd:cd14603   101 ILMAC------REIEMGKKKCERYWAQEQEP-LQTGPFTITLVKEKRLNEeVILRTLKVTFQK-ESRSVSHFQYMAWPDH 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211 1065 NTQKTTISIISLIQYLNKCKGA---PIVIHDHDGISRSATIPA-----SIIGYQKIAETsgaFVLTDVIDYIREHRALAI 1136
Cdd:cd14603   173 GIPDSPDCMLAMIELARRLQGSgpePLCVHCSAGCGRTGVICTvdyvrQLLLTQRIPPD---FSIFDVVLEMRKQRPAAV 249


                  ..
gi 392894211 1137 ST 1138
Cdd:cd14603   250 QT 251
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 903-1114 1.34e-07

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: 53.77  E-value: 1.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  903 NPLiekTRVILKgyKKQFND---NFLHANYVTCPDGMR--FILMQSPQCeilepkpakekekytemtprrnSTIEKFWWM 977
Cdd:cd14611    11 NPH---SRVCLK--PKNSNDslsTYINANYIRGYGGKEkaFIATQGPMI----------------------NTVNDFWQM 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  978 IRQEKVEQVVMTCDFLERNretglffENCSKYYPMKvdtELTFKGITVKCTNMVKVDGIERRTLCITFGDGVQlTVTHNL 1057
Cdd:cd14611    64 VWQEDSPVIVMITKLKEKN-------EKCVLYWPEK---RGIYGKVEVLVNSVKECDNYTIRNLTLKQGSQSR-SVKHYW 132

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392894211 1058 MSSWTylnTQKTTISIISLIQYLNKCK--------GAPIVIHDHDGISRSATIPASIIGYQKIAE 1114
Cdd:cd14611   133 YTSWP---DHKTPDSAQPLLQLMLDVEedrlaspgRGPVVVHCSAGIGRTGCFIATTIGCQQLKE 194
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 904-1138 1.45e-07

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 54.62  E-value: 1.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  904 PLIEKTRVILKGYKKqfNDNFLHANYVtcpDGM----RFILMQSPqceiLEpkpakekekytemtprrnSTIEKFWWMIR 979
Cdd:PHA02742   62 PCFDRNRVILKIEDG--GDDFINASYV---DGHnakgRFICTQAP----LE------------------ETALDFWQAIF 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  980 QEKVEQVVMTCDFLERNRETglffenCSKYYPMKVDTELTFKGITVKCTNMVKVDGIERRTLCIT-FGDGVQLTVTHNLM 1058
Cdd:PHA02742  115 QDQVRVIVMITKIMEDGKEA------CYPYWMPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTdTNTGASLDIKHFAY 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211 1059 SSWTY--------------LNTQKTTISIISLIQYLNKCKGAPIVIHDHDGISRSATIPASIIGYQKIAETSGAFVLTDV 1124
Cdd:PHA02742  189 EDWPHgglprdpnkfldfvLAVREADLKADVDIKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIV 268

                         250
                  ....*....|....*
gi 392894211 1125 IDYIRE-HRALAIST 1138
Cdd:PHA02742  269 RDLRKQrHNCLSLPQ 283
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 969-1138 2.28e-07

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: 52.76  E-value: 2.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  969 STIEKFWWMIRQEKVEQVVMtcdfLERNRETGLFfeNCSKYYPMKVDTELTFKG-ITVKCTNMVKVDGIERRTLCIT-FG 1046
Cdd:cd14538    27 NTTGDFWQMVWEQKSEVIAM----VTQDVEGGKV--KCHRYWPDSLNKPLICGGrLEVSLEKYQSLQDFVIRRISLRdKE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211 1047 DGVQLTVTHNLMSSWTYLNTQKTTISIISLIQYLNKC-KGAPIVIHDHDGISRSATIPA--SIIGYqkiAETSGAFVLTD 1123
Cdd:cd14538   101 TGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIhNSGPIVVHCSAGIGRTGVLITidVALGL---IERDLPFDIQD 177

                         170
                  ....*....|....*
gi 392894211 1124 VIDYIREHRALAIST 1138
Cdd:cd14538   178 IVKDLREQRQGMIQT 192
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 969-1112 2.86e-07

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: 53.33  E-value: 2.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  969 STIEKFWWMIRQEKVEQVVMTCDFLERNretglffENCSKYYPMKvdtELTFKGITVKCTNMVKVDGIERRTLCITFGdG 1048
Cdd:cd14613    81 NTVGDFWRMVWQERSPIIVMITNIEEMN-------EKCTEYWPEE---QVTYEGIEITVKQVIHADDYRLRLITLKSG-G 149

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211 1049 VQLTVTHNLMSSWTYLNTQKTTISIISLIQYLNKC------KGAPIVIHDHDGISRSATIPASIIGYQKI 1112
Cdd:cd14613   150 EERGLKHYWYTSWPDQKTPDNAPPLLQLVQEVEEArqqaepNCGPVIVHCSAGIGRTGCFIATSICCKQL 219
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 970-1132 4.94e-07

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: 51.93  E-value: 4.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  970 TIEKFWWMIRQEKVEQVVMTCDFLERNRetglffENCSKYYPmkVDTELTFKGITVKCTNMVKVDGIERRTLCITFGDGV 1049
Cdd:cd14622    27 TVEDFWRMVWEWKCHTIVMLTELQEREQ------EKCVQYWP--SEGSVTHGEITIEIKNDTLLETISIRDFLVTYNQEK 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211 1050 QLTVTHNL-MSSWTYLNTQ---KTTISIISLIQYLNKCKGA-PIVIHDHDGISRSATipasIIGYQKIAETSGAFVLTDV 1124
Cdd:cd14622    99 QTRLVRQFhFHGWPEIGIPaegKGMIDLIAAVQKQQQQTGNhPIVVHCSAGAGRTGT----FIALSNILERVKAEGLLDV 174


                  ....*...
gi 392894211 1125 IDYIREHR 1132
Cdd:cd14622   175 FQTVKSLR 182
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 955-1145 8.59e-07

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: 50.98  E-value: 8.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  955 KEKEKYTEMTPRRNSTIEKFWWMIRQEKVEQVVMTCDFLERNRetglffENCSKYYPMKVDTELTFKGITVKCTNMVKVD 1034
Cdd:cd14557    11 KEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNR------NKCAQYWPSMEEGSRAFGDVVVKINEEKICP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211 1035 GIERRTLCITFG--DGVQLTVTHNLMSSWTYLNTQKTTISIISLIQYLNKCKGA---PIVIHDHDGISRSATipasIIGY 1109
Cdd:cd14557    85 DYIIRKLNINNKkeKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFfsgPIVVHCSAGVGRTGT----YIGI 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 392894211 1110 QKIAETSGAFVLTDVIDYI---REHRALAISTpgELSYI 1145
Cdd:cd14557   161 DAMLEGLEAEGRVDVYGYVvklRRQRCLMVQV--EAQYI 197
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 969-1138 1.19e-06

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: 50.46  E-value: 1.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  969 STIEKFWWMIRQEKVEQVVMTCDFLERNRetglffENCSKYYPMKVDTELTFKGITVKCTNMVKVD-GIERRtLCITFGD 1047
Cdd:cd14539    26 GTAADFWLMVYEQQVSVIVMLVSEQENEK------QKVHRYWPTERGQALVYGAITVSLQSVRTTPtHVERI-ISIQHKD 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211 1048 GVQL-TVTHNLMSSWTYLNTQKTTISIISLIQ----YLNKCKG--APIVIHDHDGISRSATIPASIIGYQKIAETSGAFV 1120
Cdd:cd14539    99 TRLSrSVVHLQFTTWPELGLPDSPNPLLRFIEevhsHYLQQRSlqTPIVVHCSSGVGRTGAFCLLYAAVQEIEAGNGIPD 178

                         170
                  ....*....|....*...
gi 392894211 1121 LTDVIDYIREHRALAIST 1138
Cdd:cd14539   179 LPQLVRKMRQQRKYMLQE 196
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 867-1156 1.28e-06

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: 51.86  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  867 DFMKF--FKTSYE-NKVANMQSPEVSDLVKKHemdlRVANPL-IEKTRVILKGYKKQFNDNFLHANYVTCPDGMR-FILM 941
Cdd:cd14604    30 DFMRLrrLSTKYRtEKIYPTATGEKEENVKKN----RYKDILpFDHSRVKLTLKTSSQDSDYINANFIKGVYGPKaYIAT 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  942 QSPQCeilepkpakekekytemtprrnSTIEKFWWMIRQEKVEQVVMTCDFLERNRetglffENCSKYYPMKVDTELTFK 1021
Cdd:cd14604   106 QGPLA----------------------NTVIDFWRMIWEYNVAIIVMACREFEMGR------KKCERYWPLYGEEPMTFG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211 1022 GITVKCTNMVKVDGIERRTLCITFGDGvqltvTHNLmSSWTYLN--------TQKTTISIISLIQYLNKCKGAPIVIHDH 1093
Cdd:cd14604   158 PFRISCEAEQARTDYFIRTLLLEFQNE-----TRRL-YQFHYVNwpdhdvpsSFDSILDMISLMRKYQEHEDVPICIHCS 231

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392894211 1094 DGISRSATIPAsiIGYQ----KIAETSGAFVLTDVIDYIREHRALAISTPGELSYIDAVIVRLLAIQ 1156
Cdd:cd14604   232 AGCGRTGAICA--IDYTwnllKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLFEKQ 296
PHA02738 PHA02738
hypothetical protein; Provisional
 909-1145 1.86e-06

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 51.46  E-value: 1.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  909 TRVILKGYKKQfnDNFLHANYVtcpDGM----RFILMQSPQceilepkpakekekytemtprrNSTIEKFWWMIRQEKVE 984
Cdd:PHA02738   64 SRVILPAERNR--GDYINANYV---DGFeykkKFICGQAPT----------------------RQTCYDFYRMLWMEHVQ 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  985 QVVMTCDFLERNREtglffeNCSKYYPMKVDTELTFKGITVKCTNMVKVDGIERRTLCITFGDGVQLTVTHNLMSSWTYL 1064
Cdd:PHA02738  117 IIVMLCKKKENGRE------KCFPYWSDVEQGSIRFGKFKITTTQVETHPHYVKSTLLLTDGTSATQTVTHFNFTAWPDH 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211 1065 NTQKTTISIISLIQYLNKCKG----------------APIVIHDHDGISRsatipasiigyqkiaetSGAFVLTDvIDYI 1128
Cdd:PHA02738  191 DVPKNTSEFLNFVLEVRQCQKelaqeslqighnrlqpPPIVVHCNAGLGR-----------------TPCYCVVD-ISIS 252

                         250
                  ....*....|....*..
gi 392894211 1129 REHRALAISTPGELSYI 1145
Cdd:PHA02738  253 RFDACATVSIPSIVSSI 269
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 969-1104 3.16e-06

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: 49.31  E-value: 3.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  969 STIEKFWWMIRQEKVEQVVMTCDFLERNRETglffenCSKYYPmkvDTELTFKGITVKCTNMVKVDGIERRTLCITFGDG 1048
Cdd:cd14558    25 DTIADFWQMIFQKKVKVIVMLTELKEGDQEQ------CAQYWG---DEKKTYGDIEVELKDTEKSPTYTVRVFEITHLKR 95

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392894211 1049 VQ-LTVTHNLMSSWTYL---NTQKTTISIISLIQ----YLNKCKG--APIVIHDHDGISRSATIPA 1104
Cdd:cd14558    96 KDsRTVYQYQYHKWKGEelpEKPKDLVDMIKSIKqklpYKNSKHGrsVPIVVHCSDGSSRTGIFCA 161
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 970-1145 4.82e-06

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: 49.50  E-value: 4.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  970 TIEKFWWMIRQEKVEQVVMTCDFLERNRetglffENCSKYYPMKvDTELTFKGITVKCTNMVKVDGIERRTLCITFGDGV 1049
Cdd:cd14614    67 TRNDFWKMVLQQKSQIIVMLTQCNEKRR------VKCDHYWPFT-EEPVAYGDITVEMLSEEEQPDWAIREFRVSYADEV 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211 1050 QlTVTHNLMSSW-----TYLNTQKTTISIISLI-QYLNKCKGaPIVIHDHDGISRSATIPASIIGYQKIAETSGAFVLTD 1123
Cdd:cd14614   140 Q-DVMHFNYTAWpdhgvPTANAAESILQFVQMVrQQAVKSKG-PMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGL 217

                         170       180
                  ....*....|....*....|..
gi 392894211 1124 VIDyIREHRALAISTPGELSYI 1145
Cdd:cd14614   218 VSE-MRSYRMSMVQTEEQYIFI 238
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 955-1145 5.42e-06

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: 49.17  E-value: 5.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  955 KEKEKYTEMTPRRNSTIEKFWWMIRQEKVEQVVMTCDFLERNRetglffENCSKYYPMKvdTELTFKGITVKCTNMVKVD 1034
Cdd:cd14620    35 KEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKE------EKCYQYWPDQ--GCWTYGNIRVAVEDCVVLV 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211 1035 GIERRTLCI----TFGDGVQLTVTHNLMSSWTYLNTQKTTISIISL---IQYLNKCKGAPIVIHDHDGISRSATipasII 1107
Cdd:cd14620   107 DYTIRKFCIqpqlPDGCKAPRLVTQLHFTSWPDFGVPFTPIGMLKFlkkVKSVNPVHAGPIVVHCSAGVGRTGT----FI 182

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 392894211 1108 GYQKIAETSGAFVLTDVIDY---IREHRALAISTPGELSYI 1145
Cdd:cd14620   183 VIDAMIDMMHAEQKVDVFEFvsrIRNQRPQMVQTDMQYSFI 223
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 909-1102 5.42e-06

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: 49.38  E-value: 5.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  909 TRVILKGYKKQ--FNDnFLHANYVTCPDgmrfilmqspqceiLEPKPAKEKEKYTEMTPRRNSTIEKFWWMIRQEKVEQV 986
Cdd:cd14544    16 TRVILKDRDPNvpGSD-YINANYIRNEN--------------EGPTTDENAKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  987 VMTCDFLERNRetglffENCSKYYPMKVDTElTFKGITVKCTNMVKVDGIERRTLCITFGDGVQLT--VTHNLMSSWTYL 1064
Cdd:cd14544    81 VMTTKEVERGK------NKCVRYWPDEGMQK-QYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDPIreIWHYQYLSWPDH 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 392894211 1065 NTQKTTISIISLIQYLNKCKGA-----PIVIHDHDGISRSATI 1102
Cdd:cd14544   154 GVPSDPGGVLNFLEDVNQRQESlphagPIVVHCSAGIGRTGTF 196
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 924-1149 6.03e-06

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: 48.44  E-value: 6.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  924 FLHANYVtcpDGMrfilmQSPQCEILEPKPAKekekytemtprrnSTIEKFWWMIRQEKVEQVVMTCDFLERNRetglff 1003
Cdd:cd17668     1 YINANYV---DGY-----NKPKAYIAAQGPLK-------------STAEDFWRMIWEHNVEVIVMITNLVEKGR------ 53

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211 1004 ENCSKYYPMKVDTELTFKGITVKCTNMVKVDGIERRTLCIT-------FGDGVQLTVTHNLMSSWTYLNTQKTTISIISL 1076
Cdd:cd17668    54 RKCDQYWPADGSEEYGNFLVTQKSVQVLAYYTVRNFTLRNTkikkgsqKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTF 133

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392894211 1077 IQYLNKCKGA---PIVIHDHDGISRSATIPASIIGYQKIAEtSGAFVLTDVIDYIREHRALAISTPGELSYI-DAVI 1149
Cdd:cd17668   134 VRKASYAKRHavgPVVVHCSAGVGRTGTYIVLDSMLQQIQH-EGTVNIFGFLKHIRSQRNYLVQTEEQYVFIhDALV 209
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 909-1145 6.08e-06

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: 49.04  E-value: 6.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  909 TRVILKGYKKQFNDnFLHANYVtcPDGMR---FILMQSPqceilepkpakekekytemTPrrnSTIEKFWWMIRQEKVEQ 985
Cdd:cd14615    12 SRVKLSVQSHSTDD-YINANYM--PGYNSkkeFIAAQGP-------------------LP---NTVKDFWRMVWEKNVYA 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  986 VVMTCDFLERNRetglffENCSKYYPMKvdTELTFKGITVKCTNMVKVDGIERRTLCITFGDGVQL-TVTHNLMSSWTYL 1064
Cdd:cd14615    67 IVMLTKCVEQGR------TKCEEYWPSK--QKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESrTVRHFHFTSWPDH 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211 1065 NTQKTTISIIS----LIQYLNKC-KGAPIVIHDHDGISRSAT-IPASIIGYQkiAETSGAFVLTDVIDYIREHRALAIST 1138
Cdd:cd14615   139 GVPETTDLLINfrhlVREYMKQNpPNSPILVHCSAGVGRTGTfIAIDRLIYQ--IENENVVDVYGIVYDLRMHRPLMVQT 216


                  ....*..
gi 392894211 1139 pgELSYI 1145
Cdd:cd14615   217 --EDQYV 221
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 970-1104 7.96e-06

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: 48.03  E-value: 7.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  970 TIEKFWWMIRQEKVEQVVMTCDFLERNRetglffENCSKYYPmkVDTELTFKGITVKCTNMVKVDGIERRTLCITFGDGV 1049
Cdd:cd14552    26 TVEDFWRMIWEWKSCSIVMLTEIKERSQ------NKCAQYWP--EDGSVSSGDITVELKDQTDYEDYTLRDFLVTKGKGG 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211 1050 QLTVTHNL-MSSWTYL---NTQKTTISIISLIQYLNKCKG-APIVIHDHDGISRSATIPA 1104
Cdd:cd14552    98 STRTVRQFhFHGWPEVgipDNGKGMIDLIAAVQKQQQQSGnHPITVHCSAGAGRTGTFCA 157
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 969-1153 1.07e-05

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: 48.35  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  969 STIEKFWWMIRQEKVEQVVMTCDFLERNRetglffENCSKYYPMKVdTELTFKGITVKCTN-MVKVDGIERRTLCITFGD 1047
Cdd:cd14619    51 QTVGDFWRMIWEQQSSTIVMLTNCMEAGR------VKCEHYWPLDY-TPCTYGHLRVTVVSeEVMENWTVREFLLKQVEE 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211 1048 GVQLTVTHNLMSSWTYLNTQKTTISIIS----LIQYLN-KCKGAPIVIHDHDGISRSATIPASIIGYQKIaETSGAFVLT 1122
Cdd:cd14619   124 QKTLSVRHFHFTAWPDHGVPSSTDTLLAfrrlLRQWLDqTMSGGPTVVHCSAGVGRTGTLIALDVLLQQL-QSEGLLGPF 202

                         170       180       190
                  ....*....|....*....|....*....|.
gi 392894211 1123 DVIDYIREHRALAISTPGELSYIDAVIVRLL 1153
Cdd:cd14619   203 SFVQKMRENRPLMVQTESQYVFLHQCILDFL 233
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 970-1150 1.43e-05

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: 47.63  E-value: 1.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  970 TIEKFWWMIRQEKVEQVVMTCDFLERNRETglffenCSKYYPMKVdTELTFKGITVKCTNMVKVDGIERRTLCITFGD-G 1048
Cdd:cd14618    52 TIEDFWRLVWEQQVCNIIMLTVGMENGRVL------CDHYWPSES-TPVSYGHITVHLLAQSSEDEWTRREFKLWHEDlR 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211 1049 VQLTVTHNLMSSWTYLNTQKTTISIISLIQ----YLNKCKGA-PIVIHDHDGISRSATIPASIIGYQKIAETSGAFVLtD 1123
Cdd:cd14618   125 KERRVKHLHYTAWPDHGIPESTSSLMAFRElvreHVQATKGKgPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVF-N 203

                         170       180
                  ....*....|....*....|....*..
gi 392894211 1124 VIDYIREHRALAISTPGELSYIDAVIV 1150
Cdd:cd14618   204 TVYILRMHRYLMIQTLSQYIFLHSCIL 230
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 907-1130 1.46e-05

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: 48.09  E-value: 1.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  907 EKTRVIL-KGYKKQFNDNFLHANYVTcpdgmrfilmqsPQCEIlEPKPAKEKEKYTEMTPRRNSTIEKFWWMIRQEKVEQ 985
Cdd:cd14605    15 DHTRVVLhDGDPNEPVSDYINANIIM------------PEFET-KCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  986 VVMTCDFLERNRetglffENCSKYYPmkvdTELTFKGITVKCTNMVKV----DGIERRTLCITFGDG-VQLTVTHNLMSS 1060
Cdd:cd14605    82 IVMTTKEVERGK------SKCVKYWP----DEYALKEYGVMRVRNVKEsaahDYILRELKLSKVGQGnTERTVWQYHFRT 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392894211 1061 WTYLNTQKTTISIISLIQYLNK-----CKGAPIVIHDHDGISRsatipasiigyqkiaetSGAFVLTDV-IDYIRE 1130
Cdd:cd14605   152 WPDHGVPSDPGGVLDFLEEVHHkqesiMDAGPVVVHCSAGIGR-----------------TGTFIVIDIlIDIIRE 210
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 969-1101 1.56e-05

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: 47.32  E-value: 1.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  969 STIEKFWWMIRQEKVEQVVMTCDfLERNretglffENCSKYYPMKvDTELTFKGITVKCTN-MVKVDGIERRTLCITF-- 1045
Cdd:cd14550    25 HTIKDFWQMIWDHNSQTIVMLTD-NELN-------EDEPIYWPTK-EKPLECETFKVTLSGeDHSCLSNEIRLIVRDFil 95

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211 1046 ---GDGVQLTVTHNLMSSWTYLNT-QKTTISIISLIQYLNKCKGAPIVIHDHDGISRSAT 1101
Cdd:cd14550    96 estQDDYVLEVRQFQCPSWPNPCSpIHTVFELINTVQEWAQQRDGPIVVHDRYGGVQAAT 155
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 909-1152 1.65e-05

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: 47.92  E-value: 1.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  909 TRVILKGykkqfNDNFLHANYVTcpdgmrfilMQSPQCEILEpkpakekeKYTEMTPRRNSTIEKFWWMIRQEKVEQVVM 988
Cdd:cd14600    55 TRVVLQG-----NEDYINASYVN---------MEIPSANIVN--------KYIATQGPLPHTCAQFWQVVWEQKLSLIVM 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  989 TCDFLERNRetglffENCSKYYPMKVDTeLTFKGITVKC-TNMVKVDGIERRTLCITFGDGVQLTVTHNLMSSWTYLNTQ 1067
Cdd:cd14600   113 LTTLTERGR------TKCHQYWPDPPDV-MEYGGFRVQChSEDCTIAYVFREMLLTNTQTGEERTVTHLQYVAWPDHGVP 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211 1068 KTTISIISLIQYLN--KCKGAPIVIHDHDGISRSATIPASIIGYQKIAETSGAFVLtDVIDYIREHRALAISTPGELSYI 1145
Cdd:cd14600   186 DDSSDFLEFVNYVRskRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPL-DIVRKMRDQRAMMVQTSSQYKFV 264


                  ....*..
gi 392894211 1146 DAVIVRL 1152
Cdd:cd14600   265 CEAILRV 271
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 955-1101 4.43e-05

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: 46.94  E-value: 4.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  955 KEKEKYTEMTPRRNSTIEKFWWMIRQEKVEQVVMTCDFLERnRETglffeNCSKYYPMKvdTELTFKGITVKCTNMVKVD 1034
Cdd:cd14621    92 QEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKER-KEC-----KCAQYWPDQ--GCWTYGNIRVSVEDVTVLV 163

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392894211 1035 GIERRTLCI-TFGDGV----QLTVTHNLMSSWTYLNTQKTTISIISLIQYLNKCK---GAPIVIHDHDGISRSAT 1101
Cdd:cd14621   164 DYTVRKFCIqQVGDVTnkkpQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNpqyAGAIVVHCSAGVGRTGT 238
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 907-1102 4.98e-05

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: 46.41  E-value: 4.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  907 EKTRVILKGYKKQF-NDNFLHANYVTCPdgmrfiLMQSPQCeilePKpakekeKYTEMTPRRNSTIEKFWWMIRQEKVEQ 985
Cdd:cd14606    31 DHSRVILQGRDSNIpGSDYINANYVKNQ------LLGPDEN----AK------TYIASQGCLEATVNDFWQMAWQENSRV 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  986 VVMTCDFLERNRetglffENCSKYYPmKVDTELTFKGITVKctNMVKVDGIER--RTLCITFGDGVQLT--VTHNLMSSW 1061
Cdd:cd14606    95 IVMTTREVEKGR------NKCVPYWP-EVGMQRAYGPYSVT--NCGEHDTTEYklRTLQVSPLDNGELIreIWHYQYLSW 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 392894211 1062 TYLNTQKTTISIISLIQYLNKC-----KGAPIVIHDHDGISRSATI 1102
Cdd:cd14606   166 PDHGVPSEPGGVLSFLDQINQRqeslpHAGPIIVHCSAGIGRTGTI 211
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 969-1101 5.26e-05

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: 45.92  E-value: 5.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  969 STIEKFWWMIRQEKVEQVVMTCDFLERNRETglffeNCSKYYPMKVDTELTFKGITVKCTNMVKVD-GIERRTLCITFGD 1047
Cdd:cd17658    27 HTFEDFWEMVIQQRCPVIIMLTRLVDNYSTA-----KCADYFPAEENESREFGRISVTNKKLKHSQhSITLRVLEVQYIE 101

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 392894211 1048 GVQ--LTVTHNLMSSWTYLNTQKTTISIISLIQ--YLNKCKGAPIVIHDHDGISRSAT 1101
Cdd:cd17658   102 SEEppLSVLHIQYPEWPDHGVPKDTRSVRELLKrlYGIPPSAGPIVVHCSAGIGRTGA 159
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 907-1104 5.29e-04

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: 43.11  E-value: 5.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  907 EKTRVILKGYKKQFNDNFLHANYVtcpDGMRfilmqspqceilepkpakEKEKYTEMTPRRNSTIEKFWWMIRQEKVEQV 986
Cdd:cd14623     9 EFNRVIIPVKRGEENTDYVNASFI---DGYR------------------QKDSYIASQGPLQHTIEDFWRMIWEWKSCSI 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  987 VMTCDFLERNRetglffENCSKYYPmkVDTELTFKGITVKCTNMVKVDGIERRTLCITFG-DGVQLTVTHNLMSSWTYL- 1064
Cdd:cd14623    68 VMLTELEERGQ------EKCAQYWP--SDGSVSYGDITIELKKEEECESYTVRDLLVTNTrENKSRQIRQFHFHGWPEVg 139

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 392894211 1065 --NTQKTTISIISLIQYLNKCKGA-PIVIHDHDGISRSATIPA 1104
Cdd:cd14623   140 ipSDGKGMINIIAAVQKQQQQSGNhPITVHCSAGAGRTGTFCA 182
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 969-1145 5.29e-04

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: 42.72  E-value: 5.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  969 STIEKFWWMIRQEKVEQVVMTCDFLERNRetglffENCSKYYPMkvDTELTFKGITVKCTNMVKVDGIERRTLCI----- 1043
Cdd:cd14549    25 STFDDFWRMVWEQNSAIIVMITNLVERGR------RKCDQYWPK--EGTETYGNIQVTLLSTEVLATYTVRTFSLknlkl 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211 1044 --TFGDGVQLTVTHNLMSSWTYLNTQKTTISIISLIQ---YLNKCKGAPIVIHDHDGISRSAT---IPASIigyQKIAET 1115
Cdd:cd14549    97 kkVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRkssAANPPGAGPIVVHCSAGVGRTGTyivIDSML---QQIQDK 173

                         170       180       190
                  ....*....|....*....|....*....|
gi 392894211 1116 SGAFVLtDVIDYIREHRALAISTpgELSYI 1145
Cdd:cd14549   174 GTVNVF-GFLKHIRTQRNYLVQT--EEQYI 200
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 910-1149 9.44e-04

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: 42.32  E-value: 9.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  910 RVILKGYKKQFNDNFLHANYVtcpDGMrfilmQSPQCEILEPKPAKEkekytemtprrnsTIEKFWWMIRQEKVEQVVMT 989
Cdd:cd14631     1 RVILQPVEDDPSSDYINANYI---DGY-----QRPSHYIATQGPVHE-------------TVYDFWRMIWQEQSACIVMV 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  990 CDFLERNRetglffENCSKYYPMkvDTELtFKGITVKCTNM-------VKVDGIERRtlciTFGDGVQLTVTHnlMSSWT 1062
Cdd:cd14631    60 TNLVEVGR------VKCYKYWPD--DTEV-YGDFKVTCVEMeplaeyvVRTFTLERR----GYNEIREVKQFH--FTGWP 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211 1063 YLNTQKTTISIISLIQYL---NKCKGAPIVIHDHDGISRSAT-IPASIIgyQKIAETSGAFVLTDVIDYIREHRALAIST 1138
Cdd:cd14631   125 DHGVPYHATGLLSFIRRVklsNPPSAGPIVVHCSAGAGRTGCyIVIDIM--LDMAEREGVVDIYNCVKALRSRRINMVQT 202

                         250
                  ....*....|..
gi 392894211 1139 PGELSYI-DAVI 1149
Cdd:cd14631   203 EEQYIFIhDAIL 214
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 969-1153 1.10e-03

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: 42.33  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  969 STIEKFWWMIRQEKVEQVVMTCDFLERNRetglffENCSKYYPMKVDTELTFKGITVKCTNMVKVDGIERRTLCIT---- 1044
Cdd:cd17667    83 STFEDFWRMIWEQNTGIIVMITNLVEKGR------RKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTkvkk 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211 1045 ------FGDGVQLTVTHNLMSSWTYLNTQKTTISIISLIQYLNKCKG---APIVIHDHDGISRSATIPASIIGYQKIAET 1115
Cdd:cd17667   157 gqkgnpKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTpemGPVLVHCSAGVGRTGTYIVIDSMLQQIKDK 236

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 392894211 1116 SGAFVLtDVIDYIREHRALAISTPGELSYI-DAVIVRLL 1153
Cdd:cd17667   237 STVNVL-GFLKHIRTQRNYLVQTEEQYIFIhDALLEAIL 274
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 955-1144 1.58e-03

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: 41.88  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  955 KEKEKYTEMT--PRRNsTIEKFWWMIRQEKVEQVVMTCDFLERNRetglffENCSKYYPMKVDTELTFKGiTVKCTNMVK 1032
Cdd:cd14607    59 EEAQRSYILTqgPLPN-TCCHFWLMVWQQKTKAVVMLNRIVEKDS------VKCAQYWPTDEEEVLSFKE-TGFSVKLLS 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211 1033 VDGIERRTLCI----TFGDGVQLTVTHNLMSSWTYLNTQKttiSIISLIQYLNKCKGA--------PIVIHDHDGISRSA 1100
Cdd:cd14607   131 EDVKSYYTVHLlqleNINSGETRTISHFHYTTWPDFGVPE---SPASFLNFLFKVRESgslspehgPAVVHCSAGIGRSG 207

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 392894211 1101 TIPASIIGYQKIAETSGAFV-LTDVIDYIREHRALAISTPGELSY 1144
Cdd:cd14607   208 TFSLVDTCLVLMEKKDPDSVdIKQVLLDMRKYRMGLIQTPDQLRF 252
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 909-1045 3.97e-03

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: 40.46  E-value: 3.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  909 TRVILKGYKKQFNDNFLHANYVtcpDGMR----FILMQSPQCEilepkpakekekytemtprrnsTIEKFWWMIRQEKVE 984
Cdd:cd14553    18 SRVILQPIEGVPGSDYINANYC---DGYRkqnaYIATQGPLPE----------------------TFGDFWRMVWEQRSA 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392894211  985 QVVMTCDFLERNRetglffENCSKYYPMKvDTElTFKGITVKCtnmvkVDGIERRTLCI-TF 1045
Cdd:cd14553    73 TIVMMTKLEERSR------VKCDQYWPTR-GTE-TYGLIQVTL-----LDTVELATYTVrTF 121
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 970-1104 4.74e-03

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: 40.21  E-value: 4.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894211  970 TIEKFWWMIRQEKVEQVVMTCDFLERNRetglffENCSKYYPMKVDTELTFKGITVKCTNMVKVDGIERRTLCITFGDGV 1049
Cdd:cd14602    53 TLLDFWRMIWEYSVLIIVMACMEFEMGK------KKCERYWAEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSET 126

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 392894211 1050 QlTVTHNLMSSWTYLNTQKTTISIISLI---QYLNKCKGAPIVIHDHDGISRSATIPA 1104
Cdd:cd14602   127 R-TIYQFHYKNWPDHDVPSSIDPILELIwdvRCYQEDDSVPICIHCSAGCGRTGVICA 183
 
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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