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Conserved domains on  [gi|119576022|gb|EAW55618|]
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protein tyrosine phosphatase, non-receptor type 18 (brain-derived), isoform CRA_b [Homo sapiens]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 32-185 7.88e-111

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


The actual alignment was detected with superfamily member cd14603:

Pssm-ID: 475123 [Multi-domain]  Cd Length: 266  Bit Score: 323.70  E-value: 7.88e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  32 KRCERYWAQEQEPLQTGLFCITLIKEKWLNEDIMLRTLKVTFQKESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARRLQ 111
Cdd:cd14603  113 KKCERYWAQEQEPLQTGPFTITLVKEKRLNEEVILRTLKVTFQKESRSVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQ 192

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119576022 112 GSGPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIPPDFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTVAQMF 185
Cdd:cd14603  193 GSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQMF 266
 
Name Accession Description Interval E-value
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 32-185 7.88e-111

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: 323.70  E-value: 7.88e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  32 KRCERYWAQEQEPLQTGLFCITLIKEKWLNEDIMLRTLKVTFQKESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARRLQ 111
Cdd:cd14603  113 KKCERYWAQEQEPLQTGPFTITLVKEKRLNEEVILRTLKVTFQKESRSVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQ 192

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119576022 112 GSGPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIPPDFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTVAQMF 185
Cdd:cd14603  193 GSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQMF 266
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
32-183 1.48e-56

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 183.98  E-value: 1.48e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022   32 KRCERYWAQEQE-PLQTGLFCITLIKEKWLNEDIMLRTLKVTF--QKESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEAR 108
Cdd:pfam00102  82 EKCAQYWPEEEGeSLEYGDFTVTLKKEKEDEKDYTVRTLEVSNggSEETRTVKHFHYTGWPDHGVPESPNSLLDLLRKVR 161

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119576022  109 RLQGSGPE-PLCVHCSAGCGRTGVLCTVDYVRQLLLTQmipPDFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTVAQ 183
Cdd:pfam00102 162 KSSLDGRSgPIVVHCSAGIGRTGTFIAIDIALQQLEAE---GEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
32-183 8.42e-54

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 177.85  E-value: 8.42e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022    32 KRCERYWAQEQ-EPLQTGLFCITLIKEKWLnEDIMLRTLKVTF--QKESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEAR 108
Cdd:smart00194 109 EKCAQYWPDEEgEPLTYGDITVTLKSVEKV-DDYTIRTLEVTNtgCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVR 187

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119576022   109 RLQGSGPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQmipPDFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTVAQ 183
Cdd:smart00194 188 KSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAG---KEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
24-177 7.52e-21

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 90.92  E-value: 7.52e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  24 AVLAG--EFSKR---CERYW-AQEQEPLQTglFCITLIKEKWLNEDIMLRTLKVTFQ---KESRSVYQLQYMSWPDRGVP 94
Cdd:COG5599  106 VVLASddEISKPkvkMPVYFrQDGEYGKYE--VSSELTESIQLRDGIEARTYVLTIKgtgQKKIEIPVLHVKNWPDHGAI 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  95 SSP--DHMLAMVEEARRLQGSGPEPLCVHCSAGCGRTGVLCTVDYVRQlLLTQMIPPDFSLFDVVLKMRKQR-PAAVQTE 171
Cdd:COG5599  184 SAEalKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSK-SINALVQITLSVEEIVIDMRTSRnGGMVQTS 262


                 ....*.
gi 119576022 172 EQYRFL 177
Cdd:COG5599  263 EQLDVL 268
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 32-193 1.66e-16

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 79.30  E-value: 1.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  32 KRCERYWAQEQE-PLQTGLFCIT---LIKEKWLNEDIMLRTLKVTfqKESRSVYQLQYMSWPDRGVPSSPDHMLAMV--- 104
Cdd:PHA02746 152 EKCFELWTKEEDsELAFGRFVAKildIIEELSFTKTRLMITDKIS--DTSREIHHFWFPDWPDNGIPTGMAEFLELInkv 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022 105 -EEARRL------QGSGPEPLCVHCSAGCGRTGVLCTVD-YVRQLLLTQMIppdfSLFDVVLKMRKQRPAAVQTEEQYRF 176
Cdd:PHA02746 230 nEEQAELikqadnDPQTLGPIVVHCSAGIGRAGTFCAIDnALEQLEKEKEV----CLGEIVLKIRKQRHSSVFLPEQYAF 305

                        170
                 ....*....|....*..
gi 119576022 177 LYHTVAQMFCSTLQNAS 193
Cdd:PHA02746 306 CYKALKYAIIEEAKKKF 322
 
Name Accession Description Interval E-value
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 32-185 7.88e-111

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: 323.70  E-value: 7.88e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  32 KRCERYWAQEQEPLQTGLFCITLIKEKWLNEDIMLRTLKVTFQKESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARRLQ 111
Cdd:cd14603  113 KKCERYWAQEQEPLQTGPFTITLVKEKRLNEEVILRTLKVTFQKESRSVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQ 192

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119576022 112 GSGPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIPPDFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTVAQMF 185
Cdd:cd14603  193 GSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQMF 266
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 32-179 6.90e-93

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: 275.84  E-value: 6.90e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  32 KRCERYWAQEQEP-LQTGLFCITLIKEKWLNEDIMLRTLKVTFQKESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARRL 110
Cdd:cd14542   54 KKCERYWPEEGEEqLQFGPFKISLEKEKRVGPDFLIRTLKVTFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDY 133

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119576022 111 QGSGPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIPPDFSLFDVVLKMRKQRPAAVQTEEQYRFLYH 179
Cdd:cd14542  134 QGSEDVPICVHCSAGCGRTGTICAIDYVWNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 32-185 5.51e-59

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: 190.44  E-value: 5.51e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  32 KRCERYWAQE-QEPLQTGLFCITLIKEKWLNEDImLRTLKVTFQKESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARRL 110
Cdd:cd14602   81 KKCERYWAEPgEMQLEFGPFSVTCEAEKRKSDYI-IRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCY 159

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119576022 111 QGSGPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIPPDFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTVAQMF 185
Cdd:cd14602  160 QEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIELF 234
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
32-183 1.48e-56

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 183.98  E-value: 1.48e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022   32 KRCERYWAQEQE-PLQTGLFCITLIKEKWLNEDIMLRTLKVTF--QKESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEAR 108
Cdd:pfam00102  82 EKCAQYWPEEEGeSLEYGDFTVTLKKEKEDEKDYTVRTLEVSNggSEETRTVKHFHYTGWPDHGVPESPNSLLDLLRKVR 161

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119576022  109 RLQGSGPE-PLCVHCSAGCGRTGVLCTVDYVRQLLLTQmipPDFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTVAQ 183
Cdd:pfam00102 162 KSSLDGRSgPIVVHCSAGIGRTGTFIAIDIALQQLEAE---GEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
32-183 8.42e-54

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 177.85  E-value: 8.42e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022    32 KRCERYWAQEQ-EPLQTGLFCITLIKEKWLnEDIMLRTLKVTF--QKESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEAR 108
Cdd:smart00194 109 EKCAQYWPDEEgEPLTYGDITVTLKSVEKV-DDYTIRTLEVTNtgCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVR 187

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119576022   109 RLQGSGPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQmipPDFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTVAQ 183
Cdd:smart00194 188 KSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAG---KEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 32-179 2.38e-53

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: 174.40  E-value: 2.38e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  32 KRCERYWAQEQE-PLQTGLFCITLIKEKWLnEDIMLRTLKVTFQK--ESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEAR 108
Cdd:cd00047   54 EKCERYWPEEGGkPLEYGDITVTLVSEEEL-SDYTIRTLELSPKGcsESREVTHLHYTGWPDHGVPSSPEDLLALVRRVR 132

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119576022 109 RLQGSGPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIPpdfSLFDVVLKMRKQRPAAVQTEEQYRFLYH 179
Cdd:cd00047  133 KEARKPNGPIVVHCSAGVGRTGTFIAIDILLERLEAEGEV---DVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 32-185 4.15e-50

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: 169.34  E-value: 4.15e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  32 KRCERYWAQE-QEPLQTGLFCITLIKEKWLNeDIMLRTLKVTFQKESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARRL 110
Cdd:cd14604  140 KKCERYWPLYgEEPMTFGPFRISCEAEQART-DYFIRTLLLEFQNETRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKY 218

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119576022 111 QGSGPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIPPDFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTVAQMF 185
Cdd:cd14604  219 QEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLF 293
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 33-179 4.89e-44

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: 150.86  E-value: 4.89e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  33 RCERYWAQEQEPLQTGLFCITLIKEKWLNE-DIMLRTLKVTF-QKESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARRL 110
Cdd:cd18533   56 KCDQYWPSGEYEGEYGDLTVELVSEEENDDgGFIVREFELSKeDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKREL 135

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119576022 111 QGSGPE--PLCVHCSAGCGRTGVLCTVDYVRQLL---LTQMIPPDFSL---FDVVLKMRKQRPAAVQTEEQYRFLYH 179
Cdd:cd18533  136 NDSASLdpPIIVHCSAGVGRTGTFIALDSLLDELkrgLSDSQDLEDSEdpvYEIVNQLRKQRMSMVQTLRQYIFLYD 212
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
79-183 1.95e-38

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 132.87  E-value: 1.95e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022    79 SVYQLQYMSWPDRGVPSSPDHMLAMVEEARRLQGSGPE--PLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIPPDFslFDV 156
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESsgPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGEVDI--FDT 78

                           90       100
                   ....*....|....*....|....*..
gi 119576022   157 VLKMRKQRPAAVQTEEQYRFLYHTVAQ 183
Cdd:smart00404  79 VKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 79-183 1.95e-38

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: 132.87  E-value: 1.95e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022    79 SVYQLQYMSWPDRGVPSSPDHMLAMVEEARRLQGSGPE--PLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIPPDFslFDV 156
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESsgPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGEVDI--FDT 78

                           90       100
                   ....*....|....*....|....*..
gi 119576022   157 VLKMRKQRPAAVQTEEQYRFLYHTVAQ 183
Cdd:smart00012  79 VKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 33-183 3.62e-35

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: 128.73  E-value: 3.62e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  33 RCERYWAQEQEPLQTGLFCITLIKEKwLNEDIMLRTLKVTFQKES---RSVYQLQYMSWPDRGVPSSPDHMLAMVEEARR 109
Cdd:cd14544   93 KCVRYWPDEGMQKQYGPYRVQNVSEH-DTTDYTLRELQVSKLDQGdpiREIWHYQYLSWPDHGVPSDPGGVLNFLEDVNQ 171

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119576022 110 LQGSGPE--PLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIPPDFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTVAQ 183
Cdd:cd14544  172 RQESLPHagPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLDCDIDIQKTIQMVRSQRSGMVQTEAQYKFIYVAVAQ 247
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 33-184 1.28e-34

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: 125.95  E-value: 1.28e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  33 RCERYWA-QEQEPL-QTGLFCITLIKEKWLnEDIMLRTLKVTFQK--ESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEAR 108
Cdd:cd14538   57 KCHRYWPdSLNKPLiCGGRLEVSLEKYQSL-QDFVIRRISLRDKEtgEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMR 135

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119576022 109 RLQGSGpePLCVHCSAGCGRTGVLCTVDYVrQLLLTQMIPpdFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTVAQM 184
Cdd:cd14538  136 RIHNSG--PIVVHCSAGIGRTGVLITIDVA-LGLIERDLP--FDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEV 206
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 32-178 1.36e-34

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: 126.31  E-value: 1.36e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  32 KRCERYWAQEQEPLQTGLFCITLIKEKWLNEDIMlRTLKVTFQKESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARRLQ 111
Cdd:cd14548   79 VKCDHYWPFDQDPVYYGDITVTMLSESVLPDWTI-REFKLERGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYI 157

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119576022 112 GSGPEPLCVHCSAGCGRTGVLCTVDYvrqlLLTQMIPPDF-SLFDVVLKMRKQRPAAVQTEEQYRFLY 178
Cdd:cd14548  158 KQEKGPTIVHCSAGVGRTGTFIALDR----LLQQIESEDYvDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 33-176 4.07e-30

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


Pssm-ID: 350389 [Multi-domain]  Cd Length: 212  Bit Score: 114.35  E-value: 4.07e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  33 RCERYWAQEQEPLQTGLFCITLIKEKwLNEDIMLRTLKVTFQK--ESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARRL 110
Cdd:cd14541   60 KCHQYWPDLGETMQFGNLQITCVSEE-VTPSFAFREFILTNTNtgEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQN 138

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119576022 111 QGSGPEPLCVHCSAGCGRTGVLCTVDYVrqLLLTQMIPPDFSLfDVVLKMRKQRPAAVQTEEQYRF 176
Cdd:cd14541  139 RVGMVEPTVVHCSAGIGRTGVLITMETA--MCLIEANEPVYPL-DIVRTMRDQRAMLIQTPSQYRF 201
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 33-181 1.02e-29

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


Pssm-ID: 350444 [Multi-domain]  Cd Length: 207  Bit Score: 112.92  E-value: 1.02e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  33 RCERYWA-QEQEPLQTGLFCITLIKEKWLnEDIMLRTLKVTFQK--ESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARR 109
Cdd:cd14596   57 KCHRYWPeTLQEPMELENYQLRLENYQAL-QYFIIRIIKLVEKEtgENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRK 135

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119576022 110 LQGSGpePLCVHCSAGCGRTGVLCTVDYVRQLLLTQMippDFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTV 181
Cdd:cd14596  136 VHNTG--PIVVHCSAGIGRAGVLICVDVLLSLIEKDL---SFNIKDIVREMRQQRYGMIQTKDQYLFCYKVV 202
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 31-178 1.03e-29

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


Pssm-ID: 350393 [Multi-domain]  Cd Length: 231  Bit Score: 113.64  E-value: 1.03e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  31 SKRCERYWAQEQEP---LQTGLFCITLIKEKwLNEDIMLRTLKVTFQK--ESRSVYQLQYMSWPDRGVPSSPDHMLAMVE 105
Cdd:cd14545   78 QIKCAQYWPQGEGNamiFEDTGLKVTLLSEE-DKSYYTVRTLELENLKtqETREVLHFHYTTWPDFGVPESPAAFLNFLQ 156

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119576022 106 EARR--LQGSGPEPLCVHCSAGCGRTGVLCTVDYVrQLLLTQMIPPDFSLFDVVLKMRKQRPAAVQTEEQYRFLY 178
Cdd:cd14545  157 KVREsgSLSSDVGPPVVHCSAGIGRSGTFCLVDTC-LVLIEKGNPSSVDVKKVLLEMRKYRMGLIQTPDQLRFSY 230
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 32-178 3.38e-29

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: 113.61  E-value: 3.38e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  32 KRCERYWAQEQEP-LQTGLFCITLIkEKWLNEDIMLRTLKV--TFQKESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEAR 108
Cdd:cd14543  112 VKCGQYWPLEEGSsLRYGDLTVTNL-SVENKEHYKKTTLEIhnTETDESRQVTHFQFTSWPDFGVPSSAAALLDFLGEVR 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022 109 R-----LQGSGPE--------PLCVHCSAGCGRTGVLCTVDyvrqLLLTQMipPDFSLFDV---VLKMRKQRPAAVQTEE 172
Cdd:cd14543  191 QqqalaVKAMGDRwkghppgpPIVVHCSAGIGRTGTFCTLD----ICLSQL--EDVGTLNVmqtVRRMRTQRAFSIQTPD 264


                 ....*.
gi 119576022 173 QYRFLY 178
Cdd:cd14543  265 QYYFCY 270
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 33-183 3.41e-28

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: 110.74  E-value: 3.41e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  33 RCERYWAQEQEPLQTGLFCITLIKEKwLNEDIMLRTLKVTFQKES---RSVYQLQYMSWPDRGVPSSPDHMLAMVEEARR 109
Cdd:cd14606  108 KCVPYWPEVGMQRAYGPYSVTNCGEH-DTTEYKLRTLQVSPLDNGeliREIWHYQYLSWPDHGVPSEPGGVLSFLDQINQ 186

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119576022 110 LQGSGPE--PLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIPPDFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTVAQ 183
Cdd:cd14606  187 RQESLPHagPIIVHCSAGIGRTGTIIVIDMLMENISTKGLDCDIDIQKTIQMVRAQRSGMVQTEAQYKFIYVAIAQ 262
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 33-185 6.75e-28

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


Pssm-ID: 350449 [Multi-domain]  Cd Length: 212  Bit Score: 108.49  E-value: 6.75e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  33 RCERYWAQEQEPLQTGLFCITLIKEKWlNEDIMLRTLKVTFQ--KESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARRL 110
Cdd:cd14601   60 KCHQYWPEPSGSSSYGGFQVTCHSEEG-NPAYVFREMTLTNLekNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNK 138

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119576022 111 QGSGPEPLCVHCSAGCGRTGVLCTVDYVrqLLLTQMIPPDFSLfDVVLKMRKQRPAAVQTEEQYRFLYHTVAQMF 185
Cdd:cd14601  139 RAGKDEPVVVHCSAGIGRTGVLITMETA--MCLIECNQPVYPL-DIVRTMRDQRAMMIQTPSQYRFVCEAILKVY 210
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 33-181 5.84e-27

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: 106.51  E-value: 5.84e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  33 RCERYWAQEQEPLQTGLFCITLIKEKWLnEDIMLR--TLKVTFQKESRSVYQLQYMSWPDRGVPSSPDHMLA---MVEEA 107
Cdd:cd14619   81 KCEHYWPLDYTPCTYGHLRVTVVSEEVM-ENWTVRefLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAfrrLLRQW 159

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119576022 108 RRLQGSGpEPLCVHCSAGCGRTGVLCTVDY-VRQLLLTQMIPPdfslFDVVLKMRKQRPAAVQTEEQYRFLYHTV 181
Cdd:cd14619  160 LDQTMSG-GPTVVHCSAGVGRTGTLIALDVlLQQLQSEGLLGP----FSFVQKMRENRPLMVQTESQYVFLHQCI 229
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 33-181 2.25e-26

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: 103.89  E-value: 2.25e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  33 RCERYWAQEQEpLQTGLFCITLIKEKwLNEDIMLRTLKVTFQKE--SRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARRL 110
Cdd:cd14552   55 KCAQYWPEDGS-VSSGDITVELKDQT-DYEDYTLRDFLVTKGKGgsTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQ 132

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119576022 111 QG-SGPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIppdFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTV 181
Cdd:cd14552  133 QQqSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGV---LDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 33-183 2.93e-26

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


Pssm-ID: 350388 [Multi-domain]  Cd Length: 219  Bit Score: 104.08  E-value: 2.93e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  33 RCERYWAQ---EQEPLQTGLFCITliKEKWLNEDIML-RTLKV--TFQKESRSVYQLQYMSWPDRGVPSSPDHMLAMVEE 106
Cdd:cd14540   57 KCFRYWPTlggEHDALTFGEYKVS--TKFSVSSGCYTtTGLRVkhTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEE 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022 107 AR--RLQGSG-------PEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQMiPPDfsLFDVVLKMRKQRPAAVQTEEQYRFL 177
Cdd:cd14540  135 INsvRRHTNQdvaghnrNPPTLVHCSAGVGRTGVVILADLMLYCLDHNE-ELD--IPRVLALLRHQRMLLVQTLAQYKFV 211


                 ....*.
gi 119576022 178 YHTVAQ 183
Cdd:cd14540  212 YNVLIQ 217
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 33-181 3.19e-26

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


Pssm-ID: 350445 [Multi-domain]  Cd Length: 234  Bit Score: 104.53  E-value: 3.19e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  33 RCERYWAQE-------QEPLQtglfcITLIKEKWLnEDIMLRTLKV--TFQKESRSVYQLQYMSWPDRGVPSSPDHMLAM 103
Cdd:cd14597   84 KCQRYWPEIlgkttmvDNRLQ-----LTLVRMQQL-KNFVIRVLELedIQTREVRHITHLNFTAWPDHDTPSQPEQLLTF 157

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119576022 104 VEEARRLQGSGpePLCVHCSAGCGRTGVLCTVDYVRQLLLTQMippDFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTV 181
Cdd:cd14597  158 ISYMRHIHKSG--PIITHCSAGIGRSGTLICIDVVLGLISKDL---DFDISDIVRTMRLQRHGMVQTEDQYIFCYQVI 230
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 33-181 4.65e-26

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


Pssm-ID: 350453 [Multi-domain]  Cd Length: 253  Bit Score: 104.71  E-value: 4.65e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  33 RCERYWAQEQEPLQTGLFCITLIKEKwLNEDIMLRTLKVTFQKE---SRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARR 109
Cdd:cd14605   95 KCVKYWPDEYALKEYGVMRVRNVKES-AAHDYILRELKLSKVGQgntERTVWQYHFRTWPDHGVPSDPGGVLDFLEEVHH 173

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119576022 110 LQGS--GPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIPPDFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTV 181
Cdd:cd14605  174 KQESimDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVDCDIDVPKTIQMVRSQRSGMVQTEAQYRFIYMAV 247
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 29-179 5.03e-26

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: 103.63  E-value: 5.03e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  29 EFSKRCERYWAQEqEPLQTGLFCITL--IKEKwlnEDIMLRTLKVTFQKESRSVYQLQYMSWPDRGVPSSPDHMLAMVEE 106
Cdd:cd14547   77 EAKEKCAQYWPEE-ENETYGDFEVTVqsVKET---DGYTVRKLTLKYGGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQE 152

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119576022 107 AR--RLQGSGPEPLCVHCSAGCGRTGV-LCTVDYVRQLLltqmippDFSLFDV---VLKMRKQRPAAVQTEEQYRFLYH 179
Cdd:cd14547  153 VEeaRQTEPHRGPIVVHCSAGIGRTGCfIATSIGCQQLR-------EEGVVDVlgiVCQLRLDRGGMVQTAEQYEFVHR 224
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 33-178 5.69e-26

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: 102.93  E-value: 5.69e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  33 RCERYW-AQEQEPLQTGLFCITLIKEKWLNEDIMLRTLKVTfQKES----RSVYQLQYMSWPDRGVPsspDHMLAMVEEA 107
Cdd:cd17658   58 KCADYFpAEENESREFGRISVTNKKLKHSQHSITLRVLEVQ-YIESeeppLSVLHIQYPEWPDHGVP---KDTRSVRELL 133

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119576022 108 RRLQGSGPE--PLCVHCSAGCGRTGVLCTVDY-VRQLLLTQMIPPDFSlfDVVLKMRKQRPAAVQTEEQYRFLY 178
Cdd:cd17658  134 KRLYGIPPSagPIVVHCSAGIGRTGAYCTIHNtIRRILEGDMSAVDLS--KTVRKFRSQRIGMVQTQDQYIFCY 205
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 31-183 1.22e-25

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


Pssm-ID: 350394 [Multi-domain]  Cd Length: 208  Bit Score: 102.14  E-value: 1.22e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  31 SKRCERYWAQEQEPLQtGLFCITLIKEKWLNEDIMLRT--LKVTFQKESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEAR 108
Cdd:cd14546   54 VKQCARYWPEEGSEVY-HIYEVHLVSEHIWCDDYLVRSfyLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVN 132

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119576022 109 RLQGSGPEPLCVHCSAGCGRTGVLCTVDyvrqLLLTQMIP--PDFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTVAQ 183
Cdd:cd14546  133 KSYRGRSCPIVVHCSDGAGRTGTYILID----MVLNRMAKgaKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 33-177 1.62e-25

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


Pssm-ID: 350448 [Multi-domain]  Cd Length: 274  Bit Score: 103.78  E-value: 1.62e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  33 RCERYWAQEQEPLQTGLFCITLIKEKWlNEDIMLRTLKVTFQK--ESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARRL 110
Cdd:cd14600  123 KCHQYWPDPPDVMEYGGFRVQCHSEDC-TIAYVFREMLLTNTQtgEERTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRSK 201

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119576022 111 QGSGpEPLCVHCSAGCGRTGVLCTVDYVrqLLLTQMIPPDFSLfDVVLKMRKQRPAAVQTEEQYRFL 177
Cdd:cd14600  202 RVEN-EPVLVHCSAGIGRTGVLVTMETA--MCLTERNQPVYPL-DIVRKMRDQRAMMVQTSSQYKFV 264
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 15-178 1.04e-24

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: 99.73  E-value: 1.04e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  15 LEARGGRegavlagefskRCERYWAQEQEPlQTGLFCITLikekwLNEDIM----LRTL--------KVTFQKESRSVYQ 82
Cdd:cd14549   48 LVERGRR-----------KCDQYWPKEGTE-TYGNIQVTL-----LSTEVLatytVRTFslknlklkKVKGRSSERVVYQ 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  83 LQYMSWPDRGVPSSPDHMLAMVEEARRLQGSGPEPLCVHCSAGCGRTGVLCTVD-YVRQLLLTQMIppdfSLFDVVLKMR 161
Cdd:cd14549  111 YHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTGTYIVIDsMLQQIQDKGTV----NVFGFLKHIR 186

                        170
                 ....*....|....*..
gi 119576022 162 KQRPAAVQTEEQYRFLY 178
Cdd:cd14549  187 TQRNYLVQTEEQYIFIH 203
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 31-183 1.40e-24

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


Pssm-ID: 350456 [Multi-domain]  Cd Length: 277  Bit Score: 101.26  E-value: 1.40e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  31 SKRCERYWAQEQEplQTGLFCITLIKEKWLNEDI----MLRTLKVT--FQKESRSVYQLQYMSWPDRGVPSSPDHMLAMV 104
Cdd:cd14608  103 SLKCAQYWPQKEE--KEMIFEDTNLKLTLISEDIksyyTVRQLELEnlTTQETREILHFHYTTWPDFGVPESPASFLNFL 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022 105 EEARRLQGSGPE--PLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIPPDFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTVA 182
Cdd:cd14608  181 FKVRESGSLSPEhgPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVI 260


                 .
gi 119576022 183 Q 183
Cdd:cd14608  261 E 261
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 34-178 1.81e-24

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: 99.63  E-value: 1.81e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  34 CERYWAQEQEPLQTGLFCITLIKEKWLNEDIMlRTLKV---TFQKEsRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARR- 109
Cdd:cd14618   82 CDHYWPSESTPVSYGHITVHLLAQSSEDEWTR-REFKLwheDLRKE-RRVKHLHYTAWPDHGIPESTSSLMAFRELVREh 159

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119576022 110 ---LQGSGpePLCVHCSAGCGRTGVLCTVD-YVRQLLLTQMIppdfSLFDVVLKMRKQRPAAVQTEEQYRFLY 178
Cdd:cd14618  160 vqaTKGKG--PTLVHCSAGVGRSGTFIALDrLLRQLKEEKVV----DVFNTVYILRMHRYLMIQTLSQYIFLH 226
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 32-180 2.63e-24

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


Pssm-ID: 350402 [Multi-domain]  Cd Length: 238  Bit Score: 99.52  E-value: 2.63e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  32 KRCERYWAQEQEpLQTGLFCITLIKEKWLNEDImLRTLKVTFQK--ESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARR 109
Cdd:cd14554   89 EKCHQYWPAERS-ARYQYFVVDPMAEYNMPQYI-LREFKVTDARdgQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHK 166

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119576022 110 L--QGSGPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIppdFSLFDVVLKMRKQRPAAVQTEEQYRFLYHT 180
Cdd:cd14554  167 TkeQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGV---VDVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 32-178 4.13e-24

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


Pssm-ID: 350404 [Multi-domain]  Cd Length: 201  Bit Score: 97.86  E-value: 4.13e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  32 KRCERYWAqEQEPLQTGLFCITLIKEKwLNEDIMLRTLKVT----FQKESRSVYQLQYMSWP-DRGVPSSPDHMLAMVEE 106
Cdd:cd14556   53 QSCPQYWP-DEGSGTYGPIQVEFVSTT-IDEDVISRIFRLQnttrPQEGYRMVQQFQFLGWPrDRDTPPSKRALLKLLSE 130

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119576022 107 ARRLQG-SGPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIppdFSLFDVVLKMRKQRPAAVQTEEQYRFLY 178
Cdd:cd14556  131 VEKWQEqSGEGPIVVHCLNGVGRSGVFCAISSVCERIKVENV---VDVFQAVKTLRNHRPNMVETEEQYKFCY 200
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 33-184 6.15e-24

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: 98.42  E-value: 6.15e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  33 RCERYWAQEQEPLQTGLFCITLIKEKWLNEDImLRTLKVTFQKESRSVYQLQYMSWPDRGVPS--SPDHMLAMVEEARRL 110
Cdd:cd14614   96 KCDHYWPFTEEPVAYGDITVEMLSEEEQPDWA-IREFRVSYADEVQDVMHFNYTAWPDHGVPTanAAESILQFVQMVRQQ 174

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119576022 111 QGSGPEPLCVHCSAGCGRTGVLCTVDYVRQLLltqmipPDFSLFDV---VLKMRKQRPAAVQTEEQYRFLYHTVAQM 184
Cdd:cd14614  175 AVKSKGPMIIHCSAGVGRTGTFIALDRLLQHI------RDHEFVDIlglVSEMRSYRMSMVQTEEQYIFIHQCVQLM 245
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 12-183 2.17e-23

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: 96.65  E-value: 2.17e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  12 LERLEARGgregavlagefSKRCERYWAQEQEpLQTGLFCITLIKEKWlNEDIMLRTLKVTFQKE--SRSVYQLQYMSWP 89
Cdd:cd14623   70 LTELEERG-----------QEKCAQYWPSDGS-VSYGDITIELKKEEE-CESYTVRDLLVTNTREnkSRQIRQFHFHGWP 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  90 DRGVPSSPDHMLAMVEEARRLQG-SGPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIppdFSLFDVVLKMRKQRPAAV 168
Cdd:cd14623  137 EVGIPSDGKGMINIIAAVQKQQQqSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGI---LDVFQTVKSLRLQRPHMV 213

                        170
                 ....*....|....*
gi 119576022 169 QTEEQYRFLYHTVAQ 183
Cdd:cd14623  214 QTLEQYEFCYKVVQE 228
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 29-183 2.69e-23

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: 96.83  E-value: 2.69e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  29 EFSKRCERYWAQEQEPLqtGLFCITLIKEKWLNEdIMLRTLKVTFQKESRSVYQLQYMSWPDRGVPSSPD---HMLAMVE 105
Cdd:cd14612   96 EKKEKCVHYWPEKEGTY--GRFEIRVQDMKECDG-YTIRDLTIQLEEESRSVKHYWFSSWPDHQTPESAGpllRLVAEVE 172

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119576022 106 EARRLQGSgPEPLCVHCSAGCGRTGV-LCTVDYVRQLLLTQmippDFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTVAQ 183
Cdd:cd14612  173 ESRQTAAS-PGPIVVHCSAGIGRTGCfIATSIGCQQLKDTG----KVDILGIVCQLRLDRGGMIQTSEQYQFLHHTLAL 246
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 34-178 9.18e-23

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: 94.38  E-value: 9.18e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  34 CERYWAQEQeplQT-GLFCITLIKEKWLNEDImLRTLKVTF--QKESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARRL 110
Cdd:cd14558   56 CAQYWGDEK---KTyGDIEVELKDTEKSPTYT-VRVFEITHlkRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQK 131

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119576022 111 QGSGPE------PLCVHCSAGCGRTGVLCTVdyvRQLLLTQMIPPDFSLFDVVLKMRKQRPAAVQTEEQYRFLY 178
Cdd:cd14558  132 LPYKNSkhgrsvPIVVHCSDGSSRTGIFCAL---WNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 31-178 1.41e-22

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: 93.99  E-value: 1.41e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  31 SKRCERYWAQEQ-EPLQTGLFCITLIKEKWLNEDIMlRTLKVTF--QKESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEA 107
Cdd:cd14539   54 KQKVHRYWPTERgQALVYGAITVSLQSVRTTPTHVE-RIISIQHkdTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEV 132

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119576022 108 R---RLQGSGPEPLCVHCSAGCGRTGVLCTVdY--VRQLLLTQMIPpdfSLFDVVLKMRKQRPAAVQTEEQYRFLY 178
Cdd:cd14539  133 HshyLQQRSLQTPIVVHCSSGVGRTGAFCLL-YaaVQEIEAGNGIP---DLPQLVRKMRQQRKYMLQEKEHLKFCY 204
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 31-181 1.49e-22

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: 95.03  E-value: 1.49e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  31 SKRCERYW-AQEQEPL---QTGlFCITLikekwLNEDIM------LRTLKVTFQKESRSVYQLQYMSWPDRGVPSSPDHM 100
Cdd:cd14607  102 SVKCAQYWpTDEEEVLsfkETG-FSVKL-----LSEDVKsyytvhLLQLENINSGETRTISHFHYTTWPDFGVPESPASF 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022 101 LAMVEEARRLQGSGPE--PLCVHCSAGCGRTGVLCTVDYVrQLLLTQMIPPDFSLFDVVLKMRKQRPAAVQTEEQYRFLY 178
Cdd:cd14607  176 LNFLFKVRESGSLSPEhgPAVVHCSAGIGRSGTFSLVDTC-LVLMEKKDPDSVDIKQVLLDMRKYRMGLIQTPDQLRFSY 254


                 ...
gi 119576022 179 HTV 181
Cdd:cd14607  255 MAV 257
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 33-177 1.73e-22

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: 94.11  E-value: 1.73e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  33 RCERYWAQEQePLQTGLFCITLIKEKWLnEDIMLRTLKVTFQK--ESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARRL 110
Cdd:cd14615   80 KCEEYWPSKQ-KKDYGDITVTMTSEIVL-PEWTIRDFTVKNAQtnESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREY 157

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119576022 111 QGSGPE--PLCVHCSAGCGRTGVLCTVDYvrqllLTQMIPPDFS--LFDVVLKMRKQRPAAVQTEEQYRFL 177
Cdd:cd14615  158 MKQNPPnsPILVHCSAGVGRTGTFIAIDR-----LIYQIENENVvdVYGIVYDLRMHRPLMVQTEDQYVFL 223
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 33-178 3.02e-22

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: 92.97  E-value: 3.02e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  33 RCERYWAQEQEPLQT-GLFCITLIKEKwLNEDIMLRTLKVTFQKESRS---VYQLQYMSWPDRGVPSSPDHMLAMVEEAR 108
Cdd:cd14557   55 KCAQYWPSMEEGSRAfGDVVVKINEEK-ICPDYIIRKLNINNKKEKGSgreVTHIQFTSWPDHGVPEDPHLLLKLRRRVN 133

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119576022 109 RLQGSGPEPLCVHCSAGCGRTGVLCTVD-YVRQLLLTQMIppdfSLFDVVLKMRKQRPAAVQTEEQYRFLY 178
Cdd:cd14557  134 AFNNFFSGPIVVHCSAGVGRTGTYIGIDaMLEGLEAEGRV----DVYGYVVKLRRQRCLMVQVEAQYILIH 200
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 75-181 2.09e-21

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: 91.16  E-value: 2.09e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  75 KESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARRLQGSGPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQMippDFSLF 154
Cdd:cd14620  124 KAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQ---KVDVF 200

                         90       100
                 ....*....|....*....|....*..
gi 119576022 155 DVVLKMRKQRPAAVQTEEQYRFLYHTV 181
Cdd:cd14620  201 EFVSRIRNQRPQMVQTDMQYSFIYQAL 227
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 32-187 3.81e-21

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


Pssm-ID: 350476 [Multi-domain]  Cd Length: 292  Bit Score: 92.10  E-value: 3.81e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  32 KRCERYWAQEQEPlQTGLFCITLIKEKWLNEDImLRTLKVTFQK--ESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARR 109
Cdd:cd14628  135 EKCHQYWPAERSA-RYQYFVVDPMAEYNMPQYI-LREFKVTDARdgQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHK 212

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022 110 L--QGSGPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIppdFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTVAQMFCS 187
Cdd:cd14628  213 TkeQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGV---VDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYLGS 289
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 32-181 4.19e-21

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: 89.68  E-value: 4.19e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  32 KRCERYWAQEQEpLQTGLFCITlIKEKWLNEDIMLRTLKVTF--QKESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARR 109
Cdd:cd14622   55 EKCVQYWPSEGS-VTHGEITIE-IKNDTLLETISIRDFLVTYnqEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQK 132

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119576022 110 LQG-SGPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIppdFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTV 181
Cdd:cd14622  133 QQQqTGNHPIVVHCSAGAGRTGTFIALSNILERVKAEGL---LDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 33-183 5.32e-21

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


Pssm-ID: 350478 [Multi-domain]  Cd Length: 237  Bit Score: 90.47  E-value: 5.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  33 RCERYWAQEQEPLqtGLFCITLIKEKWLNEDImLRTLkvTFQK----ESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEAR 108
Cdd:cd14630   87 KCVRYWPDDTEVY--GDIKVTLIETEPLAEYV-IRTF--TVQKkgyhEIREIRQFHFTSWPDHGVPCYATGLLGFVRQVK 161

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119576022 109 RLQGSGPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIppdFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTVAQ 183
Cdd:cd14630  162 FLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGV---VDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
24-177 7.52e-21

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 90.92  E-value: 7.52e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  24 AVLAG--EFSKR---CERYW-AQEQEPLQTglFCITLIKEKWLNEDIMLRTLKVTFQ---KESRSVYQLQYMSWPDRGVP 94
Cdd:COG5599  106 VVLASddEISKPkvkMPVYFrQDGEYGKYE--VSSELTESIQLRDGIEARTYVLTIKgtgQKKIEIPVLHVKNWPDHGAI 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  95 SSP--DHMLAMVEEARRLQGSGPEPLCVHCSAGCGRTGVLCTVDYVRQlLLTQMIPPDFSLFDVVLKMRKQR-PAAVQTE 171
Cdd:COG5599  184 SAEalKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSK-SINALVQITLSVEEIVIDMRTSRnGGMVQTS 262


                 ....*.
gi 119576022 172 EQYRFL 177
Cdd:COG5599  263 EQLDVL 268
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 33-178 8.45e-21

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: 89.76  E-value: 8.45e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  33 RCERYWAQE-QEplQTGLFCITLIkekwlnEDIMLRTLKV-TFQ------KESRSVYQLQYMSWPDRGVPSSPDHMLAMV 104
Cdd:cd14553   87 KCDQYWPTRgTE--TYGLIQVTLL------DTVELATYTVrTFAlhkngsSEKREVRQFQFTAWPDHGVPEHPTPFLAFL 158

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119576022 105 eeaRRLQGSGPE---PLCVHCSAGCGRTGVLCTVDyvrqLLLTQMIPPD-FSLFDVVLKMRKQRPAAVQTEEQYRFLY 178
Cdd:cd14553  159 ---RRVKACNPPdagPIVVHCSAGVGRTGCFIVID----SMLERIKHEKtVDIYGHVTCLRAQRNYMVQTEDQYIFIH 229
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 32-187 1.05e-20

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


Pssm-ID: 350475 [Multi-domain]  Cd Length: 290  Bit Score: 90.56  E-value: 1.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  32 KRCERYWAQEQEPlQTGLFCITLIKEKWLNEDImLRTLKVTFQK--ESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARR 109
Cdd:cd14627  136 EKCHQYWPAERSA-RYQYFVVDPMAEYNMPQYI-LREFKVTDARdgQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHK 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022 110 L--QGSGPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIppdFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTVAQMFCS 187
Cdd:cd14627  214 TkeQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGV---VDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYLGS 290
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 32-178 3.06e-20

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: 87.28  E-value: 3.06e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  32 KRCERYWAQEQEPLQTGLF-----CITLIkekwlneDIMLRTL------KVTFQKESRSVYQLQYMSWPDRGVPSSPDHM 100
Cdd:cd14551   54 KKCSQYWPDQGCWTYGNLRvrvedTVVLV-------DYTTRKFciqkvnRGIGEKRVRLVTQFHFTSWPDFGVPFTPIGM 126

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119576022 101 LAMVEEARRLQGSGPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQMippDFSLFDVVLKMRKQRPAAVQTEEQYRFLY 178
Cdd:cd14551  127 LKFLKKVKSANPPRAGPIVVHCSAGVGRTGTFIVIDAMLDMMHAEG---KVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 33-178 3.60e-20

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


Pssm-ID: 350465 [Multi-domain]  Cd Length: 228  Bit Score: 87.67  E-value: 3.60e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  33 RCERYWAQEQEPLQTGLFCITLIKEKWLNEdIMLRTLKVTFQKE---SRSVYQLQYMSWPDRGVPSSPDHMLAMVEEAR- 108
Cdd:cd14617   81 KCDHYWPADQDSLYYGDLIVQMLSESVLPE-WTIREFKICSEEQldaPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVRd 159

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119576022 109 ---RLQGSGPEplCVHCSAGCGRTGVLCTVDYVRQLLLTQmipPDFSLFDVVLKMRKQRPAAVQTEEQYRFLY 178
Cdd:cd14617  160 yinRTPGSGPT--VVHCSAGVGRTGTFIALDRILQQLDSK---DSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 32-183 3.72e-20

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


Pssm-ID: 350457 [Multi-domain]  Cd Length: 281  Bit Score: 88.94  E-value: 3.72e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  32 KRCERYWAQEQEPLQTgLFCITLIKEKWLNEDIMLRT--LKVTFQKESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARR 109
Cdd:cd14609  126 KQCDRYWPDEGSSLYH-IYEVNLVSEHIWCEDFLVRSfyLKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNK 204

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119576022 110 LQGSGPEPLCVHCSAGCGRTGVLCTVDYVrqllLTQMIP--PDFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTVAQ 183
Cdd:cd14609  205 CYRGRSCPIIVHCSDGAGRTGTYILIDMV----LNRMAKgvKEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAE 276
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 26-183 5.04e-20

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


Pssm-ID: 350458 [Multi-domain]  Cd Length: 283  Bit Score: 88.58  E-value: 5.04e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  26 LAGEFSKRCERYWAQEQEPLQTgLFCITLIKEKWLNEDIMLRT--LKVTFQKESRSVYQLQYMSWPDRGVPSSPDHMLAM 103
Cdd:cd14610  122 LAENGVKQCYHYWPDEGSNLYH-IYEVNLVSEHIWCEDFLVRSfyLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLLDF 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022 104 VEEARRLQGSGPEPLCVHCSAGCGRTGVLCTVDYVrqllLTQMI--PPDFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTV 181
Cdd:cd14610  201 RRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMV----LNKMAkgAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAV 276


                 ..
gi 119576022 182 AQ 183
Cdd:cd14610  277 AE 278
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 33-178 5.48e-20

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


Pssm-ID: 350464 [Multi-domain]  Cd Length: 224  Bit Score: 87.27  E-value: 5.48e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  33 RCERYWAQEQEPLQT-GLFCITLIKEKwLNEDIMLRTLKVTFQKESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARRLQ 111
Cdd:cd14616   81 RCHQYWPEDNKPVTVfGDIVITKLMED-VQIDWTIRDLKIERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVRASR 159

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119576022 112 GSGPEPLCVHCSAGCGRTGVLCTVDYvrqllLTQMIPP-DF-SLFDVVLKMRKQRPAAVQTEEQYRFLY 178
Cdd:cd14616  160 AHDNTPMIVHCSAGVGRTGVFIALDH-----LTQHINDhDFvDIYGLVAELRSERMCMVQNLAQYIFLH 223
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 33-181 6.37e-20

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


Pssm-ID: 350403 [Multi-domain]  Cd Length: 204  Bit Score: 86.51  E-value: 6.37e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  33 RCERYWAQEQEPLqtGLFCITLIKEKWLNEDImLRTLKVTFQ--KESRSVYQLQYMSWPDRGVPSSPDHMLAMVeeaRRL 110
Cdd:cd14555   55 KCSRYWPDDTEVY--GDIKVTLVETEPLAEYV-VRTFALERRgyHEIREVRQFHFTGWPDHGVPYHATGLLGFI---RRV 128

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119576022 111 QGSGPE---PLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIppdFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTV 181
Cdd:cd14555  129 KASNPPsagPIVVHCSAGAGRTGCYIVIDIMLDMAEREGV---VDIYNCVKELRSRRVNMVQTEEQYIFIHDAI 199
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 32-187 1.19e-19

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


Pssm-ID: 350477 [Multi-domain]  Cd Length: 291  Bit Score: 87.86  E-value: 1.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  32 KRCERYWAQEQEPlQTGLFCITLIKEKWLNEDImLRTLKVTFQK--ESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARR 109
Cdd:cd14629  136 EKCHQYWPAERSA-RYQYFVVDPMAEYNMPQYI-LREFKVTDARdgQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQVHK 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022 110 L--QGSGPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIppdFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTVAQMFCS 187
Cdd:cd14629  214 TkeQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGV---VDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEYLGS 290
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 33-183 2.29e-19

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


Pssm-ID: 350474 [Multi-domain]  Cd Length: 276  Bit Score: 86.63  E-value: 2.29e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  33 RCERYWAQEQEPlQTGLFCITLIkekwlnEDIMLRTLKV-TF------QKESRSVYQLQYMSWPDRGVPSSPDHMLAMVe 105
Cdd:cd14626  125 KCDQYWPIRGTE-TYGMIQVTLL------DTVELATYSVrTFalykngSSEKREVRQFQFMAWPDHGVPEYPTPILAFL- 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022 106 eaRRLQGSGPE---PLCVHCSAGCGRTGVLCTVDyvrQLLLTQMIPPDFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTVA 182
Cdd:cd14626  197 --RRVKACNPPdagPMVVHCSAGVGRTGCFIVID---AMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALL 271


                 .
gi 119576022 183 Q 183
Cdd:cd14626  272 E 272
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 32-181 6.94e-18

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: 81.18  E-value: 6.94e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  32 KRCERYWAQEQEPlQTGLFCITLIKEKWLN----EDIMLRTLKVT--FQK---ESRSVYQLQYMSWPDRGVPSSPDHMLA 102
Cdd:cd17668   54 RKCDQYWPADGSE-EYGNFLVTQKSVQVLAyytvRNFTLRNTKIKkgSQKgrpSGRVVTQYHYTQWPDMGVPEYTLPVLT 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022 103 MVEEARRLQGSGPEPLCVHCSAGCGRTGVLCTVD-YVRQLLLTQMIppdfSLFDVVLKMRKQRPAAVQTEEQYRFLYHTV 181
Cdd:cd17668  133 FVRKASYAKRHAVGPVVVHCSAGVGRTGTYIVLDsMLQQIQHEGTV----NIFGFLKHIRSQRNYLVQTEEQYVFIHDAL 208
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 33-183 1.05e-17

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


Pssm-ID: 350480 [Multi-domain]  Cd Length: 205  Bit Score: 80.48  E-value: 1.05e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  33 RCERYWAQEQEplQTGLFCITLIKEKWLNEdIMLRTLKVTFQKES--RSVYQLQYMSWPDRGVPSSPDHMLAMVeeaRRL 110
Cdd:cd14632   55 KCSKYWPDDSD--TYGDIKITLLKTETLAE-YSVRTFALERRGYSarHEVKQFHFTSWPEHGVPYHATGLLAFI---RRV 128

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119576022 111 QGSGPE---PLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIppdFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTVAQ 183
Cdd:cd14632  129 KASTPPdagPVVVHCSAGAGRTGCYIVLDVMLDMAECEGV---VDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 33-183 1.44e-17

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: 80.45  E-value: 1.44e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  33 RCERYWAQEQEPLqtGLFCITLIKEKWLNEDIMLR-TLKVTFQKESRSVYQLQYMSWPDRGVPSSPDHMLAMVeeaRRLQ 111
Cdd:cd14631   69 KCYKYWPDDTEVY--GDFKVTCVEMEPLAEYVVRTfTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFI---RRVK 143

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119576022 112 GSGPE---PLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIppdFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTVAQ 183
Cdd:cd14631  144 LSNPPsagPIVVHCSAGAGRTGCYIVIDIMLDMAEREGV---VDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 33-178 3.85e-17

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


Pssm-ID: 350472 [Multi-domain]  Cd Length: 284  Bit Score: 80.55  E-value: 3.85e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  33 RCERYWAQEQEPLQtGLFCITLIKEKWLnEDIMLRTLKV--TFQKESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARRL 110
Cdd:cd14624  131 KCDQYWPSRGTETY-GLIQVTLLDTVEL-ATYCVRTFALykNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTC 208

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119576022 111 QGSGPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQmipPDFSLFDVVLKMRKQRPAAVQTEEQYRFLY 178
Cdd:cd14624  209 NPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHE---KTVDIYGHVTLMRAQRNYMVQTEDQYIFIH 273
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 33-183 4.23e-17

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


Pssm-ID: 350481 [Multi-domain]  Cd Length: 273  Bit Score: 80.09  E-value: 4.23e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  33 RCERYWAQEQEPLQTglFCITLIKEKWLNEDImLRTLKVTFQ--KESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARRL 110
Cdd:cd14633  124 KCCKYWPDDTEIYKD--IKVTLIETELLAEYV-IRTFAVEKRgvHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSK 200

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119576022 111 QGSGPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIppdFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTVAQ 183
Cdd:cd14633  201 SPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGV---VDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 270
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 33-183 4.54e-17

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


Pssm-ID: 350473 [Multi-domain]  Cd Length: 282  Bit Score: 80.14  E-value: 4.54e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  33 RCERYWAQEQEPlQTGLFCITLIkekwlnEDIMLRTLKV-TFQ------KESRSVYQLQYMSWPDRGVPSSPDHMLAMVE 105
Cdd:cd14625  131 KCDQYWPSRGTE-TYGMIQVTLL------DTIELATFCVrTFSlhkngsSEKREVRQFQFTAWPDHGVPEYPTPFLAFLR 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022 106 EARRLQGSGPEPLCVHCSAGCGRTGVLCTVDyvrqlLLTQMIPPD--FSLFDVVLKMRKQRPAAVQTEEQYRFLYHTVAQ 183
Cdd:cd14625  204 RVKTCNPPDAGPIVVHCSAGVGRTGCFIVID-----AMLERIKHEktVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLE 278
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 29-182 8.90e-17

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: 79.14  E-value: 8.90e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  29 EFSKRCERYWAQEQePLQTGLFCItlIKEKWLNEDIMLRTLKVTFQKESRSVYQLQYMSWPDRGVPSSPDHMLAMV---E 105
Cdd:cd14613  106 EMNEKCTEYWPEEQ-VTYEGIEIT--VKQVIHADDYRLRLITLKSGGEERGLKHYWYTSWPDQKTPDNAPPLLQLVqevE 182

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119576022 106 EARRLQGSGPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIppdFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTVA 182
Cdd:cd14613  183 EARQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGV---VDILRTTCQLRLDRGGMIQTCEQYQFVHHVLS 256
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 29-179 1.41e-16

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: 77.65  E-value: 1.41e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  29 EFSKRCERYWaqeqePLQTGLFCITLIKEKWLNE--DIMLRTLKVTFQKESRSVYQLQYMSWPDRGVPSSPDHMLAM--- 103
Cdd:cd14611   80 EKNEKCVLYW-----PEKRGIYGKVEVLVNSVKEcdNYTIRNLTLKQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLmld 154

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119576022 104 VEEARrLQGSGPEPLCVHCSAGCGRTGV-LCTVDYVRQLLLTQMIppdfSLFDVVLKMRKQRPAAVQTEEQYRFLYH 179
Cdd:cd14611  155 VEEDR-LASPGRGPVVVHCSAGIGRTGCfIATTIGCQQLKEEGVV----DVLSIVCQLRVDRGGMVQTSEQYEFVHH 226
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 32-193 1.66e-16

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 79.30  E-value: 1.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  32 KRCERYWAQEQE-PLQTGLFCIT---LIKEKWLNEDIMLRTLKVTfqKESRSVYQLQYMSWPDRGVPSSPDHMLAMV--- 104
Cdd:PHA02746 152 EKCFELWTKEEDsELAFGRFVAKildIIEELSFTKTRLMITDKIS--DTSREIHHFWFPDWPDNGIPTGMAEFLELInkv 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022 105 -EEARRL------QGSGPEPLCVHCSAGCGRTGVLCTVD-YVRQLLLTQMIppdfSLFDVVLKMRKQRPAAVQTEEQYRF 176
Cdd:PHA02746 230 nEEQAELikqadnDPQTLGPIVVHCSAGIGRAGTFCAIDnALEQLEKEKEV----CLGEIVLKIRKQRHSSVFLPEQYAF 305

                        170
                 ....*....|....*..
gi 119576022 177 LYHTVAQMFCSTLQNAS 193
Cdd:PHA02746 306 CYKALKYAIIEEAKKKF 322
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 71-185 2.44e-16

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: 78.53  E-value: 2.44e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  71 VTFQKESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARRLQGSGPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQMippD 150
Cdd:cd14621  178 VTNKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAER---K 254

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 119576022 151 FSLFDVVLKMRKQRPAAVQTEEQYRFLYHTVAQMF 185
Cdd:cd14621  255 VDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHY 289
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 98-179 6.14e-16

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


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 72.77  E-value: 6.14e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  98 DHMLAMVEEARRLQGSGPEPLCVHCSAGCGRTGVLCTVDYVRQLlltqmippDFSLFDVVLKMRKQRPA-AVQTEEQYRF 176
Cdd:cd14494   39 LAMVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLG--------GMSAEEAVRIVRLIRPGgIPQTIEQLDF 110


                 ...
gi 119576022 177 LYH 179
Cdd:cd14494  111 LIK 113
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 32-183 1.25e-15

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: 75.84  E-value: 1.25e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  32 KRCERYWAQEQEPlQTGLFCITLIKEK----WLNEDIMLRTLKVTF--------QKESRSVYQLQYMSWPDRGVPSSPDH 99
Cdd:cd17667  112 RKCDQYWPTENSE-EYGNIIVTLKSTKihacYTVRRFSIRNTKVKKgqkgnpkgRQNERTVIQYHYTQWPDMGVPEYALP 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022 100 MLAMVEEARRLQGSGPEPLCVHCSAGCGRTGVLCTVDYVRQLLltqmipPDFSLFDVV--LK-MRKQRPAAVQTEEQYRF 176
Cdd:cd17667  191 VLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQI------KDKSTVNVLgfLKhIRTQRNYLVQTEEQYIF 264


                 ....*..
gi 119576022 177 LYHTVAQ 183
Cdd:cd17667  265 IHDALLE 271
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 32-177 3.65e-15

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 75.04  E-value: 3.65e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  32 KRCERYWA-QEQEPLQTGLFCITLIKEKwLNEDIMLRTLKVTFQ--KESRSVYQLQYMSWPDRGVPSS-PD--HMLAMVE 105
Cdd:PHA02747 134 EKCYQYWClNEDGNIDMEDFRIETLKTS-VRAKYILTLIEITDKilKDSRKISHFQCSEWFEDETPSDhPDfiKFIKIID 212

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022 106 EARRLQGS--GPE-----PLCVHCSAGCGRTGVLCTVDY-VRQLLLTQMIppdfSLFDVVLKMRKQRPAAVQTEEQYRFL 177
Cdd:PHA02747 213 INRKKSGKlfNPKdallcPIVVHCSDGVGKTGIFCAVDIcLNQLVKRKAI----CLAKTAEKIREQRHAGIMNFDDYLFI 288
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 15-183 4.17e-15

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


Pssm-ID: 350446 [Multi-domain]  Cd Length: 220  Bit Score: 73.47  E-value: 4.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  15 LEARGGREgavlagefskRCERYW---AQEQEPLQTGLFCITLikeKWLNEDIMLRT----LKVTFQKESRSVYQLQYMS 87
Cdd:cd14598   49 AEEEGGRE----------KSFRYWprlGSRHNTVTYGRFKITT---RFRTDSGCYATtglkIKHLLTGQERTVWHLQYTD 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  88 WPDRGVPSSPDHMLAMVEE---ARRLQGS-----GPE-PLCVHCSAGCGRTGVLctvdyvrqLLLTQMIP--PDFSLFDV 156
Cdd:cd14598  116 WPEHGCPEDLKGFLSYLEEiqsVRRHTNStidpkSPNpPVLVHCSAGVGRTGVV--------ILSEIMIAclEHNEMLDI 187

                        170       180       190
                 ....*....|....*....|....*....|
gi 119576022 157 --VLKM-RKQRPAAVQTEEQYRFLYHTVAQ 183
Cdd:cd14598  188 prVLDMlRQQRMMMVQTLSQYTFVYKVLIQ 217
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 76-183 3.12e-13

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


Pssm-ID: 350447 [Multi-domain]  Cd Length: 287  Bit Score: 69.26  E-value: 3.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  76 ESRSVYQLQYMSWPDRGVPSSPDHMLAMVEE---ARRLQGSGPE-------PLCVHCSAGCGRTGVLCtvdyVRQLLLTQ 145
Cdd:cd14599  170 QERTVWHLQYTDWPDHGCPEEVQGFLSYLEEiqsVRRHTNSMLDstkncnpPIVVHCSAGVGRTGVVI----LTELMIGC 245

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 119576022 146 MIPPDFSLFDVVLK-MRKQRPAAVQTEEQYRFLYHTVAQ 183
Cdd:cd14599  246 LEHNEKVEVPVMLRhLREQRMFMIQTIAQYKFVYQVLIQ 284
PHA02738 PHA02738
hypothetical protein; Provisional
 32-193 3.37e-13

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 69.57  E-value: 3.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  32 KRCERYWAQ-EQEPLQTGLFCITLIK-EKWLNedIMLRTLKVTFQKES-RSVYQLQYMSWPDRGVPSSPDHMLAMVEEAR 108
Cdd:PHA02738 130 EKCFPYWSDvEQGSIRFGKFKITTTQvETHPH--YVKSTLLLTDGTSAtQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVR 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022 109 RLQ-------------GSGPEPLCVHCSAGCGRTGVLCTVDY-VRQLLLTQMIppdfSLFDVVLKMRKQRPAAVQTEEQY 174
Cdd:PHA02738 208 QCQkelaqeslqighnRLQPPPIVVHCNAGLGRTPCYCVVDIsISRFDACATV----SIPSIVSSIRNQRYYSLFIPFQY 283

                        170
                 ....*....|....*....
gi 119576022 175 RFLYHTVAQMFCSTLQNAS 193
Cdd:PHA02738 284 FFCYRAVKRYVNLTVNKVS 302
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 34-178 4.65e-12

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


Pssm-ID: 350482 [Multi-domain]  Cd Length: 206  Bit Score: 64.66  E-value: 4.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  34 CERYWAQEQE----PLQTGLFCITLikekwlNEDIMLRTLKVTF----QKESRSVYQLQYMSWPD-RGVPSSPDHMLAMV 104
Cdd:cd14634   54 CMQYWPEKTSccygPIQVEFVSADI------DEDIISRIFRICNmarpQDGYRIVQHLQYIGWPAyRDTPPSKRSILKVV 127

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119576022 105 EEARRLQ---GSGPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIppdFSLFDVVLKMRKQRPAAVQTEEQYRFLY 178
Cdd:cd14634  128 RRLEKWQeqyDGREGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNI---IDVFHTVKTLRNNKSNMVETLEQYKFVY 201
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 34-178 1.05e-11

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


Pssm-ID: 350485 [Multi-domain]  Cd Length: 207  Bit Score: 63.39  E-value: 1.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  34 CERYWA----QEQEPLQTGLFCITLikekwlNEDIMLRTLKVT----FQKESRSVYQLQYMSW-PDRGVPSSPD---HML 101
Cdd:cd14637   57 CLQYWPepglQQYGPMEVEFVSGSA------DEDIVTRLFRVQnitrLQEGHLMVRHFQFLRWsAYRDTPDSKKaflHLL 130

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119576022 102 AMVEEARRLQGSGPEplCVHCSAGCGRTGVLCTVDYVRQLLLTQMIppdFSLFDVVLKMRKQRPAAVQTEEQYRFLY 178
Cdd:cd14637  131 ASVEKWQRESGEGRT--VVHCLNGGGRSGTYCASAMILEMIRCHNI---VDVFYAVKTLRNYKPNMVETLEQYRFCY 202
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 29-178 1.66e-11

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


Pssm-ID: 350484 [Multi-domain]  Cd Length: 206  Bit Score: 62.74  E-value: 1.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  29 EFSKRCERYWAQEQE----PLQTGlfCITLIkekwLNEDIMLRTLKVTF----QKESRSVYQLQYMSWPD-RGVPSSPDH 99
Cdd:cd14636   49 DLAQGCPQYWPEEGMlrygPIQVE--CMSCS----MDCDVISRIFRICNltrpQEGYLMVQQFQYLGWAShREVPGSKRS 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022 100 MLAMVEEARRLQ---GSGPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIppdFSLFDVVLKMRKQRPAAVQTEEQYRF 176
Cdd:cd14636  123 FLKLILQVEKWQeecDEGEGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNV---VDVFHAVKTLRNSKPNMVETPEQYRF 199


                 ..
gi 119576022 177 LY 178
Cdd:cd14636  200 CY 201
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 32-183 2.18e-11

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 63.87  E-value: 2.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  32 KRCERYW-AQEQEPLQTGLFCITLIKEKWLnEDIMLRTLKVTFQKESRS--VYQLQYMSWPDRGVPSSPDHMLAMVEEAR 108
Cdd:PHA02742 133 EACYPYWmPHERGKATHGEFKIKTKKIKSF-RNYAVTNLCLTDTNTGASldIKHFAYEDWPHGGLPRDPNKFLDFVLAVR 211

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022 109 RLQGS-----------GPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIPPdfsLFDVVLKMRKQRPAAVQTEEQYRFL 177
Cdd:PHA02742 212 EADLKadvdikgenivKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIP---LLSIVRDLRKQRHNCLSLPQQYIFC 288


                 ....*.
gi 119576022 178 YHTVAQ 183
Cdd:PHA02742 289 YFIVLI 294
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 31-183 2.53e-10

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


Pssm-ID: 350483 [Multi-domain]  Cd Length: 206  Bit Score: 59.32  E-value: 2.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  31 SKRCERYWAQ----EQEPLQTGLFCITLikekwlNEDIMLRTLKVTF----QKESRSVYQLQYMSWPD-RGVPSSPDHML 101
Cdd:cd14635   51 AQLCPQYWPEngvhRHGPIQVEFVSADL------EEDIISRIFRIYNaarpQDGYRMVQQFQFLGWPMyRDTPVSKRSFL 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022 102 AMVEEARRLQ---GSGPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQMippDFSLFDVVLKMRKQRPAAVQTEEQYRFLY 178
Cdd:cd14635  125 KLIRQVDKWQeeyNGGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQR---AVDVFHAVKTLRNNKPNMVDLLDQYKFCY 201


                 ....*
gi 119576022 179 HTVAQ 183
Cdd:cd14635  202 EVALE 206
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 72-177 1.83e-09

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


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 56.97  E-value: 1.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  72 TFQKESRSVYQLqymSWPDRGVPSsPDHMLAMVE-EARRLQGSGPepLCVHCSAGCGRTGVL--CTvdyvrqLLLTQMIP 148
Cdd:cd14506   71 AFMRAGIYFYNF---GWKDYGVPS-LTTILDIVKvMAFALQEGGK--VAVHCHAGLGRTGVLiaCY------LVYALRMS 138

                         90       100
                 ....*....|....*....|....*....
gi 119576022 149 PDfslfDVVLKMRKQRPAAVQTEEQYRFL 177
Cdd:cd14506  139 AD----QAIRLVRSKRPNSIQTRGQVLCV 163
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 78-178 3.23e-09

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


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 55.35  E-value: 3.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  78 RSVYQLQYMSW-----PDRGVPSSPDHMLAMVEEARRLQGSGpEPLCVHCSAGCGRTGVLCTvdyvRQLLLTQM-IPPDf 151
Cdd:cd14505   65 LEQYQQAGITWhhlpiPDGGVPSDIAQWQELLEELLSALENG-KKVLIHCKGGLGRTGLIAA----CLLLELGDtLDPE- 138

                         90       100
                 ....*....|....*....|....*..
gi 119576022 152 slfDVVLKMRKQRPAAVQTEEQYRFLY 178
Cdd:cd14505  139 ---QAIAAVRALRPGAIQTPKQENFLH 162
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 89-177 3.65e-09

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


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 54.59  E-value: 3.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  89 PDRGVPSSP--DHMLAMVEEARrlqgSGPEPLCVHCSAGCGRTGVL--CtvdYvrqLLLTQMIPPDfslfDVVLKMRKQR 164
Cdd:cd14504   58 EDYTPPTLEqiDEFLDIVEEAN----AKNEAVLVHCLAGKGRTGTMlaC---Y---LVKTGKISAV----DAINEIRRIR 123

                         90
                 ....*....|...
gi 119576022 165 PAAVQTEEQYRFL 177
Cdd:cd14504  124 PGSIETSEQEKFV 136
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
88-179 3.67e-09

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 54.59  E-value: 3.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  88 WPDRGVPSsPDHMLAMVEEARRLQGSGpEPLCVHCSAGCGRTGvlcTVdyVRQLLLTQMIPPDfslfDVVLKMRKQRPAA 167
Cdd:COG2453   55 IPDFGAPD-DEQLQEAVDFIDEALREG-KKVLVHCRGGIGRTG---TV--AAAYLVLLGLSAE----EALARVRAARPGA 123

                         90
                 ....*....|..
gi 119576022 168 VQTEEQYRFLYH 179
Cdd:COG2453  124 VETPAQRAFLER 135
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 37-178 8.47e-07

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


Pssm-ID: 350508 [Multi-domain]  Cd Length: 205  Bit Score: 48.91  E-value: 8.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  37 YWAQEQEPLQTGLFCITLI---------KEKWLNEDIMLRTLKVTFQKESRsvyQLQYMSWPDRGVPSSPDHMLAMV--E 105
Cdd:cd17670   58 YWPSREESMNCEAFTVTLIskdrlclsnEEQIIIHDFILEATQDDYVLEVR---HFQCPKWPNPDAPISSTFELINVikE 134

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119576022 106 EARRLQGsgpePLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIppdFSLFDVVLKMRKQRPAAVQTEEQYRFLY 178
Cdd:cd17670  135 EALTRDG----PTIVHDEFGAVSAGTLCALTTLSQQLENENA---VDVYQVAKMINLMRPGVFTDIEQYQFLY 200
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 88-177 1.47e-06

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


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 48.55  E-value: 1.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  88 WPDRGVPSSPD-HMLA-MVEEAR-------RLQGSGP-----EPLCV-HCSAGCGRTGVL-CTvdyvrqlllTQMIPPD- 150
Cdd:cd14559  126 WPDHTAISSEGlKELAdLVNKSAeekrnfyKSKGSSAindknKLLPViHCRAGVGRTGQLaAA---------MELNKSPn 196

                         90       100
                 ....*....|....*....|....*....
gi 119576022 151 -FSLFDVVLKMRKQRPA-AVQTEEQYRFL 177
Cdd:cd14559  197 nLSVEDIVSDMRTSRNGkMVQKDEQLDTL 225
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 37-181 3.95e-05

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


Pssm-ID: 350507 [Multi-domain]  Cd Length: 204  Bit Score: 44.21  E-value: 3.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  37 YWAQEQEPLQTGLFCITLI---------KEKWLNEDIMLRTLKVTFQKESRsvyQLQYMSWPDRGVPSSPDHMLAMV--E 105
Cdd:cd17669   58 YWPNKDEPINCETFKVTLIaeehkclsnEEKLIIQDFILEATQDDYVLEVR---HFQCPKWPNPDSPISKTFELISIikE 134

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119576022 106 EARRLQGsgpePLCVHCSAGCGRTGVLCTVDYVRQLLLTQmipPDFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTV 181
Cdd:cd17669  135 EAANRDG----PMIVHDEHGGVTAGTFCALTTLMHQLEKE---NSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 66-182 1.56e-03

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 39.95  E-value: 1.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119576022  66 LRTLKVTFQK-ESRSVYQLQYMSWPDRGVPSSPDHML-------AMVEEARRLQGSGP-EPLCVHCSAGCGRTGVLCTVD 136
Cdd:PHA02740 163 LTLLSLTDKFgQAQKISHFQYTAWPADGFSHDPDAFIdffcnidDLCADLEKHKADGKiAPIIIDCIDGISSSAVFCVFD 242

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 119576022 137 Y-VRQLLLTQMIppdfSLFDVVLKMRKQRPAAVQTEEQYRFLYHTVA 182
Cdd:PHA02740 243 IcATEFDKTGML----SIANALKKVRQKKYGCMNCLDDYVFCYHLIA 285
 
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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