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Conserved domains on  [gi|18375655|ref|NP_055184|]
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tyrosine-protein phosphatase non-receptor type 18 isoform 1 [Homo sapiens]

Protein Classification

PTPc-N18 domain-containing protein( domain architecture ID 12998670)

PTPc-N18 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 27-292 0e+00

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: 554.82  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  27 AGEFSDIQACSAAWKADGVCSTVAGSRPENVRKNRYKDVLPYDQTRVILSLLQEEGHSDYINGNFIRGVDGSLAYIATQG 106
Cdd:cd14603   1 AGEFSEIRACSAAFKADYVCSTVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 107 PLPHTLLDFWRLVWEFGVKVILMACREIENGRKRCERYWAQEQEPLQTGLFCITLIKEKWLNEDIMLRTLKVTFQKESRS 186
Cdd:cd14603  81 PLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAQEQEPLQTGPFTITLVKEKRLNEEVILRTLKVTFQKESRS 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 187 VYQLQYMSWPDRGVPSSPDHMLAMVEEARRLQGSGPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIPPDFSLFDVVLK 266
Cdd:cd14603 161 VSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSIFDVVLE 240

                       250       260
                ....*....|....*....|....*.
gi 18375655 267 MRKQRPAAVQTEEQYRFLYHTVAQMF 292
Cdd:cd14603 241 MRKQRPAAVQTEEQYEFLYHTVAQMF 266
 
Name Accession Description Interval E-value
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 27-292 0e+00

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: 554.82  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  27 AGEFSDIQACSAAWKADGVCSTVAGSRPENVRKNRYKDVLPYDQTRVILSLLQEEGHSDYINGNFIRGVDGSLAYIATQG 106
Cdd:cd14603   1 AGEFSEIRACSAAFKADYVCSTVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 107 PLPHTLLDFWRLVWEFGVKVILMACREIENGRKRCERYWAQEQEPLQTGLFCITLIKEKWLNEDIMLRTLKVTFQKESRS 186
Cdd:cd14603  81 PLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAQEQEPLQTGPFTITLVKEKRLNEEVILRTLKVTFQKESRS 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 187 VYQLQYMSWPDRGVPSSPDHMLAMVEEARRLQGSGPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIPPDFSLFDVVLK 266
Cdd:cd14603 161 VSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSIFDVVLE 240

                       250       260
                ....*....|....*....|....*.
gi 18375655 267 MRKQRPAAVQTEEQYRFLYHTVAQMF 292
Cdd:cd14603 241 MRKQRPAAVQTEEQYEFLYHTVAQMF 266
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
26-290 2.96e-109

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 323.46  E-value: 2.96e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655     26 LAGEFSDIQACsaawkADGVCSTVAGSRPENVRKNRYKDVLPYDQTRVILSLLQEEGhSDYINGNFIRGVDGSLAYIATQ 105
Cdd:smart00194   2 LEEEFEKLDRL-----KPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEG-SDYINASYIDGPNGPKAYIATQ 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655    106 GPLPHTLLDFWRLVWEFGVKVILMACREIENGRKRCERYWAQEQ-EPLQTGLFCITLIKEKWLnEDIMLRTLKVTF--QK 182
Cdd:smart00194  76 GPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEgEPLTYGDITVTLKSVEKV-DDYTIRTLEVTNtgCS 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655    183 ESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARRLQGSGPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQmipPDFSLFD 262
Cdd:smart00194 155 ETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAG---KEVDIFE 231

                          250       260
                   ....*....|....*....|....*...
gi 18375655    263 VVLKMRKQRPAAVQTEEQYRFLYHTVAQ 290
Cdd:smart00194 232 IVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
56-290 5.37e-108

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 319.19  E-value: 5.37e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655    56 NVRKNRYKDVLPYDQTRVILSllQEEGHSDYINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACREIE 135
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655   136 NGRKRCERYWAQEQE-PLQTGLFCITLIKEKWLNEDIMLRTLKVTF--QKESRSVYQLQYMSWPDRGVPSSPDHMLAMVE 212
Cdd:pfam00102  79 KGREKCAQYWPEEEGeSLEYGDFTVTLKKEKEDEKDYTVRTLEVSNggSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18375655   213 EARRLQGSGPE-PLCVHCSAGCGRTGVLCTVDYVRQLLLTQmipPDFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTVAQ 290
Cdd:pfam00102 159 KVRKSSLDGRSgPIVVHCSAGIGRTGTFIAIDIALQQLEAE---GEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 53-284 3.13e-40

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 146.69  E-value: 3.13e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655   53 RPENVRKNRYKDVLPYDQTRVILSLlQEEGHSDYINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMAC- 131
Cdd:PHA02747  48 KPENQPKNRYWDIPCWDHNRVILDS-GGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTp 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  132 REIENGRKRCERYWA-QEQEPLQTGLFCITLIKEKwLNEDIMLRTLKVTFQ--KESRSVYQLQYMSWPDRGVPSS-PD-- 205
Cdd:PHA02747 127 TKGTNGEEKCYQYWClNEDGNIDMEDFRIETLKTS-VRAKYILTLIEITDKilKDSRKISHFQCSEWFEDETPSDhPDfi 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  206 HMLAMVEEARRLQGS--GPE-----PLCVHCSAGCGRTGVLCTVDY-VRQLLLTQMIppdfSLFDVVLKMRKQRPAAVQT 277
Cdd:PHA02747 206 KFIKIIDINRKKSGKlfNPKdallcPIVVHCSDGVGKTGIFCAVDIcLNQLVKRKAI----CLAKTAEKIREQRHAGIMN 281


                 ....*..
gi 18375655  278 EEQYRFL 284
Cdd:PHA02747 282 FDDYLFI 288
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
54-284 9.93e-40

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 144.46  E-value: 9.93e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  54 PENVRKNRYKDVLPYDQTRVilsllQEEGhsDYINGNFIRGVDGSLaYIATQGPLPHTLLDFWRLVWEFGVKVI--LMAC 131
Cdd:COG5599  40 INGSPLNRFRDIQPYKETAL-----RANL--GYLNANYIQVIGNHR-YIATQYPLEEQLEDFFQMLFDNNTPVLvvLASD 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 132 REIENGRKRCERYW-AQEQEPLQTglFCITLIKEKWLNEDIMLRTLKVTFQ---KESRSVYQLQYMSWPDRGVPSSP--D 205
Cdd:COG5599 112 DEISKPKVKMPVYFrQDGEYGKYE--VSSELTESIQLRDGIEARTYVLTIKgtgQKKIEIPVLHVKNWPDHGAISAEalK 189

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 206 HMLAMVEEARRLQGSGPEPLCVHCSAGCGRTGVLCTVDYVRQlLLTQMIPPDFSLFDVVLKMRKQR-PAAVQTEEQYRFL 284
Cdd:COG5599 190 NLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSK-SINALVQITLSVEEIVIDMRTSRnGGMVQTSEQLDVL 268
 
Name Accession Description Interval E-value
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 27-292 0e+00

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: 554.82  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  27 AGEFSDIQACSAAWKADGVCSTVAGSRPENVRKNRYKDVLPYDQTRVILSLLQEEGHSDYINGNFIRGVDGSLAYIATQG 106
Cdd:cd14603   1 AGEFSEIRACSAAFKADYVCSTVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 107 PLPHTLLDFWRLVWEFGVKVILMACREIENGRKRCERYWAQEQEPLQTGLFCITLIKEKWLNEDIMLRTLKVTFQKESRS 186
Cdd:cd14603  81 PLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAQEQEPLQTGPFTITLVKEKRLNEEVILRTLKVTFQKESRS 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 187 VYQLQYMSWPDRGVPSSPDHMLAMVEEARRLQGSGPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIPPDFSLFDVVLK 266
Cdd:cd14603 161 VSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSIFDVVLE 240

                       250       260
                ....*....|....*....|....*.
gi 18375655 267 MRKQRPAAVQTEEQYRFLYHTVAQMF 292
Cdd:cd14603 241 MRKQRPAAVQTEEQYEFLYHTVAQMF 266
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 86-286 6.23e-136

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: 389.09  E-value: 6.23e-136
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  86 YINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACREIENGRKRCERYWAQEQEP-LQTGLFCITLIKE 164
Cdd:cd14542   1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEqLQFGPFKISLEKE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 165 KWLNEDIMLRTLKVTFQKESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARRLQGSGPEPLCVHCSAGCGRTGVLCTVDY 244
Cdd:cd14542  81 KRVGPDFLIRTLKVTFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRTGTICAIDY 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 18375655 245 VRQLLLTQMIPPDFSLFDVVLKMRKQRPAAVQTEEQYRFLYH 286
Cdd:cd14542 161 VWNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 59-292 1.11e-109

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: 323.72  E-value: 1.11e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  59 KNRYKDVLPYDQTRVILSLLQEEGHSDYINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACREIENGR 138
Cdd:cd14602   1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 139 KRCERYWAQE-QEPLQTGLFCITLIKEKWLNEDImLRTLKVTFQKESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARRL 217
Cdd:cd14602  81 KKCERYWAEPgEMQLEFGPFSVTCEAEKRKSDYI-IRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCY 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18375655 218 QGSGPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIPPDFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTVAQMF 292
Cdd:cd14602 160 QEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIELF 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
26-290 2.96e-109

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 323.46  E-value: 2.96e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655     26 LAGEFSDIQACsaawkADGVCSTVAGSRPENVRKNRYKDVLPYDQTRVILSLLQEEGhSDYINGNFIRGVDGSLAYIATQ 105
Cdd:smart00194   2 LEEEFEKLDRL-----KPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEG-SDYINASYIDGPNGPKAYIATQ 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655    106 GPLPHTLLDFWRLVWEFGVKVILMACREIENGRKRCERYWAQEQ-EPLQTGLFCITLIKEKWLnEDIMLRTLKVTF--QK 182
Cdd:smart00194  76 GPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEgEPLTYGDITVTLKSVEKV-DDYTIRTLEVTNtgCS 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655    183 ESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARRLQGSGPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQmipPDFSLFD 262
Cdd:smart00194 155 ETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAG---KEVDIFE 231

                          250       260
                   ....*....|....*....|....*...
gi 18375655    263 VVLKMRKQRPAAVQTEEQYRFLYHTVAQ 290
Cdd:smart00194 232 IVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
56-290 5.37e-108

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 319.19  E-value: 5.37e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655    56 NVRKNRYKDVLPYDQTRVILSllQEEGHSDYINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACREIE 135
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655   136 NGRKRCERYWAQEQE-PLQTGLFCITLIKEKWLNEDIMLRTLKVTF--QKESRSVYQLQYMSWPDRGVPSSPDHMLAMVE 212
Cdd:pfam00102  79 KGREKCAQYWPEEEGeSLEYGDFTVTLKKEKEDEKDYTVRTLEVSNggSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18375655   213 EARRLQGSGPE-PLCVHCSAGCGRTGVLCTVDYVRQLLLTQmipPDFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTVAQ 290
Cdd:pfam00102 159 KVRKSSLDGRSgPIVVHCSAGIGRTGTFIAIDIALQQLEAE---GEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 9-292 3.59e-107

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: 319.57  E-value: 3.59e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655   9 RSFLERLEARGGREGA---VLAGEFSDIQACSAAWKADGVCSTVAGSRPENVRKNRYKDVLPYDQTRVILSLLQEEGHSD 85
Cdd:cd14604   7 KKFIERVQAMKSTDHNgedNFASDFMRLRRLSTKYRTEKIYPTATGEKEENVKKNRYKDILPFDHSRVKLTLKTSSQDSD 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  86 YINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACREIENGRKRCERYWAQE-QEPLQTGLFCITLIKE 164
Cdd:cd14604  87 YINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLYgEEPMTFGPFRISCEAE 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 165 KWLNeDIMLRTLKVTFQKESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARRLQGSGPEPLCVHCSAGCGRTGVLCTVDY 244
Cdd:cd14604 167 QART-DYFIRTLLLEFQNETRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDY 245

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 18375655 245 VRQLLLTQMIPPDFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTVAQMF 292
Cdd:cd14604 246 TWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLF 293
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 86-286 7.52e-87

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: 264.15  E-value: 7.52e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  86 YINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACREIENGRKRCERYWAQEQE-PLQTGLFCITLIKE 164
Cdd:cd00047   1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGkPLEYGDITVTLVSE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 165 KWLnEDIMLRTLKVTFQK--ESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARRLQGSGPEPLCVHCSAGCGRTGVLCTV 242
Cdd:cd00047  81 EEL-SDYTIRTLELSPKGcsESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTFIAI 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 18375655 243 DYVRQLLLTQMIPpdfSLFDVVLKMRKQRPAAVQTEEQYRFLYH 286
Cdd:cd00047 160 DILLERLEAEGEV---DVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 61-285 2.58e-75

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: 235.33  E-value: 2.58e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  61 RYKDVLPYDQTRVILSLLQEEGHSDYINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACREIENGRKR 140
Cdd:cd14548   1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 141 CERYWAQEQEPLQTGLFCITLIKEKWLNEDIMlRTLKVTFQKESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARRLQGS 220
Cdd:cd14548  81 CDHYWPFDQDPVYYGDITVTMLSESVLPDWTI-REFKLERGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIKQ 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18375655 221 GPEPLCVHCSAGCGRTGVLCTVDYvrqlLLTQMIPPDF-SLFDVVLKMRKQRPAAVQTEEQYRFLY 285
Cdd:cd14548 160 EKGPTIVHCSAGVGRTGTFIALDR----LLQQIESEDYvDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 54-285 5.06e-73

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: 231.10  E-value: 5.06e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  54 PENVRKNRYKDVLPYDQTRVILSLLQEEGHSDYINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACRE 133
Cdd:cd14543  27 PANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVMTTRV 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 134 IENGRKRCERYWAQEQEP-LQTGLFCITLIkEKWLNEDIMLRTLKV--TFQKESRSVYQLQYMSWPDRGVPSSPDHMLAM 210
Cdd:cd14543 107 VERGRVKCGQYWPLEEGSsLRYGDLTVTNL-SVENKEHYKKTTLEIhnTETDESRQVTHFQFTSWPDFGVPSSAAALLDF 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 211 VEEARR-----LQGSGPE--------PLCVHCSAGCGRTGVLCTVDyvrqLLLTQMipPDFSLFDV---VLKMRKQRPAA 274
Cdd:cd14543 186 LGEVRQqqalaVKAMGDRwkghppgpPIVVHCSAGIGRTGTFCTLD----ICLSQL--EDVGTLNVmqtVRRMRTQRAFS 259

                       250
                ....*....|.
gi 18375655 275 VQTEEQYRFLY 285
Cdd:cd14543 260 IQTPDQYYFCY 270
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 86-286 1.42e-70

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: 222.51  E-value: 1.42e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  86 YINGNFIR-GVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACREIENGRKRCERYWAQEQEPLQTGLFCITLIKE 164
Cdd:cd18533   1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEYGDLTVELVSE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 165 KWLNE-DIMLRTLKVTF-QKESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARRLQGSGPE--PLCVHCSAGCGRTGVLC 240
Cdd:cd18533  81 EENDDgGFIVREFELSKeDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSASLdpPIIVHCSAGVGRTGTFI 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 18375655 241 TVDYVRQLL---LTQMIPPDFSL---FDVVLKMRKQRPAAVQTEEQYRFLYH 286
Cdd:cd18533 161 ALDSLLDELkrgLSDSQDLEDSEdpvYEIVNQLRKQRMSMVQTLRQYIFLYD 212
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 56-290 1.23e-67

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: 216.56  E-value: 1.23e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  56 NVRKNRYKDVLPYDQTRVILSLLQ-EEGHSDYINGNFIRGV-------DGSLAYIATQGPLPHTLLDFWRLVWEFGVKVI 127
Cdd:cd14544   1 NKGKNRYKNILPFDHTRVILKDRDpNVPGSDYINANYIRNEnegpttdENAKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 128 LMACREIENGRKRCERYWAQEQEPLQTGLFCITLIKEKwLNEDIMLRTLKVTFQKES---RSVYQLQYMSWPDRGVPSSP 204
Cdd:cd14544  81 VMTTKEVERGKNKCVRYWPDEGMQKQYGPYRVQNVSEH-DTTDYTLRELQVSKLDQGdpiREIWHYQYLSWPDHGVPSDP 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 205 DHMLAMVEEARRLQGSGPE--PLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIPPDFSLFDVVLKMRKQRPAAVQTEEQYR 282
Cdd:cd14544 160 GGVLNFLEDVNQRQESLPHagPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLDCDIDIQKTIQMVRSQRSGMVQTEAQYK 239


                ....*...
gi 18375655 283 FLYHTVAQ 290
Cdd:cd14544 240 FIYVAVAQ 247
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 12-284 1.02e-62

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: 204.70  E-value: 1.02e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  12 LERLEaRGGREGAVLagefsdIQACSAAWKADGVCSTVAgSRPENVRKNRYKDVLPYDQTRVILsllqeEGHSDYINGNF 91
Cdd:cd14600   4 MAQLK-KGLESGTVL------IQFEQLYRKKPGLAITCA-KLPQNMDKNRYKDVLPYDATRVVL-----QGNEDYINASY 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  92 ----IRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACREIENGRKRCERYWAQEQEPLQTGLFCITLIKEKWl 167
Cdd:cd14600  71 vnmeIPSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPDVMEYGGFRVQCHSEDC- 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 168 NEDIMLRTLKVTFQK--ESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARRLQGSGpEPLCVHCSAGCGRTGVLCTVDYV 245
Cdd:cd14600 150 TIAYVFREMLLTNTQtgEERTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRSKRVEN-EPVLVHCSAGIGRTGVLVTMETA 228

                       250       260       270
                ....*....|....*....|....*....|....*....
gi 18375655 246 rqLLLTQMIPPDFSLfDVVLKMRKQRPAAVQTEEQYRFL 284
Cdd:cd14600 229 --MCLTERNQPVYPL-DIVRKMRDQRAMMVQTSSQYKFV 264
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 60-288 1.48e-62

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: 202.81  E-value: 1.48e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  60 NRYKDVLPYDQTRVILSLLQEEGHSDYINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACREIENGRK 139
Cdd:cd14619   1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 140 RCERYWAQEQEPLQTGLFCITLIKEKWLnEDIMLR--TLKVTFQKESRSVYQLQYMSWPDRGVPSSPDHMLA---MVEEA 214
Cdd:cd14619  81 KCEHYWPLDYTPCTYGHLRVTVVSEEVM-ENWTVRefLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAfrrLLRQW 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18375655 215 RRLQGSGpEPLCVHCSAGCGRTGVLCTVDY-VRQLLLTQMIPPdfslFDVVLKMRKQRPAAVQTEEQYRFLYHTV 288
Cdd:cd14619 160 LDQTMSG-GPTVVHCSAGVGRTGTLIALDVlLQQLQSEGLLGP----FSFVQKMRENRPLMVQTESQYVFLHQCI 229
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 55-288 2.83e-62

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: 201.98  E-value: 2.83e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  55 ENVRKNRYKDVLPYDQTRVilsLLQEEGhsDYINGNFIRGVDG--SLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACR 132
Cdd:cd14597   2 ENRKKNRYKNILPYDTTRV---PLGDEG--GYINASFIKMPVGdeEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQ 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 133 EIENGRKRCERYWAQE-------QEPLQtglfcITLIKEKWLnEDIMLRTLKV--TFQKESRSVYQLQYMSWPDRGVPSS 203
Cdd:cd14597  77 EVEGGKIKCQRYWPEIlgkttmvDNRLQ-----LTLVRMQQL-KNFVIRVLELedIQTREVRHITHLNFTAWPDHDTPSQ 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 204 PDHMLAMVEEARRLQGSGpePLCVHCSAGCGRTGVLCTVDYVRQLLLTQMippDFSLFDVVLKMRKQRPAAVQTEEQYRF 283
Cdd:cd14597 151 PEQLLTFISYMRHIHKSG--PIITHCSAGIGRSGTLICIDVVLGLISKDL---DFDISDIVRTMRLQRHGMVQTEDQYIF 225


                ....*
gi 18375655 284 LYHTV 288
Cdd:cd14597 226 CYQVI 230
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 60-285 6.79e-62

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: 200.94  E-value: 6.79e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  60 NRYKDVLPYDQTRVILSLLQEEGHSDYINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACREIENGRK 139
Cdd:cd14618   1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 140 RCERYWAQEQEPLQTGLFCITLIKEKWLNEDIMlRTLKV---TFQKEsRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARR 216
Cdd:cd14618  81 LCDHYWPSESTPVSYGHITVHLLAQSSEDEWTR-REFKLwheDLRKE-RRVKHLHYTAWPDHGIPESTSSLMAFRELVRE 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18375655 217 ----LQGSGpePLCVHCSAGCGRTGVLCTVD-YVRQLLLTQMIppdfSLFDVVLKMRKQRPAAVQTEEQYRFLY 285
Cdd:cd14618 159 hvqaTKGKG--PTLVHCSAGVGRSGTFIALDrLLRQLKEEKVV----DVFNTVYILRMHRYLMIQTLSQYIFLH 226
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 51-290 2.34e-61

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: 200.88  E-value: 2.34e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  51 GSRPENVRKNRYKDVLPYDQTRVILsllqeEGH------SDYINGNFIRG---VDGSLA--YIATQGPLPHTLLDFWRLV 119
Cdd:cd14606  13 GQRPENKSKNRYKNILPFDHSRVIL-----QGRdsnipgSDYINANYVKNqllGPDENAktYIASQGCLEATVNDFWQMA 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 120 WEFGVKVILMACREIENGRKRCERYWAQEQEPLQTGLFCITLIKEKwLNEDIMLRTLKVTFQKES---RSVYQLQYMSWP 196
Cdd:cd14606  88 WQENSRVIVMTTREVEKGRNKCVPYWPEVGMQRAYGPYSVTNCGEH-DTTEYKLRTLQVSPLDNGeliREIWHYQYLSWP 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 197 DRGVPSSPDHMLAMVEEARRLQGSGPE--PLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIPPDFSLFDVVLKMRKQRPAA 274
Cdd:cd14606 167 DHGVPSEPGGVLSFLDQINQRQESLPHagPIIVHCSAGIGRTGTIIVIDMLMENISTKGLDCDIDIQKTIQMVRAQRSGM 246

                       250
                ....*....|....*.
gi 18375655 275 VQTEEQYRFLYHTVAQ 290
Cdd:cd14606 247 VQTEAQYKFIYVAIAQ 262
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 60-286 4.90e-61

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: 198.39  E-value: 4.90e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  60 NRYKDVLPYDQTRVILSLLQEEGHSDYINGNFIRGVDG-SLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACREIENgR 138
Cdd:cd14547   1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGeEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA-K 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 139 KRCERYWAQEqEPLQTGLFCITL--IKEKwlnEDIMLRTLKVTFQKESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEAR- 215
Cdd:cd14547  80 EKCAQYWPEE-ENETYGDFEVTVqsVKET---DGYTVRKLTLKYGGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEe 155

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18375655 216 -RLQGSGPEPLCVHCSAGCGRTGV-LCTVDYVRQLLltqmippDFSLFDV---VLKMRKQRPAAVQTEEQYRFLYH 286
Cdd:cd14547 156 aRQTEPHRGPIVVHCSAGIGRTGCfIATSIGCQQLR-------EEGVVDVlgiVCQLRLDRGGMVQTAEQYEFVHR 224
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 86-291 5.77e-61

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: 197.60  E-value: 5.77e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  86 YINGNFIRGVDGS--LAYIATQGPLPHTLLDFWRLVWEFGVKVILMACREIENGRKRCERYWA-QEQEPL-QTGLFCITL 161
Cdd:cd14538   1 YINASHIRIPVGGdtYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPdSLNKPLiCGGRLEVSL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 162 IKEKWLnEDIMLRTLKVTFQK--ESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARRLQGSGpePLCVHCSAGCGRTGVL 239
Cdd:cd14538  81 EKYQSL-QDFVIRRISLRDKEtgEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIHNSG--PIVVHCSAGIGRTGVL 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 18375655 240 CTVDYVrQLLLTQMIPpdFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTVAQM 291
Cdd:cd14538 158 ITIDVA-LGLIERDLP--FDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEV 206
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 59-285 2.04e-60

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: 197.23  E-value: 2.04e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  59 KNRYKDVLPYDQTRVILSLLQEEghSDYINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACREIENGR 138
Cdd:cd14545   1 LNRYRDRDPYDHDRSRVKLKQGD--NDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 139 KRCERYWAQEQEP---LQTGLFCITLIKEKwLNEDIMLRTLKVTFQK--ESRSVYQLQYMSWPDRGVPSSPDHMLAMVEE 213
Cdd:cd14545  79 IKCAQYWPQGEGNamiFEDTGLKVTLLSEE-DKSYYTVRTLELENLKtqETREVLHFHYTTWPDFGVPESPAAFLNFLQK 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18375655 214 ARR--LQGSGPEPLCVHCSAGCGRTGVLCTVDYVrQLLLTQMIPPDFSLFDVVLKMRKQRPAAVQTEEQYRFLY 285
Cdd:cd14545 158 VREsgSLSSDVGPPVVHCSAGIGRSGTFCLVDTC-LVLIEKGNPSSVDVKKVLLEMRKYRMGLIQTPDQLRFSY 230
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 56-285 3.19e-58

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: 191.46  E-value: 3.19e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  56 NVRKNRYKDVLPYDQTRVILSLLQEEGHSDYINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACREIE 135
Cdd:cd14553   3 NKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 136 NGRKRCERYWAQE-QEplQTGLFCITLIkekwlnEDIMLRTLKV-TFQ------KESRSVYQLQYMSWPDRGVPSSPDHM 207
Cdd:cd14553  83 RSRVKCDQYWPTRgTE--TYGLIQVTLL------DTVELATYTVrTFAlhkngsSEKREVRQFQFTAWPDHGVPEHPTPF 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 208 LAMVeeaRRLQGSGPE---PLCVHCSAGCGRTGVLCTVDyvrqLLLTQMIPPD-FSLFDVVLKMRKQRPAAVQTEEQYRF 283
Cdd:cd14553 155 LAFL---RRVKACNPPdagPIVVHCSAGVGRTGCFIVID----SMLERIKHEKtVDIYGHVTCLRAQRNYMVQTEDQYIF 227


                ..
gi 18375655 284 LY 285
Cdd:cd14553 228 IH 229
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 54-287 3.04e-57

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: 189.27  E-value: 3.04e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  54 PENVRKNRYKDVLPYDQTRVILSLLQEEGHSDYINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACRE 133
Cdd:cd14554   4 PCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 134 IENGRKRCERYWAQEQEpLQTGLFCITLIKEKWLNEDImLRTLKVTFQK--ESRSVYQLQYMSWPDRGVPSSPDHMLAMV 211
Cdd:cd14554  84 REMGREKCHQYWPAERS-ARYQYFVVDPMAEYNMPQYI-LREFKVTDARdgQSRTVRQFQFTDWPEQGVPKSGEGFIDFI 161

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18375655 212 EEARRL--QGSGPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIppdFSLFDVVLKMRKQRPAAVQTEEQYRFLYHT 287
Cdd:cd14554 162 GQVHKTkeQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGV---VDVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 60-284 4.24e-57

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: 188.49  E-value: 4.24e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  60 NRYKDVLPYDQTRVILSLlQEEGHSDYINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACREIENGRK 139
Cdd:cd14615   1 NRYNNVLPYDISRVKLSV-QSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 140 RCERYWAQEQePLQTGLFCITLIKEKWLnEDIMLRTLKVTFQK--ESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARRL 217
Cdd:cd14615  80 KCEEYWPSKQ-KKDYGDITVTMTSEIVL-PEWTIRDFTVKNAQtnESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREY 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18375655 218 QGSGPE--PLCVHCSAGCGRTGVLCTVDYvrqllLTQMIPPDFS--LFDVVLKMRKQRPAAVQTEEQYRFL 284
Cdd:cd14615 158 MKQNPPnsPILVHCSAGVGRTGTFIAIDR-----LIYQIENENVvdVYGIVYDLRMHRPLMVQTEDQYVFL 223
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 55-288 2.51e-55

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: 184.84  E-value: 2.51e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  55 ENVRKNRYKDVLPYDQTRVILSL--LQEEGhSDYINGNFI--------RGVDGSLAYIATQGPLPHTLLDFWRLVWEFGV 124
Cdd:cd14605   1 ENKNKNRYKNILPFDHTRVVLHDgdPNEPV-SDYINANIImpefetkcNNSKPKKSYIATQGCLQNTVNDFWRMVFQENS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 125 KVILMACREIENGRKRCERYWAQEQEPLQTGLFCITLIKEKwLNEDIMLRTLKVTFQKE---SRSVYQLQYMSWPDRGVP 201
Cdd:cd14605  80 RVIVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKES-AAHDYILRELKLSKVGQgntERTVWQYHFRTWPDHGVP 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 202 SSPDHMLAMVEEARRLQGS--GPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIPPDFSLFDVVLKMRKQRPAAVQTEE 279
Cdd:cd14605 159 SDPGGVLDFLEEVHHKQESimDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVDCDIDVPKTIQMVRSQRSGMVQTEA 238


                ....*....
gi 18375655 280 QYRFLYHTV 288
Cdd:cd14605 239 QYRFIYMAV 247
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 47-291 7.40e-55

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


Pssm-ID: 350462 [Multi-domain]  Cd Length: 245  Bit Score: 183.17  E-value: 7.40e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  47 STVAGSRPENVRKNRYKDVLPYDQTRVILSLLQEEGHSDYINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKV 126
Cdd:cd14614   3 PHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 127 ILMACREIENGRKRCERYWAQEQEPLQTGLFCITLIKEKWLNEDImLRTLKVTFQKESRSVYQLQYMSWPDRGVPS--SP 204
Cdd:cd14614  83 IVMLTQCNEKRRVKCDHYWPFTEEPVAYGDITVEMLSEEEQPDWA-IREFRVSYADEVQDVMHFNYTAWPDHGVPTanAA 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 205 DHMLAMVEEARRLQGSGPEPLCVHCSAGCGRTGVLCTVDYVRQLLltqmipPDFSLFDV---VLKMRKQRPAAVQTEEQY 281
Cdd:cd14614 162 ESILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHI------RDHEFVDIlglVSEMRSYRMSMVQTEEQY 235

                       250
                ....*....|
gi 18375655 282 RFLYHTVAQM 291
Cdd:cd14614 236 IFIHQCVQLM 245
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 60-285 9.53e-55

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: 182.43  E-value: 9.53e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  60 NRYKDVLPYDQTRVILSLLQEEGHSDYINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACREIENGRK 139
Cdd:cd14617   1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 140 RCERYWAQEQEPLQTGLFCITLIKEKWLNEdIMLRTLKVTFQKE---SRSVYQLQYMSWPDRGVPSSPDHMLAMVEEAR- 215
Cdd:cd14617  81 KCDHYWPADQDSLYYGDLIVQMLSESVLPE-WTIREFKICSEEQldaPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVRd 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18375655 216 ---RLQGSGPEplCVHCSAGCGRTGVLCTVDYVRQLLLTQmipPDFSLFDVVLKMRKQRPAAVQTEEQYRFLY 285
Cdd:cd14617 160 yinRTPGSGPT--VVHCSAGVGRTGTFIALDRILQQLDSK---DSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 47-290 1.21e-53

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


Pssm-ID: 350458 [Multi-domain]  Cd Length: 283  Bit Score: 181.41  E-value: 1.21e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  47 STVAGSRPENVRKNRYKDVLPYDQTRVILSLLQEEGHSDYINGNFIRGVDG-SLAYIATQGPLPHTLLDFWRLVWEFGVK 125
Cdd:cd14610  35 ATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMDHDPrNPAYIATQGPLPATVADFWQMVWESGCV 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 126 VILMACREIENGRKRCERYWAQEQEPLQTgLFCITLIKEKWLNEDIMLRT--LKVTFQKESRSVYQLQYMSWPDRGVPSS 203
Cdd:cd14610 115 VIVMLTPLAENGVKQCYHYWPDEGSNLYH-IYEVNLVSEHIWCEDFLVRSfyLKNLQTNETRTVTQFHFLSWNDQGVPAS 193

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 204 PDHMLAMVEEARRLQGSGPEPLCVHCSAGCGRTGVLCTVDYVrqllLTQMI--PPDFSLFDVVLKMRKQRPAAVQTEEQY 281
Cdd:cd14610 194 TRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMV----LNKMAkgAKEIDIAATLEHLRDQRPGMVQTKEQF 269


                ....*....
gi 18375655 282 RFLYHTVAQ 290
Cdd:cd14610 270 EFALTAVAE 278
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 85-283 2.47e-53

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: 177.91  E-value: 2.47e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  85 DYINGNF----IRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACREIENGRKRCERYWAQEQEPLQTGLFCIT 160
Cdd:cd14541   1 DYINANYvnmeIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGETMQFGNLQIT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 161 LIKEKwLNEDIMLRTLKVTFQK--ESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARRLQGSGPEPLCVHCSAGCGRTGV 238
Cdd:cd14541  81 CVSEE-VTPSFAFREFILTNTNtgEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGIGRTGV 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 18375655 239 LCTVDYVrqLLLTQMIPPDFSLfDVVLKMRKQRPAAVQTEEQYRF 283
Cdd:cd14541 160 LITMETA--MCLIEANEPVYPL-DIVRTMRDQRAMLIQTPSQYRF 201
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 47-290 9.16e-53

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: 178.69  E-value: 9.16e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  47 STVAGSRPENVRKNRYKDVLPYDQTRVILSLLQEEGHSDYINGNFIRGVDGSL-AYIATQGPLPHTLLDFWRLVWEFGVK 125
Cdd:cd14609  33 TCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIEHDPRMpAYIATQGPLSHTIADFWQMVWENGCT 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 126 VILMACREIENGRKRCERYWAQEQEPLQTgLFCITLIKEKWLNEDIMLRT--LKVTFQKESRSVYQLQYMSWPDRGVPSS 203
Cdd:cd14609 113 VIVMLTPLVEDGVKQCDRYWPDEGSSLYH-IYEVNLVSEHIWCEDFLVRSfyLKNVQTQETRTLTQFHFLSWPAEGIPSS 191

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 204 PDHMLAMVEEARRLQGSGPEPLCVHCSAGCGRTGVLCTVDYVrqllLTQMIP--PDFSLFDVVLKMRKQRPAAVQTEEQY 281
Cdd:cd14609 192 TRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMV----LNRMAKgvKEIDIAATLEHVRDQRPGMVRTKDQF 267


                ....*....
gi 18375655 282 RFLYHTVAQ 290
Cdd:cd14609 268 EFALTAVAE 276
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 86-285 1.52e-52

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: 175.62  E-value: 1.52e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  86 YINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACREIENGRKRCERYWAQEQEPlQTGLFCITLikek 165
Cdd:cd14549   1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTE-TYGNIQVTL---- 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 166 wLNEDIM----LRTL--------KVTFQKESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARRLQGSGPEPLCVHCSAGC 233
Cdd:cd14549  76 -LSTEVLatytVRTFslknlklkKVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGV 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 18375655 234 GRTGVLCTVD-YVRQLLLTQMIppdfSLFDVVLKMRKQRPAAVQTEEQYRFLY 285
Cdd:cd14549 155 GRTGTYIVIDsMLQQIQDKGTV----NVFGFLKHIRTQRNYLVQTEEQYIFIH 203
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 54-290 3.68e-52

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: 176.18  E-value: 3.68e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  54 PENVRKNRYKDVLPYDQTRVILSLLQ-EEGHSDYINGNFIRGVDGS-LAYIATQGPLPHTLLDFWRLVWEFGVKVILMAC 131
Cdd:cd14612  13 PGHASKDRYKTILPNPQSRVCLRRAGsQEEEGSYINANYIRGYDGKeKAYIATQGPMLNTVSDFWEMVWQEECPIIVMIT 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 132 ReIENGRKRCERYWAQEQEPLqtGLFCITLIKEKWLNEdIMLRTLKVTFQKESRSVYQLQYMSWPDRGVPSSPD---HML 208
Cdd:cd14612  93 K-LKEKKEKCVHYWPEKEGTY--GRFEIRVQDMKECDG-YTIRDLTIQLEEESRSVKHYWFSSWPDHQTPESAGpllRLV 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 209 AMVEEARRLQGSgPEPLCVHCSAGCGRTGV-LCTVDYVRQLLLTQmippDFSLFDVVLKMRKQRPAAVQTEEQYRFLYHT 287
Cdd:cd14612 169 AEVEESRQTAAS-PGPIVVHCSAGIGRTGCfIATSIGCQQLKDTG----KVDILGIVCQLRLDRGGMIQTSEQYQFLHHT 243


                ...
gi 18375655 288 VAQ 290
Cdd:cd14612 244 LAL 246
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 55-290 3.71e-52

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


Pssm-ID: 350478 [Multi-domain]  Cd Length: 237  Bit Score: 175.98  E-value: 3.71e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  55 ENVRKNRYKDVLPYDQTRVILSLLQEEGHSDYINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACREI 134
Cdd:cd14630   2 ENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 135 ENGRKRCERYWAQEQEPLqtGLFCITLIKEKWLNEDImLRTLkvTFQK----ESRSVYQLQYMSWPDRGVPSSPDHMLAM 210
Cdd:cd14630  82 EVGRVKCVRYWPDDTEVY--GDIKVTLIETEPLAEYV-IRTF--TVQKkgyhEIREIRQFHFTSWPDHGVPCYATGLLGF 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 211 VEEARRLQGSGPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIppdFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTVAQ 290
Cdd:cd14630 157 VRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGV---VDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 86-288 3.99e-52

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


Pssm-ID: 350444 [Multi-domain]  Cd Length: 207  Bit Score: 174.55  E-value: 3.99e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  86 YINGNFIRGVDGS--LAYIATQGPLPHTLLDFWRLVWEFGVKVILMACREIENGRKRCERYWA-QEQEPLQTGLFCITLI 162
Cdd:cd14596   1 YINASYITMPVGEeeLFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPeTLQEPMELENYQLRLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 163 KEKWLnEDIMLRTLKVTFQK--ESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARRLQGSGpePLCVHCSAGCGRTGVLC 240
Cdd:cd14596  81 NYQAL-QYFIIRIIKLVEKEtgENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNTG--PIVVHCSAGIGRAGVLI 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 18375655 241 TVDYVRQLLLTQMippDFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTV 288
Cdd:cd14596 158 CVDVLLSLIEKDL---SFNIKDIVREMRQQRYGMIQTKDQYLFCYKVV 202
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 54-290 5.24e-52

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


Pssm-ID: 350456 [Multi-domain]  Cd Length: 277  Bit Score: 176.75  E-value: 5.24e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  54 PENVRKNRYKDVLPYDQTRVILsllqEEGHSDYINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACRE 133
Cdd:cd14608  23 PKNKNRNRYRDVSPFDHSRIKL----HQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRV 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 134 IENGRKRCERYWAQEQEplQTGLFCITLIKEKWLNEDI----MLRTLKVT--FQKESRSVYQLQYMSWPDRGVPSSPDHM 207
Cdd:cd14608  99 MEKGSLKCAQYWPQKEE--KEMIFEDTNLKLTLISEDIksyyTVRQLELEnlTTQETREILHFHYTTWPDFGVPESPASF 176

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 208 LAMVEEARRLQGSGPE--PLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIPPDFSLFDVVLKMRKQRPAAVQTEEQYRFLY 285
Cdd:cd14608 177 LNFLFKVRESGSLSPEhgPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSY 256


                ....*
gi 18375655 286 HTVAQ 290
Cdd:cd14608 257 LAVIE 261
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 29-290 2.28e-51

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: 174.84  E-value: 2.28e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  29 EFSDIQACSAawkaDGVCSTVAGSRPENVRKNRYKDVLPYDQTRVILSLL--QEEGHSDYINGNFIRGVDGSLAYIATQG 106
Cdd:cd17667   4 DFEEVQRCTA----DMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLpgKDSKHSDYINANYVDGYNKAKAYIATQG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 107 PLPHTLLDFWRLVWEFGVKVILMACREIENGRKRCERYWAQEQEPlQTGLFCITLIKEK----WLNEDIMLRTLKVTF-- 180
Cdd:cd17667  80 PLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSE-EYGNIIVTLKSTKihacYTVRRFSIRNTKVKKgq 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 181 ------QKESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARRLQGSGPEPLCVHCSAGCGRTGVLCTVDYVRQLLltqmi 254
Cdd:cd17667 159 kgnpkgRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQI----- 233

                       250       260       270
                ....*....|....*....|....*....|....*....
gi 18375655 255 pPDFSLFDVV--LK-MRKQRPAAVQTEEQYRFLYHTVAQ 290
Cdd:cd17667 234 -KDKSTVNVLgfLKhIRTQRNYLVQTEEQYIFIHDALLE 271
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 56-290 3.01e-51

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: 174.84  E-value: 3.01e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  56 NVRKNRYKDVLPYDQTRVILSLLQEEGHSDYINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACREIE 135
Cdd:cd14626  41 NKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEE 120

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 136 NGRKRCERYWAQEQEPlQTGLFCITLIkekwlnEDIMLRTLKV-TF------QKESRSVYQLQYMSWPDRGVPSSPDHML 208
Cdd:cd14626 121 KSRVKCDQYWPIRGTE-TYGMIQVTLL------DTVELATYSVrTFalykngSSEKREVRQFQFMAWPDHGVPEYPTPIL 193

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 209 AMVeeaRRLQGSGPE---PLCVHCSAGCGRTGVLCTVDyvrQLLLTQMIPPDFSLFDVVLKMRKQRPAAVQTEEQYRFLY 285
Cdd:cd14626 194 AFL---RRVKACNPPdagPMVVHCSAGVGRTGCFIVID---AMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIH 267


                ....*
gi 18375655 286 HTVAQ 290
Cdd:cd14626 268 EALLE 272
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 49-294 5.21e-50

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: 171.84  E-value: 5.21e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  49 VAGSRPENVRKNRYKDVLPYDQTRVILSLLQEEGHSDYINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVIL 128
Cdd:cd14628  45 ISANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVV 124

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 129 MACREIENGRKRCERYWAQEQEPlQTGLFCITLIKEKWLNEDImLRTLKVTFQK--ESRSVYQLQYMSWPDRGVPSSPDH 206
Cdd:cd14628 125 MLTKLREMGREKCHQYWPAERSA-RYQYFVVDPMAEYNMPQYI-LREFKVTDARdgQSRTVRQFQFTDWPEQGVPKSGEG 202

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 207 MLAMVEEARRL--QGSGPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIppdFSLFDVVLKMRKQRPAAVQTEEQYRFL 284
Cdd:cd14628 203 FIDFIGQVHKTkeQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGV---VDIFQTVKMLRTQRPAMVQTEDQYQFC 279

                       250
                ....*....|
gi 18375655 285 YHTVAQMFCS 294
Cdd:cd14628 280 YRAALEYLGS 289
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 54-288 7.78e-50

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: 170.53  E-value: 7.78e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  54 PENVRKNRYKDVLPYDQTRVILsllqEEGHSDYINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACRE 133
Cdd:cd14607  22 PENRNRNRYRDVSPYDHSRVKL----QNTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRI 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 134 IENGRKRCERYW-AQEQEPL---QTGlFCITLikekwLNEDIM------LRTLKVTFQKESRSVYQLQYMSWPDRGVPSS 203
Cdd:cd14607  98 VEKDSVKCAQYWpTDEEEVLsfkETG-FSVKL-----LSEDVKsyytvhLLQLENINSGETRTISHFHYTTWPDFGVPES 171

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 204 PDHMLAMVEEARRLQGSGPE--PLCVHCSAGCGRTGVLCTVDYVrQLLLTQMIPPDFSLFDVVLKMRKQRPAAVQTEEQY 281
Cdd:cd14607 172 PASFLNFLFKVRESGSLSPEhgPAVVHCSAGIGRSGTFSLVDTC-LVLMEKKDPDSVDIKQVLLDMRKYRMGLIQTPDQL 250


                ....*..
gi 18375655 282 RFLYHTV 288
Cdd:cd14607 251 RFSYMAV 257
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 49-294 4.12e-49

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: 169.53  E-value: 4.12e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  49 VAGSRPENVRKNRYKDVLPYDQTRVILSLLQEEGHSDYINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVIL 128
Cdd:cd14627  46 ISANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVV 125

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 129 MACREIENGRKRCERYWAQEQEPlQTGLFCITLIKEKWLNEDImLRTLKVTFQK--ESRSVYQLQYMSWPDRGVPSSPDH 206
Cdd:cd14627 126 MLTKLREMGREKCHQYWPAERSA-RYQYFVVDPMAEYNMPQYI-LREFKVTDARdgQSRTVRQFQFTDWPEQGVPKSGEG 203

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 207 MLAMVEEARRL--QGSGPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIppdFSLFDVVLKMRKQRPAAVQTEEQYRFL 284
Cdd:cd14627 204 FIDFIGQVHKTkeQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGV---VDIFQTVKMLRTQRPAMVQTEDEYQFC 280

                       250
                ....*....|
gi 18375655 285 YHTVAQMFCS 294
Cdd:cd14627 281 YQAALEYLGS 290
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 86-290 9.60e-49

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


Pssm-ID: 350388 [Multi-domain]  Cd Length: 219  Bit Score: 166.09  E-value: 9.60e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  86 YINGNFIRGVDGS--LAYIATQGPLPHTLLDFWRLVWEFGVKVILMACREIENGRKRCERYWAQ---EQEPLQTGLFCIT 160
Cdd:cd14540   1 YINASHITATVGGkqRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTlggEHDALTFGEYKVS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 161 liKEKWLNEDIML-RTLKV--TFQKESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEAR--RLQGSG-------PEPLCVH 228
Cdd:cd14540  81 --TKFSVSSGCYTtTGLRVkhTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINsvRRHTNQdvaghnrNPPTLVH 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18375655 229 CSAGCGRTGVLCTVDYVRQLLLTQMiPPDFSLfdVVLKMRKQRPAAVQTEEQYRFLYHTVAQ 290
Cdd:cd14540 159 CSAGVGRTGVVILADLMLYCLDHNE-ELDIPR--VLALLRHQRMLLVQTLAQYKFVYNVLIQ 217
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 86-290 2.37e-48

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: 164.92  E-value: 2.37e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  86 YINGNFIRGVDG-SLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACREIENGRKRCERYWAQEQEPLQtGLFCITLIKE 164
Cdd:cd14546   1 YINASTIYDHDPrNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVY-HIYEVHLVSE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 165 KWLNEDIMLRT--LKVTFQKESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARRLQGSGPEPLCVHCSAGCGRTGVLCTV 242
Cdd:cd14546  80 HIWCDDYLVRSfyLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRTGTYILI 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 18375655 243 DyvrqLLLTQMIP--PDFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTVAQ 290
Cdd:cd14546 160 D----MVLNRMAKgaKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 85-292 4.40e-48

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: 164.35  E-value: 4.40e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  85 DYINGNFIRGVDGSLA----YIATQGPLPHTLLDFWRLVWEFGVKVILMACREIENGRKRCERYWAQEQEPLQTGLFCIT 160
Cdd:cd14601   1 DYINANYINMEIPSSSiinrYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSSSYGGFQVT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 161 LIKEKWlNEDIMLRTLKVTFQ--KESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARRLQGSGPEPLCVHCSAGCGRTGV 238
Cdd:cd14601  81 CHSEEG-NPAYVFREMTLTNLekNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTGV 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 18375655 239 LCTVDYVrqLLLTQMIPPDFSLfDVVLKMRKQRPAAVQTEEQYRFLYHTVAQMF 292
Cdd:cd14601 160 LITMETA--MCLIECNQPVYPL-DIVRTMRDQRAMMIQTPSQYRFVCEAILKVY 210
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 61-290 2.01e-47

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


Pssm-ID: 350471 [Multi-domain]  Cd Length: 228  Bit Score: 163.29  E-value: 2.01e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  61 RYKDVLPYDQTRVILSLLQEEGHSDYINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACREIENGRKR 140
Cdd:cd14623   1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 141 CERYWAQEQEpLQTGLFCITLIKEKwLNEDIMLRTLKVTFQKE--SRSVYQLQYMSWPDRGVPSSPDHMLAMVEEA-RRL 217
Cdd:cd14623  81 CAQYWPSDGS-VSYGDITIELKKEE-ECESYTVRDLLVTNTREnkSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVqKQQ 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18375655 218 QGSGPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIppdFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTVAQ 290
Cdd:cd14623 159 QQSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGI---LDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 86-288 2.92e-47

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: 161.67  E-value: 2.92e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  86 YINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACREIENGRKRCERYWAQEQEpLQTGLFCITLIKEK 165
Cdd:cd14552   1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGS-VSSGDITVELKDQT 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 166 wLNEDIMLRTLKVTFQKE--SRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARRLQG-SGPEPLCVHCSAGCGRTGVLCTV 242
Cdd:cd14552  80 -DYEDYTLRDFLVTKGKGgsTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQqSGNHPITVHCSAGAGRTGTFCAL 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 18375655 243 DYVRQLLLTQMIppdFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTV 288
Cdd:cd14552 159 STVLERVKAEGV---LDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 49-294 3.56e-47

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: 164.51  E-value: 3.56e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  49 VAGSRPENVRKNRYKDVLPYDQTRVILSLLQEEGHSDYINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVIL 128
Cdd:cd14629  46 ISANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVV 125

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 129 MACREIENGRKRCERYWAQEQEPlQTGLFCITLIKEKWLNEDImLRTLKVTFQK--ESRSVYQLQYMSWPDRGVPSSPDH 206
Cdd:cd14629 126 MLTKLREMGREKCHQYWPAERSA-RYQYFVVDPMAEYNMPQYI-LREFKVTDARdgQSRTIRQFQFTDWPEQGVPKTGEG 203

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 207 MLAMVEEARRL--QGSGPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIppdFSLFDVVLKMRKQRPAAVQTEEQYRFL 284
Cdd:cd14629 204 FIDFIGQVHKTkeQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGV---VDMFQTVKTLRTQRPAMVQTEDQYQLC 280

                       250
                ....*....|
gi 18375655 285 YHTVAQMFCS 294
Cdd:cd14629 281 YRAALEYLGS 290
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 60-285 1.07e-46

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


Pssm-ID: 350464 [Multi-domain]  Cd Length: 224  Bit Score: 160.84  E-value: 1.07e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  60 NRYKDVLPYDQTRVilSLLQEEG--HSDYINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACREIENG 137
Cdd:cd14616   1 NRFPNIKPYNNNRV--KLIADAGvpGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 138 RKRCERYWAQEQEPLQT-GLFCITLIKEKwLNEDIMLRTLKVTFQKESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARR 216
Cdd:cd14616  79 RIRCHQYWPEDNKPVTVfGDIVITKLMED-VQIDWTIRDLKIERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVRA 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18375655 217 LQGSGPEPLCVHCSAGCGRTGVLCTVDYvrqllLTQMIPP-DF-SLFDVVLKMRKQRPAAVQTEEQYRFLY 285
Cdd:cd14616 158 SRAHDNTPMIVHCSAGVGRTGVFIALDH-----LTQHINDhDFvDIYGLVAELRSERMCMVQNLAQYIFLH 223
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 41-290 1.41e-46

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


Pssm-ID: 350447 [Multi-domain]  Cd Length: 287  Bit Score: 162.86  E-value: 1.41e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  41 KADGVCSTVAgsRPENVRKNRYKDVLPYDQTRVILsLLQEEGHSDYINGNFIRGVDG--SLAYIATQGPLPHTLLDFWRL 118
Cdd:cd14599  25 KADGVFTTAT--LPENAERNRIREVVPYEENRVEL-VPTKENNTGYINASHIKVTVGgeEWHYIATQGPLPHTCHDFWQM 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 119 VWEFGVKVILMACREIENGRKRCERYWAQ---EQEPLQTGLFCITlikEKWLNEDIMLRT--LKVT--FQKESRSVYQLQ 191
Cdd:cd14599 102 VWEQGVNVIAMVTAEEEGGRSKSHRYWPKlgsKHSSATYGKFKVT---TKFRTDSGCYATtgLKVKhlLSGQERTVWHLQ 178

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 192 YMSWPDRGVPSSPDHMLAMVEE---ARRLQGSGPE-------PLCVHCSAGCGRTGVLCtvdyVRQLLLTQMIPPDFSLF 261
Cdd:cd14599 179 YTDWPDHGCPEEVQGFLSYLEEiqsVRRHTNSMLDstkncnpPIVVHCSAGVGRTGVVI----LTELMIGCLEHNEKVEV 254

                       250       260       270
                ....*....|....*....|....*....|
gi 18375655 262 DVVLK-MRKQRPAAVQTEEQYRFLYHTVAQ 290
Cdd:cd14599 255 PVMLRhLREQRMFMIQTIAQYKFVYQVLIQ 284
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 50-290 1.93e-46

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: 162.13  E-value: 1.93e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  50 AGSRPENVRKNRYKDVLPYDQTRVILSLLQEEGHSDYINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILM 129
Cdd:cd14633  34 SAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIM 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 130 ACREIENGRKRCERYWAQEQEPLQTglFCITLIKEKWLNEDImLRTLKVTFQ--KESRSVYQLQYMSWPDRGVPSSPDHM 207
Cdd:cd14633 114 VTNLVEVGRVKCCKYWPDDTEIYKD--IKVTLIETELLAEYV-IRTFAVEKRgvHEIREIRQFHFTGWPDHGVPYHATGL 190

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 208 LAMVEEARRLQGSGPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIppdFSLFDVVLKMRKQRPAAVQTEEQYRFLYHT 287
Cdd:cd14633 191 LGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGV---VDIYNCVRELRSRRVNMVQTEEQYVFIHDA 267


                ...
gi 18375655 288 VAQ 290
Cdd:cd14633 268 ILE 270
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 56-290 3.88e-46

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: 161.41  E-value: 3.88e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  56 NVRKNRYKDVLPYDQTRVILSLLQEEGHSDYINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACREIE 135
Cdd:cd14625  47 NKPKNRYANVIAYDHSRVILQPIEGIMGSDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEE 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 136 NGRKRCERYWAQEQEPlQTGLFCITLIkekwlnEDIMLRTLKV-TF------QKESRSVYQLQYMSWPDRGVPSSPDHML 208
Cdd:cd14625 127 KSRIKCDQYWPSRGTE-TYGMIQVTLL------DTIELATFCVrTFslhkngSSEKREVRQFQFTAWPDHGVPEYPTPFL 199

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 209 AMVEEARRLQGSGPEPLCVHCSAGCGRTGVLCTVDyvrqlLLTQMIPPD--FSLFDVVLKMRKQRPAAVQTEEQYRFLYH 286
Cdd:cd14625 200 AFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVID-----AMLERIKHEktVDIYGHVTLMRSQRNYMVQTEDQYSFIHD 274


                ....
gi 18375655 287 TVAQ 290
Cdd:cd14625 275 ALLE 278
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 62-288 6.24e-46

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: 159.34  E-value: 6.24e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  62 YKDVLPYDQTRVILSLLQEEGHSDYINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACREIENGRKRC 141
Cdd:cd14620   1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 142 ERYWAqEQEPLQTGLF------CITLIkekwlneDIMLRTLKVTFQ-----KESRSVYQLQYMSWPDRGVPSSPDHMLAM 210
Cdd:cd14620  81 YQYWP-DQGCWTYGNIrvavedCVVLV-------DYTIRKFCIQPQlpdgcKAPRLVTQLHFTSWPDFGVPFTPIGMLKF 152

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18375655 211 VEEARRLQGSGPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQMippDFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTV 288
Cdd:cd14620 153 LKKVKSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQ---KVDVFEFVSRIRNQRPQMVQTDMQYSFIYQAL 227
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 56-290 9.47e-45

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: 157.97  E-value: 9.47e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  56 NVRKNRYKDVLPYDQTRVILSLLQEEGHSDYINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACREIE 135
Cdd:cd14624  47 NKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEE 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 136 NGRKRCERYWAQEQEPLQtGLFCITLIKEKWLnEDIMLRTLKV--TFQKESRSVYQLQYMSWPDRGVPSSPDHMLAMVEE 213
Cdd:cd14624 127 RSRVKCDQYWPSRGTETY-GLIQVTLLDTVEL-ATYCVRTFALykNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRR 204

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18375655 214 ARRLQGSGPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQmipPDFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTVAQ 290
Cdd:cd14624 205 VKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHE---KTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLE 278
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 54-289 1.64e-43

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


Pssm-ID: 350461 [Multi-domain]  Cd Length: 258  Bit Score: 153.86  E-value: 1.64e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  54 PENVRKNRYKDVLPYDQTRVIL-SLLQEEGHSDYINGNFIRGVDGS-LAYIATQGPLPHTLLDFWRLVWEFGVKVILMAC 131
Cdd:cd14613  23 PGLVRKNRYKTILPNPHSRVCLtSPDQDDPLSSYINANYIRGYGGEeKVYIATQGPTVNTVGDFWRMVWQERSPIIVMIT 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 132 rEIENGRKRCERYWAQEQePLQTGLFCItlIKEKWLNEDIMLRTLKVTFQKESRSVYQLQYMSWPDRGVPSSPDHMLAM- 210
Cdd:cd14613 103 -NIEEMNEKCTEYWPEEQ-VTYEGIEIT--VKQVIHADDYRLRLITLKSGGEERGLKHYWYTSWPDQKTPDNAPPLLQLv 178

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 211 --VEEARRLQGSGPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIppdFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTV 288
Cdd:cd14613 179 qeVEEARQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGV---VDILRTTCQLRLDRGGMIQTCEQYQFVHHVL 255


                .
gi 18375655 289 A 289
Cdd:cd14613 256 S 256
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 13-292 5.39e-43

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: 153.64  E-value: 5.39e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  13 ERLEARGGREGAVLAGEFSDIQACSAAWKADgvcstvAGSRPENVRKNRYKDVLPYDQTRVILSLLQEEGHSDYINGNFI 92
Cdd:cd14621  15 EEINRRMADDNKLFREEFNALPACPIQATCE------AASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINASFI 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  93 RGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACREIENGRKRCERYWAQEQeplqtglfCITLIKEKWLNEDIM 172
Cdd:cd14621  89 NGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQG--------CWTYGNIRVSVEDVT 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 173 L------------RTLKVTFQKESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARRLQGSGPEPLCVHCSAGCGRTGVLC 240
Cdd:cd14621 161 VlvdytvrkfciqQVGDVTNKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFI 240

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 18375655 241 TVDYVRQLLLTQMippDFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTVAQMF 292
Cdd:cd14621 241 VIDAMLDMMHAER---KVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHY 289
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 86-285 7.07e-43

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


Pssm-ID: 350496 [Multi-domain]  Cd Length: 206  Bit Score: 150.31  E-value: 7.07e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  86 YINGNFIRGVD-GSLA-YIATQGPLPHTLLDFWRLVWEFGVKVILMACREIENGRK-RCERYW-AQEQEPLQTGLFCITL 161
Cdd:cd17658   1 YINASLVETPAsESLPkFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFpAEENESREFGRISVTN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 162 IKEKWLNEDIMLRTLKVTfQKES----RSVYQLQYMSWPDRGVpssPDHMLAMVEEARRLQGSGPE--PLCVHCSAGCGR 235
Cdd:cd17658  81 KKLKHSQHSITLRVLEVQ-YIESeeppLSVLHIQYPEWPDHGV---PKDTRSVRELLKRLYGIPPSagPIVVHCSAGIGR 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 18375655 236 TGVLCTVDY-VRQLLLTQMIPPDFSlfDVVLKMRKQRPAAVQTEEQYRFLY 285
Cdd:cd17658 157 TGAYCTIHNtIRRILEGDMSAVDLS--KTVRKFRSQRIGMVQTQDQYIFCY 205
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 86-285 3.05e-42

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


Pssm-ID: 350387 [Multi-domain]  Cd Length: 205  Bit Score: 148.69  E-value: 3.05e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  86 YINGNFIRGVDGSLA-YIATQGPLPHTLLDFWRLVWEFGVKVILMACREIENGRKRCERYWAQEQ-EPLQTGLFCITLIK 163
Cdd:cd14539   1 YINASLIEDLTPYCPrFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERgQALVYGAITVSLQS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 164 EKWLNEDIMlRTLKVTF--QKESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEAR---RLQGSGPEPLCVHCSAGCGRTGV 238
Cdd:cd14539  81 VRTTPTHVE-RIISIQHkdTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHshyLQQRSLQTPIVVHCSSGVGRTGA 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 18375655 239 LCTVdY--VRQLLLTQMIPpdfSLFDVVLKMRKQRPAAVQTEEQYRFLY 285
Cdd:cd14539 160 FCLL-YaaVQEIEAGNGIP---DLPQLVRKMRQQRKYMLQEKEHLKFCY 204
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 85-288 1.05e-41

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: 147.07  E-value: 1.05e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  85 DYINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACREIENGRKRCERYWAQEQEpLQTGLFCITlIKE 164
Cdd:cd14622   1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGS-VTHGEITIE-IKN 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 165 KWLNEDIMLRTLKVTF--QKESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEA-RRLQGSGPEPLCVHCSAGCGRTGVLCT 241
Cdd:cd14622  79 DTLLETISIRDFLVTYnqEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVqKQQQQTGNHPIVVHCSAGAGRTGTFIA 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 18375655 242 VDYVRQLLLTQMIppdFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTV 288
Cdd:cd14622 159 LSNILERVKAEGL---LDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 86-285 1.16e-41

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: 146.90  E-value: 1.16e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  86 YINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACREIENGRKRCERYWAQEQEPLQT-GLFCITLIKE 164
Cdd:cd14557   1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAfGDVVVKINEE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 165 KwLNEDIMLRTLKVTFQKESRS---VYQLQYMSWPDRGVPSSPDHMLAMVEEARRLQGSGPEPLCVHCSAGCGRTGVLCT 241
Cdd:cd14557  81 K-ICPDYIIRKLNINNKKEKGSgreVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYIG 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 18375655 242 VD-YVRQLLLTQMIppdfSLFDVVLKMRKQRPAAVQTEEQYRFLY 285
Cdd:cd14557 160 IDaMLEGLEAEGRV----DVYGYVVKLRRQRCLMVQVEAQYILIH 200
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 86-285 1.74e-41

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: 146.38  E-value: 1.74e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  86 YINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACREIENGRKRCERYWAQEQeplQT-GLFCITLIKE 164
Cdd:cd14558   1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEK---KTyGDIEVELKDT 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 165 KWLNEDImLRTLKVTF--QKESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARRLQGSGPE------PLCVHCSAGCGRT 236
Cdd:cd14558  78 EKSPTYT-VRVFEITHlkRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNSkhgrsvPIVVHCSDGSSRT 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 18375655 237 GVLCTvdyVRQLLLTQMIPPDFSLFDVVLKMRKQRPAAVQTEEQYRFLY 285
Cdd:cd14558 157 GIFCA---LWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 86-288 3.20e-41

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: 145.89  E-value: 3.20e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  86 YINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACREIENGRKRCERYWAQEQEPlQTGLFCITLIKEK 165
Cdd:cd17668   1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSE-EYGNFLVTQKSVQ 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 166 WLN----EDIMLRTLKVT--FQK---ESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARRLQGSGPEPLCVHCSAGCGRT 236
Cdd:cd17668  80 VLAyytvRNFTLRNTKIKkgSQKgrpSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGRT 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 18375655 237 GVLCTVD-YVRQLLLTQMIppdfSLFDVVLKMRKQRPAAVQTEEQYRFLYHTV 288
Cdd:cd17668 160 GTYIVLDsMLQQIQHEGTV----NIFGFLKHIRSQRNYLVQTEEQYVFIHDAL 208
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 86-285 9.50e-41

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: 144.47  E-value: 9.50e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  86 YINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMaCREIENGRKRCERYWAqEQEPLQTGLFCITLIKEK 165
Cdd:cd14556   1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVM-LNQLDPKDQSCPQYWP-DEGSGTYGPIQVEFVSTT 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 166 wLNEDIMLRTLKVT----FQKESRSVYQLQYMSWP-DRGVPSSPDHMLAMVEEARRLQG-SGPEPLCVHCSAGCGRTGVL 239
Cdd:cd14556  79 -IDEDVISRIFRLQnttrPQEGYRMVQQFQFLGWPrDRDTPPSKRALLKLLSEVEKWQEqSGEGPIVVHCLNGVGRSGVF 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 18375655 240 CTVDYVRQLLLTQMIppdFSLFDVVLKMRKQRPAAVQTEEQYRFLY 285
Cdd:cd14556 158 CAISSVCERIKVENV---VDVFQAVKTLRNHRPNMVETEEQYKFCY 200
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 86-288 1.77e-40

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: 143.90  E-value: 1.77e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  86 YINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACREIENGRKRCERYWAQEQEPLqtGLFCITLIKEK 165
Cdd:cd14555   1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEVY--GDIKVTLVETE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 166 WLNEDImLRTLKVTFQ--KESRSVYQLQYMSWPDRGVPSSPDHMLAMVeeaRRLQGSGPE---PLCVHCSAGCGRTGVLC 240
Cdd:cd14555  79 PLAEYV-VRTFALERRgyHEIREVRQFHFTGWPDHGVPYHATGLLGFI---RRVKASNPPsagPIVVHCSAGAGRTGCYI 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 18375655 241 TVDYVRQLLLTQMIppdFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTV 288
Cdd:cd14555 155 VIDIMLDMAEREGV---VDIYNCVKELRSRRVNMVQTEEQYIFIHDAI 199
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 53-284 3.13e-40

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 146.69  E-value: 3.13e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655   53 RPENVRKNRYKDVLPYDQTRVILSLlQEEGHSDYINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMAC- 131
Cdd:PHA02747  48 KPENQPKNRYWDIPCWDHNRVILDS-GGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTp 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  132 REIENGRKRCERYWA-QEQEPLQTGLFCITLIKEKwLNEDIMLRTLKVTFQ--KESRSVYQLQYMSWPDRGVPSS-PD-- 205
Cdd:PHA02747 127 TKGTNGEEKCYQYWClNEDGNIDMEDFRIETLKTS-VRAKYILTLIEITDKilKDSRKISHFQCSEWFEDETPSDhPDfi 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  206 HMLAMVEEARRLQGS--GPE-----PLCVHCSAGCGRTGVLCTVDY-VRQLLLTQMIppdfSLFDVVLKMRKQRPAAVQT 277
Cdd:PHA02747 206 KFIKIIDINRKKSGKlfNPKdallcPIVVHCSDGVGKTGIFCAVDIcLNQLVKRKAI----CLAKTAEKIREQRHAGIMN 281


                 ....*..
gi 18375655  278 EEQYRFL 284
Cdd:PHA02747 282 FDDYLFI 288
PHA02738 PHA02738
hypothetical protein; Provisional
 56-300 6.48e-40

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 145.84  E-value: 6.48e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655   56 NVRKNRYKDVLPYDQTRVILSllQEEGHSDYINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACREIE 135
Cdd:PHA02738  49 NRKLNRYLDAVCFDHSRVILP--AERNRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKE 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  136 NGRKRCERYWAQ-EQEPLQTGLFCITLIK-EKWLNedIMLRTLKVTFQKES-RSVYQLQYMSWPDRGVPSSPDHMLAMVE 212
Cdd:PHA02738 127 NGREKCFPYWSDvEQGSIRFGKFKITTTQvETHPH--YVKSTLLLTDGTSAtQTVTHFNFTAWPDHDVPKNTSEFLNFVL 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  213 EARRLQ-------------GSGPEPLCVHCSAGCGRTGVLCTVDY-VRQLLLTQMIppdfSLFDVVLKMRKQRPAAVQTE 278
Cdd:PHA02738 205 EVRQCQkelaqeslqighnRLQPPPIVVHCNAGLGRTPCYCVVDIsISRFDACATV----SIPSIVSSIRNQRYYSLFIP 280

                        250       260
                 ....*....|....*....|..
gi 18375655  279 EQYRFLYHTVAQMFCSTLQNAS 300
Cdd:PHA02738 281 FQYFFCYRAVKRYVNLTVNKVS 302
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
54-284 9.93e-40

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 144.46  E-value: 9.93e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  54 PENVRKNRYKDVLPYDQTRVilsllQEEGhsDYINGNFIRGVDGSLaYIATQGPLPHTLLDFWRLVWEFGVKVI--LMAC 131
Cdd:COG5599  40 INGSPLNRFRDIQPYKETAL-----RANL--GYLNANYIQVIGNHR-YIATQYPLEEQLEDFFQMLFDNNTPVLvvLASD 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 132 REIENGRKRCERYW-AQEQEPLQTglFCITLIKEKWLNEDIMLRTLKVTFQ---KESRSVYQLQYMSWPDRGVPSSP--D 205
Cdd:COG5599 112 DEISKPKVKMPVYFrQDGEYGKYE--VSSELTESIQLRDGIEARTYVLTIKgtgQKKIEIPVLHVKNWPDHGAISAEalK 189

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 206 HMLAMVEEARRLQGSGPEPLCVHCSAGCGRTGVLCTVDYVRQlLLTQMIPPDFSLFDVVLKMRKQR-PAAVQTEEQYRFL 284
Cdd:COG5599 190 NLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSK-SINALVQITLSVEEIVIDMRTSRnGGMVQTSEQLDVL 268
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 72-290 1.26e-39

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: 142.08  E-value: 1.26e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  72 RVILSLLQEEGHSDYINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACREIENGRKRCERYWAQEQEP 151
Cdd:cd14631   1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTEV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 152 LqtGLFCITLIKEKWLNEDIMLR-TLKVTFQKESRSVYQLQYMSWPDRGVPSSPDHMLAMVeeaRRLQGSGPE---PLCV 227
Cdd:cd14631  81 Y--GDFKVTCVEMEPLAEYVVRTfTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFI---RRVKLSNPPsagPIVV 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18375655 228 HCSAGCGRTGVLCTVDYVRQLLLTQMIppdFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTVAQ 290
Cdd:cd14631 156 HCSAGAGRTGCYIVIDIMLDMAEREGV---VDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 59-286 3.21e-39

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: 141.21  E-value: 3.21e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  59 KNRYKDVLPYDQTRVILSLLQ-EEGHSDYINGNFIRGVDG-SLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACREIEN 136
Cdd:cd14611   2 KNRYKTILPNPHSRVCLKPKNsNDSLSTYINANYIRGYGGkEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 137 GRKrCERYWaqeqePLQTGLFCITLIKEKWLNE--DIMLRTLKVTFQKESRSVYQLQYMSWPDRGVPSSPDHMLAM---V 211
Cdd:cd14611  82 NEK-CVLYW-----PEKRGIYGKVEVLVNSVKEcdNYTIRNLTLKQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLmldV 155

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18375655 212 EEaRRLQGSGPEPLCVHCSAGCGRTGV-LCTVDYVRQLLLTQMIppdfSLFDVVLKMRKQRPAAVQTEEQYRFLYH 286
Cdd:cd14611 156 EE-DRLASPGRGPVVVHCSAGIGRTGCfIATTIGCQQLKEEGVV----DVLSIVCQLRVDRGGMVQTSEQYEFVHH 226
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 53-300 8.85e-38

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 140.16  E-value: 8.85e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655   53 RPENVRKNRYKDVLPYDQTRVILS-------------------LLQEEGHSDYINGNFIRGVDGSLAYIATQGPLPHTLL 113
Cdd:PHA02746  48 KKENLKKNRFHDIPCWDHSRVVINaheslkmfdvgdsdgkkieVTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSE 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  114 DFWRLVWEFGVKVILmACREIENGRKRCERYWAQEQE-PLQTGLFC---ITLIKEKWLNEDIMLRTLKVTfqKESRSVYQ 189
Cdd:PHA02746 128 DFFKLISEHESQVIV-SLTDIDDDDEKCFELWTKEEDsELAFGRFVakiLDIIEELSFTKTRLMITDKIS--DTSREIHH 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  190 LQYMSWPDRGVPSSPDHMLAMV----EEARRL------QGSGPEPLCVHCSAGCGRTGVLCTVD-YVRQLLLTQMIppdf 258
Cdd:PHA02746 205 FWFPDWPDNGIPTGMAEFLELInkvnEEQAELikqadnDPQTLGPIVVHCSAGIGRAGTFCAIDnALEQLEKEKEV---- 280

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 18375655  259 SLFDVVLKMRKQRPAAVQTEEQYRFLYHTVAQMFCSTLQNAS 300
Cdd:PHA02746 281 CLGEIVLKIRKQRHSSVFLPEQYAFCYKALKYAIIEEAKKKF 322
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 186-290 1.47e-37

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: 1.47e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655    186 SVYQLQYMSWPDRGVPSSPDHMLAMVEEARRLQGSGPE--PLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIPPDFslFDV 263
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESsgPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGEVDI--FDT 78

                           90       100
                   ....*....|....*....|....*..
gi 18375655    264 VLKMRKQRPAAVQTEEQYRFLYHTVAQ 290
Cdd:smart00012  79 VKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
186-290 1.47e-37

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 132.87  E-value: 1.47e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655    186 SVYQLQYMSWPDRGVPSSPDHMLAMVEEARRLQGSGPE--PLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIPPDFslFDV 263
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESsgPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGEVDI--FDT 78

                           90       100
                   ....*....|....*....|....*..
gi 18375655    264 VLKMRKQRPAAVQTEEQYRFLYHTVAQ 290
Cdd:smart00404  79 VKELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 86-290 1.65e-37

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: 135.95  E-value: 1.65e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  86 YINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACREIENGRKRCERYWAQEQEplQTGLFCITLIKEK 165
Cdd:cd14632   1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSD--TYGDIKITLLKTE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 166 WLNEdIMLRTLKVTFQKES--RSVYQLQYMSWPDRGVPSSPDHMLAMVeeaRRLQGSGPE---PLCVHCSAGCGRTGVLC 240
Cdd:cd14632  79 TLAE-YSVRTFALERRGYSarHEVKQFHFTSWPEHGVPYHATGLLAFI---RRVKASTPPdagPVVVHCSAGAGRTGCYI 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 18375655 241 TVDYVRQLLLTQMIppdFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTVAQ 290
Cdd:cd14632 155 VLDVMLDMAECEGV---VDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 86-285 1.99e-37

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: 135.81  E-value: 1.99e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  86 YINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACREIENGRKRCERYWAQEQEPLQTGLF-----CIT 160
Cdd:cd14551   1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTYGNLRvrvedTVV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 161 LIkekwlneDIMLRTL------KVTFQKESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARRLQGSGPEPLCVHCSAGCG 234
Cdd:cd14551  81 LV-------DYTTRKFciqkvnRGIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVG 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 18375655 235 RTGVLCTVDYVRQLLLTQMippDFSLFDVVLKMRKQRPAAVQTEEQYRFLY 285
Cdd:cd14551 154 RTGTFIVIDAMLDMMHAEG---KVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 55-290 3.92e-37

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 137.83  E-value: 3.92e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655   55 ENVRKNRYKDVLPYDQTRVILSLlqEEGHSDYINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACREI 134
Cdd:PHA02742  51 KNMKKCRYPDAPCFDRNRVILKI--EDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIM 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  135 ENGRKRCERYW-AQEQEPLQTGLFCITLIKEKWLnEDIMLRTLKVTFQKESRS--VYQLQYMSWPDRGVPSSPDHMLAMV 211
Cdd:PHA02742 129 EDGKEACYPYWmPHERGKATHGEFKIKTKKIKSF-RNYAVTNLCLTDTNTGASldIKHFAYEDWPHGGLPRDPNKFLDFV 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  212 EEARRLQGS-----------GPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIPPdfsLFDVVLKMRKQRPAAVQTEEQ 280
Cdd:PHA02742 208 LAVREADLKadvdikgenivKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIP---LLSIVRDLRKQRHNCLSLPQQ 284

                        250
                 ....*....|
gi 18375655  281 YRFLYHTVAQ 290
Cdd:PHA02742 285 YIFCYFIVLI 294
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 86-290 1.60e-33

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


Pssm-ID: 350446 [Multi-domain]  Cd Length: 220  Bit Score: 125.86  E-value: 1.60e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  86 YINGNFIRGVDGSLA--YIATQGPLPHTLLDFWRLVWEFGVKVILMACREIENGRKRCERYW---AQEQEPLQTGLFCIT 160
Cdd:cd14598   1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWprlGSRHNTVTYGRFKIT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 161 LikeKWLNEDIMLRT----LKVTFQKESRSVYQLQYMSWPDRGVPSSPDHMLAMVEE---ARRLQGS-----GPE-PLCV 227
Cdd:cd14598  81 T---RFRTDSGCYATtglkIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEiqsVRRHTNStidpkSPNpPVLV 157

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18375655 228 HCSAGCGRTGVLctvdyvrqLLLTQMIP--PDFSLFDV--VLKM-RKQRPAAVQTEEQYRFLYHTVAQ 290
Cdd:cd14598 158 HCSAGVGRTGVV--------ILSEIMIAclEHNEMLDIprVLDMlRQQRMMMVQTLSQYTFVYKVLIQ 217
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 86-285 8.36e-24

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: 98.55  E-value: 8.36e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  86 YINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMaCREIENGrKRCERYWAQEQE----PLQTGLFCITl 161
Cdd:cd14634   1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVM-LNEMDAA-QLCMQYWPEKTSccygPIQVEFVSAD- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 162 ikekwLNEDIMLRTLKVTF----QKESRSVYQLQYMSWPD-RGVPSSPDHMLAMVEEARRLQ---GSGPEPLCVHCSAGC 233
Cdd:cd14634  78 -----IDEDIISRIFRICNmarpQDGYRIVQHLQYIGWPAyRDTPPSKRSILKVVRRLEKWQeqyDGREGRTVVHCLNGG 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 18375655 234 GRTGVLCTVDYVRQLLLTQMIppdFSLFDVVLKMRKQRPAAVQTEEQYRFLY 285
Cdd:cd14634 153 GRSGTFCAICSVCEMIQQQNI---IDVFHTVKTLRNNKSNMVETLEQYKFVY 201
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 86-285 1.72e-23

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: 97.79  E-value: 1.72e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  86 YINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMaCREIENGRKrCERYWAQEQE----PLQTGlfCITL 161
Cdd:cd14636   1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVM-LNEVDLAQG-CPQYWPEEGMlrygPIQVE--CMSC 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 162 IkekwLNEDIMLRTLKVTF----QKESRSVYQLQYMSWPD-RGVPSSPDHMLAMVEEARRLQ---GSGPEPLCVHCSAGC 233
Cdd:cd14636  77 S----MDCDVISRIFRICNltrpQEGYLMVQQFQYLGWAShREVPGSKRSFLKLILQVEKWQeecDEGEGRTIIHCLNGG 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 18375655 234 GRTGVLCTVDYVRQLLLTQMIppdFSLFDVVLKMRKQRPAAVQTEEQYRFLY 285
Cdd:cd14636 153 GRSGMFCAISIVCEMIKRQNV---VDVFHAVKTLRNSKPNMVETPEQYRFCY 201
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 86-285 2.46e-22

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


Pssm-ID: 350485 [Multi-domain]  Cd Length: 207  Bit Score: 94.59  E-value: 2.46e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  86 YINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACR-EIENGRKRCERYWA----QEQEPLQTGLFCIT 160
Cdd:cd14637   1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQlNQSNSAWPCLQYWPepglQQYGPMEVEFVSGS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 161 likekwLNEDIMLRTLKVT----FQKESRSVYQLQYMSW-PDRGVPSSPD---HMLAMVEEARRLQGSGPEplCVHCSAG 232
Cdd:cd14637  81 ------ADEDIVTRLFRVQnitrLQEGHLMVRHFQFLRWsAYRDTPDSKKaflHLLASVEKWQRESGEGRT--VVHCLNG 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 18375655 233 CGRTGVLCTVDYVRQLLLTQMIppdFSLFDVVLKMRKQRPAAVQTEEQYRFLY 285
Cdd:cd14637 153 GGRSGTYCASAMILEMIRCHNI---VDVFYAVKTLRNYKPNMVETLEQYRFCY 202
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 86-285 3.84e-21

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: 91.28  E-value: 3.84e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  86 YINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMacreIENGRKRCER---YWAQEQEPLQTGLFCITLI 162
Cdd:cd17670   1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVM----LPDNQGLAEDefvYWPSREESMNCEAFTVTLI 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 163 ---------KEKWLNEDIMLRTLKVTFQKESRsvyQLQYMSWPDRGVPSSPDHMLAMV--EEARRLQGsgpePLCVHCSA 231
Cdd:cd17670  77 skdrlclsnEEQIIIHDFILEATQDDYVLEVR---HFQCPKWPNPDAPISSTFELINVikEEALTRDG----PTIVHDEF 149

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 18375655 232 GCGRTGVLCTVDYVRQLLLTQMIppdFSLFDVVLKMRKQRPAAVQTEEQYRFLY 285
Cdd:cd17670 150 GAVSAGTLCALTTLSQQLENENA---VDVYQVAKMINLMRPGVFTDIEQYQFLY 200
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 86-285 3.01e-20

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: 88.59  E-value: 3.01e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  86 YINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMaCREIENGrKRCERYWAQ----EQEPLQTGLFCITl 161
Cdd:cd14635   1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVM-LNDVDPA-QLCPQYWPEngvhRHGPIQVEFVSAD- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 162 ikekwLNEDIMLRTLKVTF----QKESRSVYQLQYMSWP-DRGVPSSPDHMLAMVEEARRLQ---GSGPEPLCVHCSAGC 233
Cdd:cd14635  78 -----LEEDIISRIFRIYNaarpQDGYRMVQQFQFLGWPmYRDTPVSKRSFLKLIRQVDKWQeeyNGGEGRTVVHCLNGG 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 18375655 234 GRTGVLCTVDYVRQLLLTQMippDFSLFDVVLKMRKQRPAAVQTEEQYRFLY 285
Cdd:cd14635 153 GRSGTFCAISIVCEMLRHQR---AVDVFHAVKTLRNNKPNMVDLLDQYKFCY 201
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 86-288 3.01e-19

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


Pssm-ID: 350507 [Multi-domain]  Cd Length: 204  Bit Score: 85.82  E-value: 3.01e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  86 YINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMacreIENGRKRCER---YWAQEQEPLQTGLFCITLI 162
Cdd:cd17669   1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVM----LPDGQNMAEDefvYWPNKDEPINCETFKVTLI 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 163 ---------KEKWLNEDIMLRTLKVTFQKESRsvyQLQYMSWPDRGVPSSPDHMLAMV--EEARRLQGsgpePLCVHCSA 231
Cdd:cd17669  77 aeehkclsnEEKLIIQDFILEATQDDYVLEVR---HFQCPKWPNPDSPISKTFELISIikEEAANRDG----PMIVHDEH 149

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 18375655 232 GCGRTGVLCTVDYVRQLLLTQmipPDFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTV 288
Cdd:cd17669 150 GGVTAGTFCALTTLMHQLEKE---NSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 86-285 1.88e-16

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


Pssm-ID: 350398 [Multi-domain]  Cd Length: 200  Bit Score: 77.75  E-value: 1.88e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  86 YINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACREIENGrkRCERYWAQEQEPLQTGLFCITLIKEK 165
Cdd:cd14550   1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTKEKPLECETFKVTLSGED 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 166 W--LNEDIMLRT----LKVT---FQKESRsvyQLQYMSWPDrgvPSSPDH-MLAMVEEARRLQGSGPEPLCVHCSAGCGR 235
Cdd:cd14550  79 HscLSNEIRLIVrdfiLESTqddYVLEVR---QFQCPSWPN---PCSPIHtVFELINTVQEWAQQRDGPIVVHDRYGGVQ 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 18375655 236 TGVLCTVdyvrQLLLTQMIppDFSLFDV--VLKMRKQ-RPAAVQTEEQYRFLY 285
Cdd:cd14550 153 AATFCAL----TTLHQQLE--HESSVDVyqVAKLYHLmRPGVFTSKEDYQFLY 199
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 205-286 1.19e-15

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: 1.19e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 205 DHMLAMVEEARRLQGSGPEPLCVHCSAGCGRTGVLCTVDYVRQLlltqmippDFSLFDVVLKMRKQRPA-AVQTEEQYRF 283
Cdd:cd14494  39 LAMVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLG--------GMSAEEAVRIVRLIRPGgIPQTIEQLDF 110


                ...
gi 18375655 284 LYH 286
Cdd:cd14494 111 LIK 113
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 179-284 2.50e-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: 2.50e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 179 TFQKESRSVYQLqymSWPDRGVPSsPDHMLAMVE-EARRLQGSGPepLCVHCSAGCGRTGVL--CTvdyvrqLLLTQMIP 255
Cdd:cd14506  71 AFMRAGIYFYNF---GWKDYGVPS-LTTILDIVKvMAFALQEGGK--VAVHCHAGLGRTGVLiaCY------LVYALRMS 138

                        90       100
                ....*....|....*....|....*....
gi 18375655 256 PDfslfDVVLKMRKQRPAAVQTEEQYRFL 284
Cdd:cd14506 139 AD----QAIRLVRSKRPNSIQTRGQVLCV 163
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
195-286 4.03e-09

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 54.98  E-value: 4.03e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 195 WPDRGVPSsPDHMLAMVEEARRLQGSGpEPLCVHCSAGCGRTGvlcTVdyVRQLLLTQMIPPDfslfDVVLKMRKQRPAA 274
Cdd:COG2453  55 IPDFGAPD-DEQLQEAVDFIDEALREG-KKVLVHCRGGIGRTG---TV--AAAYLVLLGLSAE----EALARVRAARPGA 123

                        90
                ....*....|..
gi 18375655 275 VQTEEQYRFLYH 286
Cdd:COG2453 124 VETPAQRAFLER 135
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 51-289 4.49e-09

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 57.67  E-value: 4.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655   51 GSRPENVRKNRYKD-VLPYDQTRVILSLLQEEGHSDYINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILM 129
Cdd:PHA02740  42 ANKACAQAENKAKDeNLALHITRLLHRRIKLFNDEKVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVL 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  130 ACREIEngrKRC-ERYWAQEQEPLQT-GLFCITLIkEKWLNEDIMLRTLKVTFQK-ESRSVYQLQYMSWPDRGVPSSPDH 206
Cdd:PHA02740 122 ISRHAD---KKCfNQFWSLKEGCVITsDKFQIETL-EIIIKPHFNLTLLSLTDKFgQAQKISHFQYTAWPADGFSHDPDA 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655  207 ML-------AMVEEARRLQGSGP-EPLCVHCSAGCGRTGVLCTVDY-VRQLLLTQMIppdfSLFDVVLKMRKQRPAAVQT 277
Cdd:PHA02740 198 FIdffcnidDLCADLEKHKADGKiAPIIIDCIDGISSSAVFCVFDIcATEFDKTGML----SIANALKKVRQKKYGCMNC 273

                        250
                 ....*....|..
gi 18375655  278 EEQYRFLYHTVA 289
Cdd:PHA02740 274 LDDYVFCYHLIA 285
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 185-285 4.64e-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: 4.64e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 185 RSVYQLQYMSW-----PDRGVPSSPDHMLAMVEEARRLQGSGpEPLCVHCSAGCGRTGVLCTvdyvRQLLLTQM-IPPDf 258
Cdd:cd14505  65 LEQYQQAGITWhhlpiPDGGVPSDIAQWQELLEELLSALENG-KKVLIHCKGGLGRTGLIAA----CLLLELGDtLDPE- 138

                        90       100
                ....*....|....*....|....*..
gi 18375655 259 slfDVVLKMRKQRPAAVQTEEQYRFLY 285
Cdd:cd14505 139 ---QAIAAVRALRPGAIQTPKQENFLH 162
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 196-284 5.00e-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: 5.00e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 196 PDRGVPSSP--DHMLAMVEEARrlqgSGPEPLCVHCSAGCGRTGVL--CtvdYvrqLLLTQMIPPDfslfDVVLKMRKQR 271
Cdd:cd14504  58 EDYTPPTLEqiDEFLDIVEEAN----AKNEAVLVHCLAGKGRTGTMlaC---Y---LVKTGKISAV----DAINEIRRIR 123

                        90
                ....*....|...
gi 18375655 272 PAAVQTEEQYRFL 284
Cdd:cd14504 124 PGSIETSEQEKFV 136
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 195-284 2.17e-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: 2.17e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18375655 195 WPDRGVPSSPD-HMLA-MVEEAR-------RLQGSGP-----EPLCV-HCSAGCGRTGVL-CTvdyvrqlllTQMIPPD- 257
Cdd:cd14559 126 WPDHTAISSEGlKELAdLVNKSAeekrnfyKSKGSSAindknKLLPViHCRAGVGRTGQLaAA---------MELNKSPn 196

                        90       100
                ....*....|....*....|....*....
gi 18375655 258 -FSLFDVVLKMRKQRPA-AVQTEEQYRFL 284
Cdd:cd14559 197 nLSVEDIVSDMRTSRNGkMVQKDEQLDTL 225
 
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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