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Conserved domains on  [gi|17508629|ref|NP_491316|]
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Inactive protein-tyrosine phosphatase egg-5 [Caenorhabditis elegans]

Protein Classification

protein tyrosine phosphatase family protein( domain architecture ID 12193126)

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

CATH:  3.90.190.10
EC:  3.1.3.-
Gene Ontology:  GO:0004721|GO:0006470
PubMed:  27514797|17057753

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
407-660 1.51e-71

Protein tyrosine phosphatase, catalytic domain;


:

Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 234.09  E-value: 1.51e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629    407 GMERRFEILENSVNH-IPFTHSASDNNQEKCRNPRVHCRDSTRIALQFPRGQyLGDFIHANRISGKPLFNEFIMTQAPMK 485
Cdd:smart00194   1 GLEEEFEKLDRLKPDdESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGE-GSDYINASYIDGPNGPKAYIATQGPLP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629    486 NTVDDFWRMVWQEEVPYIVMLTSRKE--PERCEYYWPKSPSDPAVTvpGGLRIENFGVYQAPDplFRVTHLRLIGPDR-E 562
Cdd:smart00194  80 STVEDFWRMVWEQKVTVIVMLTELVEkgREKCAQYWPDEEGEPLTY--GDITVTLKSVEKVDD--YTIRTLEVTNTGCsE 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629    563 ERHVEHWQ----GDVNNSSNMYSPLNILRLLRNASK----PVVIHDHLGVSRAACLVAAEIAICSLLRGPTykYPVQRAV 634
Cdd:smart00194 156 TRTVTHYHytnwPDHGVPESPESILDLIRAVRKSQStstgPIVVHCSAGVGRTGTFIAIDILLQQLEAGKE--VDIFEIV 233

                          250       260
                   ....*....|....*....|....*.
gi 17508629    635 QFLRQRRPFSIETPMQYIFVHRLVAF 660
Cdd:smart00194 234 KELRSQRPGMVQTEEQYIFLYRAILE 259
 
Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
407-660 1.51e-71

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 234.09  E-value: 1.51e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629    407 GMERRFEILENSVNH-IPFTHSASDNNQEKCRNPRVHCRDSTRIALQFPRGQyLGDFIHANRISGKPLFNEFIMTQAPMK 485
Cdd:smart00194   1 GLEEEFEKLDRLKPDdESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGE-GSDYINASYIDGPNGPKAYIATQGPLP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629    486 NTVDDFWRMVWQEEVPYIVMLTSRKE--PERCEYYWPKSPSDPAVTvpGGLRIENFGVYQAPDplFRVTHLRLIGPDR-E 562
Cdd:smart00194  80 STVEDFWRMVWEQKVTVIVMLTELVEkgREKCAQYWPDEEGEPLTY--GDITVTLKSVEKVDD--YTIRTLEVTNTGCsE 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629    563 ERHVEHWQ----GDVNNSSNMYSPLNILRLLRNASK----PVVIHDHLGVSRAACLVAAEIAICSLLRGPTykYPVQRAV 634
Cdd:smart00194 156 TRTVTHYHytnwPDHGVPESPESILDLIRAVRKSQStstgPIVVHCSAGVGRTGTFIAIDILLQQLEAGKE--VDIFEIV 233

                          250       260
                   ....*....|....*....|....*.
gi 17508629    635 QFLRQRRPFSIETPMQYIFVHRLVAF 660
Cdd:smart00194 234 KELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
432-659 1.09e-64

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 214.80  E-value: 1.09e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629   432 NQEKCRNPRVHCRDSTRIALQFPRGQylGDFIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKE 511
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGDPGP--SDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629   512 --PERCEYYWPKSPSDPavTVPGGLRIENFG-VYQAPDPLFRVTHLRLIGPDrEERHVEHWQ------GDVNNSSNmySP 582
Cdd:pfam00102  79 kgREKCAQYWPEEEGES--LEYGDFTVTLKKeKEDEKDYTVRTLEVSNGGSE-ETRTVKHFHytgwpdHGVPESPN--SL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629   583 LNILRLLRNAS-----KPVVIHDHLGVSRAACLVAAEIAICSLLRGPTYKypVQRAVQFLRQRRPFSIETPMQYIFVHRL 657
Cdd:pfam00102 154 LDLLRKVRKSSldgrsGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVD--IFQIVKELRSQRPGMVQTLEQYIFLYDA 231


                  ..
gi 17508629   658 VA 659
Cdd:pfam00102 232 IL 233
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 462-656 1.66e-50

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: 175.17  E-value: 1.66e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 462 FIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKEPER--CEYYWPKSPSDPAVTvpGGLRIENF 539
Cdd:cd00047   1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGRekCERYWPEEGGKPLEY--GDITVTLV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 540 GVYQAPDplFRVTHLRLIGPD-REERHVEHWQ-------GDVNNSSNMYSPLNILR-LLRNASKPVVIHDHLGVSRAACL 610
Cdd:cd00047  79 SEEELSD--YTIRTLELSPKGcSESREVTHLHytgwpdhGVPSSPEDLLALVRRVRkEARKPNGPIVVHCSAGVGRTGTF 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 17508629 611 VAAEIAICSLLRGPtyKYPVQRAVQFLRQRRPFSIETPMQYIFVHR 656
Cdd:cd00047 157 IAIDILLERLEAEG--EVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 432-655 3.24e-25

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 107.01  E-value: 3.24e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629  432 NQEKCRNPRVHCRDSTRIALQfPRGQYLGDFIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKE 511
Cdd:PHA02747  51 NQPKNRYWDIPCWDHNRVILD-SGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPTKG 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629  512 ---PERCEYYWpkSPSDPAVTVPGGLRIENFGVYQAPD---PLFRVTHLRLigpdREERHVEHWQ----GDVNNSSNM-- 579
Cdd:PHA02747 130 tngEEKCYQYW--CLNEDGNIDMEDFRIETLKTSVRAKyilTLIEITDKIL----KDSRKISHFQcsewFEDETPSDHpd 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629  580 -YSPLNILRLLRNAS-----------KPVVIHDHLGVSRAACLVAAEIAICSLLRGPTYKYPvqRAVQFLRQRRPFSIET 647
Cdd:PHA02747 204 fIKFIKIIDINRKKSgklfnpkdallCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLA--KTAEKIREQRHAGIMN 281


                 ....*...
gi 17508629  648 PMQYIFVH 655
Cdd:PHA02747 282 FDDYLFIQ 289
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
409-661 1.17e-11

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 66.27  E-value: 1.17e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 409 ERRFEIL--ENSVNHIPFTHSASDNNQEKCRNPRVHCRDSTRIAlqfPRGQYLgdfiHANRISGKPLfNEFIMTQAPMKN 486
Cdd:COG5599  17 NSRLSTLtnELAPSHNDPQYLQNINGSPLNRFRDIQPYKETALR---ANLGYL----NANYIQVIGN-HRYIATQYPLEE 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 487 TVDDFWRMVWQEEVPYIVMLTSRKE----PERCEYYWPKSPSDPAVTVpgglRIENFGVYQ-APDPLFRVTHLRLIGPDR 561
Cdd:COG5599  89 QLEDFFQMLFDNNTPVLVVLASDDEiskpKVKMPVYFRQDGEYGKYEV----SSELTESIQlRDGIEARTYVLTIKGTGQ 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 562 EER-----HVEHWQGDVNNSSNMYSPLN--ILRLLRNASK---PVVIHDHLGVSRAACLVAAEIAICSLLRGPTYKYPVQ 631
Cdd:COG5599 165 KKIeipvlHVKNWPDHGAISAEALKNLAdlIDKKEKIKDPdklLPVVHCRAGVGRTGTLIACLALSKSINALVQITLSVE 244

                       250       260       270
                ....*....|....*....|....*....|.
gi 17508629 632 RAVQFLR-QRRPFSIETPMQYIFvhrLVAFF 661
Cdd:COG5599 245 EIVIDMRtSRNGGMVQTSEQLDV---LVKLA 272
 
Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
407-660 1.51e-71

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 234.09  E-value: 1.51e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629    407 GMERRFEILENSVNH-IPFTHSASDNNQEKCRNPRVHCRDSTRIALQFPRGQyLGDFIHANRISGKPLFNEFIMTQAPMK 485
Cdd:smart00194   1 GLEEEFEKLDRLKPDdESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGE-GSDYINASYIDGPNGPKAYIATQGPLP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629    486 NTVDDFWRMVWQEEVPYIVMLTSRKE--PERCEYYWPKSPSDPAVTvpGGLRIENFGVYQAPDplFRVTHLRLIGPDR-E 562
Cdd:smart00194  80 STVEDFWRMVWEQKVTVIVMLTELVEkgREKCAQYWPDEEGEPLTY--GDITVTLKSVEKVDD--YTIRTLEVTNTGCsE 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629    563 ERHVEHWQ----GDVNNSSNMYSPLNILRLLRNASK----PVVIHDHLGVSRAACLVAAEIAICSLLRGPTykYPVQRAV 634
Cdd:smart00194 156 TRTVTHYHytnwPDHGVPESPESILDLIRAVRKSQStstgPIVVHCSAGVGRTGTFIAIDILLQQLEAGKE--VDIFEIV 233

                          250       260
                   ....*....|....*....|....*.
gi 17508629    635 QFLRQRRPFSIETPMQYIFVHRLVAF 660
Cdd:smart00194 234 KELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
432-659 1.09e-64

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 214.80  E-value: 1.09e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629   432 NQEKCRNPRVHCRDSTRIALQFPRGQylGDFIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKE 511
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGDPGP--SDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629   512 --PERCEYYWPKSPSDPavTVPGGLRIENFG-VYQAPDPLFRVTHLRLIGPDrEERHVEHWQ------GDVNNSSNmySP 582
Cdd:pfam00102  79 kgREKCAQYWPEEEGES--LEYGDFTVTLKKeKEDEKDYTVRTLEVSNGGSE-ETRTVKHFHytgwpdHGVPESPN--SL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629   583 LNILRLLRNAS-----KPVVIHDHLGVSRAACLVAAEIAICSLLRGPTYKypVQRAVQFLRQRRPFSIETPMQYIFVHRL 657
Cdd:pfam00102 154 LDLLRKVRKSSldgrsGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVD--IFQIVKELRSQRPGMVQTLEQYIFLYDA 231


                  ..
gi 17508629   658 VA 659
Cdd:pfam00102 232 IL 233
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 462-656 1.66e-50

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: 175.17  E-value: 1.66e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 462 FIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKEPER--CEYYWPKSPSDPAVTvpGGLRIENF 539
Cdd:cd00047   1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGRekCERYWPEEGGKPLEY--GDITVTLV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 540 GVYQAPDplFRVTHLRLIGPD-REERHVEHWQ-------GDVNNSSNMYSPLNILR-LLRNASKPVVIHDHLGVSRAACL 610
Cdd:cd00047  79 SEEELSD--YTIRTLELSPKGcSESREVTHLHytgwpdhGVPSSPEDLLALVRRVRkEARKPNGPIVVHCSAGVGRTGTF 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 17508629 611 VAAEIAICSLLRGPtyKYPVQRAVQFLRQRRPFSIETPMQYIFVHR 656
Cdd:cd00047 157 IAIDILLERLEAEG--EVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 424-655 4.80e-35

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: 134.41  E-value: 4.80e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 424 FTHSASDNNQEKCRNPRVHCRDSTRIALQFPRGQYLGDFIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYI 503
Cdd:cd14543  21 FLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVI 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 504 VMLTSRKEPER--CEYYWPksPSDPAVTVPGGLRIENFGVYQAPDplFRVTHLRLI-GPDREERHVEHWQ----GDVNNS 576
Cdd:cd14543 101 VMTTRVVERGRvkCGQYWP--LEEGSSLRYGDLTVTNLSVENKEH--YKKTTLEIHnTETDESRQVTHFQftswPDFGVP 176

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 577 SNMYSPLNILRLLRNASK-----------------PVVIHDHLGVSRAACLVAAEIAICSLLRGPTYKypVQRAVQFLRQ 639
Cdd:cd14543 177 SSAAALLDFLGEVRQQQAlavkamgdrwkghppgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLN--VMQTVRRMRT 254

                       250
                ....*....|....*.
gi 17508629 640 RRPFSIETPMQYIFVH 655
Cdd:cd14543 255 QRAFSIQTPDQYYFCY 270
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 447-656 1.87e-29

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: 116.73  E-value: 1.87e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 447 TRIALQFPRGQYLGDFIHANRISGKPLFNE-FIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKE-PERCEYYWPKSPs 524
Cdd:cd14547  12 SRVCLPSVDDDPLSSYINANYIRGYDGEEKaYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEaKEKCAQYWPEEE- 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 525 dpavtvpgGLRIENFGV---YQAPDPLFRVTHLrLIGPDREERHVEH-WQGDVNNSSNMYSPLNILRLLR---------N 591
Cdd:cd14547  91 --------NETYGDFEVtvqSVKETDGYTVRKL-TLKYGGEKRYLKHyWYTSWPDHKTPEAAQPLLSLVQeveearqteP 161

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17508629 592 ASKPVVIHDHLGVSRAACLVAAEIAICSLLrgPTYKYPVQRAVQFLRQRRPFSIETPMQYIFVHR 656
Cdd:cd14547 162 HRGPIVVHCSAGIGRTGCFIATSIGCQQLR--EEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 445-655 4.65e-29

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: 115.53  E-value: 4.65e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 445 DSTRIALQFPRGQYLGDFIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTS--RKEPERCEYYWPKS 522
Cdd:cd14548   9 DHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQcmEKGRVKCDHYWPFD 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 523 pSDPavTVPGGLRIENFGVYQAPDplFRVTHLRLIGPDrEERHVEHWQ----GDVNNSSNMYSPLNILRLLR----NASK 594
Cdd:cd14548  89 -QDP--VYYGDITVTMLSESVLPD--WTIREFKLERGD-EVRSVRQFHftawPDHGVPEAPDSLLRFVRLVRdyikQEKG 162

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17508629 595 PVVIHDHLGVSRAACLvaaeIAICSLLRGPTYKYPVQ--RAVQFLRQRRPFSIETPMQYIFVH 655
Cdd:cd14548 163 PTIVHCSAGVGRTGTF----IALDRLLQQIESEDYVDifGIVYDLRKHRPLMVQTEAQYIFLH 221
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 422-661 5.59e-29

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: 116.09  E-value: 5.59e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 422 IPfTHSASDNNQEKCRNPRvhcrdsTRIALQFPRGQY-LGDFIHANRI---SGKPlfNEFIMTQAPMKNTVDDFWRMVWQ 497
Cdd:cd14612  12 IP-GHASKDRYKTILPNPQ------SRVCLRRAGSQEeEGSYINANYIrgyDGKE--KAYIATQGPMLNTVSDFWEMVWQ 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 498 EEVPYIVMLTSRKE-PERCEYYWPKSPSDPAvtvPGGLRIEnfGVYQAPDPLFRVTHLRLIGpdrEERHVEH-WQGDVNN 575
Cdd:cd14612  83 EECPIIVMITKLKEkKEKCVHYWPEKEGTYG---RFEIRVQ--DMKECDGYTIRDLTIQLEE---ESRSVKHyWFSSWPD 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 576 SSNMYSPLNILRLLRNASK---------PVVIHDHLGVSRAACLVAAEIAiCSLLRGpTYKYPVQRAVQFLRQRRPFSIE 646
Cdd:cd14612 155 HQTPESAGPLLRLVAEVEEsrqtaaspgPIVVHCSAGIGRTGCFIATSIG-CQQLKD-TGKVDILGIVCQLRLDRGGMIQ 232

                       250
                ....*....|....*
gi 17508629 647 TPMQYIFVHRLVAFF 661
Cdd:cd14612 233 TSEQYQFLHHTLALY 247
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 463-655 1.51e-27

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: 110.80  E-value: 1.51e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 463 IHANRISGKPLFNE-FIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKEP--ERCEYYWpksPSDPAVTVPGGLRIENF 539
Cdd:cd18533   2 INASYITLPGTSSKrYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENgrEKCDQYW---PSGEYEGEYGDLTVELV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 540 GVYQAPDPLFRVTHLRLIGPDREERHVEHWQ----GDVNNSSNMYSPLNILRLLR------NASKPVVIHDHLGVSRAAC 609
Cdd:cd18533  79 SEEENDDGGFIVREFELSKEDGKVKKVYHIQykswPDFGVPDSPEDLLTLIKLKRelndsaSLDPPIIVHCSAGVGRTGT 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 17508629 610 LVAAEiAICSLLRGPTYKY--------PVQRAVQFLRQRRPFSIETPMQYIFVH 655
Cdd:cd18533 159 FIALD-SLLDELKRGLSDSqdledsedPVYEIVNQLRKQRMSMVQTLRQYIFLY 211
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 461-654 7.35e-27

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: 108.96  E-value: 7.35e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 461 DFIHAN----RISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKEPER--CEYYWPkspsDPAVTVPGGl 534
Cdd:cd14541   1 DYINANyvnmEIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRvkCHQYWP----DLGETMQFG- 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 535 RIENFGVYQAPDPLFRVTHLRLIGPD-REERHVEHWQ-------GDVNNSSNMYSPLNILRLLR-NASKPVVIHDHLGVS 605
Cdd:cd14541  76 NLQITCVSEEVTPSFAFREFILTNTNtGEERHITQMQylawpdhGVPDDSSDFLDFVKRVRQNRvGMVEPTVVHCSAGIG 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 17508629 606 RAACLVAAEIAICsLLRGPTYKYPVQrAVQFLRQRRPFSIETPMQYIFV 654
Cdd:cd14541 156 RTGVLITMETAMC-LIEANEPVYPLD-IVRTMRDQRAMLIQTPSQYRFV 202
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 462-657 3.66e-26

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


Pssm-ID: 350388 [Multi-domain]  Cd Length: 219  Bit Score: 107.16  E-value: 3.66e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 462 FIHANRIS----GKPLFneFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKE--PERCEYYWPKSPSDPAVTVPGGLR 535
Cdd:cd14540   1 YINASHITatvgGKQRF--YIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEggREKCFRYWPTLGGEHDALTFGEYK 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 536 I-----ENFGVYQAPDplFRVTHLrligPDREERHVEHWQ----------GDVNNSSNMYSPLNILRL-------LRNAS 593
Cdd:cd14540  79 VstkfsVSSGCYTTTG--LRVKHT----LSGQSRTVWHLQytdwpdhgcpEDVSGFLDFLEEINSVRRhtnqdvaGHNRN 152

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17508629 594 KPVVIHDHLGVSRAACLVAAEIAICSLLRGPTYKYPvqRAVQFLRQRRPFSIETPMQYIFVHRL 657
Cdd:cd14540 153 PPTLVHCSAGVGRTGVVILADLMLYCLDHNEELDIP--RVLALLRHQRMLLVQTLAQYKFVYNV 214
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 437-655 3.02e-25

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: 104.64  E-value: 3.02e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 437 RNPRVHCRDSTRIALQFPRGQYLGDFIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKEPER-- 514
Cdd:cd14618   2 RYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRvl 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 515 CEYYWPkSPSDPAVTvpGGLRIENFGvyQAPDPLFRVTHLRLI-GPDREERHVEHWQ-------GDVNNSSNMYSPLNIL 586
Cdd:cd14618  82 CDHYWP-SESTPVSY--GHITVHLLA--QSSEDEWTRREFKLWhEDLRKERRVKHLHytawpdhGIPESTSSLMAFRELV 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17508629 587 RLLRNASK---PVVIHDHLGVSRAACLVAAEIAICSLLRGPTYKypVQRAVQFLRQRRPFSIETPMQYIFVH 655
Cdd:cd14618 157 REHVQATKgkgPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVD--VFNTVYILRMHRYLMIQTLSQYIFLH 226
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 432-654 3.13e-25

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


Pssm-ID: 350448 [Multi-domain]  Cd Length: 274  Bit Score: 106.09  E-value: 3.13e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 432 NQEKCRNPRVHCRDSTRIALQFPRgqylgDFIHAN----RISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLT 507
Cdd:cd14600  40 NMDKNRYKDVLPYDATRVVLQGNE-----DYINASyvnmEIPSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLIVMLT 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 508 SRKEPER--CEYYWPKSPSdpaVTVPGGLRI----ENFGVYQapdpLFR---VTHLRligpDREERHVEHWQ-------G 571
Cdd:cd14600 115 TLTERGRtkCHQYWPDPPD---VMEYGGFRVqchsEDCTIAY----VFRemlLTNTQ----TGEERTVTHLQyvawpdhG 183

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 572 DVNNSSNMYSPLNILRLLRNASKPVVIHDHLGVSRAACLVAAEIAICSLLRG-PTYKYPVqraVQFLRQRRPFSIETPMQ 650
Cdd:cd14600 184 VPDDSSDFLEFVNYVRSKRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNqPVYPLDI---VRKMRDQRAMMVQTSSQ 260


                ....
gi 17508629 651 YIFV 654
Cdd:cd14600 261 YKFV 264
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 432-655 3.24e-25

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 107.01  E-value: 3.24e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629  432 NQEKCRNPRVHCRDSTRIALQfPRGQYLGDFIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKE 511
Cdd:PHA02747  51 NQPKNRYWDIPCWDHNRVILD-SGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPTKG 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629  512 ---PERCEYYWpkSPSDPAVTVPGGLRIENFGVYQAPD---PLFRVTHLRLigpdREERHVEHWQ----GDVNNSSNM-- 579
Cdd:PHA02747 130 tngEEKCYQYW--CLNEDGNIDMEDFRIETLKTSVRAKyilTLIEITDKIL----KDSRKISHFQcsewFEDETPSDHpd 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629  580 -YSPLNILRLLRNAS-----------KPVVIHDHLGVSRAACLVAAEIAICSLLRGPTYKYPvqRAVQFLRQRRPFSIET 647
Cdd:PHA02747 204 fIKFIKIIDINRKKSgklfnpkdallCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLA--KTAEKIREQRHAGIMN 281


                 ....*...
gi 17508629  648 PMQYIFVH 655
Cdd:PHA02747 282 FDDYLFIQ 289
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 445-656 8.50e-25

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: 103.43  E-value: 8.50e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 445 DSTRIALQFPRGQYLGDFIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKEPER--CEYYWP-- 520
Cdd:cd14619  10 DWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRvkCEHYWPld 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 521 KSP---SDPAVTVPGGLRIENFGVYQapdplFRVTHLRligpDREERHVEHWQ----GDVNNSSNMYSPLNILRLLRN-- 591
Cdd:cd14619  90 YTPctyGHLRVTVVSEEVMENWTVRE-----FLLKQVE----EQKTLSVRHFHftawPDHGVPSSTDTLLAFRRLLRQwl 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17508629 592 ----ASKPVVIHDHLGVSRAACLVAAEIAICSLLR----GPtYKYpvqraVQFLRQRRPFSIETPMQYIFVHR 656
Cdd:cd14619 161 dqtmSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSegllGP-FSF-----VQKMRENRPLMVQTESQYVFLHQ 227
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 462-653 1.30e-24

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: 102.07  E-value: 1.30e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 462 FIHANRIS----GKPLFneFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKEPER--CEYYWPKSPSDPAVtVPGGLR 535
Cdd:cd14538   1 YINASHIRipvgGDTYH--YIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKvkCHRYWPDSLNKPLI-CGGRLE 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 536 I--------ENFGVYqapdpLFRVTHLrligPDREERHVEH-----WQgdvnNSSNMYSPLNILRLLRNA-----SKPVV 597
Cdd:cd14538  78 VslekyqslQDFVIR-----RISLRDK----ETGEVHHITHlnfttWP----DHGTPQSADPLLRFIRYMrrihnSGPIV 144

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17508629 598 IHDHLGVSRAACLVAAEIAICSLLRGPTYKypVQRAVQFLRQRRPFSIETPMQYIF 653
Cdd:cd14538 145 VHCSAGIGRTGVLITIDVALGLIERDLPFD--IQDIVKDLREQRQGMIQTKDQYIF 198
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 462-656 2.64e-24

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: 101.14  E-value: 2.64e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 462 FIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKE--PERCEYYWPKSPSDPAvtvpGGLRIENF 539
Cdd:cd14551   1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKErkEKKCSQYWPDQGCWTY----GNLRVRVE 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 540 GVYQAPDPLFRVTHLRLIGPDREER--------HVEHWQgdvnNSSNMYSPLNILRLLRNA-------SKPVVIHDHLGV 604
Cdd:cd14551  77 DTVVLVDYTTRKFCIQKVNRGIGEKrvrlvtqfHFTSWP----DFGVPFTPIGMLKFLKKVksanpprAGPIVVHCSAGV 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 17508629 605 SRAACLVAAEiAICSLLRGPTyKYPVQRAVQFLRQRRPFSIETPMQYIFVHR 656
Cdd:cd14551 153 GRTGTFIVID-AMLDMMHAEG-KVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 461-654 8.29e-24

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: 100.02  E-value: 8.29e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 461 DFIHANRIS----GKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKEPER--CEYYWPKsPSDPAVTvpGGL 534
Cdd:cd14601   1 DYINANYINmeipSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRvkCHQYWPE-PSGSSSY--GGF 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 535 RIENFGVYQAPDPLFR---VTHLRligpDREERHVEHWQ-------GDVNNSSNMyspLNILRLLRN----ASKPVVIHD 600
Cdd:cd14601  78 QVTCHSEEGNPAYVFRemtLTNLE----KNESRPLTQIQyiawpdhGVPDDSSDF---LDFVCLVRNkragKDEPVVVHC 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 17508629 601 HLGVSRAACLVAAEIAICsLLRGPTYKYPVQrAVQFLRQRRPFSIETPMQYIFV 654
Cdd:cd14601 151 SAGIGRTGVLITMETAMC-LIECNQPVYPLD-IVRTMRDQRAMMIQTPSQYRFV 202
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 447-661 1.35e-23

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: 100.71  E-value: 1.35e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 447 TRIALQFP-RGQYLGDFIHANRISGkplFNE----FIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKEP-ERCEYYWP 520
Cdd:cd14613  40 SRVCLTSPdQDDPLSSYINANYIRG---YGGeekvYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEMnEKCTEYWP 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 521 KSPsdpavTVPGGLRIENFGVYQAPDPLFRVTHLRligPDREERHVEH-----WQgDVNNSSNMYSPLNILRLLRNASK- 594
Cdd:cd14613 117 EEQ-----VTYEGIEITVKQVIHADDYRLRLITLK---SGGEERGLKHywytsWP-DQKTPDNAPPLLQLVQEVEEARQq 187

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17508629 595 ------PVVIHDHLGVSRAACLVAAEIaICSLLRGPTYKYPVQRAVQfLRQRRPFSIETPMQYIFVHRLVAFF 661
Cdd:cd14613 188 aepncgPVIVHCSAGIGRTGCFIATSI-CCKQLRNEGVVDILRTTCQ-LRLDRGGMIQTCEQYQFVHHVLSLY 258
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 432-655 1.58e-23

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: 100.16  E-value: 1.58e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 432 NQEKCRNPRVHCRDSTRIALQFPRGQYLGDFIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKE 511
Cdd:cd14553   3 NKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 512 PER--CEYYWPKSPSDpavtVPGGLRIENFGVYQAPDPLFRVTHLRLIGpDREERHVEHWQ-------GDVNNSSNMysp 582
Cdd:cd14553  83 RSRvkCDQYWPTRGTE----TYGLIQVTLLDTVELATYTVRTFALHKNG-SSEKREVRQFQftawpdhGVPEHPTPF--- 154

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17508629 583 LNILRLLR----NASKPVVIHDHLGVSRAACLVAAEIAICSLLRGPTYKypVQRAVQFLRQRRPFSIETPMQYIFVH 655
Cdd:cd14553 155 LAFLRRVKacnpPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVD--IYGHVTCLRAQRNYMVQTEDQYIFIH 229
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 432-661 1.39e-22

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: 97.53  E-value: 1.39e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 432 NQEKCRNPRVHCRDSTRIALQ-FPRGQYLGDFIHANRI----SGKPLFNE---FIMTQAPMKNTVDDFWRMVWQEEVPYI 503
Cdd:cd14544   1 NKGKNRYKNILPFDHTRVILKdRDPNVPGSDYINANYIrnenEGPTTDENaktYIATQGCLENTVSDFWSMVWQENSRVI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 504 VMLTsrKEPER----CEYYWPKSPSDPAVtvpGGLRIENFGVYQAPDPLFRVTHLRLIGPDREERHVEHWQ----GDVNN 575
Cdd:cd14544  81 VMTT--KEVERgknkCVRYWPDEGMQKQY---GPYRVQNVSEHDTTDYTLRELQVSKLDQGDPIREIWHYQylswPDHGV 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 576 SSNMYSPLNILRLL------RNASKPVVIHDHLGVSRAACLVAAEIAICSLLR-GPTYKYPVQRAVQFLRQRRPFSIETP 648
Cdd:cd14544 156 PSDPGGVLNFLEDVnqrqesLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRkGLDCDIDIQKTIQMVRSQRSGMVQTE 235

                       250
                ....*....|...
gi 17508629 649 MQYIFVHRLVAFF 661
Cdd:cd14544 236 AQYKFIYVAVAQY 248
PHA02738 PHA02738
hypothetical protein; Provisional
 425-661 1.50e-22

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 99.23  E-value: 1.50e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629  425 THSASDNNQEKCRNPRVHCRDSTRIALqfPRGQYLGDFIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIV 504
Cdd:PHA02738  42 TFNAEKKNRKLNRYLDAVCFDHSRVIL--PAERNRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIV 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629  505 MLTSRKE--PERCEYYWpkSPSDPAVTVPGGLRIENFGVYQAPDplFRVTHLRLIGPDREERHVEHW-------QGDVNN 575
Cdd:PHA02738 120 MLCKKKEngREKCFPYW--SDVEQGSIRFGKFKITTTQVETHPH--YVKSTLLLTDGTSATQTVTHFnftawpdHDVPKN 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629  576 SSNMyspLNILRLLRNASK-----------------PVVIHDHLGVSRAACLVAAEIAICSLLRGPTYKYPvqRAVQFLR 638
Cdd:PHA02738 196 TSEF---LNFVLEVRQCQKelaqeslqighnrlqppPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIP--SIVSSIR 270

                        250       260
                 ....*....|....*....|...
gi 17508629  639 QRRPFSIETPMQYIFVHRLVAFF 661
Cdd:PHA02738 271 NQRYYSLFIPFQYFFCYRAVKRY 293
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 459-655 2.18e-22

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: 96.53  E-value: 2.18e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 459 LGDFIHANRISGKPLFNE-FIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKEP-ERCEYYWPKSPSdpavtVPGGLRI 536
Cdd:cd14611  27 LSTYINANYIRGYGGKEKaFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEKnEKCVLYWPEKRG-----IYGKVEV 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 537 ENFGVYQAPDPLFRVTHLRLIGPDREERHVEHWQGDVNNSSNMYSPLNIL-------RLLRNASKPVVIHDHLGVSRAAC 609
Cdd:cd14611 102 LVNSVKECDNYTIRNLTLKQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLmldveedRLASPGRGPVVVHCSAGIGRTGC 181

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 17508629 610 LVAAEIAICSLlrGPTYKYPVQRAVQFLRQRRPFSIETPMQYIFVH 655
Cdd:cd14611 182 FIATTIGCQQL--KEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 445-658 3.37e-22

catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type tyrosine-protein phosphatase J (PTPRJ or R-PTP-J), also known as receptor-type tyrosine-protein phosphatase eta (R-PTP-eta) or density-enhanced phosphatase 1 (DEP-1) OR CD148, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRJ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (eight in PTPRJ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed in various cell types including epithelial, hematopoietic, and endothelial cells. It plays a role in cell adhesion, migration, proliferation and differentiation. It dephosphorylates or contributes to the dephosphorylation of various substrates including protein kinases such as FLT3, PDGFRB, MET, RET (variant MEN2A), VEGFR-2, LYN, SRC, MAPK1, MAPK3, and EGFR, as well as PIK3R1 and PIK3R2.


Pssm-ID: 350463 [Multi-domain]  Cd Length: 229  Bit Score: 96.04  E-value: 3.37e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 445 DSTRIALQFPRGQYlGDFIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKEPER--CEYYWP-- 520
Cdd:cd14615  10 DISRVKLSVQSHST-DDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRtkCEEYWPsk 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 521 --KSPSDPAVTVPGGLRIENFGVYQapdplFRVTHLRligpDREERHVEHWQ----GDVNNSSNMYSPLNILRLLRNASK 594
Cdd:cd14615  89 qkKDYGDITVTMTSEIVLPEWTIRD-----FTVKNAQ----TNESRTVRHFHftswPDHGVPETTDLLINFRHLVREYMK 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 595 ------PVVIHDHLGVSRAACLVAAEIAICSLLRGPTYKypVQRAVQFLRQRRPFSIETPMQYIFVHRLV 658
Cdd:cd14615 160 qnppnsPILVHCSAGVGRTGTFIAIDRLIYQIENENVVD--VYGIVYDLRMHRPLMVQTEDQYVFLNQCA 227
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 428-662 3.13e-21

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: 94.12  E-value: 3.13e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 428 ASDNNQEKCRNPRVHCRDSTRIALQFPRGQYLGDFIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLT 507
Cdd:cd14603  26 GRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMAC 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 508 SRKE--PERCEYYWPkSPSDPAVTVPgglrienFGVYQA------PDPLFRVthLRLIGPDrEERHVEHWQ-------GD 572
Cdd:cd14603 106 REIEmgKKKCERYWA-QEQEPLQTGP-------FTITLVkekrlnEEVILRT--LKVTFQK-ESRSVSHFQymawpdhGI 174

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 573 VNNSSNMYSPLNILRLLRNASK-PVVIHDHLGVSRAACLVAAEIaICSLL---RGPTyKYPVQRAVQFLRQRRPFSIETP 648
Cdd:cd14603 175 PDSPDCMLAMIELARRLQGSGPePLCVHCSAGCGRTGVICTVDY-VRQLLltqRIPP-DFSIFDVVLEMRKQRPAAVQTE 252

                       250
                ....*....|....
gi 17508629 649 MQYIFVHRLVAFFF 662
Cdd:cd14603 253 EQYEFLYHTVAQMF 266
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 432-656 3.35e-21

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: 93.36  E-value: 3.35e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 432 NQEKCRNPRVHCRDSTRIALQFPRGQYLGDFIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKE 511
Cdd:cd14554   6 NKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLRE 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 512 --PERCEYYWpksPSDPAVTVpGGLRIENFGVYQAPDPL---FRVTHLRligpDREERHVEHWQ-GDVNNSSNMYSPLNI 585
Cdd:cd14554  86 mgREKCHQYW---PAERSARY-QYFVVDPMAEYNMPQYIlreFKVTDAR----DGQSRTVRQFQfTDWPEQGVPKSGEGF 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 586 LRLLRNASK---------PVVIHDHLGVSRAACLVAAEIAicslLRGPTYKYPVQ--RAVQFLRQRRPFSIETPMQYIFV 654
Cdd:cd14554 158 IDFIGQVHKtkeqfgqegPITVHCSAGVGRTGVFITLSIV----LERMRYEGVVDvfQTVKLLRTQRPAMVQTEDQYQFC 233


                ..
gi 17508629 655 HR 656
Cdd:cd14554 234 YR 235
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 413-661 4.90e-21

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 94.30  E-value: 4.90e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629  413 EILENSVNHI-----PFT--HSASDNNQEKCRNPRVHCRDSTRIALQFPRGqyLGDFIHANRISGKPLFNEFIMTQAPMK 485
Cdd:PHA02742  26 EILKEEHEHImqeivAFScnESLELKNMKKCRYPDAPCFDRNRVILKIEDG--GDDFINASYVDGHNAKGRFICTQAPLE 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629  486 NTVDDFWRMVWQEEVPYIVMLTS--RKEPERCEYYWpkSPSDPAVTVPGGLRIENFGVYQAPDplFRVTHLRL----IGP 559
Cdd:PHA02742 104 ETALDFWQAIFQDQVRVIVMITKimEDGKEACYPYW--MPHERGKATHGEFKIKTKKIKSFRN--YAVTNLCLtdtnTGA 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629  560 DREERHV--EHW-QGDVNNSSNMYspLNILRLLRNA---------------SKPVVIHDHLGVSRAACLVAaeIAICSLL 621
Cdd:PHA02742 180 SLDIKHFayEDWpHGGLPRDPNKF--LDFVLAVREAdlkadvdikgenivkEPPILVHCSAGLDRAGAFCA--IDICISK 255

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 17508629  622 RGPTYKYPVQRAVQFLRQRRPFSIETPMQYIFVHRLVAFF 661
Cdd:PHA02742 256 YNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCYFIVLIF 295
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 462-655 5.57e-21

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: 91.64  E-value: 5.57e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 462 FIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKEPER--CEYYWPKSPS----DPAVTVpggLR 535
Cdd:cd14549   1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRrkCDQYWPKEGTetygNIQVTL---LS 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 536 IENFGVYQAPDPLFRVTHLRLIGPDREERHVEHWQgdvnnssnmY----------SPLNILRLLRNASK-------PVVI 598
Cdd:cd14549  78 TEVLATYTVRTFSLKNLKLKKVKGRSSERVVYQYH---------YtqwpdhgvpdYTLPVLSFVRKSSAanppgagPIVV 148

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17508629 599 HDHLGVSRAACLvaaeIAICSLLRGPTYKYPVQRA--VQFLRQRRPFSIETPMQYIFVH 655
Cdd:cd14549 149 HCSAGVGRTGTY----IVIDSMLQQIQDKGTVNVFgfLKHIRTQRNYLVQTEEQYIFIH 203
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 426-655 5.97e-21

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: 93.62  E-value: 5.97e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 426 HSASDNNQEKCRNPRVHCRDSTRIALQFPRGQYLGDFIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVM 505
Cdd:cd14625  41 HSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVM 120

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 506 LTSRKEPER--CEYYWPKSPSDP----AVTVPGGLRIENFGVyqapdplfRVTHLRLIGpDREERHVEHWQGDV--NNSS 577
Cdd:cd14625 121 MTKLEEKSRikCDQYWPSRGTETygmiQVTLLDTIELATFCV--------RTFSLHKNG-SSEKREVRQFQFTAwpDHGV 191

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 578 NMYsPLNILRLLRNA-------SKPVVIHDHLGVSRAACLVAAEiAICSLLRgPTYKYPVQRAVQFLRQRRPFSIETPMQ 650
Cdd:cd14625 192 PEY-PTPFLAFLRRVktcnppdAGPIVVHCSAGVGRTGCFIVID-AMLERIK-HEKTVDIYGHVTLMRSQRNYMVQTEDQ 268


                ....*
gi 17508629 651 YIFVH 655
Cdd:cd14625 269 YSFIH 273
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 439-656 8.99e-21

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the first PTP domain (repeat 1).


Pssm-ID: 350468 [Multi-domain]  Cd Length: 229  Bit Score: 91.93  E-value: 8.99e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 439 PRVHCRDSTRIALQFPRGQYLGDFIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKE--PERCE 516
Cdd:cd14620   2 PNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKErkEEKCY 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 517 YYWPkspsDPAVTVPGGLRI--ENFGV------------YQAPD---PLFRVTHLrligpdreerHVEHWQgdvnNSSNM 579
Cdd:cd14620  82 QYWP----DQGCWTYGNIRVavEDCVVlvdytirkfciqPQLPDgckAPRLVTQL----------HFTSWP----DFGVP 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 580 YSPLNILRLLRNA-------SKPVVIHDHLGVSRAACLVAAEiAICSLLRGPTyKYPVQRAVQFLRQRRPFSIETPMQYI 652
Cdd:cd14620 144 FTPIGMLKFLKKVksvnpvhAGPIVVHCSAGVGRTGTFIVID-AMIDMMHAEQ-KVDVFEFVSRIRNQRPQMVQTDMQYS 221


                ....
gi 17508629 653 FVHR 656
Cdd:cd14620 222 FIYQ 225
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 467-658 3.68e-20

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: 89.42  E-value: 3.68e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 467 RISGKPLFneFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTsrKEPER----CEYYWPKSPSDPAVTVPGGLRIENFGVY 542
Cdd:cd14596  10 PVGEEELF--YIATQGPLPSTIDDFWQMVWENRSDVIAMMT--REVERgkvkCHRYWPETLQEPMELENYQLRLENYQAL 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 543 QApdplFRVTHLRLIGPDREERH-VEHWQ----GDVNNSSNMYSPLNILRLLR--NASKPVVIHDHLGVSRAACLVAAEI 615
Cdd:cd14596  86 QY----FIIRIIKLVEKETGENRlIKHLQfttwPDHGTPQSSDQLVKFICYMRkvHNTGPIVVHCSAGIGRAGVLICVDV 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 17508629 616 AICSLLRGPTYKypVQRAVQFLRQRRPFSIETPMQYIFVHRLV 658
Cdd:cd14596 162 LLSLIEKDLSFN--IKDIVREMRQQRYGMIQTKDQYLFCYKVV 202
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 432-655 3.71e-20

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: 91.25  E-value: 3.71e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 432 NQEKCRNPRVHCRDSTRIALQFPRGQYLGDFIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKE 511
Cdd:cd14626  41 NKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEE 120

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 512 PER--CEYYWPKSPSDP----AVTVPGGLRIENFGVyqapdplfRVTHLRLIGPDrEERHVEHWQGDV--NNSSNMYsPL 583
Cdd:cd14626 121 KSRvkCDQYWPIRGTETygmiQVTLLDTVELATYSV--------RTFALYKNGSS-EKREVRQFQFMAwpDHGVPEY-PT 190

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17508629 584 NILRLLRNA-------SKPVVIHDHLGVSRAACLVAAEIAICSLLRGPTYKypVQRAVQFLRQRRPFSIETPMQYIFVH 655
Cdd:cd14626 191 PILAFLRRVkacnppdAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVD--IYGHVTCMRSQRNYMVQTEDQYIFIH 267
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 432-661 5.02e-20

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: 90.46  E-value: 5.02e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 432 NQEKCRNPRVHCRDSTRIALQ-FPRGQYLGDFIHAN---------RISGKPLfNEFIMTQAPMKNTVDDFWRMVWQEEVP 501
Cdd:cd14605   2 NKNKNRYKNILPFDHTRVVLHdGDPNEPVSDYINANiimpefetkCNNSKPK-KSYIATQGCLQNTVNDFWRMVFQENSR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 502 YIVMLTsrKEPER----CEYYWpksPSDPAVTVPGGLRIENFGVYQAPDPLFRVTHLRLIGPDREERHVehWQ------- 570
Cdd:cd14605  81 VIVMTT--KEVERgkskCVKYW---PDEYALKEYGVMRVRNVKESAAHDYILRELKLSKVGQGNTERTV--WQyhfrtwp 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 571 -----GDVNNSSNMYSPLNILRLLRNASKPVVIHDHLGVSRAACLVAAEIAIcSLLR--GPTYKYPVQRAVQFLRQRRPF 643
Cdd:cd14605 154 dhgvpSDPGGVLDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILI-DIIRekGVDCDIDVPKTIQMVRSQRSG 232

                       250
                ....*....|....*...
gi 17508629 644 SIETPMQYIFVHRLVAFF 661
Cdd:cd14605 233 MVQTEAQYRFIYMAVQHY 250
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 423-655 8.80e-20

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: 90.10  E-value: 8.80e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 423 PFTHSASDNNQEKCRNPRVHCRDSTRIALQFPRGQYLGDFIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPY 502
Cdd:cd14633  31 PWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTAS 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 503 IVMLTSRKEPER--CEYYWPKSPS---DPAVTVpgglrIENFGVYQAPDPLFRVTHlRLIGPDREERHVeHWQGDVNNSS 577
Cdd:cd14633 111 IIMVTNLVEVGRvkCCKYWPDDTEiykDIKVTL-----IETELLAEYVIRTFAVEK-RGVHEIREIRQF-HFTGWPDHGV 183

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 578 NMYSP--LNILRLLRNASK----PVVIHDHLGVSRAACLVAAEIAICSLLRGPTYKypVQRAVQFLRQRRPFSIETPMQY 651
Cdd:cd14633 184 PYHATglLGFVRQVKSKSPpnagPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVD--IYNCVRELRSRRVNMVQTEEQY 261


                ....
gi 17508629 652 IFVH 655
Cdd:cd14633 262 VFIH 265
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 432-661 1.03e-19

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: 89.55  E-value: 1.03e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 432 NQEKCRNPRVHCRDSTRIALQFPRGQYLG-DFIHANRISGKPLFNE-----FIMTQAPMKNTVDDFWRMVWQEEVPYIVM 505
Cdd:cd14606  18 NKSKNRYKNILPFDHSRVILQGRDSNIPGsDYINANYVKNQLLGPDenaktYIASQGCLEATVNDFWQMAWQENSRVIVM 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 506 LTSRKEPER--CEYYWPKSPSDPAVtvpGGLRIENFGVYQAPDplFRVTHLRLIGPDREE--RHVEHWQ-------GDVN 574
Cdd:cd14606  98 TTREVEKGRnkCVPYWPEVGMQRAY---GPYSVTNCGEHDTTE--YKLRTLQVSPLDNGEliREIWHYQylswpdhGVPS 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 575 NSSNMYSPLNILRL----LRNASkPVVIHDHLGVSRAACLVAAEIAICSL-LRGPTYKYPVQRAVQFLRQRRPFSIETPM 649
Cdd:cd14606 173 EPGGVLSFLDQINQrqesLPHAG-PIIVHCSAGIGRTGTIIVIDMLMENIsTKGLDCDIDIQKTIQMVRAQRSGMVQTEA 251

                       250
                ....*....|..
gi 17508629 650 QYIFVHRLVAFF 661
Cdd:cd14606 252 QYKFIYVAIAQF 263
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 426-658 1.11e-19

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: 89.18  E-value: 1.11e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 426 HSASDNNQEKCRNPRVHC--RDSTRIALQFPRGQYLGDFIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYI 503
Cdd:cd14614   4 HFAADLPVNRCKNRYTNIlpYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQII 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 504 VMLTSRKEPER--CEYYWPKSpSDPAVTvpGGLRIENFGVYQAPDPLFRvtHLRLIGPDREERHV--------EHWQGDV 573
Cdd:cd14614  84 VMLTQCNEKRRvkCDHYWPFT-EEPVAY--GDITVEMLSEEEQPDWAIR--EFRVSYADEVQDVMhfnytawpDHGVPTA 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 574 NNSSNMYSPLNILRLLRNASK-PVVIHDHLGVSRAACLVAAEiaiCSLLRGPTYKY-PVQRAVQFLRQRRPFSIETPMQY 651
Cdd:cd14614 159 NAAESILQFVQMVRQQAVKSKgPMIIHCSAGVGRTGTFIALD---RLLQHIRDHEFvDILGLVSEMRSYRMSMVQTEEQY 235


                ....*..
gi 17508629 652 IFVHRLV 658
Cdd:cd14614 236 IFIHQCV 242
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 424-663 1.34e-19

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: 89.67  E-value: 1.34e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 424 FTHSASDNNQEKCRNPRVHCRDSTRIALqFPRGQYLGDFIHANRI----SGKPLfnEFIMTQAPMKNTVDDFWRMVWQEE 499
Cdd:cd14599  30 FTTATLPENAERNRIREVVPYEENRVEL-VPTKENNTGYINASHIkvtvGGEEW--HYIATQGPLPHTCHDFWQMVWEQG 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 500 VPYIVMLTSRKEPERCE--YYWPKSPSDPAVTVPGGLRI-ENF----GVYQAPDplFRVTHLrLIGPDREERHVEH--W- 569
Cdd:cd14599 107 VNVIAMVTAEEEGGRSKshRYWPKLGSKHSSATYGKFKVtTKFrtdsGCYATTG--LKVKHL-LSGQERTVWHLQYtdWp 183

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 570 -QGDVNNSSNMYSPLNILRLLR-----------NASKPVVIHDHLGVSRAACLVAAEIAICSLLRGPTYKYPVQraVQFL 637
Cdd:cd14599 184 dHGCPEEVQGFLSYLEEIQSVRrhtnsmldstkNCNPPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVM--LRHL 261

                       250       260
                ....*....|....*....|....*.
gi 17508629 638 RQRRPFSIETPMQYIFVHRLVAFFFR 663
Cdd:cd14599 262 REQRMFMIQTIAQYKFVYQVLIQFLK 287
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 359-662 2.07e-19

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: 89.61  E-value: 2.07e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 359 KRVQAFKANVLADRDrvrvagQFYNNIRIGKRMFGAARKAKYLSTIIGgmERRFEILENSVNHI-PFTHSasdnnqekcr 437
Cdd:cd14604  11 ERVQAMKSTDHNGED------NFASDFMRLRRLSTKYRTEKIYPTATG--EKEENVKKNRYKDIlPFDHS---------- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 438 nprvhcrdstRIALQFPRGQYLGDFIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKEPER--C 515
Cdd:cd14604  73 ----------RVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRkkC 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 516 EYYWPKSPSDPAVTVPGGLRIENfgvYQAPDPLFRVThlRLIGPDREER-----HVEHWQgDVNNSSNMYSPLNILRLLR 590
Cdd:cd14604 143 ERYWPLYGEEPMTFGPFRISCEA---EQARTDYFIRT--LLLEFQNETRrlyqfHYVNWP-DHDVPSSFDSILDMISLMR 216

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17508629 591 NASK----PVVIHDHLGVSRAACLVAAEIAICSLLRGP-TYKYPVQRAVQFLRQRRPFSIETPMQYIFVHRLVAFFF 662
Cdd:cd14604 217 KYQEhedvPICIHCSAGCGRTGAICAIDYTWNLLKAGKiPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLF 293
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 445-656 3.19e-19

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


Pssm-ID: 350465 [Multi-domain]  Cd Length: 228  Bit Score: 87.28  E-value: 3.19e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 445 DSTRIALQFPRGQYLGDFIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKEPER--CEYYWpks 522
Cdd:cd14617  10 DSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRvkCDHYW--- 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 523 PSDPAVTVPGGLRIENFGvyQAPDPLFRVTHLRLIGPD--REERHVEHWQ----GDVNNSSNMYSPLNILRLLR------ 590
Cdd:cd14617  87 PADQDSLYYGDLIVQMLS--ESVLPEWTIREFKICSEEqlDAPRLVRHFHytvwPDHGVPETTQSLIQFVRTVRdyinrt 164

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17508629 591 NASKPVVIHDHLGVSRAACLVAAEIAICSLLRGPTYKypVQRAVQFLRQRRPFSIETPMQYIFVHR 656
Cdd:cd14617 165 PGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVD--IYGAVHDLRLHRVHMVQTECQYVYLHQ 228
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 462-656 4.45e-19

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: 85.94  E-value: 4.45e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 462 FIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKE--PERCEYYWPKSPSDPAVTvpGGLRIENF 539
Cdd:cd14542   1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEmgKKKCERYWPEEGEEQLQF--GPFKISLE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 540 GVYQ-APDPLFRVTHLRLigpDREER-----HVEHWQgDVNNSSNMYSPLNILRLLR----NASKPVVIHDHLGVSRAAC 609
Cdd:cd14542  79 KEKRvGPDFLIRTLKVTF---QKESRtvyqfHYTAWP-DHGVPSSVDPILDLVRLVRdyqgSEDVPICVHCSAGCGRTGT 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 17508629 610 LVAAEIAICSLLRGP-TYKYPVQRAVQFLRQRRPFSIETPMQYIFVHR 656
Cdd:cd14542 155 ICAIDYVWNLLKTGKiPEEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 405-656 4.67e-19

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: 88.25  E-value: 4.67e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 405 IGGMERRFEILENSVNHIP-FTHSASDNNQEKCRNPRVHCRDSTRIALQFPRGQYLGDFIHANRISGKPLFNEFIMTQAP 483
Cdd:cd14628  24 VTGMELEFKRLASSKAHTSrFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGP 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 484 MKNTVDDFWRMVWQEEVPYIVMLTSRKE--PERCEYYWPKSPSdpavtvpggLRIENFGV-----YQAPDPL---FRVTH 553
Cdd:cd14628 104 LAETTEDFWRMLWEHNSTIVVMLTKLREmgREKCHQYWPAERS---------ARYQYFVVdpmaeYNMPQYIlreFKVTD 174

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 554 LRligpDREERHVEHWQ-GDVNNSSNMYSPLNILRLLRNASK---------PVVIHDHLGVSRAACLVAAEIaicsLLRG 623
Cdd:cd14628 175 AR----DGQSRTVRQFQfTDWPEQGVPKSGEGFIDFIGQVHKtkeqfgqdgPISVHCSAGVGRTGVFITLSI----VLER 246

                       250       260       270
                ....*....|....*....|....*....|....*
gi 17508629 624 PTYKYPVQ--RAVQFLRQRRPFSIETPMQYIFVHR 656
Cdd:cd14628 247 MRYEGVVDifQTVKMLRTQRPAMVQTEDQYQFCYR 281
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 476-663 5.66e-19

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: 86.18  E-value: 5.66e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 476 EFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKEP--ERCEYYWPKSPSDPAVTVPGGLRI-----ENFGVYQAPDpl 548
Cdd:cd14598  17 DYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGgrEKSFRYWPRLGSRHNTVTYGRFKIttrfrTDSGCYATTG-- 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 549 FRVTHLrLIGPDREERHVEH--W--QGDVNNSSNMYSPLNILRLLR----------NASKPVVIHDHLGVSRAACLVAAE 614
Cdd:cd14598  95 LKIKHL-LTGQERTVWHLQYtdWpeHGCPEDLKGFLSYLEEIQSVRrhtnstidpkSPNPPVLVHCSAGVGRTGVVILSE 173

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 17508629 615 IAICSLLRGPTYKYPvqRAVQFLRQRRPFSIETPMQYIFVHRLVAFFFR 663
Cdd:cd14598 174 IMIACLEHNEMLDIP--RVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 430-655 7.29e-19

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: 86.62  E-value: 7.29e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 430 DNNQEKCRNPRVHCRDSTRIALQFPRGQYLGDFIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSR 509
Cdd:cd14630   1 DENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 510 KEPER--CEYYWPKSpsdpaVTVPGGLRIENFGVYQAPDPLFRVTHLRLIGPD--REER--HVEHW--QGDVNNSSNMYS 581
Cdd:cd14630  81 VEVGRvkCVRYWPDD-----TEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHeiREIRqfHFTSWpdHGVPCYATGLLG 155

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17508629 582 PLNILRLLRNA-SKPVVIHDHLGVSRAACLVAAEIAICslLRGPTYKYPVQRAVQFLRQRRPFSIETPMQYIFVH 655
Cdd:cd14630 156 FVRQVKFLNPPdAGPIVVHCSAGAGRTGCFIAIDIMLD--MAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVH 228
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 427-656 8.64e-19

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: 87.77  E-value: 8.64e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 427 SASDNNQEKCRNPRVHCRDSTRIALQFPRGQYLGDFIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVML 506
Cdd:cd14621  47 ASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMV 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 507 TSRKEPE--RCEYYWPkspsDPAVTVPGGLRIENFGVYQAPDPLFRVTHLRLIG------PDR--EERHVEHWQgdvnNS 576
Cdd:cd14621 127 TNLKERKecKCAQYWP----DQGCWTYGNIRVSVEDVTVLVDYTVRKFCIQQVGdvtnkkPQRliTQFHFTSWP----DF 198

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 577 SNMYSPLNILRLLRNA-------SKPVVIHDHLGVSRAACLVAAEiAICSLLrGPTYKYPVQRAVQFLRQRRPFSIETPM 649
Cdd:cd14621 199 GVPFTPIGMLKFLKKVkncnpqyAGAIVVHCSAGVGRTGTFIVID-AMLDMM-HAERKVDVYGFVSRIRAQRCQMVQTDM 276


                ....*..
gi 17508629 650 QYIFVHR 656
Cdd:cd14621 277 QYVFIYQ 283
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 405-656 9.29e-19

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: 87.48  E-value: 9.29e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 405 IGGMERRFEILENSVNHIP-FTHSASDNNQEKCRNPRVHCRDSTRIALQFPRGQYLGDFIHANRISGKPLFNEFIMTQAP 483
Cdd:cd14627  25 VTGMELEFKRLANSKAHTSrFISANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGP 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 484 MKNTVDDFWRMVWQEEVPYIVMLTSRKE--PERCEYYWPKSPSdpavtvpggLRIENFGV-----YQAPDPL---FRVTH 553
Cdd:cd14627 105 LAETTEDFWRMLWENNSTIVVMLTKLREmgREKCHQYWPAERS---------ARYQYFVVdpmaeYNMPQYIlreFKVTD 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 554 LRligpDREERHVEHWQ-GDVNNSSNMYSPLNILRLLRNASK---------PVVIHDHLGVSRAACLVAAEIaicsLLRG 623
Cdd:cd14627 176 AR----DGQSRTVRQFQfTDWPEQGVPKSGEGFIDFIGQVHKtkeqfgqdgPISVHCSAGVGRTGVFITLSI----VLER 247

                       250       260       270
                ....*....|....*....|....*....|....*
gi 17508629 624 PTYKYPVQ--RAVQFLRQRRPFSIETPMQYIFVHR 656
Cdd:cd14627 248 MRYEGVVDifQTVKMLRTQRPAMVQTEDEYQFCYQ 282
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 426-655 2.21e-18

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: 85.86  E-value: 2.21e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 426 HSASDNNQEKCRNPRVHCRDSTRIALQFPRGQ--YLGDFIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYI 503
Cdd:cd17667  21 HSNHPDNKHKNRYINILAYDHSRVKLRPLPGKdsKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGII 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 504 VMLTSRKEPER--CEYYWPKSPSDPAVTVPGGLRIEN-FGVYQAPDPLFRVTHL-RLIGPDREERHVEH--WQGDVNNSS 577
Cdd:cd17667 101 VMITNLVEKGRrkCDQYWPTENSEEYGNIIVTLKSTKiHACYTVRRFSIRNTKVkKGQKGNPKGRQNERtvIQYHYTQWP 180

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 578 NMYSP---LNILRLLRNASK-------PVVIHDHLGVSRAACLvaaeIAICSLLRGPTYKYPVQrAVQFL---RQRRPFS 644
Cdd:cd17667 181 DMGVPeyaLPVLTFVRRSSAartpemgPVLVHCSAGVGRTGTY----IVIDSMLQQIKDKSTVN-VLGFLkhiRTQRNYL 255

                       250
                ....*....|.
gi 17508629 645 IETPMQYIFVH 655
Cdd:cd17667 256 VQTEEQYIFIH 266
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 432-660 2.67e-18

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: 84.88  E-value: 2.67e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 432 NQEKCRNPRVHCRDSTRIALqfprGQYlGDFIHANRISgKPLFNE---FIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTS 508
Cdd:cd14597   3 NRKKNRYKNILPYDTTRVPL----GDE-GGYINASFIK-MPVGDEefvYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQ 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 509 RKEPE--RCEYYWPKSPSDPAVtVPGGLRIENFGVYQAPDPLFRVTHLRLIgPDREERHVEH-----WQgDVNNSSNMYS 581
Cdd:cd14597  77 EVEGGkiKCQRYWPEILGKTTM-VDNRLQLTLVRMQQLKNFVIRVLELEDI-QTREVRHITHlnftaWP-DHDTPSQPEQ 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 582 PLNILRLLRN--ASKPVVIHDHLGVSRAACLVAAEIAICSLLRgpTYKYPVQRAVQFLRQRRPFSIETPMQYIFVHRLVA 659
Cdd:cd14597 154 LLTFISYMRHihKSGPIITHCSAGIGRSGTLICIDVVLGLISK--DLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVIL 231


                .
gi 17508629 660 F 660
Cdd:cd14597 232 Y 232
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 424-655 3.81e-18

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: 85.55  E-value: 3.81e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 424 FTHSASDNNQEKCRNPRVHCRDSTRIALQFPRGQYLGDFIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYI 503
Cdd:cd14624  39 WEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATV 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 504 VMLTSRKEPER--CEYYWPKSPSDpavtVPGGLRIENFGVYQAPDPLFRVTHLRLIGpDREERHVEHWQGDVNNSSNM-Y 580
Cdd:cd14624 119 VMMTKLEERSRvkCDQYWPSRGTE----TYGLIQVTLLDTVELATYCVRTFALYKNG-SSEKREVRQFQFTAWPDHGVpE 193

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 581 SPLNILRLLRNA-------SKPVVIHDHLGVSRAACLVAAEIAICSLLRGPTYKypVQRAVQFLRQRRPFSIETPMQYIF 653
Cdd:cd14624 194 HPTPFLAFLRRVktcnppdAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVD--IYGHVTLMRAQRNYMVQTEDQYIF 271


                ..
gi 17508629 654 VH 655
Cdd:cd14624 272 IH 273
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 462-656 6.92e-18

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: 82.57  E-value: 6.92e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 462 FIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKEPER--CEYYWPKSPSDPAVTVPGGLRIENF 539
Cdd:cd14557   1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRnkCAQYWPSMEEGSRAFGDVVVKINEE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 540 GVYqaPDPLFRVTHLRLIGPDREERHVEHWQGDVNNSSNMYSPLNILRLLR---NA-----SKPVVIHDHLGVSRAACLv 611
Cdd:cd14557  81 KIC--PDYIIRKLNINNKKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRrrvNAfnnffSGPIVVHCSAGVGRTGTY- 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 17508629 612 aaeIAICSLLRG-------PTYKYPVQravqfLRQRRPFSIETPMQYIFVHR 656
Cdd:cd14557 158 ---IGIDAMLEGleaegrvDVYGYVVK-----LRRQRCLMVQVEAQYILIHQ 201
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 448-655 1.01e-17

catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350479 [Multi-domain]  Cd Length: 218  Bit Score: 82.76  E-value: 1.01e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 448 RIALQFPRGQYLGDFIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKEPER--CEYYWPKSpsd 525
Cdd:cd14631   1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRvkCYKYWPDD--- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 526 paVTVPGGLRIENFGVYQAPDPLFRVTHLRLIGPDrEERHVE--HWQGDVNNSSNmYSPLNILRLLRN-------ASKPV 596
Cdd:cd14631  78 --TEVYGDFKVTCVEMEPLAEYVVRTFTLERRGYN-EIREVKqfHFTGWPDHGVP-YHATGLLSFIRRvklsnppSAGPI 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17508629 597 VIHDHLGVSRAACLVAAEIAICSLLRGPTYKypVQRAVQFLRQRRPFSIETPMQYIFVH 655
Cdd:cd14631 154 VVHCSAGAGRTGCYIVIDIMLDMAEREGVVD--IYNCVKALRSRRINMVQTEEQYIFIH 210
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 437-653 2.11e-17

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: 82.05  E-value: 2.11e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 437 RNPRVHCRDSTRIALQFPRGQylGDFIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTS--RKEPER 514
Cdd:cd14545   3 RYRDRDPYDHDRSRVKLKQGD--NDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKlmEKGQIK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 515 CEYYWPKSPSDPAVTVPGGLRIENFGVYQAPDPLFRVTHL-RLIGPdrEERHVEHWQ-------GdVNNSSNMYspLNIL 586
Cdd:cd14545  81 CAQYWPQGEGNAMIFEDTGLKVTLLSEEDKSYYTVRTLELeNLKTQ--ETREVLHFHyttwpdfG-VPESPAAF--LNFL 155

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17508629 587 RLLRNAS------KPVVIHDHLGVSRAACLVAAEIAICSLLRGPTYKYPVQRAVQFLRQRRPFSIETPMQYIF 653
Cdd:cd14545 156 QKVRESGslssdvGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPSSVDVKKVLLEMRKYRMGLIQTPDQLRF 228
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 462-655 2.64e-17

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: 80.89  E-value: 2.64e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 462 FIHANRISG-KPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKEPE--RCEYYWPKSPSDPAVTvpGGLRIEN 538
Cdd:cd14539   1 YINASLIEDlTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEkqKVHRYWPTERGQALVY--GAITVSL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 539 FGVYQAPDPLFRVTHLRLiGPDREERHVEHWQ-GDVNNSSNMYSPLNILRLL----------RNASKPVVIHDHLGVSR- 606
Cdd:cd14539  79 QSVRTTPTHVERIISIQH-KDTRLSRSVVHLQfTTWPELGLPDSPNPLLRFIeevhshylqqRSLQTPIVVHCSSGVGRt 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 17508629 607 -AACLVAAeiAICSLLRG-PTYKYPvqRAVQFLRQRRPFSIETPMQYIFVH 655
Cdd:cd14539 158 gAFCLLYA--AVQEIEAGnGIPDLP--QLVRKMRQQRKYMLQEKEHLKFCY 204
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 462-655 2.97e-17

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: 80.73  E-value: 2.97e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 462 FIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKEPER--CEYYWPKSPS---DPAVTVpggLRI 536
Cdd:cd14555   1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRvkCSRYWPDDTEvygDIKVTL---VET 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 537 ENFGVYqapdpLFRVTHLRLIGPD--REER--HVEHW--QGDVNNSSNMYSPLNILRLLRNASK-PVVIHDHLGVSRAAC 609
Cdd:cd14555  78 EPLAEY-----VVRTFALERRGYHeiREVRqfHFTGWpdHGVPYHATGLLGFIRRVKASNPPSAgPIVVHCSAGAGRTGC 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 17508629 610 LVAAEIAICSLLRGPTYKypVQRAVQFLRQRRPFSIETPMQYIFVH 655
Cdd:cd14555 153 YIVIDIMLDMAEREGVVD--IYNCVKELRSRRVNMVQTEEQYIFIH 196
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 411-660 3.36e-17

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 83.54  E-value: 3.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629  411 RFEILENS-VNHIPF----THSASDNNQEKCRNPRVHCRDSTRIALQ-------FPRGQYLG------------DFIHAN 466
Cdd:PHA02746  25 EFVLLEHAeVMDIPIrgttNHFLKKENLKKNRFHDIPCWDHSRVVINaheslkmFDVGDSDGkkievtsednaeNYIHAN 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629  467 RISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLT-SRKEPERCEYYWPKsPSDPAVTvpgglrienFGVYQAP 545
Cdd:PHA02746 105 FVDGFKEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTdIDDDDEKCFELWTK-EEDSELA---------FGRFVAK 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629  546 ------DPLFRVTHLRLIG----PDREERHV--EHWQgDVNNSSNMYSPLNIL--------RLLRNASK------PVVIH 599
Cdd:PHA02746 175 ildiieELSFTKTRLMITDkisdTSREIHHFwfPDWP-DNGIPTGMAEFLELInkvneeqaELIKQADNdpqtlgPIVVH 253

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17508629  600 DHLGVSRAACLVAAEIAICSLLRGPTYKYPvqRAVQFLRQRRPFSIETPMQYIFVHRLVAF 660
Cdd:PHA02746 254 CSAGIGRAGTFCAIDNALEQLEKEKEVCLG--EIVLKIRKQRHSSVFLPEQYAFCYKALKY 312
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 462-655 3.38e-17

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


Pssm-ID: 350480 [Multi-domain]  Cd Length: 205  Bit Score: 80.87  E-value: 3.38e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 462 FIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKEPER--CEYYWPKSPS---DPAVTVpggLRI 536
Cdd:cd14632   1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRvkCSKYWPDDSDtygDIKITL---LKT 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 537 ENFGVYQapdplfrvthLRLIGPDREERHVEHWQGDVNNSS-----NMYSPLNILRLLRNA-------SKPVVIHDHLGV 604
Cdd:cd14632  78 ETLAEYS----------VRTFALERRGYSARHEVKQFHFTSwpehgVPYHATGLLAFIRRVkastppdAGPVVVHCSAGA 147

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 17508629 605 SRAACLVAAEIAI-CSLLRGPTYKYpvqRAVQFLRQRRPFSIETPMQYIFVH 655
Cdd:cd14632 148 GRTGCYIVLDVMLdMAECEGVVDIY---NCVKTLCSRRINMIQTEEQYIFIH 196
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 462-612 7.72e-17

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: 79.67  E-value: 7.72e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 462 FIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKEPERCEYYWPkSPSDPavtvpggLRIENFGV 541
Cdd:cd14550   1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDEPIYWP-TKEKP-------LECETFKV 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 542 -YQAPDPLFRVTHLRLIGPDR-----------EERHVE--HWQgdvNNSSNMYSPLNILRLLRNASK----PVVIHDHLG 603
Cdd:cd14550  73 tLSGEDHSCLSNEIRLIVRDFilestqddyvlEVRQFQcpSWP---NPCSPIHTVFELINTVQEWAQqrdgPIVVHDRYG 149


                ....*....
gi 17508629 604 VSRAACLVA 612
Cdd:cd14550 150 GVQAATFCA 158
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 565-660 9.52e-17

Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine phosphatases. Homologues detected by this profile and not by those of "PTPc" or "DSPc" are predicted to be protein phosphatases with a similar fold to DSPs and PTPs, yet with unpredicted specificities.


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 76.24  E-value: 9.52e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629    565 HVEHWQgdvnNSSNMYSPLNILRLLR---------NASKPVVIHDHLGVSRAACLVAAEIAICSLLRGpTYKYPVQRAVQ 635
Cdd:smart00012   6 HYTGWP----DHGVPESPDSILELLRavkknlnqsESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAE-AGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|....*
gi 17508629    636 FLRQRRPFSIETPMQYIFVHRLVAF 660
Cdd:smart00012  81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
565-660 9.52e-17

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 76.24  E-value: 9.52e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629    565 HVEHWQgdvnNSSNMYSPLNILRLLR---------NASKPVVIHDHLGVSRAACLVAAEIAICSLLRGpTYKYPVQRAVQ 635
Cdd:smart00404   6 HYTGWP----DHGVPESPDSILELLRavkknlnqsESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAE-AGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|....*
gi 17508629    636 FLRQRRPFSIETPMQYIFVHRLVAF 660
Cdd:smart00404  81 ELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 475-655 1.33e-16

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: 78.99  E-value: 1.33e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 475 NEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTS-RKEPERCEYYWPkspsDPAVTVPGGLRIENFGVYQAPDPLFRVTH 553
Cdd:cd14556  14 AAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQlDPKDQSCPQYWP----DEGSGTYGPIQVEFVSTTIDEDVISRIFR 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 554 L-RLIGPDREERHVEHWQ--GDVNNSSNMYSPLNILRLLRNASK--------PVVIHDHLGVSRAACLVAAEIAiCSLLR 622
Cdd:cd14556  90 LqNTTRPQEGYRMVQQFQflGWPRDRDTPPSKRALLKLLSEVEKwqeqsgegPIVVHCLNGVGRSGVFCAISSV-CERIK 168

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 17508629 623 gptykypVQR------AVQFLRQRRPFSIETPMQYIFVH 655
Cdd:cd14556 169 -------VENvvdvfqAVKTLRNHRPNMVETEEQYKFCY 200
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 430-659 1.72e-16

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: 80.49  E-value: 1.72e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 430 DNNQEKCRNPRVHCRDSTRIALQFPRGQYLGDFIHANRI-SGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTS 508
Cdd:cd14610  42 EENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPImDHDPRNPAYIATQGPLPATVADFWQMVWESGCVVIVMLTP 121

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 509 RKEP--ERCEYYWPKSPSDPAVTVPGGLRIENFgvyQAPDPLFRVTHLRLIGPDrEER-----HVEHWQgDVNNSSNMYS 581
Cdd:cd14610 122 LAENgvKQCYHYWPDEGSNLYHIYEVNLVSEHI---WCEDFLVRSFYLKNLQTN-ETRtvtqfHFLSWN-DQGVPASTRS 196

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 582 PLNILRLL----RNASKPVVIHDHLGVSRAACLVAAEIAICSLLRGPTyKYPVQRAVQFLRQRRPFSIETPMQYIFVHRL 657
Cdd:cd14610 197 LLDFRRKVnkcyRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMAKGAK-EIDIAATLEHLRDQRPGMVQTKEQFEFALTA 275


                ..
gi 17508629 658 VA 659
Cdd:cd14610 276 VA 277
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 405-656 2.33e-16

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: 80.15  E-value: 2.33e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 405 IGGMERRFEILENSVNHIP-FTHSASDNNQEKCRNPRVHCRDSTRIALQFPRGQYLGDFIHANRISGKPLFNEFIMTQAP 483
Cdd:cd14629  25 VTAMELEFKLLANSKAHTSrFISANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGP 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 484 MKNTVDDFWRMVWQEEVPYIVMLTSRKE--PERCEYYWPKSPSdpavtvpggLRIENFGV-----YQAPDPL---FRVTH 553
Cdd:cd14629 105 LAETTEDFWRMLWEHNSTIVVMLTKLREmgREKCHQYWPAERS---------ARYQYFVVdpmaeYNMPQYIlreFKVTD 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 554 LRligpDREERHVEHWQ--------------------GDVNNSSNMYSplnilrllrnASKPVVIHDHLGVSRAACLVAA 613
Cdd:cd14629 176 AR----DGQSRTIRQFQftdwpeqgvpktgegfidfiGQVHKTKEQFG----------QDGPITVHCSAGVGRTGVFITL 241

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 17508629 614 EIaicsLLRGPTYKYPVQ--RAVQFLRQRRPFSIETPMQYIFVHR 656
Cdd:cd14629 242 SI----VLERMRYEGVVDmfQTVKTLRTQRPAMVQTEDQYQLCYR 282
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 437-656 3.35e-16

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: 78.41  E-value: 3.35e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 437 RNPRVHCRDSTRIALQFPRGQYLGDFIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTS--RKEPER 514
Cdd:cd14616   2 RFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQcfEKGRIR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 515 CEYYWPKspSDPAVTVPGGLRIENFGVYQAPDPLFRVTHLRLIGPDREERHVEH--W--QGDVNNSSNMYSPLNILRLLR 590
Cdd:cd14616  82 CHQYWPE--DNKPVTVFGDIVITKLMEDVQIDWTIRDLKIERHGDYMMVRQCNFtsWpeHGVPESSAPLIHFVKLVRASR 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17508629 591 -NASKPVVIHDHLGVSRAACLVAAEIAIcSLLRGPTYkYPVQRAVQFLRQRRPFSIETPMQYIFVHR 656
Cdd:cd14616 160 aHDNTPMIVHCSAGVGRTGVFIALDHLT-QHINDHDF-VDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 461-661 3.91e-16

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: 77.74  E-value: 3.91e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 461 DFIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLT--SRKEPERCEYYWPKSPS----DPAVTVPGGL 534
Cdd:cd14622   1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTelQEREQEKCVQYWPSEGSvthgEITIEIKNDT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 535 RIENFGVYQAPDPLFRVTHLRLIgpdrEERHVEHWQgDVNNSSNMYSPLNILRLL-----RNASKPVVIHDHLGVSRAAC 609
Cdd:cd14622  81 LLETISIRDFLVTYNQEKQTRLV----RQFHFHGWP-EIGIPAEGKGMIDLIAAVqkqqqQTGNHPIVVHCSAGAGRTGT 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 17508629 610 LvaaeIAICSLLRGPTYK--YPVQRAVQFLRQRRPFSIETPMQYIFVHRLVAFF 661
Cdd:cd14622 156 F----IALSNILERVKAEglLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 429-659 4.58e-16

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: 79.31  E-value: 4.58e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 429 SDNNQEKCRNPRVHCRDSTRIALQFPRGQYLGDFIHANRI-SGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLT 507
Cdd:cd14609  39 GEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIiEHDPRMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLT 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 508 SRKEP--ERCEYYWPKSPSDPAVTVPGGLRIENFgvyQAPDPLFRVTHLRLIgPDREER-----HVEHWQGDVNNSSNmy 580
Cdd:cd14609 119 PLVEDgvKQCDRYWPDEGSSLYHIYEVNLVSEHI---WCEDFLVRSFYLKNV-QTQETRtltqfHFLSWPAEGIPSST-- 192

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 581 SPL-----NILRLLRNASKPVVIHDHLGVSRAACLVAAEIAICSLLRGpTYKYPVQRAVQFLRQRRPFSIETPMQYIFVH 655
Cdd:cd14609 193 RPLldfrrKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKG-VKEIDIAATLEHVRDQRPGMVRTKDQFEFAL 271


                ....
gi 17508629 656 RLVA 659
Cdd:cd14609 272 TAVA 275
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 462-655 1.09e-15

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: 76.56  E-value: 1.09e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 462 FIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKEPER--CEYYWPKSPSDP----AVTVPGglr 535
Cdd:cd17668   1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRrkCDQYWPADGSEEygnfLVTQKS--- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 536 IENFGVYQAPDPLFRVTHLRLIGPD--REERHVEHWQgdVNNSSNMYSP---LNILRLLRNASK-------PVVIHDHLG 603
Cdd:cd17668  78 VQVLAYYTVRNFTLRNTKIKKGSQKgrPSGRVVTQYH--YTQWPDMGVPeytLPVLTFVRKASYakrhavgPVVVHCSAG 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 17508629 604 VSRAACLvaaeIAICSLLRGPTYKYPVQ--RAVQFLRQRRPFSIETPMQYIFVH 655
Cdd:cd17668 156 VGRTGTY----IVLDSMLQQIQHEGTVNifGFLKHIRSQRNYLVQTEEQYVFIH 205
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 462-658 2.37e-15

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: 75.38  E-value: 2.37e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 462 FIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTS--RKEPERCEYYWpksPSDPAVTvPGGLRIENF 539
Cdd:cd14552   1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEikERSQNKCAQYW---PEDGSVS-SGDITVELK 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 540 GVYQAPDPLFRVTHLRLIGPDReERHVE--HWQG--DVNNSSNMYSPLNILRLLR-----NASKPVVIHDHLGVSRAACL 610
Cdd:cd14552  77 DQTDYEDYTLRDFLVTKGKGGS-TRTVRqfHFHGwpEVGIPDNGKGMIDLIAAVQkqqqqSGNHPITVHCSAGAGRTGTF 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 17508629 611 vaaeIAICSLLRGPTYK--YPVQRAVQFLRQRRPFSIETPMQYIFVHRLV 658
Cdd:cd14552 156 ----CALSTVLERVKAEgvLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 448-658 5.60e-15

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: 75.08  E-value: 5.60e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 448 RIALQFPRGQYLGDFIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKE--PERCEYYWpksPSD 525
Cdd:cd14623  12 RVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEErgQEKCAQYW---PSD 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 526 PAVTVpGGLRI-----ENFGVYQAPDPLfrVTHLRligpDREERHVE--HWQG--DVNNSSNMYSPLNILRLL-----RN 591
Cdd:cd14623  89 GSVSY-GDITIelkkeEECESYTVRDLL--VTNTR----ENKSRQIRqfHFHGwpEVGIPSDGKGMINIIAAVqkqqqQS 161

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17508629 592 ASKPVVIHDHLGVSRAACLVAAEIAICSLLRGPTYKypVQRAVQFLRQRRPFSIETPMQYIFVHRLV 658
Cdd:cd14623 162 GNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILD--VFQTVKSLRLQRPHMVQTLEQYEFCYKVV 226
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 462-653 1.23e-14

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: 73.20  E-value: 1.23e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 462 FIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKEP--ERCEYYWP---KSPSDPAVTVPgglRI 536
Cdd:cd14558   1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGdqEQCAQYWGdekKTYGDIEVELK---DT 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 537 ENFGVYQAPDplFRVTHLRligpDREER-----HVEHWQGDV--NNSSNMYSPLNILR-------LLRNASKPVVIHDHL 602
Cdd:cd14558  78 EKSPTYTVRV--FEITHLK----RKDSRtvyqyQYHKWKGEElpEKPKDLVDMIKSIKqklpyknSKHGRSVPIVVHCSD 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17508629 603 GVSRAACLvaaeiaiCSLLR----GPTYKY-PVQRAVQFLRQRRPFSIETPMQYIF 653
Cdd:cd14558 152 GSSRTGIF-------CALWNllesAETEKVvDVFQVVKALRKQRPGMVSTLEQYQF 200
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 445-662 1.56e-14

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: 73.72  E-value: 1.56e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 445 DSTRIALQFPRGQYLGDFIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKE--PERCEYYWPKS 522
Cdd:cd14602  11 DHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEmgKKKCERYWAEP 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 523 PSDPAVTVPGGLRIENfgVYQAPDPLFRVTHLRLIGPDR--EERHVEHW-QGDVNNSSN-MYSPLNILRLLR-NASKPVV 597
Cdd:cd14602  91 GEMQLEFGPFSVTCEA--EKRKSDYIIRTLKVKFNSETRtiYQFHYKNWpDHDVPSSIDpILELIWDVRCYQeDDSVPIC 168

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17508629 598 IHDHLGVSRAACLVAAEIaICSLLRGPTY--KYPVQRAVQFLRQRRPFSIETPMQYIFVHRLVAFFF 662
Cdd:cd14602 169 IHCSAGCGRTGVICAIDY-TWMLLKDGIIpeNFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIELF 234
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 426-653 8.91e-14

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: 72.37  E-value: 8.91e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 426 HSASD---------NNQEKCRNPRVHCRDSTRIALQfprgQYLGDFIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVW 496
Cdd:cd14608  10 HEASDfpcrvaklpKNKNRNRYRDVSPFDHSRIKLH----QEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVW 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 497 QEEVPYIVMLTS--RKEPERCEYYWPKSPSDPAVTVPGGLRI----ENFGVYqapdplFRVTHLRLIG-PDREERHVEHW 569
Cdd:cd14608  86 EQKSRGVVMLNRvmEKGSLKCAQYWPQKEEKEMIFEDTNLKLtlisEDIKSY------YTVRQLELENlTTQETREILHF 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 570 Q----GDVNNSSNMYSPLNILRLLRNASK------PVVIHDHLGVSRAA--CLVAAEIAICSLLRGPTyKYPVQRAVQFL 637
Cdd:cd14608 160 HyttwPDFGVPESPASFLNFLFKVRESGSlspehgPVVVHCSAGIGRSGtfCLADTCLLLMDKRKDPS-SVDIKKVLLEM 238

                       250
                ....*....|....*.
gi 17508629 638 RQRRPFSIETPMQYIF 653
Cdd:cd14608 239 RKFRMGLIQTADQLRF 254
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 477-659 1.50e-13

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: 70.17  E-value: 1.50e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 477 FIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKEP--ERCEYYWPKSPSdpavtvpgglriENFGVYQ---------AP 545
Cdd:cd14546  17 YIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENgvKQCARYWPEEGS------------EVYHIYEvhlvsehiwCD 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 546 DPLFRVTHLRLIgPDREER-----HVEHWQgDVNNSSNMYSPLNILRLL----RNASKPVVIHDHLGVSRAACLVAAEIA 616
Cdd:cd14546  85 DYLVRSFYLKNL-QTSETRtvtqfHFLSWP-DEGIPASAKPLLEFRRKVnksyRGRSCPIVVHCSDGAGRTGTYILIDMV 162

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 17508629 617 ICSLLRGpTYKYPVQRAVQFLRQRRPFSIETPMQYIFVHRLVA 659
Cdd:cd14546 163 LNRMAKG-AKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVA 204
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 476-653 1.81e-13

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: 69.80  E-value: 1.81e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 476 EFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTS---RKEPERCEYYWPKSPSDPAVTvpGGLRIENFGVYQAPDPL---- 548
Cdd:cd17658  17 KFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRlvdNYSTAKCADYFPAEENESREF--GRISVTNKKLKHSQHSItlrv 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 549 FRVTHLRLIGPDREERHVE--HW--QGDVNNSSNMYSPLNILRLLRNASKPVVIHDHLGVSRAACLVAAEIAICSLLRGP 624
Cdd:cd17658  95 LEVQYIESEEPPLSVLHIQypEWpdHGVPKDTRSVRELLKRLYGIPPSAGPIVVHCSAGIGRTGAYCTIHNTIRRILEGD 174

                       170       180
                ....*....|....*....|....*....
gi 17508629 625 TYKYPVQRAVQFLRQRRPFSIETPMQYIF 653
Cdd:cd17658 175 MSAVDLSKTVRKFRSQRIGMVQTQDQYIF 203
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
409-661 1.17e-11

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 66.27  E-value: 1.17e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 409 ERRFEIL--ENSVNHIPFTHSASDNNQEKCRNPRVHCRDSTRIAlqfPRGQYLgdfiHANRISGKPLfNEFIMTQAPMKN 486
Cdd:COG5599  17 NSRLSTLtnELAPSHNDPQYLQNINGSPLNRFRDIQPYKETALR---ANLGYL----NANYIQVIGN-HRYIATQYPLEE 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 487 TVDDFWRMVWQEEVPYIVMLTSRKE----PERCEYYWPKSPSDPAVTVpgglRIENFGVYQ-APDPLFRVTHLRLIGPDR 561
Cdd:COG5599  89 QLEDFFQMLFDNNTPVLVVLASDDEiskpKVKMPVYFRQDGEYGKYEV----SSELTESIQlRDGIEARTYVLTIKGTGQ 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 562 EER-----HVEHWQGDVNNSSNMYSPLN--ILRLLRNASK---PVVIHDHLGVSRAACLVAAEIAICSLLRGPTYKYPVQ 631
Cdd:COG5599 165 KKIeipvlHVKNWPDHGAISAEALKNLAdlIDKKEKIKDPdklLPVVHCRAGVGRTGTLIACLALSKSINALVQITLSVE 244

                       250       260       270
                ....*....|....*....|....*....|.
gi 17508629 632 RAVQFLR-QRRPFSIETPMQYIFvhrLVAFF 661
Cdd:COG5599 245 EIVIDMRtSRNGGMVQTSEQLDV---LVKLA 272
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 415-658 1.91e-11

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: 64.99  E-value: 1.91e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 415 LENSVNHIPFTHSASDNNQEKCRNPRVHCRDSTRIALQfprgQYLGDFIHANRISGKPLFNEFIMTQAPMKNTVDDFWRM 494
Cdd:cd14607   7 IRNESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQ----NTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLM 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 495 VWQEEVPYIVMLTS--RKEPERCEYYWPKSPSDPAVTVPGGLRI----ENFGVYQApdplFRVTHLRLI--GPDREERHV 566
Cdd:cd14607  83 VWQQKTKAVVMLNRivEKDSVKCAQYWPTDEEEVLSFKETGFSVkllsEDVKSYYT----VHLLQLENInsGETRTISHF 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 567 EH--WQgDVNNSSNMYSPLNILRLLRNASK------PVVIHDHLGVSRAACLVAAEIAICSLLRGPTYKYPVQRAVQFLR 638
Cdd:cd14607 159 HYttWP-DFGVPESPASFLNFLFKVRESGSlspehgPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDPDSVDIKQVLLDMR 237

                       250       260
                ....*....|....*....|
gi 17508629 639 QRRPFSIETPMQYIFVHRLV 658
Cdd:cd14607 238 KYRMGLIQTPDQLRFSYMAV 257
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 462-612 1.19e-10

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: 61.62  E-value: 1.19e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 462 FIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKEPERCEY-YWP---KSPSDPAVTV----PGG 533
Cdd:cd17670   1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEFvYWPsreESMNCEAFTVtlisKDR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 534 LRIENFGVYQAPDPLFRVTHLRLIgpdREERHVE--HWQGDVNNSSNMYSPLNILR---LLRNAskPVVIHDHLGVSRAA 608
Cdd:cd17670  81 LCLSNEEQIIIHDFILEATQDDYV---LEVRHFQcpKWPNPDAPISSTFELINVIKeeaLTRDG--PTIVHDEFGAVSAG 155


                ....
gi 17508629 609 CLVA 612
Cdd:cd17670 156 TLCA 159
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 477-657 3.98e-10

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: 60.03  E-value: 3.98e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 477 FIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKEPERCEYYWPKSPSdpavTVPGGLRIENFGVYQAPDPLFRVTHL-R 555
Cdd:cd14634  16 FIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAAQLCMQYWPEKTS----CCYGPIQVEFVSADIDEDIISRIFRIcN 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 556 LIGPDREERHVEHWQ--GDVNNSSNMYSPLNILRLLRNASK----------PVVIHDHLGVSRAACLVAAeIAICSLLRG 623
Cdd:cd14634  92 MARPQDGYRIVQHLQyiGWPAYRDTPPSKRSILKVVRRLEKwqeqydgregRTVVHCLNGGGRSGTFCAI-CSVCEMIQQ 170

                       170       180       190
                ....*....|....*....|....*....|....
gi 17508629 624 PTYkYPVQRAVQFLRQRRPFSIETPMQYIFVHRL 657
Cdd:cd14634 171 QNI-IDVFHTVKTLRNNKSNMVETLEQYKFVYEV 203
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 477-657 6.86e-10

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: 59.65  E-value: 6.86e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 477 FIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKEPERCEYYWPKSpsdpAVTVPGGLRIENFGVYQAPDPLFRVTHL-R 555
Cdd:cd14636  16 FIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQGCPQYWPEE----GMLRYGPIQVECMSCSMDCDVISRIFRIcN 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 556 LIGPDREERHVEHWQ--GDVNNSSNMYSPLNILRLLRNASK----------PVVIHDHLGVSRAACLVAAEIaICSLLRG 623
Cdd:cd14636  92 LTRPQEGYLMVQQFQylGWASHREVPGSKRSFLKLILQVEKwqeecdegegRTIIHCLNGGGRSGMFCAISI-VCEMIKR 170

                       170       180       190
                ....*....|....*....|....*....|....
gi 17508629 624 PTYkYPVQRAVQFLRQRRPFSIETPMQYIFVHRL 657
Cdd:cd14636 171 QNV-VDVFHAVKTLRNSKPNMVETPEQYRFCYDV 203
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 462-520 7.46e-10

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: 59.24  E-value: 7.46e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 462 FIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKEPERCEY-YWP 520
Cdd:cd17669   1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFvYWP 60
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 477-657 2.51e-09

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: 57.78  E-value: 2.51e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 477 FIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKEPERCEYYWPKSpsdpAVTVPGGLRIENFGVYQAPDPLFRVthLRL 556
Cdd:cd14635  16 FIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQLCPQYWPEN----GVHRHGPIQVEFVSADLEEDIISRI--FRI 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 557 IGPDREE---RHVEHWQ--GDVNNSSNMYSPLNILRLLRNASK----------PVVIHDHLGVSRAACLVAAEIaICSLL 621
Cdd:cd14635  90 YNAARPQdgyRMVQQFQflGWPMYRDTPVSKRSFLKLIRQVDKwqeeynggegRTVVHCLNGGGRSGTFCAISI-VCEML 168

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 17508629 622 RGpTYKYPVQRAVQFLRQRRPFSIETPMQYIFVHRL 657
Cdd:cd14635 169 RH-QRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEV 203
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 477-658 6.66e-07

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: 50.68  E-value: 6.66e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 477 FIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKEPER---CEYYWPkspsDPAVTVPGGLRIENFGVYQAPDPLFRVTH 553
Cdd:cd14637  16 FIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSawpCLQYWP----EPGLQQYGPMEVEFVSGSADEDIVTRLFR 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 554 LRLIGPDREE----RHVEH--WQGDVNNSSNMYSPLNILRLL-----RNASKPVVIHDHLGVSRA----ACLVAAEIAIC 618
Cdd:cd14637  92 VQNITRLQEGhlmvRHFQFlrWSAYRDTPDSKKAFLHLLASVekwqrESGEGRTVVHCLNGGGRSgtycASAMILEMIRC 171

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 17508629 619 SLLRGPTYkypvqrAVQFLRQRRPFSIETPMQYIFVHRLV 658
Cdd:cd14637 172 HNIVDVFY------AVKTLRNYKPNMVETLEQYRFCYEIA 205
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
583-660 1.82e-06

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 48.04  E-value: 1.82e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17508629 583 LNILRLLRNASKPVVIHDHLGVSRAAcLVAAEIAIcslLRGptykYPVQRAVQFLRQRRPFSIETPMQYIFVHRLVAF 660
Cdd:COG2453  70 VDFIDEALREGKKVLVHCRGGIGRTG-TVAAAYLV---LLG----LSAEEALARVRAARPGAVETPAQRAFLERFAKR 139
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 577-656 2.51e-06

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: 48.03  E-value: 2.51e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629 577 SNMYSPLNILRLLR---NASKPVVIHDHLGVSRAaCLVAAeiaiCSLLR-GPTYkyPVQRAVQFLRQRRPFSIETPMQYI 652
Cdd:cd14505  87 SDIAQWQELLEELLsalENGKKVLIHCKGGLGRT-GLIAA----CLLLElGDTL--DPEQAIAAVRALRPGAIQTPKQEN 159


                ....
gi 17508629 653 FVHR 656
Cdd:cd14505 160 FLHQ 163
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 585-656 3.02e-06

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: 46.57  E-value: 3.02e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17508629 585 ILRLLRNASK---PVVIHDHLGVSRAACLVAaeiaiCSLLRGptYKYPVQRAVQFLRQRRPFSI-ETPMQYIFVHR 656
Cdd:cd14494  45 FLEVLDQAEKpgePVLVHCKAGVGRTGTLVA-----CYLVLL--GGMSAEEAVRIVRLIRPGGIpQTIEQLDFLIK 113
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 427-663 6.66e-06

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 48.81  E-value: 6.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629  427 SASDNNQEKCR------------NPRVHCRDSTRIalqfprgqylgdfIHANRISGKPLFNEFIMTQAPMKNTVDDFWRM 494
Cdd:PHA02740  44 KACAQAENKAKdenlalhitrllHRRIKLFNDEKV-------------LDARFVDGYDFEQKFICIINLCEDACDKFLQA 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629  495 VWQEEVPYIVMLTSRKEPERCEYYWpkSPSDPAVTVPGGLRIENFGVYQAPDplFRVTHLRLIGPDREERHVEH-----W 569
Cdd:PHA02740 111 LSDNKVQIIVLISRHADKKCFNQFW--SLKEGCVITSDKFQIETLEIIIKPH--FNLTLLSLTDKFGQAQKISHfqytaW 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508629  570 QGD------------VNNSSNMYSPLNILRLLRNASkPVVIHDHLGVSRAACLVAAEIAICSLLRGPTYKYPvqRAVQFL 637
Cdd:PHA02740 187 PADgfshdpdafidfFCNIDDLCADLEKHKADGKIA-PIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIA--NALKKV 263

                        250       260
                 ....*....|....*....|....*.
gi 17508629  638 RQRRPFSIETPMQYIFVHRLVAFFFR 663
Cdd:PHA02740 264 RQKKYGCMNCLDDYVFCYHLIAAYLK 289
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 590-642 1.05e-04

dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in typical and atypical dual-specificity phosphatases (DUSPs), which function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48). Typical DUSPs, also called mitogen-activated protein kinase (MAPK) phosphatases (MKPs), deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. All MKPs contain an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain. Atypical DUSPs contain the catalytic dual specificity phosphatase domain but lack the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. Also included in this family are dual specificity phosphatase-like domains of catalytically inactive members such as serine/threonine/tyrosine-interacting protein (STYX) and serine/threonine/tyrosine interacting like 1 (STYXL1), as well as active phosphatases with substrates that are not phosphoproteins such as PTP localized to the mitochondrion 1 (PTPMT1), which is a lipid phosphatase, and laforin, which is a glycogen phosphatase.


Pssm-ID: 350348 [Multi-domain]  Cd Length: 135  Bit Score: 42.92  E-value: 1.05e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 17508629 590 RNASKPVVIHDHLGVSRAACLVAAEiaicsLLRgpTYKYPVQRAVQFLRQRRP 642
Cdd:cd14498  76 LKKGGKVLVHCQAGVSRSATIVIAY-----LMK--KYGWSLEEALELVKSRRP 121
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
584-642 1.41e-03

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 39.57  E-value: 1.41e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 17508629    584 NILRLLRNASKPVVIHDHLGVSRAACLVAAEiaicsLLRgpTYKYPVQRAVQFLRQRRP 642
Cdd:smart00195  69 EFIEDAESKGGKVLVHCQAGVSRSATLIIAY-----LMK--TRNMSLNDAYDFVKDRRP 120
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 584-642 1.98e-03

Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The enzyme's tertiary fold is highly similar to that of tyrosine-specific phosphatases, except for a "recognition" region.


Pssm-ID: 395632 [Multi-domain]  Cd Length: 127  Bit Score: 38.78  E-value: 1.98e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 17508629   584 NILRLLRNASKPVVIHDHLGVSRAACLVAAEIaICsllrgpTYKYPVQRAVQFLRQRRP 642
Cdd:pfam00782  60 EFIDDARQKGGKVLVHCQAGISRSATLIIAYL-MK------TRNLSLNEAYSFVKERRP 111
 
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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