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Conserved domains on  [gi|17507417|ref|NP_491276|]
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Protein-tyrosine phosphatase [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;
67-324 6.81e-102

Protein tyrosine phosphatase, catalytic domain;


:

Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 301.50  E-value: 6.81e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417     67 KLRDEFSE---VANKNPNVPVDAFKSNPEKNRYTDIKCIEKTRVILT-TDGASSDYIHANYVGISIKPKKFICTQGPKDS 142
Cdd:smart00194   1 GLEEEFEKldrLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKpPPGEGSDYINASYIDGPNGPKAYIATQGPLPS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417    143 TIYDFWAMVIQDNVESIIMLCKVIELARVKCEQYWPAVEGQTNTYvskgHTITINNLGVGTLspddDFINVTNLELVWAG 222
Cdd:smart00194  81 TVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTY----GDITVTLKSVEKV----DDYTIRTLEVTNTG 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417    223 --KTRSITHYQWTNWPDHGAPPINMGAINLIEAVN----YDTNPVVVHCSAGVGRSGTIVGISLIMDKMIQGINCkDMKK 296
Cdd:smart00194 153 csETRTVTHYHYTNWPDHGVPESPESILDLIRAVRksqsTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEV-DIFE 231

                          250       260
                   ....*....|....*....|....*...
gi 17507417    297 LVEEIRNQRHYAIQTEAQYMYIHRVLLE 324
Cdd:smart00194 232 IVKELRSQRPGMVQTEEQYIFLYRAILE 259
 
Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
67-324 6.81e-102

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 301.50  E-value: 6.81e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417     67 KLRDEFSE---VANKNPNVPVDAFKSNPEKNRYTDIKCIEKTRVILT-TDGASSDYIHANYVGISIKPKKFICTQGPKDS 142
Cdd:smart00194   1 GLEEEFEKldrLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKpPPGEGSDYINASYIDGPNGPKAYIATQGPLPS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417    143 TIYDFWAMVIQDNVESIIMLCKVIELARVKCEQYWPAVEGQTNTYvskgHTITINNLGVGTLspddDFINVTNLELVWAG 222
Cdd:smart00194  81 TVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTY----GDITVTLKSVEKV----DDYTIRTLEVTNTG 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417    223 --KTRSITHYQWTNWPDHGAPPINMGAINLIEAVN----YDTNPVVVHCSAGVGRSGTIVGISLIMDKMIQGINCkDMKK 296
Cdd:smart00194 153 csETRTVTHYHYTNWPDHGVPESPESILDLIRAVRksqsTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEV-DIFE 231

                          250       260
                   ....*....|....*....|....*...
gi 17507417    297 LVEEIRNQRHYAIQTEAQYMYIHRVLLE 324
Cdd:smart00194 232 IVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
90-324 4.84e-99

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 293.38  E-value: 4.84e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417    90 NPEKNRYTDIKCIEKTRVILTTDGASSDYIHANYVGISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIELA 169
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417   170 RVKCEQYWPAVEGQTNTYvskgHTITINNLGVgtlSPDDDFINVTNLELVWAG--KTRSITHYQWTNWPDHGAPPINMGA 247
Cdd:pfam00102  81 REKCAQYWPEEEGESLEY----GDFTVTLKKE---KEDEKDYTVRTLEVSNGGseETRTVKHFHYTGWPDHGVPESPNSL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417   248 INLIEAVN-----YDTNPVVVHCSAGVGRSGTIVGISLIMDKMIQGiNCKDMKKLVEEIRNQRHYAIQTEAQYMYIHRVL 322
Cdd:pfam00102 154 LDLLRKVRkssldGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAE-GEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAI 232


                  ..
gi 17507417   323 LE 324
Cdd:pfam00102 233 LE 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 118-320 6.47e-68

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: 212.53  E-value: 6.47e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 118 YIHANYVGISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIELARVKCEQYWPAVEGQTNTYvskgHTITIN 197
Cdd:cd00047   1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEY----GDITVT 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 198 NLGVgtlSPDDDFInVTNLELVWAG--KTRSITHYQWTNWPDHGAPPINMGAINLIEAVNY----DTNPVVVHCSAGVGR 271
Cdd:cd00047  77 LVSE---EELSDYT-IRTLELSPKGcsESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKearkPNGPIVVHCSAGVGR 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 17507417 272 SGTIVGISLIMDKMIQGiNCKDMKKLVEEIRNQRHYAIQTEAQYMYIHR 320
Cdd:cd00047 153 TGTFIAIDILLERLEAE-GEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 68-331 1.12e-41

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 148.23  E-value: 1.12e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417   68 LRDEFSEVANKNPNVPVDAFK--SNPEKNRYTDIKCIEKTRVILTT-DGASSDYIHANYVGISIKPKKFICTQGPKDSTI 144
Cdd:PHA02747  27 IRDEHHQIILKPFDGLIANFEkpENQPKNRYWDIPCWDHNRVILDSgGGSTSDYIHANWIDGFEDDKKFIATQGPFAETC 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  145 YDFWAMVIQDNVESIIMLCKVIEL-ARVKCEQYWPAVEGQ---TNTYVSKGHTITINNLGVGTLspdddfINVTNLELvw 220
Cdd:PHA02747 107 ADFWKAVWQEHCSIIVMLTPTKGTnGEEKCYQYWCLNEDGnidMEDFRIETLKTSVRAKYILTL------IEITDKIL-- 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  221 aGKTRSITHYQWTNWPDHGAP---PINMGAINLIEAV------NYDTN-----PVVVHCSAGVGRSGTIVGISLIMDKMI 286
Cdd:PHA02747 179 -KDSRKISHFQCSEWFEDETPsdhPDFIKFIKIIDINrkksgkLFNPKdallcPIVVHCSDGVGKTGIFCAVDICLNQLV 257

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 17507417  287 QgINCKDMKKLVEEIRNQRHYAIQTEAQYMYIHRV--LLEYFLELHK 331
Cdd:PHA02747 258 K-RKAICLAKTAEKIREQRHAGIMNFDDYLFIQPGyeVLHYFLSKIK 303
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
61-315 3.36e-36

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 132.91  E-value: 3.36e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  61 LNKGVSKLRDEFSEVANknPNVPVDAFKSNPeKNRYTDIKCIEKTRVilttdGASSDYIHANYVGIsIKPKKFICTQGPK 140
Cdd:COG5599  16 INSRLSTLTNELAPSHN--DPQYLQNINGSP-LNRFRDIQPYKETAL-----RANLGYLNANYIQV-IGNHRYIATQYPL 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 141 DSTIYDFWAMVIQDNVESIIML--CKVIELARVKCEQYWPAvEGQTNTYvskghTITINNLGVGTLSPDddfINVTNLEL 218
Cdd:COG5599  87 EEQLEDFFQMLFDNNTPVLVVLasDDEISKPKVKMPVYFRQ-DGEYGKY-----EVSSELTESIQLRDG---IEARTYVL 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 219 VWAG---KTRSITHYQWTNWPDHGAPPINM--GAINLIEAV----NYDTNPVVVHCSAGVGRSGTIVGIsLIMDKMIQ-- 287
Cdd:COG5599 158 TIKGtgqKKIEIPVLHVKNWPDHGAISAEAlkNLADLIDKKekikDPDKLLPVVHCRAGVGRTGTLIAC-LALSKSINal 236

                       250       260
                ....*....|....*....|....*....
gi 17507417 288 GINCKDMKKLVEEIRNQR-HYAIQTEAQY 315
Cdd:COG5599 237 VQITLSVEEIVIDMRTSRnGGMVQTSEQL 265
 
Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
67-324 6.81e-102

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 301.50  E-value: 6.81e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417     67 KLRDEFSE---VANKNPNVPVDAFKSNPEKNRYTDIKCIEKTRVILT-TDGASSDYIHANYVGISIKPKKFICTQGPKDS 142
Cdd:smart00194   1 GLEEEFEKldrLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKpPPGEGSDYINASYIDGPNGPKAYIATQGPLPS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417    143 TIYDFWAMVIQDNVESIIMLCKVIELARVKCEQYWPAVEGQTNTYvskgHTITINNLGVGTLspddDFINVTNLELVWAG 222
Cdd:smart00194  81 TVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTY----GDITVTLKSVEKV----DDYTIRTLEVTNTG 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417    223 --KTRSITHYQWTNWPDHGAPPINMGAINLIEAVN----YDTNPVVVHCSAGVGRSGTIVGISLIMDKMIQGINCkDMKK 296
Cdd:smart00194 153 csETRTVTHYHYTNWPDHGVPESPESILDLIRAVRksqsTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEV-DIFE 231

                          250       260
                   ....*....|....*....|....*...
gi 17507417    297 LVEEIRNQRHYAIQTEAQYMYIHRVLLE 324
Cdd:smart00194 232 IVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
90-324 4.84e-99

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 293.38  E-value: 4.84e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417    90 NPEKNRYTDIKCIEKTRVILTTDGASSDYIHANYVGISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIELA 169
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417   170 RVKCEQYWPAVEGQTNTYvskgHTITINNLGVgtlSPDDDFINVTNLELVWAG--KTRSITHYQWTNWPDHGAPPINMGA 247
Cdd:pfam00102  81 REKCAQYWPEEEGESLEY----GDFTVTLKKE---KEDEKDYTVRTLEVSNGGseETRTVKHFHYTGWPDHGVPESPNSL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417   248 INLIEAVN-----YDTNPVVVHCSAGVGRSGTIVGISLIMDKMIQGiNCKDMKKLVEEIRNQRHYAIQTEAQYMYIHRVL 322
Cdd:pfam00102 154 LDLLRKVRkssldGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAE-GEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAI 232


                  ..
gi 17507417   323 LE 324
Cdd:pfam00102 233 LE 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 118-320 6.47e-68

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: 212.53  E-value: 6.47e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 118 YIHANYVGISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIELARVKCEQYWPAVEGQTNTYvskgHTITIN 197
Cdd:cd00047   1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEY----GDITVT 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 198 NLGVgtlSPDDDFInVTNLELVWAG--KTRSITHYQWTNWPDHGAPPINMGAINLIEAVNY----DTNPVVVHCSAGVGR 271
Cdd:cd00047  77 LVSE---EELSDYT-IRTLELSPKGcsESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKearkPNGPIVVHCSAGVGR 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 17507417 272 SGTIVGISLIMDKMIQGiNCKDMKKLVEEIRNQRHYAIQTEAQYMYIHR 320
Cdd:cd00047 153 TGTFIAIDILLERLEAE-GEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 66-319 6.73e-58

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: 189.50  E-value: 6.73e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  66 SKLRDEFSEVANKNPNVPVDAFKS--NPEKNRYTDIKCIEKTRVILTTDGAS--SDYIHANYV-GISIKpKKFICTQGPK 140
Cdd:cd14543   3 RGIYEEYEDIRREPPAGTFLCSLApaNQEKNRYGDVLCLDQSRVKLPKRNGDerTDYINANFMdGYKQK-NAYIATQGPL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 141 DSTIYDFWAMVIQDNVESIIMLCKVIELARVKCEQYWPAVEGQTNTYVSkghtITINNLGVGTLspdDDFiNVTNLEL-- 218
Cdd:cd14543  82 PKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLRYGD----LTVTNLSVENK---EHY-KKTTLEIhn 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 219 VWAGKTRSITHYQWTNWPDHGAPPINMGAINLIEAV-NY---------DTN-------PVVVHCSAGVGRSGTIVGISLI 281
Cdd:cd14543 154 TETDESRQVTHFQFTSWPDFGVPSSAAALLDFLGEVrQQqalavkamgDRWkghppgpPIVVHCSAGIGRTGTFCTLDIC 233

                       250       260       270
                ....*....|....*....|....*....|....*...
gi 17507417 282 MDKMiQGINCKDMKKLVEEIRNQRHYAIQTEAQYMYIH 319
Cdd:cd14543 234 LSQL-EDVGTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 95-319 2.91e-57

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: 186.02  E-value: 2.91e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  95 RYTDIKCIEKTRVILT--TDGASSDYIHANYVGISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIELARVK 172
Cdd:cd14548   1 RYTNILPYDHSRVKLIpiNEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 173 CEQYWPAvegqTNTYVSKGHtITINNLGVGTLspdDDFInVTNLELVWAGKTRSITHYQWTNWPDHGAPPINMGAINLIE 252
Cdd:cd14548  81 CDHYWPF----DQDPVYYGD-ITVTMLSESVL---PDWT-IREFKLERGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVR 151

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17507417 253 AV----NYDTNPVVVHCSAGVGRSGTIVGIslimDKMIQGINCK---DMKKLVEEIRNQRHYAIQTEAQYMYIH 319
Cdd:cd14548 152 LVrdyiKQEKGPTIVHCSAGVGRTGTFIAL----DRLLQQIESEdyvDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 90-325 4.34e-55

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: 181.51  E-value: 4.34e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  90 NPEKNRYTDIKCIEKTRVILT---TDGASSDYIHANYV-------GISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESI 159
Cdd:cd14544   1 NKGKNRYKNILPFDHTRVILKdrdPNVPGSDYINANYIrnenegpTTDENAKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 160 IMLCKVIELARVKCEQYWPAvEGQTNTYvskgHTITINNLGVGTLSpddDFInVTNLELVWAGK---TRSITHYQWTNWP 236
Cdd:cd14544  81 VMTTKEVERGKNKCVRYWPD-EGMQKQY----GPYRVQNVSEHDTT---DYT-LRELQVSKLDQgdpIREIWHYQYLSWP 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 237 DHGAPPINMGAINLIEAVNY------DTNPVVVHCSAGVGRSGTIVGISLIMDKMI-QGINCK-DMKKLVEEIRNQRHYA 308
Cdd:cd14544 152 DHGVPSDPGGVLNFLEDVNQrqeslpHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKrKGLDCDiDIQKTIQMVRSQRSGM 231

                       250
                ....*....|....*..
gi 17507417 309 IQTEAQYMYIHRVLLEY 325
Cdd:cd14544 232 VQTEAQYKFIYVAVAQY 248
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 90-324 2.65e-52

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: 173.74  E-value: 2.65e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  90 NPEKNRYTDIKCIEKTRVILTT-DG-ASSDYIHANYVGISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIE 167
Cdd:cd14553   3 NKPKNRYANVIAYDHSRVILQPiEGvPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 168 LARVKCEQYWPAvEGqTNTY----VSKGHTITINNLGVGTLSpdddfinvtnLELVWAGKTRSITHYQWTNWPDHGAP-- 241
Cdd:cd14553  83 RSRVKCDQYWPT-RG-TETYgliqVTLLDTVELATYTVRTFA----------LHKNGSSEKREVRQFQFTAWPDHGVPeh 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 242 PINMGA-INLIEAVN-YDTNPVVVHCSAGVGRSGTIVGISLIMDKMIQGiNCKDMKKLVEEIRNQRHYAIQTEAQYMYIH 319
Cdd:cd14553 151 PTPFLAfLRRVKACNpPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHE-KTVDIYGHVTCLRAQRNYMVQTEDQYIFIH 229


                ....*
gi 17507417 320 RVLLE 324
Cdd:cd14553 230 DALLE 234
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 84-326 1.91e-51

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: 172.70  E-value: 1.91e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  84 VDAFKSNPEKNRYTDIKCIEKTRVILT--TDGASSDYIHANYVGISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIM 161
Cdd:cd14603  24 AGGRKENVKKNRYKDILPYDQTRVILSllQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILM 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 162 LCKVIELARVKCEQYWPAVEgQTNTYvskgHTITINNLGVGTLSPDddfINVTNLELVWAGKTRSITHYQWTNWPDHGAP 241
Cdd:cd14603 104 ACREIEMGKKKCERYWAQEQ-EPLQT----GPFTITLVKEKRLNEE---VILRTLKVTFQKESRSVSHFQYMAWPDHGIP 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 242 PINMGAINLIEAV-NY---DTNPVVVHCSAGVGRSGTIVGI----SLIMDKMIQgincKDMK--KLVEEIRNQRHYAIQT 311
Cdd:cd14603 176 DSPDCMLAMIELArRLqgsGPEPLCVHCSAGCGRTGVICTVdyvrQLLLTQRIP----PDFSifDVVLEMRKQRPAAVQT 251

                       250
                ....*....|....*
gi 17507417 312 EAQYMYIHRVLLEYF 326
Cdd:cd14603 252 EEQYEFLYHTVAQMF 266
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 94-320 1.83e-50

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: 168.73  E-value: 1.83e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  94 NRYTDIKCIEKTRVILT--TDGASSDYIHANYV-GISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIElAR 170
Cdd:cd14547   1 NRYKTILPNEHSRVCLPsvDDDPLSSYINANYIrGYDGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTE-AK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 171 VKCEQYWPavEGQTNTYvsKGHTITINnlgvgTLSPDDDFInVTNLELVWAGKTRSITHYQWTNWPDHGAPPINMGAINL 250
Cdd:cd14547  80 EKCAQYWP--EEENETY--GDFEVTVQ-----SVKETDGYT-VRKLTLKYGGEKRYLKHYWYTSWPDHKTPEAAQPLLSL 149

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17507417 251 IEAVNYD------TNPVVVHCSAGVGRSGTIVGISLIMDKMIQGINCkDMKKLVEEIRNQRHYAIQTEAQYMYIHR 320
Cdd:cd14547 150 VQEVEEArqtephRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVV-DVLGIVCQLRLDRGGMVQTAEQYEFVHR 224
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 118-319 3.37e-50

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: 167.14  E-value: 3.37e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 118 YIHANYVGISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIELARVKCEQYWPAvEGqTNTY----VSKGHT 193
Cdd:cd14549   1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPK-EG-TETYgniqVTLLST 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 194 ITINNLGVGTLSpdddfINVTNLELVWAGKT-RSITHYQWTNWPDHGAPPINMGAINLIE----AVNYDTNPVVVHCSAG 268
Cdd:cd14549  79 EVLATYTVRTFS-----LKNLKLKKVKGRSSeRVVYQYHYTQWPDHGVPDYTLPVLSFVRkssaANPPGAGPIVVHCSAG 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 17507417 269 VGRSGTIVgislIMDKMIQGINCK---DMKKLVEEIRNQRHYAIQTEAQYMYIH 319
Cdd:cd14549 154 VGRTGTYI----VIDSMLQQIQDKgtvNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 90-325 1.21e-49

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: 167.75  E-value: 1.21e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  90 NPEKNRYTDIKCIEKTRVILT---TDGASSDYIHANYV-----GISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIM 161
Cdd:cd14606  18 NKSKNRYKNILPFDHSRVILQgrdSNIPGSDYINANYVknqllGPDENAKTYIASQGCLEATVNDFWQMAWQENSRVIVM 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 162 LCKVIELARVKCEQYWPAVEGQT--NTYVSKG---HTITINNLGVGTLSPDDDfinvtnlelvwAGKTRSITHYQWTNWP 236
Cdd:cd14606  98 TTREVEKGRNKCVPYWPEVGMQRayGPYSVTNcgeHDTTEYKLRTLQVSPLDN-----------GELIREIWHYQYLSWP 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 237 DHGAPPINMGAINLIEAVNY------DTNPVVVHCSAGVGRSGTIVGISLIMDKM-IQGINCK-DMKKLVEEIRNQRHYA 308
Cdd:cd14606 167 DHGVPSEPGGVLSFLDQINQrqeslpHAGPIIVHCSAGIGRTGTIIVIDMLMENIsTKGLDCDiDIQKTIQMVRAQRSGM 246

                       250
                ....*....|....*..
gi 17507417 309 IQTEAQYMYIHRVLLEY 325
Cdd:cd14606 247 VQTEAQYKFIYVAIAQF 263
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 118-319 1.51e-49

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: 165.88  E-value: 1.51e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 118 YIHANYVGI-SIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIELARVKCEQYWPavegqTNTYVSKGHTITI 196
Cdd:cd18533   1 YINASYITLpGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWP-----SGEYEGEYGDLTV 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 197 NNLGVGTLspDDDFINVTNLEL-VWAGKTRSITHYQWTNWPDHGAPPINMGAINLIEAVNY------DTNPVVVHCSAGV 269
Cdd:cd18533  76 ELVSEEEN--DDGGFIVREFELsKEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRElndsasLDPPIIVHCSAGV 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17507417 270 GRSGTIVGISLIMDKMIQGIN----CKDMKKLVEEI----RNQRHYAIQTEAQYMYIH 319
Cdd:cd18533 154 GRTGTFIALDSLLDELKRGLSdsqdLEDSEDPVYEIvnqlRKQRMSMVQTLRQYIFLY 211
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 70-327 6.17e-49

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: 166.36  E-value: 6.17e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  70 DEFSEVANKNPNVPVDAFKSN-PE---KNRYTDIKCIEKTRVILT----TDGASSDYIHANYVGISIKPKKFICTQGPKD 141
Cdd:cd17667   3 EDFEEVQRCTADMNITAEHSNhPDnkhKNRYINILAYDHSRVKLRplpgKDSKHSDYINANYVDGYNKAKAYIATQGPLK 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 142 STIYDFWAMVIQDNVESIIMLCKVIELARVKCEQYWPA--VEGQTNTYVSKGHTITINNLGVGTLSpdddfINVTNLELV 219
Cdd:cd17667  83 STFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTenSEEYGNIIVTLKSTKIHACYTVRRFS-----IRNTKVKKG 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 220 WAGKT------RSITHYQWTNWPDHGAPPINMGAINLIE----AVNYDTNPVVVHCSAGVGRSGTIVgislIMDKMIQGI 289
Cdd:cd17667 158 QKGNPkgrqneRTVIQYHYTQWPDMGVPEYALPVLTFVRrssaARTPEMGPVLVHCSAGVGRTGTYI----VIDSMLQQI 233

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 17507417 290 NCK---DMKKLVEEIRNQRHYAIQTEAQYMYIHRVLLEYFL 327
Cdd:cd17667 234 KDKstvNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 90-325 1.54e-48

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: 164.42  E-value: 1.54e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  90 NPEKNRYTDIKCIEKTRVILTtDG----ASSDYIHANYV-------GISIKPKK-FICTQGPKDSTIYDFWAMVIQDNVE 157
Cdd:cd14605   2 NKNKNRYKNILPFDHTRVVLH-DGdpnePVSDYINANIImpefetkCNNSKPKKsYIATQGCLQNTVNDFWRMVFQENSR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 158 SIIMLCKVIELARVKCEQYWPavegqtNTYVSKGH-TITINNLgvgTLSPDDDFInVTNLELVWAGK---TRSITHYQWT 233
Cdd:cd14605  81 VIVMTTKEVERGKSKCVKYWP------DEYALKEYgVMRVRNV---KESAAHDYI-LRELKLSKVGQgntERTVWQYHFR 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 234 NWPDHGAPPINMGAINLIEAVNY------DTNPVVVHCSAGVGRSGTIVGISLIMDKMIQ-GINCK-DMKKLVEEIRNQR 305
Cdd:cd14605 151 TWPDHGVPSDPGGVLDFLEEVHHkqesimDAGPVVVHCSAGIGRTGTFIVIDILIDIIREkGVDCDiDVPKTIQMVRSQR 230

                       250       260
                ....*....|....*....|
gi 17507417 306 HYAIQTEAQYMYIHRVLLEY 325
Cdd:cd14605 231 SGMVQTEAQYRFIYMAVQHY 250
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 94-324 2.90e-48

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: 163.06  E-value: 2.90e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  94 NRYTDIKCIEKTRVILTTDGAS-SDYIHANYVGISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIELARVK 172
Cdd:cd14615   1 NRYNNVLPYDISRVKLSVQSHStDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRTK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 173 CEQYWPAveGQTNTYvskGHTITinNLGVGTLSPD---DDFiNVTNLElvwAGKTRSITHYQWTNWPDHGAPPINMGAIN 249
Cdd:cd14615  81 CEEYWPS--KQKKDY---GDITV--TMTSEIVLPEwtiRDF-TVKNAQ---TNESRTVRHFHFTSWPDHGVPETTDLLIN 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 250 LIEAV------NYDTNPVVVHCSAGVGRSGTIVGISLIMdKMIQGINCKDMKKLVEEIRNQRHYAIQTEAQYMYIHRVLL 323
Cdd:cd14615 150 FRHLVreymkqNPPNSPILVHCSAGVGRTGTFIAIDRLI-YQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCAL 228


                .
gi 17507417 324 E 324
Cdd:cd14615 229 D 229
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 88-326 2.56e-47

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: 162.79  E-value: 2.56e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  88 KSNPEKNRYTDIKCIEKTRVILT--TDGASSDYIHANYVGISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKV 165
Cdd:cd14604  55 EENVKKNRYKDILPFDHSRVKLTlkTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACRE 134

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 166 IELARVKCEQYWPAVEGQTNTYVSkgHTITINNLGVGTlspdDDFINVTNLElvWAGKTRSITHYQWTNWPDHGAPPINM 245
Cdd:cd14604 135 FEMGRKKCERYWPLYGEEPMTFGP--FRISCEAEQART----DYFIRTLLLE--FQNETRRLYQFHYVNWPDHDVPSSFD 206

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 246 GAINLIEAV----NYDTNPVVVHCSAGVGRSGTIVGISLIMDKMIQGINCKDMK--KLVEEIRNQRHYAIQTEAQYMYIH 319
Cdd:cd14604 207 SILDMISLMrkyqEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNvfNLIQEMRTQRHSAVQTKEQYELVH 286


                ....*..
gi 17507417 320 RVLLEYF 326
Cdd:cd14604 287 RAIAQLF 293
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 78-324 3.43e-47

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: 161.74  E-value: 3.43e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  78 KNPNVPVdafksNPEKNRYTDIKCIEKTRVILTT-DGA-SSDYIHANYVGISIKPKKFICTQGPKDSTIYDFWAMVIQDN 155
Cdd:cd14626  34 ENSNLEV-----NKPKNRYANVIAYDHSRVILTSvDGVpGSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQR 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 156 VESIIMLCKVIELARVKCEQYWPAveGQTNTY----VSKGHTITINNLGVGTLSpdddfinvtnLELVWAGKTRSITHYQ 231
Cdd:cd14626 109 TATIVMMTRLEEKSRVKCDQYWPI--RGTETYgmiqVTLLDTVELATYSVRTFA----------LYKNGSSEKREVRQFQ 176

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 232 WTNWPDHGAP----PInMGAINLIEAVN-YDTNPVVVHCSAGVGRSGTIVGISLIMDKMiQGINCKDMKKLVEEIRNQRH 306
Cdd:cd14626 177 FMAWPDHGVPeyptPI-LAFLRRVKACNpPDAGPMVVHCSAGVGRTGCFIVIDAMLERM-KHEKTVDIYGHVTCMRSQRN 254

                       250
                ....*....|....*...
gi 17507417 307 YAIQTEAQYMYIHRVLLE 324
Cdd:cd14626 255 YMVQTEDQYIFIHEALLE 272
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 118-324 6.33e-47

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: 158.69  E-value: 6.33e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 118 YIHANYVGISIKPKKF--ICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIELARVKCEQYWPAvegQTNTYVSKGHTIT 195
Cdd:cd14538   1 YINASHIRIPVGGDTYhyIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPD---SLNKPLICGGRLE 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 196 INNLGVGTLspdDDF----INVTNLElvwAGKTRSITHYQWTNWPDHGAPpinMGAINLIEAVNY-----DTNPVVVHCS 266
Cdd:cd14538  78 VSLEKYQSL---QDFvirrISLRDKE---TGEVHHITHLNFTTWPDHGTP---QSADPLLRFIRYmrrihNSGPIVVHCS 148

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17507417 267 AGVGRSGTIVGISLIMDKMIQGINCkDMKKLVEEIRNQRHYAIQTEAQYMYIHRVLLE 324
Cdd:cd14538 149 AGIGRTGVLITIDVALGLIERDLPF-DIQDIVKDLREQRQGMIQTKDQYIFCYKACLE 205
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 88-323 7.70e-47

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: 159.61  E-value: 7.70e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  88 KSNPEKNRYTDIKCIEKTRVILTTDGassDYIHANYVGISIKPKKF--ICTQGPKDSTIYDFWAMVIQDNVESIIMLCKV 165
Cdd:cd14597   1 KENRKKNRYKNILPYDTTRVPLGDEG---GYINASFIKMPVGDEEFvyIACQGPLPTTVADFWQMVWEQKSTVIAMMTQE 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 166 IELARVKCEQYWPAVEGQTnTYVSKGHTITInnlgVGTLSPDDDFINVTNLELVWAGKTRSITHYQWTNWPDHGAPPINM 245
Cdd:cd14597  78 VEGGKIKCQRYWPEILGKT-TMVDNRLQLTL----VRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPE 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 246 GAINLIEAVN--YDTNPVVVHCSAGVGRSGTIVGISLIMDKMIQGINCkDMKKLVEEIRNQRHYAIQTEAQYMYIHRVLL 323
Cdd:cd14597 153 QLLTFISYMRhiHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDF-DISDIVRTMRLQRHGMVQTEDQYIFCYQVIL 231
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 93-314 2.02e-46

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: 158.32  E-value: 2.02e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  93 KNRYTDIKCIEKTRVILTTDGASSDYIHANYVGISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIELARVK 172
Cdd:cd14545   1 LNRYRDRDPYDHDRSRVKLKQGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQIK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 173 CEQYWPAVEGQtntyvskGHTITINNLGVGTLSPDD--DFInVTNLEL--VWAGKTRSITHYQWTNWPDHGAPPINMGAI 248
Cdd:cd14545  81 CAQYWPQGEGN-------AMIFEDTGLKVTLLSEEDksYYT-VRTLELenLKTQETREVLHFHYTTWPDFGVPESPAAFL 152

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17507417 249 NLIEAV------NYDTNPVVVHCSAGVGRSGTIVGISLIMDKMIQG-INCKDMKKLVEEIRNQRHYAIQTEAQ 314
Cdd:cd14545 153 NFLQKVresgslSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGnPSSVDVKKVLLEMRKYRMGLIQTPDQ 225
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 89-320 1.41e-45

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: 156.59  E-value: 1.41e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  89 SNPEKNRYTDIKCIEKTRVILTT--DGASSDYIHANYVGISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVI 166
Cdd:cd14614  11 VNRCKNRYTNILPYDFSRVKLVSmhEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCN 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 167 ELARVKCEQYWPAVEgqtntyvskgHTITINNLGVGTLSPDD--DFInVTNLELVWAGKTRSITHYQWTNWPDHGAPPIN 244
Cdd:cd14614  91 EKRRVKCDHYWPFTE----------EPVAYGDITVEMLSEEEqpDWA-IREFRVSYADEVQDVMHFNYTAWPDHGVPTAN 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 245 MGA--INLIEAVNYDTN----PVVVHCSAGVGRSGTIVGISLIMdKMIQGINCKDMKKLVEEIRNQRHYAIQTEAQYMYI 318
Cdd:cd14614 160 AAEsiLQFVQMVRQQAVkskgPMIIHCSAGVGRTGTFIALDRLL-QHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFI 238


                ..
gi 17507417 319 HR 320
Cdd:cd14614 239 HQ 240
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 90-324 1.92e-44

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: 153.26  E-value: 1.92e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  90 NPEKNRYTDIKCIEKTRV-ILTTDG-ASSDYIHANYVGISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIE 167
Cdd:cd14630   3 NRNKNRYGNIISYDHSRVrLQLLDGdPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 168 LARVKCEQYWPavegqTNTYVSKGHTITInnlgVGTLSPDDDFINVTNLELVWAGKTRSITHYQWTNWPDHGAPPINMGA 247
Cdd:cd14630  83 VGRVKCVRYWP-----DDTEVYGDIKVTL----IETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGL 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 248 INLIEAVNY----DTNPVVVHCSAGVGRSGTIVGISLIMDkMIQGINCKDMKKLVEEIRNQRHYAIQTEAQYMYIHRVLL 323
Cdd:cd14630 154 LGFVRQVKFlnppDAGPIVVHCSAGAGRTGCFIAIDIMLD-MAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAIL 232


                .
gi 17507417 324 E 324
Cdd:cd14630 233 E 233
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 94-323 1.32e-43

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: 150.86  E-value: 1.32e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  94 NRYTDIKCIEKTRVILTTDGAS--SDYIHANYVGISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIELARV 171
Cdd:cd14618   1 NRYPHVLPYDHSRVRLSQLGGEphSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 172 KCEQYWPAvegqTNTYVSKGHtITINNLgvgTLSPDDDFinvTNLEL-VWAG---KTRSITHYQWTNWPDHGAPPINMGA 247
Cdd:cd14618  81 LCDHYWPS----ESTPVSYGH-ITVHLL---AQSSEDEW---TRREFkLWHEdlrKERRVKHLHYTAWPDHGIPESTSSL 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 248 INLIEAVN------YDTNPVVVHCSAGVGRSGTIVGISLIMDKMIQGiNCKDMKKLVEEIRNQRHYAIQTEAQYMYIHRV 321
Cdd:cd14618 150 MAFRELVRehvqatKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEE-KVVDVFNTVYILRMHRYLMIQTLSQYIFLHSC 228


                ..
gi 17507417 322 LL 323
Cdd:cd14618 229 IL 230
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 94-325 8.04e-43

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: 148.88  E-value: 8.04e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  94 NRYTDIKCIEKTRVILTTDGA--SSDYIHANYVGISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIELARV 171
Cdd:cd14619   1 NRFRNVLPYDWSRVPLKPIHEepGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 172 KCEQYWPaVEGQTNTYvskGH-TITInnlgVGTLSPDDDFINVTNLELVWAGKTRSITHYQWTNWPDHGAPPinmGAINL 250
Cdd:cd14619  81 KCEHYWP-LDYTPCTY---GHlRVTV----VSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPS---STDTL 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 251 IEAVN---------YDTNPVVVHCSAGVGRSGTIVGISLIMDKMiQGINCKDMKKLVEEIRNQRHYAIQTEAQYMYIHRV 321
Cdd:cd14619 150 LAFRRllrqwldqtMSGGPTVVHCSAGVGRTGTLIALDVLLQQL-QSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQC 228


                ....
gi 17507417 322 LLEY 325
Cdd:cd14619 229 ILDF 232
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 118-320 1.57e-42

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: 147.18  E-value: 1.57e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 118 YIHANYVGISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIELARVKCEQYWPAVEGQTNTYVSkghtITIN 197
Cdd:cd14542   1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLQFGP----FKIS 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 198 NLGVGTLSPDddfINVTNLELVWAGKTRSITHYQWTNWPDHGAPPINMGAINLIEAV----NYDTNPVVVHCSAGVGRSG 273
Cdd:cd14542  77 LEKEKRVGPD---FLIRTLKVTFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVrdyqGSEDVPICVHCSAGCGRTG 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 17507417 274 TIVGISLIMDKMIQGINCKDMK--KLVEEIRNQRHYAIQTEAQYMYIHR 320
Cdd:cd14542 154 TICAIDYVWNLLKTGKIPEEFSlfDLVREMRKQRPAMVQTKEQYELVYR 202
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 118-323 1.88e-42

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: 147.43  E-value: 1.88e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 118 YIHANYVGISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIELARVKCEQYWPAvEGQT---NTYVSKGHTI 194
Cdd:cd17668   1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPA-DGSEeygNFLVTQKSVQ 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 195 TINNLGVGTLSpdddfinVTNLELVWAGKT-----RSITHYQWTNWPDHGAPPINMGAINLIEAVNY----DTNPVVVHC 265
Cdd:cd17668  80 VLAYYTVRNFT-------LRNTKIKKGSQKgrpsgRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYakrhAVGPVVVHC 152

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17507417 266 SAGVGRSGTIVgislIMDKMIQGI---NCKDMKKLVEEIRNQRHYAIQTEAQYMYIHRVLL 323
Cdd:cd17668 153 SAGVGRTGTYI----VLDSMLQQIqheGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 81-324 1.91e-42

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: 149.42  E-value: 1.91e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  81 NVPVDAFK--SNPEKNRYTDIKCIEKTRVILTT--DGASSDYIHANYVGISIKPKKFICTQGPKDSTIYDFWAMVIQDNV 156
Cdd:cd14633  29 SAPWDSAKkdENRMKNRYGNIIAYDHSRVRLQPieGETSSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENT 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 157 ESIIMLCKVIELARVKCEQYWPavegqTNTYVSKGHTITInnlgVGTLSPDDDFINVTNLELVWAGKTRSITHYQWTNWP 236
Cdd:cd14633 109 ASIIMVTNLVEVGRVKCCKYWP-----DDTEIYKDIKVTL----IETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWP 179

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 237 DHGAPPINMGAINLIEAVNYDT----NPVVVHCSAGVGRSGTIVGISLIMDkMIQGINCKDMKKLVEEIRNQRHYAIQTE 312
Cdd:cd14633 180 DHGVPYHATGLLGFVRQVKSKSppnaGPLVVHCSAGAGRTGCFIVIDIMLD-MAEREGVVDIYNCVRELRSRRVNMVQTE 258

                       250
                ....*....|..
gi 17507417 313 AQYMYIHRVLLE 324
Cdd:cd14633 259 EQYVFIHDAILE 270
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 118-324 2.74e-42

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: 146.60  E-value: 2.74e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 118 YIHANYVGISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIELARVKCEQYWPavegqTNTYVSKGHTITIn 197
Cdd:cd14555   1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWP-----DDTEVYGDIKVTL- 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 198 nlgVGTLSPDDDFINVTNLELVWAGKTRSITHYQWTNWPDHGAPPINMGAINLIEAVNY----DTNPVVVHCSAGVGRSG 273
Cdd:cd14555  75 ---VETEPLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKAsnppSAGPIVVHCSAGAGRTG 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 17507417 274 TIVGISLIMDkMIQGINCKDMKKLVEEIRNQRHYAIQTEAQYMYIHRVLLE 324
Cdd:cd14555 152 CYIVIDIMLD-MAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 118-324 2.85e-42

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


Pssm-ID: 350480 [Multi-domain]  Cd Length: 205  Bit Score: 146.73  E-value: 2.85e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 118 YIHANYVGISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIELARVKCEQYWPAvegQTNTYvskgHTITIN 197
Cdd:cd14632   1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPD---DSDTY----GDIKIT 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 198 NLGVGTLSpdDDFINVTNLELVWAGKTRSITHYQWTNWPDHGAPPINMGAINLIEAVNY----DTNPVVVHCSAGVGRSG 273
Cdd:cd14632  74 LLKTETLA--EYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKAstppDAGPVVVHCSAGAGRTG 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 17507417 274 TIVgislIMDKMIQGINCK---DMKKLVEEIRNQRHYAIQTEAQYMYIHRVLLE 324
Cdd:cd14632 152 CYI----VLDVMLDMAECEgvvDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 118-320 3.23e-42

catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 1.


Pssm-ID: 350405 [Multi-domain]  Cd Length: 201  Bit Score: 146.51  E-value: 3.23e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 118 YIHANYVGISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIELARVKCEQYWPAVEGQTNTYvsKGHTITIN 197
Cdd:cd14557   1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAF--GDVVVKIN 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 198 NlgvgtLSPDDDFI----NVTNLElvWAGKTRSITHYQWTNWPDHGAPPINMGAINLIEAVNYDTN----PVVVHCSAGV 269
Cdd:cd14557  79 E-----EKICPDYIirklNINNKK--EKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNffsgPIVVHCSAGV 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 17507417 270 GRSGTIVGIslimDKMIQGINCK---DMKKLVEEIRNQRHYAIQTEAQYMYIHR 320
Cdd:cd14557 152 GRTGTYIGI----DAMLEGLEAEgrvDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 90-324 4.30e-42

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: 148.70  E-value: 4.30e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  90 NPEKNRYTDIKCIEKTRVILT-TDG-ASSDYIHANYVGISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIE 167
Cdd:cd14625  47 NKPKNRYANVIAYDHSRVILQpIEGiMGSDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEE 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 168 LARVKCEQYWPAveGQTNTY----VSKGHTITINNLGVGTLSpdddfinvtnLELVWAGKTRSITHYQWTNWPDHGAPPI 243
Cdd:cd14625 127 KSRIKCDQYWPS--RGTETYgmiqVTLLDTIELATFCVRTFS----------LHKNGSSEKREVRQFQFTAWPDHGVPEY 194

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 244 NMGAINLIEAVNY----DTNPVVVHCSAGVGRSGTIVGISLIMDKmIQGINCKDMKKLVEEIRNQRHYAIQTEAQYMYIH 319
Cdd:cd14625 195 PTPFLAFLRRVKTcnppDAGPIVVHCSAGVGRTGCFIVIDAMLER-IKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIH 273


                ....*
gi 17507417 320 RVLLE 324
Cdd:cd14625 274 DALLE 278
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 118-324 7.43e-42

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: 145.66  E-value: 7.43e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 118 YIHANYVGISIKPKK--FICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIELARVKCEQYWPavEGQTNTYVSKGHTIT 195
Cdd:cd14596   1 YINASYITMPVGEEElfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWP--ETLQEPMELENYQLR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 196 INNLGVgtlspdDDFINVTNLELV--WAGKTRSITHYQWTNWPDHGAPPINMGAINLIEAVN--YDTNPVVVHCSAGVGR 271
Cdd:cd14596  79 LENYQA------LQYFIIRIIKLVekETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRkvHNTGPIVVHCSAGIGR 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 17507417 272 SGTIVGISLIMDKMIQGInCKDMKKLVEEIRNQRHYAIQTEAQYMYIHRVLLE 324
Cdd:cd14596 153 AGVLICVDVLLSLIEKDL-SFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLE 204
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 94-320 9.67e-42

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: 145.83  E-value: 9.67e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  94 NRYTDIKCIEKTRVILTT--DGASSDYIHANYV-GISIKpKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIELAR 170
Cdd:cd14617   1 NRYNNILPYDSTRVKLSNvdDDPCSDYINASYIpGNNFR-REYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 171 VKCEQYWPAvegqtntyvsKGHTITINNLGVGTLSpDDDFINVTNLELVWAGKT-----RSITHYQWTNWPDHGAPPINM 245
Cdd:cd14617  80 VKCDHYWPA----------DQDSLYYGDLIVQMLS-ESVLPEWTIREFKICSEEqldapRLVRHFHYTVWPDHGVPETTQ 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 246 GAINLIEAV-NY-----DTNPVVVHCSAGVGRSGTIVgislIMDKMIQGINCKDMKKL---VEEIRNQRHYAIQTEAQYM 316
Cdd:cd14617 149 SLIQFVRTVrDYinrtpGSGPTVVHCSAGVGRTGTFI----ALDRILQQLDSKDSVDIygaVHDLRLHRVHMVQTECQYV 224


                ....
gi 17507417 317 YIHR 320
Cdd:cd14617 225 YLHQ 228
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 68-331 1.12e-41

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 148.23  E-value: 1.12e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417   68 LRDEFSEVANKNPNVPVDAFK--SNPEKNRYTDIKCIEKTRVILTT-DGASSDYIHANYVGISIKPKKFICTQGPKDSTI 144
Cdd:PHA02747  27 IRDEHHQIILKPFDGLIANFEkpENQPKNRYWDIPCWDHNRVILDSgGGSTSDYIHANWIDGFEDDKKFIATQGPFAETC 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  145 YDFWAMVIQDNVESIIMLCKVIEL-ARVKCEQYWPAVEGQ---TNTYVSKGHTITINNLGVGTLspdddfINVTNLELvw 220
Cdd:PHA02747 107 ADFWKAVWQEHCSIIVMLTPTKGTnGEEKCYQYWCLNEDGnidMEDFRIETLKTSVRAKYILTL------IEITDKIL-- 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  221 aGKTRSITHYQWTNWPDHGAP---PINMGAINLIEAV------NYDTN-----PVVVHCSAGVGRSGTIVGISLIMDKMI 286
Cdd:PHA02747 179 -KDSRKISHFQCSEWFEDETPsdhPDFIKFIKIIDINrkksgkLFNPKdallcPIVVHCSDGVGKTGIFCAVDICLNQLV 257

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 17507417  287 QgINCKDMKKLVEEIRNQRHYAIQTEAQYMYIHRV--LLEYFLELHK 331
Cdd:PHA02747 258 K-RKAICLAKTAEKIREQRHAGIMNFDDYLFIQPGyeVLHYFLSKIK 303
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 94-320 1.97e-41

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: 145.05  E-value: 1.97e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  94 NRYTDIKCIEKTRVILTTDGAS--SDYIHANYVGISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIELARV 171
Cdd:cd14616   1 NRFPNIKPYNNNRVKLIADAGVpgSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 172 KCEQYWPavegQTNTYVSKGHTITINNLgvgTLSPDDDFiNVTNLELVWAGKTRSITHYQWTNWPDHGAPPINMGAINLI 251
Cdd:cd14616  81 RCHQYWP----EDNKPVTVFGDIVITKL---MEDVQIDW-TIRDLKIERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFV 152

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17507417 252 EAVN----YDTNPVVVHCSAGVGRSGTIVGisliMDKMIQGINCK---DMKKLVEEIRNQRHYAIQTEAQYMYIHR 320
Cdd:cd14616 153 KLVRasraHDNTPMIVHCSAGVGRTGVFIA----LDHLTQHINDHdfvDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 72-318 6.16e-41

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: 144.72  E-value: 6.16e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  72 FSEVANKNPNVP--VDAFKSNPEKNRYTDIKCIEKTRVILttDGASSDYIHANYVGISIKPKKFICTQGPKDSTIYDFWA 149
Cdd:cd14607   4 YLEIRNESHDYPhrVAKYPENRNRNRYRDVSPYDHSRVKL--QNTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFWL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 150 MVIQDNVESIIMLCKVIELARVKCEQYWPAVEGQTNTYVSKGHTITINNLGVGTLSPdddfINVTNLELVWAGKTRSITH 229
Cdd:cd14607  82 MVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSFKETGFSVKLLSEDVKSYYT----VHLLQLENINSGETRTISH 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 230 YQWTNWPDHGAPPINMGAINLIEAV------NYDTNPVVVHCSAGVGRSGT--IVGISLIMDKMIQGINCkDMKKLVEEI 301
Cdd:cd14607 158 FHYTTWPDFGVPESPASFLNFLFKVresgslSPEHGPAVVHCSAGIGRSGTfsLVDTCLVLMEKKDPDSV-DIKQVLLDM 236

                       250       260
                ....*....|....*....|.
gi 17507417 302 RNQRHYAIQTEAQ----YMYI 318
Cdd:cd14607 237 RKYRMGLIQTPDQlrfsYMAV 257
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 93-325 7.88e-41

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: 144.21  E-value: 7.88e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  93 KNRYTDIKCIEKTRVILTTDGAS---SDYIHANYV-GISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIEl 168
Cdd:cd14612  18 KDRYKTILPNPQSRVCLRRAGSQeeeGSYINANYIrGYDGKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKE- 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 169 ARVKCEQYWPAVEGQTNTYvskghTITINNLgvgtlsPDDDFINVTNLELVWAGKTRSITHYQWTNWPDHGAPPINMGAI 248
Cdd:cd14612  97 KKEKCVHYWPEKEGTYGRF-----EIRVQDM------KECDGYTIRDLTIQLEEESRSVKHYWFSSWPDHQTPESAGPLL 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 249 NLIEAVNY------DTNPVVVHCSAGVGRSGTIVGISlimdkmiqgINCKDMKK--------LVEEIRNQRHYAIQTEAQ 314
Cdd:cd14612 166 RLVAEVEEsrqtaaSPGPIVVHCSAGIGRTGCFIATS---------IGCQQLKDtgkvdilgIVCQLRLDRGGMIQTSEQ 236

                       250
                ....*....|.
gi 17507417 315 YMYIHRVLLEY 325
Cdd:cd14612 237 YQFLHHTLALY 247
PHA02738 PHA02738
hypothetical protein; Provisional
 85-329 1.21e-40

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 145.84  E-value: 1.21e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417   85 DAFKSNPEKNRYTDIKCIEKTRVILTTDGASSDYIHANYVGISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCK 164
Cdd:PHA02738  44 NAEKKNRKLNRYLDAVCFDHSRVILPAERNRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCK 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  165 VIELARVKCEQYWPAVEgQTNTYVSKGHTITINnlgVGTLSpddDFINVTNLELVWAGKTRSITHYQWTNWPDHGAPPIN 244
Cdd:PHA02738 124 KKENGREKCFPYWSDVE-QGSIRFGKFKITTTQ---VETHP---HYVKSTLLLTDGTSATQTVTHFNFTAWPDHDVPKNT 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  245 MGAINLIEAV-----------------NYDTNPVVVHCSAGVGRSGT--IVGISLIMDKMIQGINckdMKKLVEEIRNQR 305
Cdd:PHA02738 197 SEFLNFVLEVrqcqkelaqeslqighnRLQPPPIVVHCNAGLGRTPCycVVDISISRFDACATVS---IPSIVSSIRNQR 273

                        250       260
                 ....*....|....*....|....
gi 17507417  306 HYAIQTEAQYMYIHRVlLEYFLEL 329
Cdd:PHA02738 274 YYSLFIPFQYFFCYRA-VKRYVNL 296
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 72-327 2.72e-40

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: 144.40  E-value: 2.72e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  72 FSEVANKNPNVPVDAF------KSNPEKNRYTDIKCIEKTRVILTT-DGA-SSDYIHANYVGISIKPKKFICTQGPKDST 143
Cdd:cd14621  28 FREEFNALPACPIQATceaaskEENKEKNRYVNILPYDHSRVHLTPvEGVpDSDYINASFINGYQEKNKFIAAQGPKEET 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 144 IYDFWAMVIQDNVESIIMLCKVIELARVKCEQYWPAVEGQT--NTYVSKGHTITINNLGVGTLSPdDDFINVTNLElvwa 221
Cdd:cd14621 108 VNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCWTygNIRVSVEDVTVLVDYTVRKFCI-QQVGDVTNKK---- 182

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 222 gKTRSITHYQWTNWPDHGAPPINMGAINLIEAVNyDTNP-----VVVHCSAGVGRSGTIVGISLIMDkMIQGINCKDMKK 296
Cdd:cd14621 183 -PQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVK-NCNPqyagaIVVHCSAGVGRTGTFIVIDAMLD-MMHAERKVDVYG 259

                       250       260       270
                ....*....|....*....|....*....|.
gi 17507417 297 LVEEIRNQRHYAIQTEAQYMYIHRVLLEYFL 327
Cdd:cd14621 260 FVSRIRAQRCQMVQTDMQYVFIYQALLEHYL 290
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 81-323 1.21e-39

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: 140.74  E-value: 1.21e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  81 NVPVDAFKsnpekNRYTDIKCIEKTRVILT----TDGasSDYIHANYVGISIKPKKFICTQGPKDSTIYDFWAMVIQDNV 156
Cdd:cd14554   2 NLPCNKFK-----NRLVNILPYESTRVCLQpirgVEG--SDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNS 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 157 ESIIMLCKVIELARVKCEQYWPAVEGQTNTYVSKgHTITINNLGVGTLSpddDFiNVTNLElvwAGKTRSITHYQWTNWP 236
Cdd:cd14554  75 TIIVMLTKLREMGREKCHQYWPAERSARYQYFVV-DPMAEYNMPQYILR---EF-KVTDAR---DGQSRTVRQFQFTDWP 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 237 DHGAPPINMGAINLIEAVNY------DTNPVVVHCSAGVGRSGTIVGISLIMDKMiQGINCKDMKKLVEEIRNQRHYAIQ 310
Cdd:cd14554 147 EQGVPKSGEGFIDFIGQVHKtkeqfgQEGPITVHCSAGVGRTGVFITLSIVLERM-RYEGVVDVFQTVKLLRTQRPAMVQ 225

                       250
                ....*....|...
gi 17507417 311 TEAQYMYIHRVLL 323
Cdd:cd14554 226 TEDQYQFCYRAAL 238
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 65-326 1.30e-39

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: 142.18  E-value: 1.30e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  65 VSKLRDEFSEVANK--------NPNVPVDAFKsnpekNRYTDIKCIEKTRVILT----TDGasSDYIHANYVGISIKPKK 132
Cdd:cd14627  25 VTGMELEFKRLANSkahtsrfiSANLPCNKFK-----NRLVNIMPYETTRVCLQpirgVEG--SDYINASFIDGYRQQKA 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 133 FICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIELARVKCEQYWPAVEGQTNTYVskghtitinnlgvgTLSPDDDF-- 210
Cdd:cd14627  98 YIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPAERSARYQYF--------------VVDPMAEYnm 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 211 -------INVTNLElvwAGKTRSITHYQWTNWPDHGAPPINMGAINLIEAVNY------DTNPVVVHCSAGVGRSGTIVG 277
Cdd:cd14627 164 pqyilreFKVTDAR---DGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKtkeqfgQDGPISVHCSAGVGRTGVFIT 240

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 17507417 278 ISLIMDKM-IQGIncKDMKKLVEEIRNQRHYAIQTEAQYMYIHRVLLEYF 326
Cdd:cd14627 241 LSIVLERMrYEGV--VDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYL 288
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 63-326 1.50e-39

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: 142.18  E-value: 1.50e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  63 KGVSKLRDEFSEVANK--------NPNVPVDAFKsnpekNRYTDIKCIEKTRVILT----TDGasSDYIHANYVGISIKP 130
Cdd:cd14628  22 ENVTGMELEFKRLASSkahtsrfiSANLPCNKFK-----NRLVNIMPYESTRVCLQpirgVEG--SDYINASFIDGYRQQ 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 131 KKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIELARVKCEQYWPAVEGQTNTYVskghtitinnlgvgTLSPDDDF 210
Cdd:cd14628  95 KAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYF--------------VVDPMAEY 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 211 ---------INVTNLElvwAGKTRSITHYQWTNWPDHGAPPINMGAINLIEAVNY------DTNPVVVHCSAGVGRSGTI 275
Cdd:cd14628 161 nmpqyilreFKVTDAR---DGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKtkeqfgQDGPISVHCSAGVGRTGVF 237

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 17507417 276 VGISLIMDKM-IQGIncKDMKKLVEEIRNQRHYAIQTEAQYMYIHRVLLEYF 326
Cdd:cd14628 238 ITLSIVLERMrYEGV--VDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYL 287
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 81-326 1.51e-39

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: 142.17  E-value: 1.51e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  81 NVPVDAFKsnpekNRYTDIKCIEKTRVILT----TDGasSDYIHANYVGISIKPKKFICTQGPKDSTIYDFWAMVIQDNV 156
Cdd:cd14629  49 NLPCNKFK-----NRLVNIMPYELTRVCLQpirgVEG--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNS 121

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 157 ESIIMLCKVIELARVKCEQYWPAVEGQTNTYVSKgHTITINNLGVGTLSPdddfINVTNLElvwAGKTRSITHYQWTNWP 236
Cdd:cd14629 122 TIVVMLTKLREMGREKCHQYWPAERSARYQYFVV-DPMAEYNMPQYILRE----FKVTDAR---DGQSRTIRQFQFTDWP 193

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 237 DHGAPPINMGAINLIEAVNY------DTNPVVVHCSAGVGRSGTIVGISLIMDKM-IQGIncKDMKKLVEEIRNQRHYAI 309
Cdd:cd14629 194 EQGVPKTGEGFIDFIGQVHKtkeqfgQDGPITVHCSAGVGRTGVFITLSIVLERMrYEGV--VDMFQTVKTLRTQRPAMV 271

                       250
                ....*....|....*..
gi 17507417 310 QTEAQYMYIHRVLLEYF 326
Cdd:cd14629 272 QTEDQYQLCYRAALEYL 288
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 117-318 2.60e-39

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: 139.00  E-value: 2.60e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 117 DYIHANYVGISIkPK-----KFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIELARVKCEQYWPAVEGqtntyvskg 191
Cdd:cd14541   1 DYINANYVNMEI-PGsgivnRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGE--------- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 192 hTITINNLGVGTLSPDD-------DFInVTNLElvwAGKTRSITHYQWTNWPDHGAPPINMGAINLIEAV---NYDTN-P 260
Cdd:cd14541  71 -TMQFGNLQITCVSEEVtpsfafrEFI-LTNTN---TGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVrqnRVGMVeP 145

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17507417 261 VVVHCSAGVGRSGTIVGISLIMDkMIQGINCKDMKKLVEEIRNQRHYAIQTEAQYMYI 318
Cdd:cd14541 146 TVVHCSAGIGRTGVLITMETAMC-LIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFV 202
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 106-324 2.91e-39

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


Pssm-ID: 350479 [Multi-domain]  Cd Length: 218  Bit Score: 139.39  E-value: 2.91e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 106 RVIL--TTDGASSDYIHANYVGISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIELARVKCEQYWPavegq 183
Cdd:cd14631   1 RVILqpVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP----- 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 184 TNTYVSKGHTITInnlgVGTLSPDDDFINVTNLELVWAGKTRSITHYQWTNWPDHGAPPINMGAINLIEAVNYD----TN 259
Cdd:cd14631  76 DDTEVYGDFKVTC----VEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSnppsAG 151

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17507417 260 PVVVHCSAGVGRSGTIVGISLIMDkMIQGINCKDMKKLVEEIRNQRHYAIQTEAQYMYIHRVLLE 324
Cdd:cd14631 152 PIVVHCSAGAGRTGCYIVIDIMLD-MAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 90-324 4.07e-39

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: 141.02  E-value: 4.07e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  90 NPEKNRYTDIKCIEKTRVILTT-DG-ASSDYIHANYVGISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIE 167
Cdd:cd14624  47 NKPKNRYANVIAYDHSRVLLSAiEGiPGSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEE 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 168 LARVKCEQYWPAVEGQTNTYVskgHTITINNLGVGTLSpdddfINVTNLELVWAGKTRSITHYQWTNWPDHGAPPINMGA 247
Cdd:cd14624 127 RSRVKCDQYWPSRGTETYGLI---QVTLLDTVELATYC-----VRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPF 198

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 248 INLIEAVNY----DTNPVVVHCSAGVGRSGTIVGISLIMDKmIQGINCKDMKKLVEEIRNQRHYAIQTEAQYMYIHRVLL 323
Cdd:cd14624 199 LAFLRRVKTcnppDAGPMVVHCSAGVGRTGCFIVIDAMLER-IKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALL 277


                .
gi 17507417 324 E 324
Cdd:cd14624 278 E 278
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 72-324 6.62e-39

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: 140.16  E-value: 6.62e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  72 FSEVANKNPNVP--VDAFKSNPEKNRYTDIKCIEKTRVILTTDgaSSDYIHANYVGISIKPKKFICTQGPKDSTIYDFWA 149
Cdd:cd14608   5 YQDIRHEASDFPcrVAKLPKNKNRNRYRDVSPFDHSRIKLHQE--DNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 150 MVIQDNVESIIMLCKVIELARVKCEQYWPAVEGQTNTYVSkghtitiNNLGVGTLSPD-DDFINVTNLEL--VWAGKTRS 226
Cdd:cd14608  83 MVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFED-------TNLKLTLISEDiKSYYTVRQLELenLTTQETRE 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 227 ITHYQWTNWPDHGAPPINMGAINLIEAV------NYDTNPVVVHCSAGVGRSGTIVGIS---LIMDKMiQGINCKDMKKL 297
Cdd:cd14608 156 ILHFHYTTWPDFGVPESPASFLNFLFKVresgslSPEHGPVVVHCSAGIGRSGTFCLADtclLLMDKR-KDPSSVDIKKV 234

                       250       260
                ....*....|....*....|....*..
gi 17507417 298 VEEIRNQRHYAIQTEAQYMYIHRVLLE 324
Cdd:cd14608 235 LLEMRKFRMGLIQTADQLRFSYLAVIE 261
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 71-328 2.39e-38

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: 138.44  E-value: 2.39e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  71 EFSEVANKNPNVPVDAFK--SNPEKNRYTDIKCIEKTRVILTtdgASSDYIHANYVGISIKP----KKFICTQGPKDSTI 144
Cdd:cd14600  19 QFEQLYRKKPGLAITCAKlpQNMDKNRYKDVLPYDATRVVLQ---GNEDYINASYVNMEIPSanivNKYIATQGPLPHTC 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 145 YDFWAMVIQDNVESIIMLCKVIELARVKCEQYWPAVEgQTNTYVSKGHTITINNLGVGTLSPDddfINVTNLElvwAGKT 224
Cdd:cd14600  96 AQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPP-DVMEYGGFRVQCHSEDCTIAYVFRE---MLLTNTQ---TGEE 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 225 RSITHYQWTNWPDHGAPPINMgaiNLIEAVNY------DTNPVVVHCSAGVGRSGTIVGISLIMDKMIQGINCKDMkKLV 298
Cdd:cd14600 169 RTVTHLQYVAWPDHGVPDDSS---DFLEFVNYvrskrvENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPL-DIV 244

                       250       260       270
                ....*....|....*....|....*....|
gi 17507417 299 EEIRNQRHYAIQTEAQYMYIHRVLLEYFLE 328
Cdd:cd14600 245 RKMRDQRAMMVQTSSQYKFVCEAILRVYEE 274
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 93-326 3.47e-38

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: 136.89  E-value: 3.47e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  93 KNRYTDIKCIEKTRVILT--TDGASSDYIHANYVGISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIELAR 170
Cdd:cd14602   1 KNRYKDILPYDHSRVELSliTSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 171 VKCEQYWpaVEGQTNTYVSKGHTITINNlgvgtLSPDDDFInVTNLELVWAGKTRSITHYQWTNWPDHGAPPINMGAINL 250
Cdd:cd14602  81 KKCERYW--AEPGEMQLEFGPFSVTCEA-----EKRKSDYI-IRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILEL 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 251 IEAVN----YDTNPVVVHCSAGVGRSGTIVGISLIMDKMIQGI--NCKDMKKLVEEIRNQRHYAIQTEAQYMYIHRVLLE 324
Cdd:cd14602 153 IWDVRcyqeDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIipENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIE 232


                ..
gi 17507417 325 YF 326
Cdd:cd14602 233 LF 234
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 71-326 9.27e-38

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: 137.44  E-value: 9.27e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  71 EFSEVANKNPN--VPVDAFKSNPEKNRYTDIKCIEKTRV-ILTTDGASSDYIHANYVGISIKPKK--FICTQGPKDSTIY 145
Cdd:cd14599  17 EYEQIPKKKADgvFTTATLPENAERNRIREVVPYEENRVeLVPTKENNTGYINASHIKVTVGGEEwhYIATQGPLPHTCH 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 146 DFWAMVIQDNVESIIMLCKVIELARVKCEQYWPAVEgqtntyvSKGHTITINNLGVGT-LSPDDDFINVTNLEL--VWAG 222
Cdd:cd14599  97 DFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLG-------SKHSSATYGKFKVTTkFRTDSGCYATTGLKVkhLLSG 169

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 223 KTRSITHYQWTNWPDHGAPPINMGAINLIE---AVNYDTN-----------PVVVHCSAGVGRSGTIVgISLIMDKMIQG 288
Cdd:cd14599 170 QERTVWHLQYTDWPDHGCPEEVQGFLSYLEeiqSVRRHTNsmldstkncnpPIVVHCSAGVGRTGVVI-LTELMIGCLEH 248

                       250       260       270
                ....*....|....*....|....*....|....*...
gi 17507417 289 INCKDMKKLVEEIRNQRHYAIQTEAQYMYIHRVLLEYF 326
Cdd:cd14599 249 NEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFL 286
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 118-325 1.62e-37

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: 134.51  E-value: 1.62e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 118 YIHANYVGISI--KPKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIELARVKCEQYWPAVEGQTNTYVSKGHTIT 195
Cdd:cd14540   1 YINASHITATVggKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEHDALTFGEYKVS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 196 INnlgvgtLSPDDDFINVTNLEL--VWAGKTRSITHYQWTNWPDHGAPPINMGAINLIEAVN---------YDTN----P 260
Cdd:cd14540  81 TK------FSVSSGCYTTTGLRVkhTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINsvrrhtnqdVAGHnrnpP 154

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17507417 261 VVVHCSAGVGRSGTIVGISLIMDKMIQGINCkDMKKLVEEIRNQRHYAIQTEAQYMYIHRVLLEY 325
Cdd:cd14540 155 TLVHCSAGVGRTGVVILADLMLYCLDHNEEL-DIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQY 218
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 226-324 1.88e-37

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


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 130.56  E-value: 1.88e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417    226 SITHYQWTNWPDHGAPPINMGAINLIEAVN------YDTNPVVVHCSAGVGRSGTIVGISLIMDKMIQGINCKDMKKLVE 299
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKknlnqsESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|....*
gi 17507417    300 EIRNQRHYAIQTEAQYMYIHRVLLE 324
Cdd:smart00012  81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
226-324 1.88e-37

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 130.56  E-value: 1.88e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417    226 SITHYQWTNWPDHGAPPINMGAINLIEAVN------YDTNPVVVHCSAGVGRSGTIVGISLIMDKMIQGINCKDMKKLVE 299
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKknlnqsESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|....*
gi 17507417    300 EIRNQRHYAIQTEAQYMYIHRVLLE 324
Cdd:smart00404  81 ELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 96-324 1.90e-37

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: 134.68  E-value: 1.90e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  96 YTDIKCIEKTRVILT-TDGA-SSDYIHANYVGISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIELARVKC 173
Cdd:cd14620   1 YPNILPYDHSRVILSqLDGIpCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 174 EQYWPAVEGQT--NTYVSKGHTI-----TINNLGVGTLSPDDdfinvtnlelvwAGKTRSITHYQWTNWPDHGAP--PIN 244
Cdd:cd14620  81 YQYWPDQGCWTygNIRVAVEDCVvlvdyTIRKFCIQPQLPDG------------CKAPRLVTQLHFTSWPDFGVPftPIG 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 245 M-GAINLIEAVN-YDTNPVVVHCSAGVGRSGTIVGISLIMDkMIQGINCKDMKKLVEEIRNQRHYAIQTEAQYMYIHRVL 322
Cdd:cd14620 149 MlKFLKKVKSVNpVHAGPIVVHCSAGVGRTGTFIVIDAMID-MMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQAL 227


                ..
gi 17507417 323 LE 324
Cdd:cd14620 228 LE 229
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 118-320 2.56e-37

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1).


Pssm-ID: 350399 [Multi-domain]  Cd Length: 202  Bit Score: 133.50  E-value: 2.56e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 118 YIHANYVGISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIELARVKCEQYWPAVEGQT--NTYVSKGHTIT 195
Cdd:cd14551   1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTygNLRVRVEDTVV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 196 INNLGVGT--LSPDDDFINvtnlelvwAGKTRSITHYQWTNWPDHGAPPINMGAINLIEAVN-----YDtNPVVVHCSAG 268
Cdd:cd14551  81 LVDYTTRKfcIQKVNRGIG--------EKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKsanppRA-GPIVVHCSAG 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 17507417 269 VGRSGTIVGISLIMDkMIQGINCKDMKKLVEEIRNQRHYAIQTEAQYMYIHR 320
Cdd:cd14551 152 VGRTGTFIVIDAMLD-MMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 118-319 7.18e-37

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: 132.59  E-value: 7.18e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 118 YIHANYVGISIKPK--KFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIELAR-VKCEQYWPAVEGQTNTYvskGH-T 193
Cdd:cd17658   1 YINASLVETPASESlpKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYStAKCADYFPAEENESREF---GRiS 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 194 ITINNLGVGTLSPDDDFINVTNLELVWAgkTRSITHYQWTNWPDHGAPPINMGAINLIEA---VNYDTNPVVVHCSAGVG 270
Cdd:cd17658  78 VTNKKLKHSQHSITLRVLEVQYIESEEP--PLSVLHIQYPEWPDHGVPKDTRSVRELLKRlygIPPSAGPIVVHCSAGIG 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 17507417 271 RSGTIVGISLIMDKMIQG-INCKDMKKLVEEIRNQRHYAIQTEAQYMYIH 319
Cdd:cd17658 156 RTGAYCTIHNTIRRILEGdMSAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 93-319 2.67e-36

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: 131.58  E-value: 2.67e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  93 KNRYTDIKCIEKTRVILTT---DGASSDYIHANYV-GISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIEl 168
Cdd:cd14611   2 KNRYKTILPNPHSRVCLKPknsNDSLSTYINANYIrGYGGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 169 ARVKCEQYWPAVEGqtntyVSKGHTITINNLgvgtlsPDDDFINVTNLELVWAGKTRSITHYQWTNWPDHGAPPINMGAI 248
Cdd:cd14611  81 KNEKCVLYWPEKRG-----IYGKVEVLVNSV------KECDNYTIRNLTLKQGSQSRSVKHYWYTSWPDHKTPDSAQPLL 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 249 NLIEAVNYD------TNPVVVHCSAGVGRSGTIVGISlimdkmiqgINCKDMKK--------LVEEIRNQRHYAIQTEAQ 314
Cdd:cd14611 150 QLMLDVEEDrlaspgRGPVVVHCSAGIGRTGCFIATT---------IGCQQLKEegvvdvlsIVCQLRVDRGGMVQTSEQ 220


                ....*
gi 17507417 315 YMYIH 319
Cdd:cd14611 221 YEFVH 225
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
61-315 3.36e-36

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 132.91  E-value: 3.36e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  61 LNKGVSKLRDEFSEVANknPNVPVDAFKSNPeKNRYTDIKCIEKTRVilttdGASSDYIHANYVGIsIKPKKFICTQGPK 140
Cdd:COG5599  16 INSRLSTLTNELAPSHN--DPQYLQNINGSP-LNRFRDIQPYKETAL-----RANLGYLNANYIQV-IGNHRYIATQYPL 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 141 DSTIYDFWAMVIQDNVESIIML--CKVIELARVKCEQYWPAvEGQTNTYvskghTITINNLGVGTLSPDddfINVTNLEL 218
Cdd:COG5599  87 EEQLEDFFQMLFDNNTPVLVVLasDDEISKPKVKMPVYFRQ-DGEYGKY-----EVSSELTESIQLRDG---IEARTYVL 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 219 VWAG---KTRSITHYQWTNWPDHGAPPINM--GAINLIEAV----NYDTNPVVVHCSAGVGRSGTIVGIsLIMDKMIQ-- 287
Cdd:COG5599 158 TIKGtgqKKIEIPVLHVKNWPDHGAISAEAlkNLADLIDKKekikDPDKLLPVVHCRAGVGRTGTLIAC-LALSKSINal 236

                       250       260
                ....*....|....*....|....*....
gi 17507417 288 GINCKDMKKLVEEIRNQR-HYAIQTEAQY 315
Cdd:COG5599 237 VQITLSVEEIVIDMRTSRnGGMVQTSEQL 265
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 118-326 3.71e-35

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: 128.55  E-value: 3.71e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 118 YIHANYVGISIKPKK--FICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIELARVKCEQYWPAVEGQTNTYVSKGHTIT 195
Cdd:cd14598   1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSRHNTVTYGRFKIT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 196 INnlgvgtLSPDDDFINVTNLEL--VWAGKTRSITHYQWTNWPDHGAPPINMGAINL---IEAVNYDTN----------P 260
Cdd:cd14598  81 TR------FRTDSGCYATTGLKIkhLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYleeIQSVRRHTNstidpkspnpP 154

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17507417 261 VVVHCSAGVGRSGTIVgISLIMDKMIQGINCKDMKKLVEEIRNQRHYAIQTEAQYMYIHRVLLEYF 326
Cdd:cd14598 155 VLVHCSAGVGRTGVVI-LSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFL 219
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 81-325 5.42e-35

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 130.51  E-value: 5.42e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417   81 NVPVDAFKS----NPEKNRYTDIKCIEKTRVILTTDGASSDYIHANYVGISIKPKKFICTQGPKDSTIYDFWAMVIQDNV 156
Cdd:PHA02742  39 IVAFSCNESlelkNMKKCRYPDAPCFDRNRVILKIEDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQV 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  157 ESIIMLCKVIELARVKCEQYWPAVEGQTNTYvskgHTITINNLGVGTLSpdddFINVTNLEL--VWAGKTRSITHYQWTN 234
Cdd:PHA02742 119 RVIVMITKIMEDGKEACYPYWMPHERGKATH----GEFKIKTKKIKSFR----NYAVTNLCLtdTNTGASLDIKHFAYED 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  235 WPDHGAPPINMGAINLIEAVNY---------------DTNPVVVHCSAGVGRSGTIVGISLIMDKMIQGINCKdMKKLVE 299
Cdd:PHA02742 191 WPHGGLPRDPNKFLDFVLAVREadlkadvdikgenivKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIP-LLSIVR 269

                        250       260
                 ....*....|....*....|....*.
gi 17507417  300 EIRNQRHYAIQTEAQYMYIHRVLLEY 325
Cdd:PHA02742 270 DLRKQRHNCLSLPQQYIFCYFIVLIF 295
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 117-325 1.06e-34

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: 126.66  E-value: 1.06e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 117 DYIHANYVGISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIELARVKCEQYWPAvEGQtntyVSKGH-TIT 195
Cdd:cd14622   1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPS-EGS----VTHGEiTIE 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 196 INNLGVGTLSPDDDFINVTNLElvwaGKTRSITHYQWTNWPDHGAPPINMGAINLIEAVNYD-----TNPVVVHCSAGVG 270
Cdd:cd14622  76 IKNDTLLETISIRDFLVTYNQE----KQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQqqqtgNHPIVVHCSAGAG 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17507417 271 RSGTIVGISLIMDKmIQGINCKDMKKLVEEIRNQRHYAIQTEAQYMYIHRVLLEY 325
Cdd:cd14622 152 RTGTFIALSNILER-VKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 93-325 2.13e-34

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: 127.67  E-value: 2.13e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  93 KNRYTDIKCIEKTRVILTT---DGASSDYIHANYV-GISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKvIEL 168
Cdd:cd14613  28 KNRYKTILPNPHSRVCLTSpdqDDPLSSYINANYIrGYGGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITN-IEE 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 169 ARVKCEQYWPAVEGqtntyVSKGHTITINNlgvgtLSPDDDFiNVTNLELVWAGKTRSITHYQWTNWPDHGAPPINMGAI 248
Cdd:cd14613 107 MNEKCTEYWPEEQV-----TYEGIEITVKQ-----VIHADDY-RLRLITLKSGGEERGLKHYWYTSWPDQKTPDNAPPLL 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 249 NLIEAVNY-------DTNPVVVHCSAGVGRSGTIVGISLIMDKMIQGiNCKDMKKLVEEIRNQRHYAIQTEAQYMYIHRV 321
Cdd:cd14613 176 QLVQEVEEarqqaepNCGPVIVHCSAGIGRTGCFIATSICCKQLRNE-GVVDILRTTCQLRLDRGGMIQTCEQYQFVHHV 254


                ....
gi 17507417 322 LLEY 325
Cdd:cd14613 255 LSLY 258
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 118-319 2.40e-34

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: 125.96  E-value: 2.40e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 118 YIHANYV-GISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIELARVKCEQYWPAVEGQTNTYvskGHtITI 196
Cdd:cd14539   1 YINASLIeDLTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQALVY---GA-ITV 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 197 NNLGVGTLSPD-DDFINVTNLElvwAGKTRSITHYQWTNWPDHGAPPINMGAINLIEAVNYDTN-------PVVVHCSAG 268
Cdd:cd14539  77 SLQSVRTTPTHvERIISIQHKD---TRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLqqrslqtPIVVHCSSG 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 17507417 269 VGRSGTIVGISLIMDKMIQGINCKDMKKLVEEIRNQRHYAIQTEAQYMYIH 319
Cdd:cd14539 154 VGRTGAFCLLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCY 204
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 118-322 6.80e-34

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: 124.69  E-value: 6.80e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 118 YIHANYVGISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIELARVKCEQYWPavegqTNTYVSKGH-TITI 196
Cdd:cd14552   1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWP-----EDGSVSSGDiTVEL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 197 NNlgvGTLSPD---DDFInVTNLElvwAGKTRSITHYQWTNWPDHGAPPINMGAINLIEAVNYD-----TNPVVVHCSAG 268
Cdd:cd14552  76 KD---QTDYEDytlRDFL-VTKGK---GGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQqqqsgNHPITVHCSAG 148

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17507417 269 VGRSGTIVGISLIMDKM-IQGIncKDMKKLVEEIRNQRHYAIQTEAQYMYIHRVL 322
Cdd:cd14552 149 AGRTGTFCALSTVLERVkAEGV--LDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 59-317 1.56e-33

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: 125.94  E-value: 1.56e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  59 HTLNKgvSKLRDEFSEVA--NKNPNVPVDAFKS-NPEKNRYTDIKCIEKTRVILTTDGA--SSDYIHANYVgISIKPKK- 132
Cdd:cd14610  12 HLKNK--NRLEKEWEALCayQAEPNATNVAQREeNVQKNRSLAVLPYDHSRIILKAENShsHSDYINASPI-MDHDPRNp 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 133 -FICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIELARVKCEQYWPAvEGqTNTYvskgHTITINnLGVGTLSPDDDFI 211
Cdd:cd14610  89 aYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPD-EG-SNLY----HIYEVN-LVSEHIWCEDFLV 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 212 NVTNLELVWAGKTRSITHYQWTNWPDHGAPPINMGAINLIEAVNY----DTNPVVVHCSAGVGRSGTIVGISLIMDKMIQ 287
Cdd:cd14610 162 RSFYLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKcyrgRSCPIIVHCSDGAGRSGTYILIDMVLNKMAK 241

                       250       260       270
                ....*....|....*....|....*....|
gi 17507417 288 GINCKDMKKLVEEIRNQRHYAIQTEAQYMY 317
Cdd:cd14610 242 GAKEIDIAATLEHLRDQRPGMVQTKEQFEF 271
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 88-317 1.74e-33

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: 125.92  E-value: 1.74e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  88 KSNPEKNRYTDIKCIEKTRVILTTDG--ASSDYIHANYVgISIKPK--KFICTQGPKDSTIYDFWAMVIQDNVESIIMLC 163
Cdd:cd14609  40 EANVKKNRNPDFVPYDHARIKLKAESnpSRSDYINASPI-IEHDPRmpAYIATQGPLSHTIADFWQMVWENGCTVIVMLT 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 164 KVIELARVKCEQYWPAvEGqtntyvSKGHTITINNLGVGTLSPDDDFINVTNLELVWAGKTRSITHYQWTNWPDHGAPPI 243
Cdd:cd14609 119 PLVEDGVKQCDRYWPD-EG------SSLYHIYEVNLVSEHIWCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGIPSS 191

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17507417 244 NMGAINLIEAVNY----DTNPVVVHCSAGVGRSGTIVGISLIMDKMIQGINCKDMKKLVEEIRNQRHYAIQTEAQYMY 317
Cdd:cd14609 192 TRPLLDFRRKVNKcyrgRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGVKEIDIAATLEHVRDQRPGMVRTKDQFEF 269
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 117-328 2.58e-33

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: 123.13  E-value: 2.58e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 117 DYIHANYVGISIKPK----KFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIELARVKCEQYWPAVEGQTntyvskgh 192
Cdd:cd14601   1 DYINANYINMEIPSSsiinRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSS-------- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 193 tiTINNLGVGTLSPDDDF------INVTNLElvwAGKTRSITHYQWTNWPDHGAPPINMGAINLIEAVN----YDTNPVV 262
Cdd:cd14601  73 --SYGGFQVTCHSEEGNPayvfreMTLTNLE---KNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRnkraGKDEPVV 147

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17507417 263 VHCSAGVGRSGTIVGISLIMdKMIQGINCKDMKKLVEEIRNQRHYAIQTEAQYMYIHRVLLEYFLE 328
Cdd:cd14601 148 VHCSAGIGRTGVLITMETAM-CLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVYEE 212
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 88-328 3.56e-31

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 120.52  E-value: 3.56e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417   88 KSNPEKNRYTDIKCIEKTRVIL---------------------TTDGASSDYIHANYVGISIKPKKFICTQGPKDSTIYD 146
Cdd:PHA02746  49 KENLKKNRFHDIPCWDHSRVVInaheslkmfdvgdsdgkkievTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSED 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  147 FWAMVIQDNVESIIMLCKvIELARVKCEQYWPAVEGQTNT---YVSKghTITInnlgVGTLSPDDDFINVTNlelVWAGK 223
Cdd:PHA02746 129 FFKLISEHESQVIVSLTD-IDDDDEKCFELWTKEEDSELAfgrFVAK--ILDI----IEELSFTKTRLMITD---KISDT 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  224 TRSITHYQWTNWPDHGAPPINMGAINLIEAVN--------------YDTNPVVVHCSAGVGRSGTIVGISLIMDKMIQGI 289
Cdd:PHA02746 199 SREIHHFWFPDWPDNGIPTGMAEFLELINKVNeeqaelikqadndpQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEK 278

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 17507417  290 NCKdMKKLVEEIRNQRHYAIQTEAQYMYIHRVLLEYFLE 328
Cdd:PHA02746 279 EVC-LGEIVLKIRKQRHSSVFLPEQYAFCYKALKYAIIE 316
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 103-324 2.00e-30

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: 116.30  E-value: 2.00e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 103 EKTRVILTTDGA--SSDYIHANYVGISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIELARVKCEQYWPA- 179
Cdd:cd14623   9 EFNRVIIPVKRGeeNTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEKCAQYWPSd 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 180 ---VEGQTNTYVSK---GHTITINNLgvgtlspdddfiNVTNLElvwAGKTRSITHYQWTNWPDHGAPPINMGAINLIEA 253
Cdd:cd14623  89 gsvSYGDITIELKKeeeCESYTVRDL------------LVTNTR---ENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAA 153

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17507417 254 VNYD-----TNPVVVHCSAGVGRSGTIVGISLIMDKM-IQGIncKDMKKLVEEIRNQRHYAIQTEAQYMYIHRVLLE 324
Cdd:cd14623 154 VQKQqqqsgNHPITVHCSAGAGRTGTFCALSTVLERVkAEGI--LDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 118-315 1.16e-27

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: 107.92  E-value: 1.16e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 118 YIHANYVgISIKPKK--FICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIELARVKCEQYWPavEGQTNTYvskgHTIT 195
Cdd:cd14546   1 YINASTI-YDHDPRNpaYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWP--EEGSEVY----HIYE 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 196 INNlgVGTLSPDDDFInVTNLEL--VWAGKTRSITHYQWTNWPDHGAPPINMGAINLIEAVNYDTN----PVVVHCSAGV 269
Cdd:cd14546  74 VHL--VSEHIWCDDYL-VRSFYLknLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRgrscPIVVHCSDGA 150

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 17507417 270 GRSGTIVGISLIMDKMIQGINCKDMKKLVEEIRNQRHYAIQTEAQY 315
Cdd:cd14546 151 GRTGTYILIDMVLNRMAKGAKEIDIAATLEHLRDQRPGMVKTKDQF 196
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 118-319 2.53e-25

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: 101.70  E-value: 2.53e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 118 YIHANYVGISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIELARVKCEQYWPaVEGQTN-------TYVSK 190
Cdd:cd14558   1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWG-DEKKTYgdievelKDTEK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 191 GHTITINNLgvgtlspdddfiNVTNLElvwAGKTRSITHYQWTNWPDHGAPPINMGAINLIEAV-------NYDTN---P 260
Cdd:cd14558  80 SPTYTVRVF------------EITHLK---RKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIkqklpykNSKHGrsvP 144

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17507417 261 VVVHCSAGVGRSGTIVGISLIMD-----KMIqginckDMKKLVEEIRNQRHYAIQTEAQYMYIH 319
Cdd:cd14558 145 IVVHCSDGSSRTGIFCALWNLLEsaeteKVV------DVFQVVKALRKQRPGMVSTLEQYQFLY 202
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 118-319 9.38e-24

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


Pssm-ID: 350404 [Multi-domain]  Cd Length: 201  Bit Score: 97.09  E-value: 9.38e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 118 YIHANYVGISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIELARvKCEQYWPAVEGQTN-----TYVS--- 189
Cdd:cd14556   1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQ-SCPQYWPDEGSGTYgpiqvEFVStti 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 190 KGHTITINNLGVGTLSPDDDFinvtnlelvwagktRSITHYQWTNWPDHGAPPINMGA-INLIEAVN-----YDTNPVVV 263
Cdd:cd14556  80 DEDVISRIFRLQNTTRPQEGY--------------RMVQQFQFLGWPRDRDTPPSKRAlLKLLSEVEkwqeqSGEGPIVV 145

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17507417 264 HCSAGVGRSGTIVGISLIMDkMIQGINCKDMKKLVEEIRNQRHYAIQTEAQYMYIH 319
Cdd:cd14556 146 HCLNGVGRSGVFCAISSVCE-RIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 118-324 1.21e-22

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: 94.32  E-value: 1.21e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 118 YIHANYVGISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKvIELARVkCEQYWPavEGQTNTYvskghtitiN 197
Cdd:cd14634   1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNE-MDAAQL-CMQYWP--EKTSCCY---------G 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 198 NLGVGTLSPD--DDFIN----VTNLELVWAGkTRSITHYQWTNWPDH-GAPPINMGAINLIEAVN-----YDTNP--VVV 263
Cdd:cd14634  68 PIQVEFVSADidEDIISrifrICNMARPQDG-YRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEkwqeqYDGREgrTVV 146

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17507417 264 HCSAGVGRSGTIVGISLIMDkMIQGINCKDMKKLVEEIRNQRHYAIQTEAQYMYIHRVLLE 324
Cdd:cd14634 147 HCLNGGGRSGTFCAICSVCE-MIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 94-315 3.37e-16

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


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 77.05  E-value: 3.37e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  94 NRYTDIKCIEKT--RVILTtdgassdyihANYVGISIKPKkFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIELARV 171
Cdd:cd14559   1 NRFTNIQTRVSTpvGKNLN----------ANRVQIGNKNV-AIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRK 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 172 KCEQYWpaveGQTNTYVSkghtITINNLGVGTLSPDDDF-INVTNLELVWAGKTRSITHYQWTNWPDHGAPPiNMGAINL 250
Cdd:cd14559  70 GLPPYF----RQSGTYGS----VTVKSKKTGKDELVDGLkADMYNLKITDGNKTITIPVVHVTNWPDHTAIS-SEGLKEL 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 251 IEAVN------------------YDTNPV--VVHCSAGVGRSGTIVGiSLIMDKMIQGINCKDMkklVEEIRNQR-HYAI 309
Cdd:cd14559 141 ADLVNksaeekrnfykskgssaiNDKNKLlpVIHCRAGVGRTGQLAA-AMELNKSPNNLSVEDI---VSDMRTSRnGKMV 216


                ....*.
gi 17507417 310 QTEAQY 315
Cdd:cd14559 217 QKDEQL 222
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 118-324 1.22e-14

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: 71.98  E-value: 1.22e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 118 YIHANYVGISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKvIELARvKCEQYWPAvEGQTNTYVSKGHTITIn 197
Cdd:cd14636   1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNE-VDLAQ-GCPQYWPE-EGMLRYGPIQVECMSC- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 198 nlgvgtlSPDDDFIN----VTNLELVWAGKTRsITHYQWTNWPDHGAPPINMGA-INLI-------EAVNYDTNPVVVHC 265
Cdd:cd14636  77 -------SMDCDVISrifrICNLTRPQEGYLM-VQQFQYLGWASHREVPGSKRSfLKLIlqvekwqEECDEGEGRTIIHC 148

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17507417 266 SAGVGRSGTIVGISLIMDkMIQGINCKDMKKLVEEIRNQRHYAIQTEAQYMYIHRVLLE 324
Cdd:cd14636 149 LNGGGRSGMFCAISIVCE-MIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 118-323 1.67e-14

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: 71.56  E-value: 1.67e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 118 YIHANYVGISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIELARVKCeQYWPA------VEGQTNTYVSKG 191
Cdd:cd17669   1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWPNkdepinCETFKVTLIAEE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 192 HTITIN--NLGVgtlspdDDFInvtnLELVWAGKTRSITHYQWTNWPDHGAP-PINMGAINLI--EAVNYDtNPVVVHCS 266
Cdd:cd17669  80 HKCLSNeeKLII------QDFI----LEATQDDYVLEVRHFQCPKWPNPDSPiSKTFELISIIkeEAANRD-GPMIVHDE 148

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17507417 267 AGVGRSGTIVGISLIMDKMIQGiNCKDMKKLVEEIRNQRHYAIQTEAQYMYIHRVLL 323
Cdd:cd17669 149 HGGVTAGTFCALTTLMHQLEKE-NSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 118-323 2.23e-14

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: 71.25  E-value: 2.23e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 118 YIHANYVGISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIELARVKCeQYWPAVEGQTNtyvSKGHTITIN 197
Cdd:cd17670   1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEF-VYWPSREESMN---CEAFTVTLI 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 198 NLGVGTLSPDD-----DFInvtnLELVWAGKTRSITHYQWTNWPDHGAP-PINMGAINLI--EAVNYDtNPVVVHCSAGV 269
Cdd:cd17670  77 SKDRLCLSNEEqiiihDFI----LEATQDDYVLEVRHFQCPKWPNPDAPiSSTFELINVIkeEALTRD-GPTIVHDEFGA 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 17507417 270 GRSGTIVGISlIMDKMIQGINCKDMKKLVEEIRNQRHYAIQTEAQYMYIHRVLL 323
Cdd:cd17670 152 VSAGTLCALT-TLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 118-324 2.74e-14

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: 70.87  E-value: 2.74e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 118 YIHANYVGISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKViELARVkCEQYWPavegqtNTYVSKGHTITIN 197
Cdd:cd14635   1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDV-DPAQL-CPQYWP------ENGVHRHGPIQVE 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 198 NLGVGTlspDDDFIN----VTNLELVWAGkTRSITHYQWTNWPDHGAPPINMGA-INLIEAVN-----YDTNP--VVVHC 265
Cdd:cd14635  73 FVSADL---EEDIISrifrIYNAARPQDG-YRMVQQFQFLGWPMYRDTPVSKRSfLKLIRQVDkwqeeYNGGEgrTVVHC 148

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17507417 266 SAGVGRSGTIVGISLIMDkMIQGINCKDMKKLVEEIRNQRHYAIQTEAQYMYIHRVLLE 324
Cdd:cd14635 149 LNGGGRSGTFCAISIVCE-MLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
230-320 7.97e-14

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 68.07  E-value: 7.97e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 230 YQWTNWPDHGAPPINM--GAINLIEAVNYDTNPVVVHCSAGVGRSGTIVGISLIMDKMiqginckDMKKLVEEIRNQRHY 307
Cdd:COG2453  50 YLHLPIPDFGAPDDEQlqEAVDFIDEALREGKKVLVHCRGGIGRTGTVAAAYLVLLGL-------SAEEALARVRAARPG 122

                        90
                ....*....|...
gi 17507417 308 AIQTEAQYMYIHR 320
Cdd:COG2453 123 AVETPAQRAFLER 135
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 118-324 3.56e-12

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: 64.93  E-value: 3.56e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 118 YIHANYVGISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKVIELARV-KCEQYWPAVEGQTN-----TYVSkg 191
Cdd:cd14637   1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGLQQYgpmevEFVS-- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 192 htitinnlgvgtLSPDDDFIN----VTNLELVWAGKTrSITHYQWTNWPDHGAPPINMGA-INLIEAVNY-----DTNPV 261
Cdd:cd14637  79 ------------GSADEDIVTrlfrVQNITRLQEGHL-MVRHFQFLRWSAYRDTPDSKKAfLHLLASVEKwqresGEGRT 145

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17507417 262 VVHCSAGVGRSGTIVGISLIMDkMIQGINCKDMKKLVEEIRNQRHYAIQTEAQYMYIHRVLLE 324
Cdd:cd14637 146 VVHCLNGGGRSGTYCASAMILE-MIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 118-286 3.96e-12

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: 64.65  E-value: 3.96e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 118 YIHANYVGISIKPKKFICTQGPKDSTIYDFWAMVIQDNVESIIMLCKViELARvKCEQYWPA------VEGQTNTYVSKG 191
Cdd:cd14550   1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDN-ELNE-DEPIYWPTkekpleCETFKVTLSGED 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 192 HTITINNLGVGTL-----SPDDDFInvtnLElvwagktrsITHYQWTNWPDHGAPPINmgAINLIEAVNYDTN----PVV 262
Cdd:cd14550  79 HSCLSNEIRLIVRdfileSTQDDYV----LE---------VRQFQCPSWPNPCSPIHT--VFELINTVQEWAQqrdgPIV 143

                       170       180
                ....*....|....*....|....
gi 17507417 263 VHCSAGVGRSGTIVGISLIMDKMI 286
Cdd:cd14550 144 VHDRYGGVQAATFCALTTLHQQLE 167
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 236-318 6.47e-09

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


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 54.21  E-value: 6.47e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 236 PDHGAPpiNMGAIN----LIEAVNYDTNPVVVHCSAGVGRSGTIVGISLIMDKMIQGInckdmkKLVEEIRNQRHYAIQT 311
Cdd:cd14504  58 EDYTPP--TLEQIDefldIVEEANAKNEAVLVHCLAGKGRTGTMLACYLVKTGKISAV------DAINEIRRIRPGSIET 129


                ....*..
gi 17507417 312 EAQYMYI 318
Cdd:cd14504 130 SEQEKFV 136
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 260-320 2.24e-08

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: 51.58  E-value: 2.24e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17507417 260 PVVVHCSAGVGRSGTIVGISLIMDKMiqgincKDMKKLVEEIRNQR-HYAIQTEAQYMYIHR 320
Cdd:cd14494  58 PVLVHCKAGVGRTGTLVACYLVLLGG------MSAEEAVRIVRLIRpGGIPQTIEQLDFLIK 113
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 250-320 6.04e-08

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: 51.88  E-value: 6.04e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17507417 250 LIEAVNYDTNpVVVHCSAGVGRSGTIVGISLIMDKMiqginCKDMKKLVEEIRNQRHYAIQTEAQYMYIHR 320
Cdd:cd14505  99 LLSALENGKK-VLIHCKGGLGRTGLIAACLLLELGD-----TLDPEQAIAAVRALRPGAIQTPKQENFLHQ 163
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 65-239 6.62e-07

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 50.35  E-value: 6.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417   65 VSKLRDEFSEVANKNPNvpvdafKSNPEKNRYTDIKCIEKtRVILTTDGASSDyihANYVGISIKPKKFICTQGPKDSTI 144
Cdd:PHA02740  35 VPEHEDEANKACAQAEN------KAKDENLALHITRLLHR-RIKLFNDEKVLD---ARFVDGYDFEQKFICIINLCEDAC 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  145 YDFWAMVIQDNVESIIMLCKvieLARVKC-EQYWPAVEGQTNTYvskghtitiNNLGVGTLSP-DDDFINVTNLELV-WA 221
Cdd:PHA02740 105 DKFLQALSDNKVQIIVLISR---HADKKCfNQFWSLKEGCVITS---------DKFQIETLEIiIKPHFNLTLLSLTdKF 172

                        170
                 ....*....|....*...
gi 17507417  222 GKTRSITHYQWTNWPDHG 239
Cdd:PHA02740 173 GQAQKISHFQYTAWPADG 190
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 227-306 1.16e-06

protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar proteins; Phosphatase and tensin homolog (PTEN) is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It dephosphorylates phosphoinositide trisphosphate. In addition to PTEN, this family includes tensins, voltage-sensitive phosphatases (VSPs), and auxilins. They all contain a protein tyrosine phosphatase-like domain although not all are active phosphatases. Tensins are intracellular proteins that act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility, and they may or may not have phosphatase activity. VSPs are phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. Auxilins are J domain-containing proteins that facilitate Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles, and they do not exhibit phosphatase activity.


Pssm-ID: 350347 [Multi-domain]  Cd Length: 160  Bit Score: 47.96  E-value: 1.16e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 227 ITHYqwtNWPDHGAPPINMgainLIEAVN-----YDTNP---VVVHCSAGVGRSGTIVgISLIMDKMIqginCKDMKKLV 298
Cdd:cd14497  63 VLHY---GFPDHHPPPLGL----LLEIVDdidswLSEDPnnvAVVHCKAGKGRTGTVI-CAYLLYYGQ----YSTADEAL 130


                ....*...
gi 17507417 299 EEIRNQRH 306
Cdd:cd14497 131 EYFAKKRF 138
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 227-319 2.82e-06

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


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 47.73  E-value: 2.82e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 227 ITHYQWtNWPDHGAPP--INMGAINLIEAVNYDTNPVVVHCSAGVGRSGTIVGISLImdkMIQGINCKDMKKLVeeiRNQ 304
Cdd:cd14506  77 IYFYNF-GWKDYGVPSltTILDIVKVMAFALQEGGKVAVHCHAGLGRTGVLIACYLV---YALRMSADQAIRLV---RSK 149

                        90
                ....*....|....*
gi 17507417 305 RHYAIQTEAQYMYIH 319
Cdd:cd14506 150 RPNSIQTRGQVLCVR 164
PTP-IVa cd14500
protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), ...
 126-309 1.11e-05

protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), also known as protein-tyrosine phosphatases of regenerating liver (PRLs) constitute a family of small, prenylated phosphatases that are the most oncogenic of all PTPs. They stimulate progression from G1 into S phase during mitosis and enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. They associate with magnesium transporters of the cyclin M (CNNM) family, which results in increased intracellular magnesium levels that promote oncogenic transformation. Vertebrates contain three members: PRL-1, PRL-2, and PRL-3.


Pssm-ID: 350350 [Multi-domain]  Cd Length: 156  Bit Score: 44.90  E-value: 1.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 126 ISIKPKKFICTQGPKDSTIYDFwamviqdnvesiIMLCK---VIELARVkCEQywpavegqtnTYvskghtitinnlgvg 202
Cdd:cd14500   8 IEYKGMRFLITDAPTDSNLPLY------------IKELKkynVTDLVRV-CEP----------TY--------------- 49

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 203 tlspDDDfinvtnlELVWAGktrsITHYQWTnWPDHGAPPINM--GAINLIEAVNYDTNP----VVVHCSAGVGRSGTIV 276
Cdd:cd14500  50 ----DKE-------PLEKAG----IKVHDWP-FDDGSPPPDDVvdDWLDLLKTRFKEEGKpgacIAVHCVAGLGRAPVLV 113

                       170       180       190
                ....*....|....*....|....*....|...
gi 17507417 277 GISLIMDKMiqginckDMKKLVEEIRNQRHYAI 309
Cdd:cd14500 114 AIALIELGM-------KPEDAVEFIRKKRRGAI 139
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 211-304 1.26e-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: 41.38  E-value: 1.26e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 211 INVTNlELVWAGKTRSITHYQWtNWPDHgaPPINMG-----AINLIEAVNYDTNPVVVHCSAGVGRSGTIVgISLIMDKm 285
Cdd:cd14498  31 LNVAG-EPPPNKFPDGIKYLRI-PIEDS--PDEDILshfeeAIEFIEEALKKGGKVLVHCQAGVSRSATIV-IAYLMKK- 104

                        90
                ....*....|....*....
gi 17507417 286 iQGINCKDMKKLVEEIRNQ 304
Cdd:cd14498 105 -YGWSLEEALELVKSRRPI 122
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 247-302 1.94e-04

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: 40.71  E-value: 1.94e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 17507417   247 AINLIEAVNYDTNPVVVHCSAGVGRSGTIVgISLIMDKMiqGINCKDMKKLVEEIR 302
Cdd:pfam00782  58 AVEFIDDARQKGGKVLVHCQAGISRSATLI-IAYLMKTR--NLSLNEAYSFVKERR 110
PTP-IVa3 cd18535
protein tyrosine phosphatase type IVA 3; Protein tyrosine phosphatase type IVA 3 (PTP-IVa3), ...
 234-320 5.11e-04

protein tyrosine phosphatase type IVA 3; Protein tyrosine phosphatase type IVA 3 (PTP-IVa3), also known as protein-tyrosine phosphatase of regenerating liver 3 (PRL-3), stimulates progression from G1 into S phase during mitosis and enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. It exerts its oncogenic functions through activation of PI3K/Akt, which is a key regulator of the rapamycin-sensitive mTOR complex 1. PRL-3 is a member of the PTP-IVa/PRL family of small, prenylated phosphatases that are the most oncogenic of all PTPs. PRLs associate with magnesium transporters of the cyclin M (CNNM) family, which results in increased intracellular magnesium levels that promote oncogenic transformation.


Pssm-ID: 350511 [Multi-domain]  Cd Length: 154  Bit Score: 40.01  E-value: 5.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 234 NWP-DHGAPP---INMGAINLIEAvNYDTNP---VVVHCSAGVGRSGTIVGISLIMDKMiqginckDMKKLVEEIRNQRH 306
Cdd:cd18535  63 DWPfDDGAPPpgkVVEDWLSLLKT-KFCEDPgccVAVHCVAGLGRAPVLVALALIESGM-------KYEDAIQFIRQKRR 134

                        90
                ....*....|....
gi 17507417 307 YAIQTEaQYMYIHR 320
Cdd:cd18535 135 GAINSK-QLTYLEK 147
PTPMT1 cd14524
protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or ...
 247-284 9.03e-04

protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or PTP localized to the mitochondrion 1 (PTPMT1), also called phosphoinositide lipid phosphatase (PLIP), phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1, or PTEN-like phosphatase, is a lipid phosphatase or phosphatidylglycerophosphatase (EC 3.1.3.27) which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG). It is targeted to the mitochondrion by an N-terminal signal sequence and is found anchored to the matrix face of the inner membrane. It is essential for the biosynthesis of cardiolipin, a mitochondrial-specific phospholipid regulating the membrane integrity and activities of the organelle. PTPMT1 also plays a crucial role in hematopoietic stem cell (HSC) function, and has been shown to display activity toward phosphoprotein substrates.


Pssm-ID: 350374 [Multi-domain]  Cd Length: 149  Bit Score: 39.17  E-value: 9.03e-04
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 17507417 247 AINLIEAVNYDTNPVVVHCSAGVGRSGTIVGISLIMDK 284
Cdd:cd14524  78 GVDFILKHREKGKSVYVHCKAGRGRSATIVACYLIQHK 115
DSP_DUSP4 cd14640
dual specificity phosphatase domain of dual specificity protein phosphatase 4; Dual ...
 229-287 1.20e-03

dual specificity phosphatase domain of dual specificity protein phosphatase 4; Dual specificity protein phosphatase 4 (DUSP4), also called mitogen-activated protein kinase (MAPK) phosphatase 2 (MKP-2), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other MKPs, it deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. It belongs to the class I subfamily and is a mitogen- and stress-inducible nuclear MKP. DUSP4 regulates either ERK or c-JUN N-terminal kinase (JNK), depending on the cell type. It dephosphorylates nuclear JNK and induces apoptosis in diffuse large B cell lymphoma (DLBCL) cells. It acts as a negative regulator of macrophage M1 activation and inhibits inflammation during macrophage-adipocyte interaction. It has been linked to different aspects of cancer: it may have a role in the development of ovarian cancers, oesophagogastric rib metastasis, and pancreatic tumours; it may also be a candidate tumor suppressor gene, with its deletion implicated in breast cancer, prostate cancer, and gliomas. DUSP4/MKP-2 contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.


Pssm-ID: 350488 [Multi-domain]  Cd Length: 141  Bit Score: 38.86  E-value: 1.20e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17507417 229 HYQWTNWP--DHGAPPIN---MGAINLIEAVNYDTNPVVVHCSAGVGRSGTIVGISLIMDKMIQ 287
Cdd:cd14640  44 HYQYKCIPveDNHKADISswfMEAIEYIDSVKDCNGRVLVHCQAGISRSATICLAYLMMKKRVR 107
PTP-IVa2 cd18536
protein tyrosine phosphatase type IVA 2; Protein tyrosine phosphatase type IVA 2 (PTP-IVa2), ...
 234-320 1.30e-03

protein tyrosine phosphatase type IVA 2; Protein tyrosine phosphatase type IVA 2 (PTP-IVa2), also known as protein-tyrosine phosphatase of regenerating liver 2 (PRL-2), stimulates progression from G1 into S phase during mitosis and promotes tumors. It regulates tumor cell migration and invasion through an ERK-dependent signaling pathway. Its overexpression correlates with breast tumor formation and progression. PRL-2 is a member of the PTP-IVa/PRL family of small, prenylated phosphatases that are the most oncogenic of all PTPs. PRLs associate with magnesium transporters of the cyclin M (CNNM) family, which results in increased intracellular magnesium levels that promote oncogenic transformation.


Pssm-ID: 350512 [Multi-domain]  Cd Length: 155  Bit Score: 38.83  E-value: 1.30e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 234 NWP-DHGAPPINM---GAINLIEAvNYDTNP---VVVHCSAGVGRSGTIVGISLIMDKMiqginckDMKKLVEEIRNQRH 306
Cdd:cd18536  64 DWPfDDGAPPPNQivdDWLNLLKT-KFREEPgccVAVHCVAGLGRAPVLVALALIECGM-------KYEDAVQFIRQKRR 135

                        90
                ....*....|....
gi 17507417 307 YAIQTEaQYMYIHR 320
Cdd:cd18536 136 GAFNSK-QLLYLEK 148
DSP_bac cd14527
unknown subfamily of bacterial and plant dual specificity protein phosphatases; This subfamily ...
 237-324 1.36e-03

unknown subfamily of bacterial and plant dual specificity protein phosphatases; This subfamily is composed of uncharacterized bacterial and plant dual-specificity protein phosphatases. DUSPs function as a protein-serine/threonine phosphatases (EC 3.1.3.16) and a protein-tyrosine-phosphatases (EC 3.1.3.48).


Pssm-ID: 350376 [Multi-domain]  Cd Length: 136  Bit Score: 38.41  E-value: 1.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 237 DHGAPPIN--MGAINLIEAVNYDTNPVVVHCSAGVGRSGTIVGISLIMDKMiqginCKDMKKLVEEIRNQRHYAIQTEAq 314
Cdd:cd14527  53 DLVAPTPEqlERAVAWIEELRAQGGPVLVHCALGYGRSATVVAAWLLAYGR-----AKSVAEAEALIRAARPQVVLNPA- 126

                        90
                ....*....|
gi 17507417 315 ymyiHRVLLE 324
Cdd:cd14527 127 ----QRKALE 132
PTP-IVa1 cd18537
protein tyrosine phosphatase type IVA 1; Protein tyrosine phosphatase type IVA 1 (PTP-IVa1), ...
 234-320 1.89e-03

protein tyrosine phosphatase type IVA 1; Protein tyrosine phosphatase type IVA 1 (PTP-IVa1), also known as protein-tyrosine phosphatase of regenerating liver 1 (PRL-1), stimulates progression from G1 into S phase during mitosis and enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. It may play a role in the development and maintenance of differentiating epithelial tissues. PRL-1 promotes cell growth and migration by activating both the ERK1/2 and RhoA pathways. It is a member of the PTP-IVa/PRL family of small, prenylated phosphatases that are the most oncogenic of all PTPs. PRLs associate with magnesium transporters of the cyclin M (CNNM) family, which results in increased intracellular magnesium levels that promote oncogenic transformation.


Pssm-ID: 350513 [Multi-domain]  Cd Length: 167  Bit Score: 38.90  E-value: 1.89e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 234 NWP-DHGAPPINMGAINLIEAVN--YDTNP---VVVHCSAGVGRSGTIVGISLIMDKMiqginckDMKKLVEEIRNQRHY 307
Cdd:cd18537  67 DWPfDDGAPPSNQIVDDWLNLLKvkFREEPgccIAVHCVAGLGRAPVLVALALIECGM-------KYEDAVQFIRQKRRG 139

                        90
                ....*....|...
gi 17507417 308 AIQTEaQYMYIHR 320
Cdd:cd18537 140 AFNSK-QLLYLEK 151
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 235-316 2.03e-03

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 38.46  E-value: 2.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417  235 WP-DHGAPP---INMGAINLIEAV---NYDTNPVV-VHCSAGVGRSGTIVGISLIMDkmiqgincKDMKKL--VEEIRNQ 304
Cdd:PTZ00242  67 WPfDDGAPPpkaVIDNWLRLLDQEfakQSTPPETIaVHCVAGLGRAPILVALALVEY--------GGMEPLdaVGFVREK 138

                         90
                 ....*....|...
gi 17507417  305 RHYAI-QTEAQYM 316
Cdd:PTZ00242 139 RKGAInQTQLQFL 151
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
247-304 2.06e-03

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 38.03  E-value: 2.06e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 17507417    247 AINLIEAVNYDTNPVVVHCSAGVGRSGTIVgISLIMDKMiqGINCKDMKKLVEEIRNQ 304
Cdd:smart00195  67 AVEFIEDAESKGGKVLVHCQAGVSRSATLI-IAYLMKTR--NMSLNDAYDFVKDRRPI 121
DSP_MKP_classIII cd14568
dual specificity phosphatase domain of class III mitogen-activated protein kinase phosphatase; ...
 247-302 2.43e-03

dual specificity phosphatase domain of class III mitogen-activated protein kinase phosphatase; Mitogen-activated protein kinase (MAPK) phosphatases (MKPs) are eukaryotic dual-specificity phosphatases (DUSPs) that act on MAPKs and function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). They deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. Based on sequence homology, subcellular localization and substrate specificity, 10 MKPs can be subdivided into three subfamilies (class I-III). Class III MKPs consist of DUSP8, DUSP10/MKP-5 and DUSP16/MKP-7, and are JNK/p38-selective phosphatases, which are found in both the cell nucleus and cytoplasm. 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.


Pssm-ID: 350416 [Multi-domain]  Cd Length: 140  Bit Score: 37.78  E-value: 2.43e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17507417 247 AINLIEAVNYDTNPVVVHCSAGVGRSGTIVgISLIMDKMiqGINCKDMKKLVEEIR 302
Cdd:cd14568  68 AVEFIEKARASNKRVLVHCLAGISRSATIA-IAYIMKHM--RMSLDDAYRFVKEKR 120
PTZ00393 PTZ00393
protein tyrosine phosphatase; Provisional
 235-296 2.77e-03

protein tyrosine phosphatase; Provisional


Pssm-ID: 240399  Cd Length: 241  Bit Score: 38.76  E-value: 2.77e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17507417  235 WPDHGAPPINMGA--INLIEAVNYDTNPVVVHCSAGVGRSGTIVGISLI---MDKMIQGINCKDMKK 296
Cdd:PTZ00393 145 FPDGDAPTVDIVSnwLTIVNNVIKNNRAVAVHCVAGLGRAPVLASIVLIefgMDPIDAIVFIRDRRK 211
DSP_MKP cd14512
dual specificity phosphatase domain of mitogen-activated protein kinase phosphatase; ...
 247-302 4.66e-03

dual specificity phosphatase domain of mitogen-activated protein kinase phosphatase; Mitogen-activated protein kinase (MAPK) phosphatases (MKPs) are eukaryotic dual-specificity phosphatases (DUSPs) that act on MAPKs, which are involved in gene regulation, cell proliferation, programmed cell death and stress responses, as an important feedback control mechanism that limits MAPK cascades. MKPs, also referred to as typical DUSPs, function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). They 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. Based on sequence homology, subcellular localization and substrate specificity, 10 MKPs can be subdivided into three subfamilies (class I-III).


Pssm-ID: 350362 [Multi-domain]  Cd Length: 136  Bit Score: 37.08  E-value: 4.66e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17507417 247 AINLIEAVNYDTNPVVVHCSAGVGRSGTIVgISLIMDKMIQGINckDMKKLVEEIR 302
Cdd:cd14512  68 AIEFIEEAKASNGGVLVHCLAGISRSATIA-IAYLMKRMRMSLD--EAYDFVKEKR 120
PTP_PTEN cd14509
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ...
 236-307 5.33e-03

protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; Phosphatase and tensin homolog (PTEN), also phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN or mutated in multiple advanced cancers 1 (MMAC1), is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It is a critical endogenous inhibitor of phosphoinositide signaling. It dephosphorylates phosphoinositide trisphosphate, and therefore, has the function of negatively regulating Akt. The PTEN/PI3K/AKT pathway regulates the signaling of multiple biological processes such as apoptosis, metabolism, cell proliferation, and cell growth. PTEN contains an N-terminal PIP-binding domain, a protein tyrosine phosphatase (PTP)-like catalytic domain, a regulatory C2 domain responsible for its cellular location, a C-tail containing phosphorylation sites, and a C-terminal PDZ domain.


Pssm-ID: 350359 [Multi-domain]  Cd Length: 158  Bit Score: 37.18  E-value: 5.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507417 236 PDHGAPPINMGAINLIEAVNY----DTNPVVVHCSAGVGRSGTIVGISLIMDKMIQG----------INCKDMKKLVeeI 301
Cdd:cd14509  68 DDHNPPPLELIKPFCEDVDEWlkedEKNVAAVHCKAGKGRTGVMICCYLLYLGKFPSakealdfygaKRTKNKKGVT--I 145


                ....*.
gi 17507417 302 RNQRHY 307
Cdd:cd14509 146 PSQRRY 151
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 260-326 6.29e-03

bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa TpbA; This subfamily contains bacterial protein tyrosine phosphatases (PTPs) and dual-specificity phosphatases (DUSPs) related to Pseudomonas aeruginosa TpbA, a DUSP that negatively regulates biofilm formation by converting extracellular quorum sensing signals and to Mycobacterium tuberculosis PtpB, a PTP virulence factor that attenuates host immune defenses by interfering with signal transduction pathways in macrophages. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides, while DUSPs function as protein-serine/threonine phosphatases (EC 3.1.3.16) and PTPs.


Pssm-ID: 350378 [Multi-domain]  Cd Length: 158  Bit Score: 36.97  E-value: 6.29e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17507417 260 PVVVHCSAGVGRSGTIVGISLI-MDKMIQGINcKDMKKLVEEIRNQRHYaIQTEAQYMYIHRVLLEYF 326
Cdd:cd14529  91 PVLIHCKHGKDRTGLVSALYRIvYGGSKEEAN-EDYRLSNRHLEGLRSG-IALDSKGGVKGRYLAAYF 156
DSP_DUSP19 cd14523
dual specificity phosphatase domain of dual specificity protein phosphatase 19; Dual ...
 247-302 9.90e-03

dual specificity phosphatase domain of dual specificity protein phosphatase 19; Dual specificity protein phosphatase 19 (DUSP19), also called low molecular weight dual specificity phosphatase 3 (LMW-DSP3) or stress-activated protein kinase (SAPK) pathway-regulating phosphatase 1 (SKRP1), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. DUSP19 interacts with the MAPK kinase MKK7, a JNK activator, and inactivates the JNK MAPK pathway.


Pssm-ID: 350373 [Multi-domain]  Cd Length: 137  Bit Score: 36.18  E-value: 9.90e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17507417 247 AINLIEAVNYDTNPVVVHCSAGVGRSGTIVgISLIMDKmiQGINCKDMKKLVEEIR 302
Cdd:cd14523  68 CFEFIDEAKSQDGVVLVHCNAGVSRSASIV-IGYLMAT--ENLSFEDAFSLVKNAR 120
 
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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