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Conserved domains on  [gi|15990529|gb|AAH15660|]
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Protein tyrosine phosphatase, non-receptor type 1 [Homo sapiens]

Protein Classification

PTPc-N1 domain-containing protein( domain architecture ID 12998687)

PTPc-N1 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 16-292 0e+00

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: 641.69  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  16 WAAIYQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHF 95
Cdd:cd14608   1 WAAIYQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  96 WEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFH 175
Cdd:cd14608  81 WEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFH 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 176 YTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRK 255
Cdd:cd14608 161 YTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRK 240

                       250       260       270
                ....*....|....*....|....*....|....*..
gi 15990529 256 FRMGLIQTADQLRFSYLAVIEGAKFIMGDSSVQDQWK 292
Cdd:cd14608 241 FRMGLIQTADQLRFSYLAVIEGAKFIMGDSSVQDQWK 277
 
Name Accession Description Interval E-value
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 16-292 0e+00

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: 641.69  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  16 WAAIYQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHF 95
Cdd:cd14608   1 WAAIYQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  96 WEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFH 175
Cdd:cd14608  81 WEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFH 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 176 YTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRK 255
Cdd:cd14608 161 YTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRK 240

                       250       260       270
                ....*....|....*....|....*....|....*..
gi 15990529 256 FRMGLIQTADQLRFSYLAVIEGAKFIMGDSSVQDQWK 292
Cdd:cd14608 241 FRMGLIQTADQLRFSYLAVIEGAKFIMGDSSVQDQWK 277
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
3-276 2.61e-116

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 340.41  E-value: 2.61e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529      3 MEKEFEQIDKSGSWaaiyqdirheasDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQ---EDNDYINASLIKMEEAQR 79
Cdd:smart00194   2 LEEEFEKLDRLKPD------------DESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPppgEGSDYINASYIDGPNGPK 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529     80 SYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDtnLKLTLISEDIKSYYTVRQLE 159
Cdd:smart00194  70 AYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGD--ITVTLKSVEKVDDYTIRTLE 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529    160 LENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGslSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRK 239
Cdd:smart00194 148 VTNTGCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQ--STSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGK 225

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 15990529    240 dpsSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 276
Cdd:smart00194 226 ---EVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
40-276 6.06e-112

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 328.43  E-value: 6.06e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529    40 NKNRNRYRDVSPFDHSRIKL--HQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKG 117
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLtgDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529   118 SLKCAQYWPQKEEKEMIFEDtnLKLTLISE-DIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLF 196
Cdd:pfam00102  81 REKCAQYWPEEEGESLEYGD--FTVTLKKEkEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529   197 KVRESgSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDpssVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 276
Cdd:pfam00102 159 KVRKS-SLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGE---VDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 20-281 3.71e-54

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 182.51  E-value: 3.71e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529   20 YQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQED--NDYINASLIKMEEAQRSYILTQGPLPNTCGHFWE 97
Cdd:PHA02742  32 HEHIMQEIVAFSCNESLELKNMKKCRYPDAPCFDRNRVILKIEDggDDFINASYVDGHNAKGRFICTQAPLEETALDFWQ 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529   98 MVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEdtnlKLTLISEDIKS--YYTVRQLELENLTTQETREILHFH 175
Cdd:PHA02742 112 AIFQDQVRVIVMITKIMEDGKEACYPYWMPHERGKATHG----EFKIKTKKIKSfrNYAVTNLCLTDTNTGASLDIKHFA 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  176 YTTWPDFGVPESPASFLNFLFKVRE---------SGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRkdpSSVDI 246
Cdd:PHA02742 188 YEDWPHGGLPRDPNKFLDFVLAVREadlkadvdiKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNER---AIIPL 264

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 15990529  247 KKVLLEMRKFRMGLIQTADQLRFSYLAVIEGAKFI 281
Cdd:PHA02742 265 LSIVRDLRKQRHNCLSLPQQYIFCYFIVLIFAKLM 299
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
36-267 7.98e-41

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 146.77  E-value: 7.98e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  36 KLPKNKNRNRYRDVSPFDHSRIklhQEDNDYINASLIKMEEAQRsYILTQGPLPNTCGHFWEMVWEQKSRGVVML--NRV 113
Cdd:COG5599  38 QNINGSPLNRFRDIQPYKETAL---RANLGYLNANYIQVIGNHR-YIATQYPLEEQLEDFFQMLFDNNTPVLVVLasDDE 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 114 MEKGSLKCAQYWPQKEEkemifedtNLKLTLISEDIKSYYTVRQLELENL------TTQETREILHFHYTTWPDFGVPES 187
Cdd:COG5599 114 ISKPKVKMPVYFRQDGE--------YGKYEVSSELTESIQLRDGIEARTYvltikgTGQKKIEIPVLHVKNWPDHGAISA 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 188 PAsFLNFLFKVRES-GSLSPEHGPVVVHCSAGIGRSGTFcLADTCLLLMDKRKDPSSVDIKKVLLEMRKFR-MGLIQTAD 265
Cdd:COG5599 186 EA-LKNLADLIDKKeKIKDPDKLLPVVHCRAGVGRTGTL-IACLALSKSINALVQITLSVEEIVIDMRTSRnGGMVQTSE 263


                ..
gi 15990529 266 QL 267
Cdd:COG5599 264 QL 265
 
Name Accession Description Interval E-value
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 16-292 0e+00

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: 641.69  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  16 WAAIYQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHF 95
Cdd:cd14608   1 WAAIYQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  96 WEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFH 175
Cdd:cd14608  81 WEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFH 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 176 YTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRK 255
Cdd:cd14608 161 YTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRK 240

                       250       260       270
                ....*....|....*....|....*....|....*..
gi 15990529 256 FRMGLIQTADQLRFSYLAVIEGAKFIMGDSSVQDQWK 292
Cdd:cd14608 241 FRMGLIQTADQLRFSYLAVIEGAKFIMGDSSVQDQWK 277
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 18-274 9.40e-171

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: 478.69  E-value: 9.40e-171
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  18 AIYQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWE 97
Cdd:cd14607   2 PLYLEIRNESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFWL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  98 MVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYT 177
Cdd:cd14607  82 MVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSFKETGFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYT 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 178 TWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKrKDPSSVDIKKVLLEMRKFR 257
Cdd:cd14607 162 TWPDFGVPESPASFLNFLFKVRESGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEK-KDPDSVDIKQVLLDMRKYR 240

                       250
                ....*....|....*..
gi 15990529 258 MGLIQTADQLRFSYLAV 274
Cdd:cd14607 241 MGLIQTPDQLRFSYMAV 257
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 41-272 1.29e-170

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: 477.27  E-value: 1.29e-170
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  41 KNRNRYRDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLK 120
Cdd:cd14545   1 LNRYRDRDPYDHDRSRVKLKQGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQIK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 121 CAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRE 200
Cdd:cd14545  81 CAQYWPQGEGNAMIFEDTGLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQKVRE 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15990529 201 SGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRkDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYL 272
Cdd:cd14545 161 SGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKG-NPSSVDVKKVLLEMRKYRMGLIQTPDQLRFSYL 231
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
3-276 2.61e-116

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 340.41  E-value: 2.61e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529      3 MEKEFEQIDKSGSWaaiyqdirheasDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQ---EDNDYINASLIKMEEAQR 79
Cdd:smart00194   2 LEEEFEKLDRLKPD------------DESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPppgEGSDYINASYIDGPNGPK 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529     80 SYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDtnLKLTLISEDIKSYYTVRQLE 159
Cdd:smart00194  70 AYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGD--ITVTLKSVEKVDDYTIRTLE 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529    160 LENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGslSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRK 239
Cdd:smart00194 148 VTNTGCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQ--STSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGK 225

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 15990529    240 dpsSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 276
Cdd:smart00194 226 ---EVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
40-276 6.06e-112

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 328.43  E-value: 6.06e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529    40 NKNRNRYRDVSPFDHSRIKL--HQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKG 117
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLtgDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529   118 SLKCAQYWPQKEEKEMIFEDtnLKLTLISE-DIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLF 196
Cdd:pfam00102  81 REKCAQYWPEEEGESLEYGD--FTVTLKKEkEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529   197 KVRESgSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDpssVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 276
Cdd:pfam00102 159 KVRKS-SLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGE---VDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 66-271 1.21e-91

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: 275.32  E-value: 1.21e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  66 YINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDtnLKLTLI 145
Cdd:cd00047   1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYGD--ITVTLV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 146 SEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVREsgSLSPEHGPVVVHCSAGIGRSGTF 225
Cdd:cd00047  79 SEEELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRK--EARKPNGPIVVHCSAGVGRTGTF 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15990529 226 CLADTCLLLMDKRKDpssVDIKKVLLEMRKFRMGLIQTADQLRFSY 271
Cdd:cd00047 157 IAIDILLERLEAEGE---VDVFEIVKALRKQRPGMVQTLEQYEFIY 199
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 20-272 3.84e-87

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: 266.54  E-value: 3.84e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  20 YQDIRHE--ASDFPCrvAKLPKNKNRNRYRDVSPFDHSRIKL----HQEDNDYINASLIKMEEAQRSYILTQGPLPNTCG 93
Cdd:cd14543   9 YEDIRREppAGTFLC--SLAPANQEKNRYGDVLCLDQSRVKLpkrnGDERTDYINANFMDGYKQKNAYIATQGPLPKTYS 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  94 HFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDtnLKLTLISEDIKSYYTVRQLELENLTTQETREILH 173
Cdd:cd14543  87 DFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLRYGD--LTVTNLSVENKEHYKKTTLEIHNTETDESRQVTH 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 174 FHYTTWPDFGVPESPASFLNFLFKVRESGSLS-----------PEHGPVVVHCSAGIGRSGTFCLADTCLllmDKRKDPS 242
Cdd:cd14543 165 FQFTSWPDFGVPSSAAALLDFLGEVRQQQALAvkamgdrwkghPPGPPIVVHCSAGIGRTGTFCTLDICL---SQLEDVG 241

                       250       260       270
                ....*....|....*....|....*....|
gi 15990529 243 SVDIKKVLLEMRKFRMGLIQTADQLRFSYL 272
Cdd:cd14543 242 TLNVMQTVRRMRTQRAFSIQTPDQYYFCYK 271
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 45-269 3.85e-75

catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar proteins; R3 subfamily receptor-type phosphotyrosine phosphatases (RPTP) are characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. Vertebrate members include receptor-type tyrosine-protein phosphatase-like O (PTPRO), J (PTPRJ), Q (PTPRQ), B (PTPRB), V (PTPRV) and H (PTPRH). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Most members are PTPs, except for PTPRQ, which dephosphorylates phosphatidylinositide substrates. PTPRV is characterized only in rodents; its function has been lost in humans. Both vertebrate and invertebrate R3 subfamily RPTPs are involved in the control of a variety of cellular processes, including cell growth, differentiation, mitotic cycle and oncogenic transformation.


Pssm-ID: 350396 [Multi-domain]  Cd Length: 222  Bit Score: 234.17  E-value: 3.85e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  45 RYRDVSPFDHSRIKLHQ----EDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLK 120
Cdd:cd14548   1 RYTNILPYDHSRVKLIPineeEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 121 CAQYWPqKEEKEMIFEDtnLKLTLISEDIKSYYTVRQLELENltTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRE 200
Cdd:cd14548  81 CDHYWP-FDQDPVYYGD--ITVTMLSESVLPDWTIREFKLER--GDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRD 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15990529 201 sgSLSPEHGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRF 269
Cdd:cd14548 156 --YIKQEKGPTIVHCSAGVGRTGTFIALDR---LLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIF 219
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 40-274 7.15e-74

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: 231.97  E-value: 7.15e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  40 NKNRNRYRDVSPFDHSRIKLHQEDN-----DYINASLIKMEEAQR-------SYILTQGPLPNTCGHFWEMVWEQKSRGV 107
Cdd:cd14544   1 NKGKNRYKNILPFDHTRVILKDRDPnvpgsDYINANYIRNENEGPttdenakTYIATQGCLENTVSDFWSMVWQENSRVI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 108 VMLNRVMEKGSLKCAQYWPQKEEKEmifEDTNLKLTLISEDIKSYYTVRQLELENL-TTQETREILHFHYTTWPDFGVPE 186
Cdd:cd14544  81 VMTTKEVERGKNKCVRYWPDEGMQK---QYGPYRVQNVSEHDTTDYTLRELQVSKLdQGDPIREIWHYQYLSWPDHGVPS 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 187 SPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQ 266
Cdd:cd14544 158 DPGGVLNFLEDVNQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLDCDIDIQKTIQMVRSQRSGMVQTEAQ 237


                ....*...
gi 15990529 267 LRFSYLAV 274
Cdd:cd14544 238 YKFIYVAV 245
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 40-278 1.34e-73

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: 230.75  E-value: 1.34e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  40 NKNRNRYRDVSPFDHSRIKLHQ----EDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVME 115
Cdd:cd14553   3 NKPKNRYANVIAYDHSRVILQPiegvPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 116 KGSLKCAQYWPQK--EEKEMIFedtnlkLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLN 193
Cdd:cd14553  83 RSRVKCDQYWPTRgtETYGLIQ------VTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLA 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 194 FLFKVRESGslSPEHGPVVVHCSAGIGRSGTFCLADTCLllmDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLA 273
Cdd:cd14553 157 FLRRVKACN--PPDAGPIVVHCSAGVGRTGCFIVIDSML---ERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDA 231


                ....*
gi 15990529 274 VIEGA 278
Cdd:cd14553 232 LLEAV 236
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 35-269 6.75e-72

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: 227.43  E-value: 6.75e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  35 AKLPKNKNRNRYRDVSPFDHSRIKLhQEDNDYINASLIKMEEAQRS----YILTQGPLPNTCGHFWEMVWEQKSRGVVML 110
Cdd:cd14600  35 AKLPQNMDKNRYKDVLPYDATRVVL-QGNEDYINASYVNMEIPSANivnkYIATQGPLPHTCAQFWQVVWEQKLSLIVML 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 111 NRVMEKGSLKCAQYWPQKEEkemIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPAS 190
Cdd:cd14600 114 TTLTERGRTKCHQYWPDPPD---VMEYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTVTHLQYVAWPDHGVPDDSSD 190

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15990529 191 FLNFLFKVResgSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKvllEMRKFRMGLIQTADQLRF 269
Cdd:cd14600 191 FLEFVNYVR---SKRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVR---KMRDQRAMMVQTSSQYKF 263
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 66-276 1.06e-67

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: 214.16  E-value: 1.06e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  66 YINASLIKM--EEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDtNLKLT 143
Cdd:cd14538   1 YINASHIRIpvGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKPLICGG-RLEVS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 144 LISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVResgsLSPEHGPVVVHCSAGIGRSG 223
Cdd:cd14538  80 LEKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMR----RIHNSGPIVVHCSAGIGRTG 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15990529 224 TFCLADTCLLLMDKRKDpssVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 276
Cdd:cd14538 156 VLITIDVALGLIERDLP---FDIQDIVKDLREQRQGMIQTKDQYIFCYKACLE 205
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 44-269 2.26e-67

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: 214.30  E-value: 2.26e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  44 NRYRDVSPFDHSRIKL----HQEDnDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSL 119
Cdd:cd14615   1 NRYNNVLPYDISRVKLsvqsHSTD-DYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 120 KCAQYWPQKEEKEMifedTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVR 199
Cdd:cd14615  80 KCEEYWPSKQKKDY----GDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVR 155

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 200 ESGSLSPEHGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRF 269
Cdd:cd14615 156 EYMKQNPPNSPILVHCSAGVGRTGTFIAIDR---LIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVF 222
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 65-269 2.54e-67

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: 213.34  E-value: 2.54e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  65 DYINASLIKME----EAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQkEEKEMIFEdtNL 140
Cdd:cd14541   1 DYINANYVNMEipgsGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPD-LGETMQFG--NL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 141 KLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEhgPVVVHCSAGIG 220
Cdd:cd14541  78 QITCVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVE--PTVVHCSAGIG 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15990529 221 RSGTFCLADTCLLLMDKRKDPSSVDIKKvllEMRKFRMGLIQTADQLRF 269
Cdd:cd14541 156 RTGVLITMETAMCLIEANEPVYPLDIVR---TMRDQRAMLIQTPSQYRF 201
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 66-269 4.47e-67

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: 212.60  E-value: 4.47e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  66 YINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMifedTNLKLTLI 145
Cdd:cd14549   1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETY----GNIQVTLL 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 146 SEDIKSYYTVRQLELENL------TTQETREILHFHYTTWPDFGVPESPASFLNFlfkVRESGSLSPEH-GPVVVHCSAG 218
Cdd:cd14549  77 STEVLATYTVRTFSLKNLklkkvkGRSSERVVYQYHYTQWPDHGVPDYTLPVLSF---VRKSSAANPPGaGPIVVHCSAG 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15990529 219 IGRSGTFCLADTCLLLMdkrKDPSSVDIKKVLLEMRKFRMGLIQTADQLRF 269
Cdd:cd14549 154 VGRTGTYIVIDSMLQQI---QDKGTVNVFGFLKHIRTQRNYLVQTEEQYIF 201
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 66-271 1.52e-66

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: 211.34  E-value: 1.52e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  66 YINASLIKMEEA-QRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFedtNLKLTL 144
Cdd:cd18533   1 YINASYITLPGTsSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEYG---DLTVEL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 145 IS--EDIKSYYTVRQLELeNLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRS 222
Cdd:cd18533  78 VSeeENDDGGFIVREFEL-SKEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSASLDPPIIVHCSAGVGRT 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15990529 223 GTFCLADTCLLLMDK----RKDPSSVD--IKKVLLEMRKFRMGLIQTADQLRFSY 271
Cdd:cd18533 157 GTFIALDSLLDELKRglsdSQDLEDSEdpVYEIVNQLRKQRMSMVQTLRQYIFLY 211
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 39-275 2.31e-65

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: 209.30  E-value: 2.31e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  39 KNKNRNRYRDVSPFDHSRIKLHQEdNDYINASLIKMEEAQRS--YILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEK 116
Cdd:cd14597   2 ENRKKNRYKNILPYDTTRVPLGDE-GGYINASFIKMPVGDEEfvYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQEVEG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 117 GSLKCAQYWPQKEEKEMIFEDtNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLF 196
Cdd:cd14597  81 GKIKCQRYWPEILGKTTMVDN-RLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLLTFIS 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15990529 197 KVRESGSLspehGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDpssVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVI 275
Cdd:cd14597 160 YMRHIHKS----GPIITHCSAGIGRSGTLICIDVVLGLISKDLD---FDISDIVRTMRLQRHGMVQTEDQYIFCYQVIL 231
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 44-269 6.24e-64

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: 205.51  E-value: 6.24e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  44 NRYRDVSPFDHSRIKL----HQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSL 119
Cdd:cd14619   1 NRFRNVLPYDWSRVPLkpihEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 120 KCAQYWPQkEEKEMIFEdtNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVR 199
Cdd:cd14619  81 KCEHYWPL-DYTPCTYG--HLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLR 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 200 ESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKdpsSVDIKKVLLEMRKFRMGLIQTADQLRF 269
Cdd:cd14619 158 QWLDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEG---LLGPFSFVQKMRENRPLMVQTESQYVF 224
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 39-274 3.27e-63

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: 204.48  E-value: 3.27e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  39 KNKNRNRYRDVSPFDHSRIKLHQED-----NDYINASLIKME--------EAQRSYILTQGPLPNTCGHFWEMVWEQKSR 105
Cdd:cd14605   1 ENKNKNRYKNILPFDHTRVVLHDGDpnepvSDYINANIIMPEfetkcnnsKPKKSYIATQGCLQNTVNDFWRMVFQENSR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 106 GVVMLNRVMEKGSLKCAQYWPqkeEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQET-REILHFHYTTWPDFGV 184
Cdd:cd14605  81 VIVMTTKEVERGKSKCVKYWP---DEYALKEYGVMRVRNVKESAAHDYILRELKLSKVGQGNTeRTVWQYHFRTWPDHGV 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 185 PESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTA 264
Cdd:cd14605 158 PSDPGGVLDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVDCDIDVPKTIQMVRSQRSGMVQTE 237

                       250
                ....*....|
gi 15990529 265 DQLRFSYLAV 274
Cdd:cd14605 238 AQYRFIYMAV 247
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 38-281 3.97e-63

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: 204.73  E-value: 3.97e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  38 PKNKNRNRYRDVSPFDHSRIKLHQEDN-----DYINASLIK-----MEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGV 107
Cdd:cd14606  16 PENKSKNRYKNILPFDHSRVILQGRDSnipgsDYINANYVKnqllgPDENAKTYIASQGCLEATVNDFWQMAWQENSRVI 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 108 VMLNRVMEKGSLKCAQYWPqkeEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQET-REILHFHYTTWPDFGVPE 186
Cdd:cd14606  96 VMTTREVEKGRNKCVPYWP---EVGMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGELiREIWHYQYLSWPDHGVPS 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 187 SPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQ 266
Cdd:cd14606 173 EPGGVLSFLDQINQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLDCDIDIQKTIQMVRAQRSGMVQTEAQ 252

                       250
                ....*....|....*
gi 15990529 267 LRFSYLAViegAKFI 281
Cdd:cd14606 253 YKFIYVAI---AQFI 264
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 44-269 4.61e-63

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: 203.01  E-value: 4.61e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  44 NRYRDVSPFDHSRIKLHQEDND----YINASLIK---MEEaqRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEK 116
Cdd:cd14547   1 NRYKTILPNEHSRVCLPSVDDDplssYINANYIRgydGEE--KAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 117 gSLKCAQYWPqkEEKEMIFEDtnLKLTLISEDIKSYYTVRQLELENLTtqETREILHFHYTTWPDFGVPESPASFLNFLF 196
Cdd:cd14547  79 -KEKCAQYWP--EEENETYGD--FEVTVQSVKETDGYTVRKLTLKYGG--EKRYLKHYWYTSWPDHKTPEAAQPLLSLVQ 151

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15990529 197 KVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTClllMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRF 269
Cdd:cd14547 152 EVEEARQTEPHRGPIVVHCSAGIGRTGCFIATSIG---CQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEF 221
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 38-276 1.42e-61

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: 201.03  E-value: 1.42e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  38 PKNKNRNRYRDVSPFDHSRIKLH------QEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLN 111
Cdd:cd17667  25 PDNKHKNRYINILAYDHSRVKLRplpgkdSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMIT 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 112 RVMEKGSLKCAQYWPQKEEKEMifedTNLKLTLISEDIKSYYTVRQLELENLTT-----------QETREILHFHYTTWP 180
Cdd:cd17667 105 NLVEKGRRKCDQYWPTENSEEY----GNIIVTLKSTKIHACYTVRRFSIRNTKVkkgqkgnpkgrQNERTVIQYHYTQWP 180

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 181 DFGVPESPASFLNFLfkVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLEMRKFRMGL 260
Cdd:cd17667 181 DMGVPEYALPVLTFV--RRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDS---MLQQIKDKSTVNVLGFLKHIRTQRNYL 255

                       250
                ....*....|....*.
gi 15990529 261 IQTADQLRFSYLAVIE 276
Cdd:cd17667 256 VQTEEQYIFIHDALLE 271
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 44-272 2.23e-61

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: 198.99  E-value: 2.23e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  44 NRYRDVSPFDHSRIKLHQEDN----DYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSL 119
Cdd:cd14617   1 NRYNNILPYDSTRVKLSNVDDdpcsDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 120 KCAQYWPQKEEKeMIFEDtnLKLTLISEDIKSYYTVRQLELENLTTQET-REILHFHYTTWPDFGVPESPASFLNFLFKV 198
Cdd:cd14617  81 KCDHYWPADQDS-LYYGD--LIVQMLSESVLPEWTIREFKICSEEQLDApRLVRHFHYTVWPDHGVPETTQSLIQFVRTV 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15990529 199 RESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDkRKDpsSVDIKKVLLEMRKFRMGLIQTADQlrFSYL 272
Cdd:cd14617 158 RDYINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLD-SKD--SVDIYGAVHDLRLHRVHMVQTECQ--YVYL 226
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 1-278 7.32e-61

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: 199.11  E-value: 7.32e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529   1 MEMEKEFEQIDKSgswaaiyQDIRHEASDfpcrvakLPKNKNRNRYRDVSPFDHSRIKLHQED----NDYINASLIKMEE 76
Cdd:cd14626  16 LKFSQEYESIDPG-------QQFTWENSN-------LEVNKPKNRYANVIAYDHSRVILTSVDgvpgSDYINANYIDGYR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  77 AQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQK--EEKEMIfedtnlKLTLISEDIKSYYT 154
Cdd:cd14626  82 KQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRgtETYGMI------QVTLLDTVELATYS 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 155 VRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGslSPEHGPVVVHCSAGIGRSGTFCLADTcllL 234
Cdd:cd14626 156 VRTFALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACN--PPDAGPMVVHCSAGVGRTGCFIVIDA---M 230

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 15990529 235 MDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEGA 278
Cdd:cd14626 231 LERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAA 274
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 20-276 1.05e-60

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: 198.51  E-value: 1.05e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  20 YQDIRHEASDF------PCRVAKLPKNKNRNRYRDVSPFDHSRIKL----HQEDNDYINASLIKMEEAQRSYILTQGPLP 89
Cdd:cd14603   4 FSEIRACSAAFkadyvcSTVAGGRKENVKKNRYKDILPYDQTRVILsllqEEGHSDYINANFIKGVDGSRAYIATQGPLS 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  90 NTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMI--FEDTNLKLTLISEDIksyyTVRQLELEnlTTQE 167
Cdd:cd14603  84 HTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAQEQEPLQTgpFTITLVKEKRLNEEV----ILRTLKVT--FQKE 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 168 TREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEhgPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIK 247
Cdd:cd14603 158 SRSVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPE--PLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSIF 235

                       250       260
                ....*....|....*....|....*....
gi 15990529 248 KVLLEMRKFRMGLIQTADQLRFSYLAVIE 276
Cdd:cd14603 236 DVVLEMRKQRPAAVQTEEQYEFLYHTVAQ 264
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 66-276 1.54e-59

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: 193.83  E-value: 1.54e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  66 YINASLIKMEE--AQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLT 143
Cdd:cd14540   1 YINASHITATVggKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEHDALTFGEYKVS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 144 LISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRE----SGSLSPEHG---PVVVHCS 216
Cdd:cd14540  81 TKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSvrrhTNQDVAGHNrnpPTLVHCS 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 217 AGIGRSGTFCLADTCLLLMDKRKDpssVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 276
Cdd:cd14540 161 AGVGRTGVVILADLMLYCLDHNEE---LDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQ 217
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 22-274 7.09e-59

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: 192.80  E-value: 7.09e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  22 DIRHEASDfpcrvakLPKNKNRNRYRDVSPFDHSRIKL----HQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWE 97
Cdd:cd14614   1 DIPHFAAD-------LPVNRCKNRYTNILPYDFSRVKLvsmhEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWK 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  98 MVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKeMIFEDTNLKltLISEDIKSYYTVRQLELEnlTTQETREILHFHYT 177
Cdd:cd14614  74 MVLQQKSQIIVMLTQCNEKRRVKCDHYWPFTEEP-VAYGDITVE--MLSEEEQPDWAIREFRVS--YADEVQDVMHFNYT 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 178 TWPDFGVPESPA--SFLNFLFKVRESGSLSPehGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLEMRK 255
Cdd:cd14614 149 AWPDHGVPTANAaeSILQFVQMVRQQAVKSK--GPMIIHCSAGVGRTGTFIALDR---LLQHIRDHEFVDILGLVSEMRS 223

                       250
                ....*....|....*....
gi 15990529 256 FRMGLIQTADQLRFSYLAV 274
Cdd:cd14614 224 YRMSMVQTEEQYIFIHQCV 242
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 1-277 7.33e-59

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: 194.16  E-value: 7.33e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529   1 MEMEKEFEQIDKsgswaaiyqdirheASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQED----NDYINASLIKMEE 76
Cdd:cd14625  22 LKLSQEYESIDP--------------GQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEgimgSDYINANYIDGYR 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  77 AQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFedtnLKLTLISEDIKSYYTVR 156
Cdd:cd14625  88 KQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTETYGM----IQVTLLDTIELATFCVR 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 157 QLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGslSPEHGPVVVHCSAGIGRSGTFCLADTcllLMD 236
Cdd:cd14625 164 TFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCN--PPDAGPIVVHCSAGVGRTGCFIVIDA---MLE 238

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 15990529 237 KRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEG 277
Cdd:cd14625 239 RIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEA 279
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 3-276 6.73e-58

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: 191.81  E-value: 6.73e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529   3 MEKEFEQIDK-SGSWAAIyqdIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDN----DYINASLIkMEEA 77
Cdd:cd14610   9 MEDHLKNKNRlEKEWEAL---CAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENShshsDYINASPI-MDHD 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  78 QR--SYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQkeekemifEDTNL----KLTLISEDIKS 151
Cdd:cd14610  85 PRnpAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPD--------EGSNLyhiyEVNLVSEHIWC 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 152 Y-YTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVREsgSLSPEHGPVVVHCSAGIGRSGTFCLADT 230
Cdd:cd14610 157 EdFLVRSFYLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNK--CYRGRSCPIIVHCSDGAGRSGTYILIDM 234

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 15990529 231 CLLLMdkRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 276
Cdd:cd14610 235 VLNKM--AKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 278
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 66-276 6.86e-58

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: 189.19  E-value: 6.86e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  66 YINASLIKME--EAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMifEDTNLKLT 143
Cdd:cd14596   1 YINASYITMPvgEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPM--ELENYQLR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 144 LISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLspehGPVVVHCSAGIGRSG 223
Cdd:cd14596  79 LENYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNT----GPIVVHCSAGIGRAG 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15990529 224 TFCLADTCLLLMDKRkdpSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 276
Cdd:cd14596 155 VLICVDVLLSLIEKD---LSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLE 204
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 3-276 5.77e-57

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: 189.09  E-value: 5.77e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529   3 MEKEFEQIDK-SGSWAAIyqdIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDN----DYINAS-LIKMEE 76
Cdd:cd14609   7 MEDHLRNRDRlAKEWQAL---CAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNpsrsDYINASpIIEHDP 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  77 AQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEK-EMIFEdtnlkLTLISEDIKSY-YT 154
Cdd:cd14609  84 RMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSlYHIYE-----VNLVSEHIWCEdFL 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 155 VRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVREsgSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLL 234
Cdd:cd14609 159 VRSFYLKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNK--CYRGRSCPIIVHCSDGAGRTGTYILIDMVLNR 236

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 15990529 235 MdkRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 276
Cdd:cd14609 237 M--AKGVKEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAE 276
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 66-276 1.28e-56

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: 185.73  E-value: 1.28e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  66 YINASLIkMEEAQRS--YILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQK-EEKEMIFEdtnlkL 142
Cdd:cd14546   1 YINASTI-YDHDPRNpaYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEgSEVYHIYE-----V 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 143 TLISEDIKS-YYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRESgslspEHG---PVVVHCSAG 218
Cdd:cd14546  75 HLVSEHIWCdDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKS-----YRGrscPIVVHCSDG 149

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15990529 219 IGRSGTFCLADtcLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 276
Cdd:cd14546 150 AGRTGTYILID--MVLNRMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 37-272 2.73e-56

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: 186.19  E-value: 2.73e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  37 LPKNKNRNRYRDVSPFDHSRIKL-----HQEDNDYINASLIK-MEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVML 110
Cdd:cd14612  12 IPGHASKDRYKTILPNPQSRVCLrragsQEEEGSYINANYIRgYDGKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMI 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 111 NRVMEKGSlKCAQYWPQKEEKEMIFEdtnlkltLISEDIKSY--YTVRQLELEnlTTQETREILHFHYTTWPDFGVPESP 188
Cdd:cd14612  92 TKLKEKKE-KCVHYWPEKEGTYGRFE-------IRVQDMKECdgYTIRDLTIQ--LEEESRSVKHYWFSSWPDHQTPESA 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 189 ASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADT-CLLLmdkrKDPSSVDIKKVLLEMRKFRMGLIQTADQL 267
Cdd:cd14612 162 GPLLRLVAEVEESRQTAASPGPIVVHCSAGIGRTGCFIATSIgCQQL----KDTGKVDILGIVCQLRLDRGGMIQTSEQY 237


                ....*
gi 15990529 268 RFSYL 272
Cdd:cd14612 238 QFLHH 242
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 30-274 3.33e-56

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: 187.83  E-value: 3.33e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  30 FPCRVAKLPKNKNRNRYRDVSPFDHSRIKL----HQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSR 105
Cdd:cd14604  47 YPTATGEKEENVKKNRYKDILPFDHSRVKLtlktSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVA 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 106 GVVMLNRVMEKGSLKCAQYWPQKEEKEMIFedTNLKLTLISEDIKSYYTVRQLELEnlTTQETREILHFHYTTWPDFGVP 185
Cdd:cd14604 127 IIVMACREFEMGRKKCERYWPLYGEEPMTF--GPFRISCEAEQARTDYFIRTLLLE--FQNETRRLYQFHYVNWPDHDVP 202

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 186 ESPASFLNFLFKVRESGslSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTAD 265
Cdd:cd14604 203 SSFDSILDMISLMRKYQ--EHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKE 280


                ....*....
gi 15990529 266 QLRFSYLAV 274
Cdd:cd14604 281 QYELVHRAI 289
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 65-276 6.07e-56

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: 183.99  E-value: 6.07e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  65 DYINASLIKMEEAQRS----YILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEmifEDTNL 140
Cdd:cd14601   1 DYINANYINMEIPSSSiinrYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSS---SYGGF 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 141 KLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEhgPVVVHCSAGIG 220
Cdd:cd14601  78 QVTCHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDE--PVVVHCSAGIG 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15990529 221 RSGTFCLADTCLLLMDKRKDPSSVDIKKVlleMRKFRMGLIQTADQLRFSYLAVIE 276
Cdd:cd14601 156 RTGVLITMETAMCLIECNQPVYPLDIVRT---MRDQRAMMIQTPSQYRFVCEAILK 208
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 44-269 9.09e-56

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: 184.38  E-value: 9.09e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  44 NRYRDVSPFDHSRIKLHQ----EDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSL 119
Cdd:cd14618   1 NRYPHVLPYDHSRVRLSQlggePHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 120 KCAQYWPQKEEKemiFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVR 199
Cdd:cd14618  81 LCDHYWPSESTP---VSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVR 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 200 ESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKdpsSVDIKKVLLEMRKFRMGLIQTADQLRF 269
Cdd:cd14618 158 EHVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEK---VVDVFNTVYILRMHRYLMIQTLSQYIF 224
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 1-277 1.26e-55

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: 185.71  E-value: 1.26e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529   1 MEMEKEFEQIDKsgswaaiyqdirheASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQED----NDYINASLIKMEE 76
Cdd:cd14624  22 LKFSQEYESIDP--------------GQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEgipgSDYINANYIDGYR 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  77 AQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFedtnLKLTLISEDIKSYYTVR 156
Cdd:cd14624  88 KQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTETYGL----IQVTLLDTVELATYCVR 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 157 QLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGslSPEHGPVVVHCSAGIGRSGTFCLADTcllLMD 236
Cdd:cd14624 164 TFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCN--PPDAGPMVVHCSAGVGRTGCFIVIDA---MLE 238

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 15990529 237 KRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEG 277
Cdd:cd14624 239 RIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEA 279
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 39-277 1.93e-55

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: 183.69  E-value: 1.93e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  39 KNKNRNRYRDVSPFDHSRIKLHQED----NDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVM 114
Cdd:cd14630   2 ENRNKNRYGNIISYDHSRVRLQLLDgdphSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 115 EKGSLKCAQYWPQKEEkemIFEDtnLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNF 194
Cdd:cd14630  82 EVGRVKCVRYWPDDTE---VYGD--IKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGF 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 195 LFKVRESGslSPEHGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAV 274
Cdd:cd14630 157 VRQVKFLN--PPDAGPIVVHCSAGAGRTGCFIAIDI---MLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAI 231


                ...
gi 15990529 275 IEG 277
Cdd:cd14630 232 LEA 234
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 20-281 3.71e-54

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 182.51  E-value: 3.71e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529   20 YQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQED--NDYINASLIKMEEAQRSYILTQGPLPNTCGHFWE 97
Cdd:PHA02742  32 HEHIMQEIVAFSCNESLELKNMKKCRYPDAPCFDRNRVILKIEDggDDFINASYVDGHNAKGRFICTQAPLEETALDFWQ 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529   98 MVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEdtnlKLTLISEDIKS--YYTVRQLELENLTTQETREILHFH 175
Cdd:PHA02742 112 AIFQDQVRVIVMITKIMEDGKEACYPYWMPHERGKATHG----EFKIKTKKIKSfrNYAVTNLCLTDTNTGASLDIKHFA 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  176 YTTWPDFGVPESPASFLNFLFKVRE---------SGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRkdpSSVDI 246
Cdd:PHA02742 188 YEDWPHGGLPRDPNKFLDFVLAVREadlkadvdiKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNER---AIIPL 264

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 15990529  247 KKVLLEMRKFRMGLIQTADQLRFSYLAVIEGAKFI 281
Cdd:PHA02742 265 LSIVRDLRKQRHNCLSLPQQYIFCYFIVLIFAKLM 299
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 43-276 6.79e-54

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: 179.65  E-value: 6.79e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  43 RNRYRDVSPFDHSRIKLH----QEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGS 118
Cdd:cd14602   1 KNRYKDILPYDHSRVELSlitsDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 119 LKCAQYWpqKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLttQETREILHFHYTTWPDFGVPESPASFLNFLFKV 198
Cdd:cd14602  81 KKCERYW--AEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFN--SETRTIYQFHYKNWPDHDVPSSIDPILELIWDV 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15990529 199 ResgSLSP-EHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 276
Cdd:cd14602 157 R---CYQEdDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIE 232
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 44-269 1.44e-53

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: 178.56  E-value: 1.44e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  44 NRYRDVSPFDHSRIKLHQE----DNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSL 119
Cdd:cd14616   1 NRFPNIKPYNNNRVKLIADagvpGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 120 KCAQYWPQKEEKEMIFEDtnLKLTLISEDIKSYYTVRQLELENltTQETREILHFHYTTWPDFGVPESPASFLNFLFKVR 199
Cdd:cd14616  81 RCHQYWPEDNKPVTVFGD--IVITKLMEDVQIDWTIRDLKIER--HGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVR 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 200 esGSLSPEHGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRF 269
Cdd:cd14616 157 --ASRAHDNTPMIVHCSAGVGRTGVFIALDH---LTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIF 221
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 35-273 1.88e-53

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: 178.49  E-value: 1.88e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  35 AKLPKNKNRNRYRDVSPFDHSRIKLHQ----EDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVML 110
Cdd:cd14554   1 ANLPCNKFKNRLVNILPYESTRVCLQPirgvEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 111 NRVMEKGSLKCAQYWPQKEEKEMIFedtnlkltLISEDIKSY----YTVRQLELENLTTQETREILHFHYTTWPDFGVPE 186
Cdd:cd14554  81 TKLREMGREKCHQYWPAERSARYQY--------FVVDPMAEYnmpqYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPK 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 187 SPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCladTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQ 266
Cdd:cd14554 153 SGEGFIDFIGQVHKTKEQFGQEGPITVHCSAGVGRTGVFI---TLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQ 229


                ....*..
gi 15990529 267 LRFSYLA 273
Cdd:cd14554 230 YQFCYRA 236
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 66-271 1.23e-52

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: 175.26  E-value: 1.23e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  66 YINASLIK-MEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDtnLKLTL 144
Cdd:cd14539   1 YINASLIEdLTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQALVYGA--ITVSL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 145 ISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLS-PEHGPVVVHCSAGIGRSG 223
Cdd:cd14539  79 QSVRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQrSLQTPIVVHCSSGVGRTG 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15990529 224 TFCLADTCLLLMdkRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSY 271
Cdd:cd14539 159 AFCLLYAAVQEI--EAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCY 204
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 46-276 2.25e-52

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: 175.51  E-value: 2.25e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  46 YRDVSPFDHSRIKLHQED----NDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKC 121
Cdd:cd14620   1 YPNILPYDHSRVILSQLDgipcSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 122 AQYWPQkeekEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTT---QETREILHFHYTTWPDFGVPESPASFLNFLFKV 198
Cdd:cd14620  81 YQYWPD----QGCWTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPdgcKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKV 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15990529 199 ResgSLSPEH-GPVVVHCSAGIGRSGTFCLADTCLLLMDKRKdpsSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 276
Cdd:cd14620 157 K---SVNPVHaGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQ---KVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 26-277 2.41e-52

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: 176.77  E-value: 2.41e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  26 EASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLH----QEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWE 101
Cdd:cd14633  26 EGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQpiegETSSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWH 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 102 QKSRGVVMLNRVMEKGSLKCAQYWPQKEEkemIFEDtnLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPD 181
Cdd:cd14633 106 ENTASIIMVTNLVEVGRVKCCKYWPDDTE---IYKD--IKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPD 180

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 182 FGVPESPASFLNFLFKVRESGslSPEHGPVVVHCSAGIGRSGTFCLADtclLLMDKRKDPSSVDIKKVLLEMRKFRMGLI 261
Cdd:cd14633 181 HGVPYHATGLLGFVRQVKSKS--PPNAGPLVVHCSAGAGRTGCFIVID---IMLDMAEREGVVDIYNCVRELRSRRVNMV 255

                       250
                ....*....|....*.
gi 15990529 262 QTADQLRFSYLAVIEG 277
Cdd:cd14633 256 QTEEQYVFIHDAILEA 271
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 66-271 2.09e-51

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: 171.84  E-value: 2.09e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  66 YINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEdtNLKLTLI 145
Cdd:cd14542   1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLQFG--PFKISLE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 146 SEDIKSY-YTVRQLELEnlTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEhgPVVVHCSAGIGRSGT 224
Cdd:cd14542  79 KEKRVGPdFLIRTLKVT--FQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDV--PICVHCSAGCGRTGT 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15990529 225 FCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSY 271
Cdd:cd14542 155 ICAIDYVWNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVY 201
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 32-287 4.65e-51

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: 174.06  E-value: 4.65e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  32 CRVAKLPKNKNRNRYRDVSPFDHSRIKLHQ----EDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGV 107
Cdd:cd14621  44 CEAASKEENKEKNRYVNILPYDHSRVHLTPvegvPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATI 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 108 VMLNRVMEKGSLKCAQYWPQkeekEMIFEDTNLKLTLISEDIKSYYTVRQLELENL----TTQETREILHFHYTTWPDFG 183
Cdd:cd14621 124 VMVTNLKERKECKCAQYWPD----QGCWTYGNIRVSVEDVTVLVDYTVRKFCIQQVgdvtNKKPQRLITQFHFTSWPDFG 199

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 184 VPESPASFLNFLFKVResgSLSPEH-GPVVVHCSAGIGRSGTFCLADTCLLLMDKRKdpsSVDIKKVLLEMRKFRMGLIQ 262
Cdd:cd14621 200 VPFTPIGMLKFLKKVK---NCNPQYaGAIVVHCSAGVGRTGTFIVIDAMLDMMHAER---KVDVYGFVSRIRAQRCQMVQ 273

                       250       260
                ....*....|....*....|....*
gi 15990529 263 TADQLRFSYLAVIEgaKFIMGDSSV 287
Cdd:cd14621 274 TDMQYVFIYQALLE--HYLYGDTEL 296
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 20-276 9.89e-51

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: 173.26  E-value: 9.89e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  20 YQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKL--HQEDND-YINASLIK--MEEAQRSYILTQGPLPNTCGH 94
Cdd:cd14599  18 YEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELvpTKENNTgYINASHIKvtVGGEEWHYIATQGPLPHTCHD 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  95 FWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHF 174
Cdd:cd14599  98 FWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHL 177

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 175 HYTTWPDFGVPESPASFLNFLFKV----RESGSLSPE----HGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKdpsSVDI 246
Cdd:cd14599 178 QYTDWPDHGCPEEVQGFLSYLEEIqsvrRHTNSMLDStkncNPPIVVHCSAGVGRTGVVILTELMIGCLEHNE---KVEV 254

                       250       260       270
                ....*....|....*....|....*....|
gi 15990529 247 KKVLLEMRKFRMGLIQTADQLRFSYLAVIE 276
Cdd:cd14599 255 PVMLRHLREQRMFMIQTIAQYKFVYQVLIQ 284
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 3-276 1.79e-50

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


Pssm-ID: 350476 [Multi-domain]  Cd Length: 292  Bit Score: 172.61  E-value: 1.79e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529   3 MEKEFEQIDKSGSWAAiyqdiRHEASDFPCrvaklpkNKNRNRYRDVSPFDHSRIKLHQ----EDNDYINASLIKMEEAQ 78
Cdd:cd14628  27 MELEFKRLASSKAHTS-----RFISANLPC-------NKFKNRLVNIMPYESTRVCLQPirgvEGSDYINASFIDGYRQQ 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  79 RSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFedtnLKLTLISEDIKSYYTVRQL 158
Cdd:cd14628  95 KAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQY----FVVDPMAEYNMPQYILREF 170

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 159 ELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCladTCLLLMDKR 238
Cdd:cd14628 171 KVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFI---TLSIVLERM 247

                       250       260       270
                ....*....|....*....|....*....|....*...
gi 15990529 239 KDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 276
Cdd:cd14628 248 RYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALE 285
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 3-276 4.01e-49

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


Pssm-ID: 350475 [Multi-domain]  Cd Length: 290  Bit Score: 169.14  E-value: 4.01e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529   3 MEKEFEQIDKSGSWAAiyqdiRHEASDFPCrvaklpkNKNRNRYRDVSPFDHSRIKLHQ----EDNDYINASLIKMEEAQ 78
Cdd:cd14627  28 MELEFKRLANSKAHTS-----RFISANLPC-------NKFKNRLVNIMPYETTRVCLQPirgvEGSDYINASFIDGYRQQ 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  79 RSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFedtnLKLTLISEDIKSYYTVRQL 158
Cdd:cd14627  96 KAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPAERSARYQY----FVVDPMAEYNMPQYILREF 171

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 159 ELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCladTCLLLMDKR 238
Cdd:cd14627 172 KVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFI---TLSIVLERM 248

                       250       260       270
                ....*....|....*....|....*....|....*...
gi 15990529 239 KDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 276
Cdd:cd14627 249 RYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALE 286
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 66-276 4.44e-49

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: 165.86  E-value: 4.44e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  66 YINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEkemIFEDtnLKLTLI 145
Cdd:cd14555   1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTE---VYGD--IKVTLV 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 146 SEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGslSPEHGPVVVHCSAGIGRSGTF 225
Cdd:cd14555  76 ETEPLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASN--PPSAGPIVVHCSAGAGRTGCY 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15990529 226 CLADTcllLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 276
Cdd:cd14555 154 IVIDI---MLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 66-271 1.46e-48

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: 164.49  E-value: 1.46e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  66 YINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKemiFEDtnLKLTLI 145
Cdd:cd14558   1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKT---YGD--IEVELK 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 146 SEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRESG----SLSPEHGPVVVHCSAGIGR 221
Cdd:cd14558  76 DTEKSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLpyknSKHGRSVPIVVHCSDGSSR 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15990529 222 SGTFCladtCLL-LMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSY 271
Cdd:cd14558 156 TGIFC----ALWnLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 66-275 5.48e-48

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: 163.23  E-value: 5.48e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  66 YINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMifedTNLKLTLI 145
Cdd:cd17668   1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEY----GNFLVTQK 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 146 SEDIKSYYTVRQLELENLTT--------QETREILHFHYTTWPDFGVPESPASFLNFLFKvrESGSLSPEHGPVVVHCSA 217
Cdd:cd17668  77 SVQVLAYYTVRNFTLRNTKIkkgsqkgrPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRK--ASYAKRHAVGPVVVHCSA 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15990529 218 GIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVI 275
Cdd:cd17668 155 GVGRTGTYIVLDS---MLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 45-276 1.40e-47

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


Pssm-ID: 350471 [Multi-domain]  Cd Length: 228  Bit Score: 162.91  E-value: 1.40e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  45 RYRDVSPFDHSRI----KLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLK 120
Cdd:cd14623   1 RVLQIIPYEFNRViipvKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 121 CAQYWPQkeEKEMIFEDTNLKLTliSEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRE 200
Cdd:cd14623  81 CAQYWPS--DGSVSYGDITIELK--KEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQK 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15990529 201 SGSLSPEHgPVVVHCSAGIGRSGTFCLADTCLllmDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 276
Cdd:cd14623 157 QQQQSGNH-PITVHCSAGAGRTGTFCALSTVL---ERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 35-276 3.34e-47

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


Pssm-ID: 350477 [Multi-domain]  Cd Length: 291  Bit Score: 164.13  E-value: 3.34e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  35 AKLPKNKNRNRYRDVSPFDHSRIKLHQ----EDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVML 110
Cdd:cd14629  48 ANLPCNKFKNRLVNIMPYELTRVCLQPirgvEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVML 127

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 111 NRVMEKGSLKCAQYWPQKEEKEMIFedtnLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPAS 190
Cdd:cd14629 128 TKLREMGREKCHQYWPAERSARYQY----FVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEG 203

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 191 FLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCladTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFS 270
Cdd:cd14629 204 FIDFIGQVHKTKEQFGQDGPITVHCSAGVGRTGVFI---TLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLC 280


                ....*.
gi 15990529 271 YLAVIE 276
Cdd:cd14629 281 YRAALE 286
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 66-271 7.97e-47

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: 160.32  E-value: 7.97e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  66 YINASLIKMEEAQR--SYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSL-KCAQYWPQKEEKEMIFEDTNLKL 142
Cdd:cd17658   1 YINASLVETPASESlpKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPAEENESREFGRISVTN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 143 TLISEDIKSyYTVRQLELENLTTQET-REILHFHYTTWPDFGVPESPASFLNFLfkvRESGSLSPEHGPVVVHCSAGIGR 221
Cdd:cd17658  81 KKLKHSQHS-ITLRVLEVQYIESEEPpLSVLHIQYPEWPDHGVPKDTRSVRELL---KRLYGIPPSAGPIVVHCSAGIGR 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15990529 222 SGTFCLADTCLLLMDKrKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSY 271
Cdd:cd17658 157 TGAYCTIHNTIRRILE-GDMSAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 43-269 1.37e-46

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: 160.08  E-value: 1.37e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  43 RNRYRDVSPFDHSRIKLHQEDND-----YINASLIK-MEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEK 116
Cdd:cd14611   2 KNRYKTILPNPHSRVCLKPKNSNdslstYINANYIRgYGGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 117 GSlKCAQYWPqkeEKEMIFEDTNLKLTLISEdiKSYYTVRQLELENltTQETREILHFHYTTWPDFGVPESPASFLNFLF 196
Cdd:cd14611  82 NE-KCVLYWP---EKRGIYGKVEVLVNSVKE--CDNYTIRNLTLKQ--GSQSRSVKHYWYTSWPDHKTPDSAQPLLQLML 153

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15990529 197 KVRESGSLSPEHGPVVVHCSAGIGRSGTFcLADT--CLLLmdkrKDPSSVDIKKVLLEMRKFRMGLIQTADQLRF 269
Cdd:cd14611 154 DVEEDRLASPGRGPVVVHCSAGIGRTGCF-IATTigCQQL----KEEGVVDVLSIVCQLRVDRGGMVQTSEQYEF 223
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 66-271 1.70e-46

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: 159.31  E-value: 1.70e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  66 YINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMifedTNLKLTLI 145
Cdd:cd14551   1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTY----GNLRVRVE 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 146 SEDIKSYYTVRQL----ELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVResgSLSPEH-GPVVVHCSAGIG 220
Cdd:cd14551  77 DTVVLVDYTTRKFciqkVNRGIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVK---SANPPRaGPIVVHCSAGVG 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15990529 221 RSGTFCLADTcllLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSY 271
Cdd:cd14551 154 RTGTFIVIDA---MLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
PHA02738 PHA02738
hypothetical protein; Provisional
 39-274 2.05e-46

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 162.79  E-value: 2.05e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529   39 KNKNRNRYRDVSPFDHSRIKLHQEDN--DYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEK 116
Cdd:PHA02738  48 KNRKLNRYLDAVCFDHSRVILPAERNrgDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKEN 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  117 GSLKCAQYWPQKEEKEMIFedTNLKLTLISEDIKSYYTVRQLELENlTTQETREILHFHYTTWPDFGVPESPASFLNFLF 196
Cdd:PHA02738 128 GREKCFPYWSDVEQGSIRF--GKFKITTTQVETHPHYVKSTLLLTD-GTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVL 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  197 KVRES-----------GSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKdpsSVDIKKVLLEMRKFRMGLIQTAD 265
Cdd:PHA02738 205 EVRQCqkelaqeslqiGHNRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACA---TVSIPSIVSSIRNQRYYSLFIPF 281


                 ....*....
gi 15990529  266 QLRFSYLAV 274
Cdd:PHA02738 282 QYFFCYRAV 290
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 66-274 7.91e-46

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: 157.43  E-value: 7.91e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  66 YINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPqkEEKEMIFEDTNLKLTli 145
Cdd:cd14552   1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWP--EDGSVSSGDITVELK-- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 146 SEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEHgPVVVHCSAGIGRSGTF 225
Cdd:cd14552  77 DQTDYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSGNH-PITVHCSAGAGRTGTF 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15990529 226 CLADTCLllmDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAV 274
Cdd:cd14552 156 CALSTVL---ERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 7-274 8.02e-46

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 161.35  E-value: 8.02e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529    7 FEQIDKSGSWAAIYQDiRHEASDFPCRVAK----LPKNKNRNRYRDVSPFDHSRIKLH---------------------Q 61
Cdd:PHA02746  15 FDKTNHAKFCEFVLLE-HAEVMDIPIRGTTnhflKKENLKKNRFHDIPCWDHSRVVINaheslkmfdvgdsdgkkievtS 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529   62 EDND--YINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVmEKGSLKCAQYWPQKEEKEMIFEDTN 139
Cdd:PHA02746  94 EDNAenYIHANFVDGFKEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTDI-DDDDEKCFELWTKEEDSELAFGRFV 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  140 LKLTLISEDikSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRE--------SGSLSPEHGPV 211
Cdd:PHA02746 173 AKILDIIEE--LSFTKTRLMITDKISDTSREIHHFWFPDWPDNGIPTGMAEFLELINKVNEeqaelikqADNDPQTLGPI 250

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15990529  212 VVHCSAGIGRSGTFCLADTCLLLMDKRKdpsSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAV 274
Cdd:PHA02746 251 VVHCSAGIGRAGTFCAIDNALEQLEKEK---EVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 43-269 1.48e-45

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: 158.49  E-value: 1.48e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  43 RNRYRDVSPFDHSRIKLHQEDND-----YINASLIK-MEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEK 116
Cdd:cd14613  28 KNRYKTILPNPHSRVCLTSPDQDdplssYINANYIRgYGGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 117 GSlKCAQYWPqkeEKEMIFE--DTNLKLTLISEDiksyYTVRQLELEnlTTQETREILHFHYTTWPDFGVPESPASFLNF 194
Cdd:cd14613 108 NE-KCTEYWP---EEQVTYEgiEITVKQVIHADD----YRLRLITLK--SGGEERGLKHYWYTSWPDQKTPDNAPPLLQL 177

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15990529 195 LFKVRESGSLSPE-HGPVVVHCSAGIGRSGTFCLADTCLLLMdkrKDPSSVDIKKVLLEMRKFRMGLIQTADQLRF 269
Cdd:cd14613 178 VQEVEEARQQAEPnCGPVIVHCSAGIGRTGCFIATSICCKQL---RNEGVVDILRTTCQLRLDRGGMIQTCEQYQF 250
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 66-266 4.20e-45

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: 155.37  E-value: 4.20e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  66 YINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTli 145
Cdd:cd14557   1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKIN-- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 146 SEDIKSYYTVRQLELENLTTQET-REILHFHYTTWPDFGVPESPasflNFLFKVRE-----SGSLSpehGPVVVHCSAGI 219
Cdd:cd14557  79 EEKICPDYIIRKLNINNKKEKGSgREVTHIQFTSWPDHGVPEDP----HLLLKLRRrvnafNNFFS---GPIVVHCSAGV 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15990529 220 GRSGTFCLADTcllLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQ 266
Cdd:cd14557 152 GRTGTYIGIDA---MLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQ 195
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 64-277 8.29e-45

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: 155.18  E-value: 8.29e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  64 NDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEkemIFEDtnLKLT 143
Cdd:cd14631  13 SDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTE---VYGD--FKVT 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 144 LISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGslSPEHGPVVVHCSAGIGRSG 223
Cdd:cd14631  88 CVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSN--PPSAGPIVVHCSAGAGRTG 165

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15990529 224 TFCLADtclLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEG 277
Cdd:cd14631 166 CYIVID---IMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEA 216
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 66-277 3.66e-44

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: 153.28  E-value: 3.66e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  66 YINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPqkEEKEMIfedTNLKLTLI 145
Cdd:cd14632   1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWP--DDSDTY---GDIKITLL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 146 SEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVResGSLSPEHGPVVVHCSAGIGRSGTF 225
Cdd:cd14632  76 KTETLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVK--ASTPPDAGPVVVHCSAGAGRTGCY 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15990529 226 CLADtclLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEG 277
Cdd:cd14632 154 IVLD---VMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEA 202
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 38-269 2.82e-42

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 151.31  E-value: 2.82e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529   38 PKNKNRNRYRDVSPFDHSRIKLHQ---EDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVM 114
Cdd:PHA02747  49 PENQPKNRYWDIPCWDHNRVILDSgggSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPTK 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  115 E-KGSLKCAQYWPQKEEKEMIFEDTNLKLTLISedIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLN 193
Cdd:PHA02747 129 GtNGEEKCYQYWCLNEDGNIDMEDFRIETLKTS--VRAKYILTLIEITDKILKDSRKISHFQCSEWFEDETPSDHPDFIK 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  194 FLFKV----RESGSL-SPEHG---PVVVHCSAGIGRSGTFCLADTCLLLMDKRKdpsSVDIKKVLLEMRKFRMGLIQTAD 265
Cdd:PHA02747 207 FIKIIdinrKKSGKLfNPKDAllcPIVVHCSDGVGKTGIFCAVDICLNQLVKRK---AICLAKTAEKIREQRHAGIMNFD 283


                 ....
gi 15990529  266 QLRF 269
Cdd:PHA02747 284 DYLF 287
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
170-276 1.84e-41

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 142.50  E-value: 1.84e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529    170 EILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDpsSVDIKKV 249
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAG--EVDIFDT 78

                           90       100
                   ....*....|....*....|....*..
gi 15990529    250 LLEMRKFRMGLIQTADQLRFSYLAVIE 276
Cdd:smart00404  79 VKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 170-276 1.84e-41

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: 142.50  E-value: 1.84e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529    170 EILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDpsSVDIKKV 249
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAG--EVDIFDT 78

                           90       100
                   ....*....|....*....|....*..
gi 15990529    250 LLEMRKFRMGLIQTADQLRFSYLAVIE 276
Cdd:smart00012  79 VKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 66-276 2.16e-41

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: 146.27  E-value: 2.16e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  66 YINASLIKME--EAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLT 143
Cdd:cd14598   1 YINASHIKVTvgGKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSRHNTVTYGRFKIT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 144 LISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKV----RESGSLSPEHG---PVVVHCS 216
Cdd:cd14598  81 TRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIqsvrRHTNSTIDPKSpnpPVLVHCS 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 217 AGIGRSGTFCLADTCLLLMDKRKdpsSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 276
Cdd:cd14598 161 AGVGRTGVVILSEIMIACLEHNE---MLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQ 217
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
36-267 7.98e-41

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 146.77  E-value: 7.98e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  36 KLPKNKNRNRYRDVSPFDHSRIklhQEDNDYINASLIKMEEAQRsYILTQGPLPNTCGHFWEMVWEQKSRGVVML--NRV 113
Cdd:COG5599  38 QNINGSPLNRFRDIQPYKETAL---RANLGYLNANYIQVIGNHR-YIATQYPLEEQLEDFFQMLFDNNTPVLVVLasDDE 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 114 MEKGSLKCAQYWPQKEEkemifedtNLKLTLISEDIKSYYTVRQLELENL------TTQETREILHFHYTTWPDFGVPES 187
Cdd:COG5599 114 ISKPKVKMPVYFRQDGE--------YGKYEVSSELTESIQLRDGIEARTYvltikgTGQKKIEIPVLHVKNWPDHGAISA 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 188 PAsFLNFLFKVRES-GSLSPEHGPVVVHCSAGIGRSGTFcLADTCLLLMDKRKDPSSVDIKKVLLEMRKFR-MGLIQTAD 265
Cdd:COG5599 186 EA-LKNLADLIDKKeKIKDPDKLLPVVHCRAGVGRTGTL-IACLALSKSINALVQITLSVEEIVIDMRTSRnGGMVQTSE 263


                ..
gi 15990529 266 QL 267
Cdd:COG5599 264 QL 265
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 65-274 7.99e-39

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: 138.98  E-value: 7.99e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  65 DYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQkeEKEMIFEDTNLKLTl 144
Cdd:cd14622   1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPS--EGSVTHGEITIEIK- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 145 iSEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEHgPVVVHCSAGIGRSGT 224
Cdd:cd14622  78 -NDTLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTGNH-PIVVHCSAGAGRTGT 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15990529 225 FCLADTcllLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAV 274
Cdd:cd14622 156 FIALSN---ILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 66-271 1.34e-38

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: 138.31  E-value: 1.34e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  66 YINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRvMEKGSLKCAQYWPQKEEKEMifedTNLKLTLI 145
Cdd:cd14556   1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQ-LDPKDQSCPQYWPDEGSGTY----GPIQVEFV 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 146 SEDIKSYYTVRQLELENLT--TQETREILHFHYTTWPDFG-VPESPASFLNFLFKV----RESGSlspehGPVVVHCSAG 218
Cdd:cd14556  76 STTIDEDVISRIFRLQNTTrpQEGYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVekwqEQSGE-----GPIVVHCLNG 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15990529 219 IGRSGTFCladTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSY 271
Cdd:cd14556 151 VGRSGVFC---AISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 66-271 6.13e-33

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: 123.20  E-value: 6.13e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  66 YINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGslKCAQYWPQKeEKEMIFEdtNLKLTLI 145
Cdd:cd14550   1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTK-EKPLECE--TFKVTLS 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 146 SEDIKSY-----YTVRQLELENltTQETR--EILHFHYTTWPDfgvPESPAS-FLNFLFKVRESGSLSpeHGPVVVHCSA 217
Cdd:cd14550  76 GEDHSCLsneirLIVRDFILES--TQDDYvlEVRQFQCPSWPN---PCSPIHtVFELINTVQEWAQQR--DGPIVVHDRY 148

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15990529 218 GIGRSGTFCLADTcllLMDKRKDPSSVDIKKV--LLEMRkfRMGLIQTADQLRFSY 271
Cdd:cd14550 149 GGVQAATFCALTT---LHQQLEHESSVDVYQVakLYHLM--RPGVFTSKEDYQFLY 199
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 66-276 4.48e-27

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: 107.41  E-value: 4.48e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  66 YINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRvMEKGSLkCAQYWPQKEEKEMifedTNLKLTLI 145
Cdd:cd14634   1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNE-MDAAQL-CMQYWPEKTSCCY----GPIQVEFV 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 146 SEDIKSYYTVRQLELENLTTQET--REILHFHYTTWPDFgvPESPASFLNFLFKVRESGSLSPEH----GPVVVHCSAGI 219
Cdd:cd14634  75 SADIDEDIISRIFRICNMARPQDgyRIVQHLQYIGWPAY--RDTPPSKRSILKVVRRLEKWQEQYdgreGRTVVHCLNGG 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15990529 220 GRSGTFC-LADTCLLLMDKrkdpSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 276
Cdd:cd14634 153 GRSGTFCaICSVCEMIQQQ----NIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 66-276 1.36e-26

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: 106.15  E-value: 1.36e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  66 YINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSL-KCAQYWPQKEEKEMIFEDTNLKLTL 144
Cdd:cd14637   1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGLQQYGPMEVEFVSGS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 145 ISEDIKSyytvRQLELENLTTQETREIL--HFHYTTWPDF-GVPESPASFLNFLFKV----RESGSlspehGPVVVHCSA 217
Cdd:cd14637  81 ADEDIVT----RLFRVQNITRLQEGHLMvrHFQFLRWSAYrDTPDSKKAFLHLLASVekwqRESGE-----GRTVVHCLN 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15990529 218 GIGRSGTFCladTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 276
Cdd:cd14637 152 GGGRSGTYC---ASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 40-282 2.27e-24

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 102.35  E-value: 2.27e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529   40 NKNRNRYRD------VSPFDHSRIKLhQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRV 113
Cdd:PHA02740  47 AQAENKAKDenlalhITRLLHRRIKL-FNDEKVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRH 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  114 MEKgslKC-AQYWPQKEEKEMIFEDTNLK-LTLIsedIKSYYTVRQLELENLTTQEtREILHFHYTTWPDFGVPESPASF 191
Cdd:PHA02740 126 ADK---KCfNQFWSLKEGCVITSDKFQIEtLEII---IKPHFNLTLLSLTDKFGQA-QKISHFQYTAWPADGFSHDPDAF 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  192 LNFLFKVRESGSLSPEH------GPVVVHCSAGIGRSGTFCLADTCLLLMDKrkdPSSVDIKKVLLEMRKFRMGLIQTAD 265
Cdd:PHA02740 199 IDFFCNIDDLCADLEKHkadgkiAPIIIDCIDGISSSAVFCVFDICATEFDK---TGMLSIANALKKVRQKKYGCMNCLD 275

                        250
                 ....*....|....*....
gi 15990529  266 QLRFSY--LAVIEGAKFIM 282
Cdd:PHA02740 276 DYVFCYhlIAAYLKEKFDI 294
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 66-275 2.86e-24

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: 99.68  E-value: 2.86e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  66 YINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAqYWPQKEEKeMIFEdtNLKLTLI 145
Cdd:cd17669   1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPNKDEP-INCE--TFKVTLI 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 146 SEDIKSYYTVRQLELENLTTQETR-----EILHFHYTTWPDfgvPESPASFLNFLFKVRESGSlSPEHGPVVVHCSAGIG 220
Cdd:cd17669  77 AEEHKCLSNEEKLIIQDFILEATQddyvlEVRHFQCPKWPN---PDSPISKTFELISIIKEEA-ANRDGPMIVHDEHGGV 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15990529 221 RSGTFCLADTcllLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVI 275
Cdd:cd17669 153 TAGTFCALTT---LMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 66-276 5.65e-23

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: 96.30  E-value: 5.65e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  66 YINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVmEKGSLkCAQYWPQKEekemIFEDTNLKLTLI 145
Cdd:cd14635   1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDV-DPAQL-CPQYWPENG----VHRHGPIQVEFV 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 146 SEDIKSYYTVRQLELENLTTQET--REILHFHYTTWPDFgvPESPASFLNFLFKVRESGSLSPEH----GPVVVHCSAGI 219
Cdd:cd14635  75 SADLEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMY--RDTPVSKRSFLKLIRQVDKWQEEYnggeGRTVVHCLNGG 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15990529 220 GRSGTFC-LADTCLLLMDKRkdpsSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 276
Cdd:cd14635 153 GRSGTFCaISIVCEMLRHQR----AVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 66-275 1.92e-22

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: 94.75  E-value: 1.92e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  66 YINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVML--NRVMEKGSLkcaQYWPQKEEKemiFEDTNLKLT 143
Cdd:cd17670   1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdNQGLAEDEF---VYWPSREES---MNCEAFTVT 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 144 LISEDIKSYYTVRQLELENLTTQETR-----EILHFHYTTWPDfgvPESPASFLNFLFKVRESGSLSPEhGPVVVHCSAG 218
Cdd:cd17670  75 LISKDRLCLSNEEQIIIHDFILEATQddyvlEVRHFQCPKWPN---PDAPISSTFELINVIKEEALTRD-GPTIVHDEFG 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15990529 219 IGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVI 275
Cdd:cd17670 151 AVSAGTLCALTT---LSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 66-276 1.94e-22

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: 94.71  E-value: 1.94e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  66 YINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRV-MEKGslkCAQYWPqkEEKEMIFEDTNLKLTL 144
Cdd:cd14636   1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVdLAQG---CPQYWP--EEGMLRYGPIQVECMS 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 145 ISEDIKsyYTVRQLELENLTTQETREIL--HFHYTTWPDF-GVPESPASFLNFLFKVRESGSLSPE-HGPVVVHCSAGIG 220
Cdd:cd14636  76 CSMDCD--VISRIFRICNLTRPQEGYLMvqQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEECDEgEGRTIIHCLNGGG 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15990529 221 RSGTFClADTCLLLMDKRKDpsSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 276
Cdd:cd14636 154 RSGMFC-AISIVCEMIKRQN--VVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
144-269 2.95e-12

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 63.84  E-value: 2.95e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 144 LISEDIKSYYTVRQLELENLTTQETREILHFHYTtWPDFGVPEsPASFLNFLFKVREsgsLSPEHGPVVVHCSAGIGRSG 223
Cdd:COG2453  21 LKREGIDAVVSLTEEEELLLGLLEEAGLEYLHLP-IPDFGAPD-DEQLQEAVDFIDE---ALREGKKVLVHCRGGIGRTG 95

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 15990529 224 TFCLadtCLLLMDKrkdpssVDIKKVLLEMRKFRMGLIQTADQLRF 269
Cdd:COG2453  96 TVAA---AYLVLLG------LSAEEALARVRAARPGAVETPAQRAF 132
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 44-267 5.08e-10

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: 59.34  E-value: 5.08e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529  44 NRYRDVSpfdhSRIKLhqEDNDYINASLIKMEEaQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVML--NRVMEKGSLKc 121
Cdd:cd14559   1 NRFTNIQ----TRVST--PVGKNLNANRVQIGN-KNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLasNKDIQRKGLP- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 122 aQYWPQKEEKEmifedtnlKLTLISEDIKSYYTVRQLELE--NLTT---QETREILHFHYTTWPDFG------------- 183
Cdd:cd14559  73 -PYFRQSGTYG--------SVTVKSKKTGKDELVDGLKADmyNLKItdgNKTITIPVVHVTNWPDHTaisseglkeladl 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 184 VPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFcLADTCLLlmdkrKDPSSVDIKKVLLEMRKFRMG-LIQ 262
Cdd:cd14559 144 VNKSAEEKRNFYKSKGSSAINDKNKLLPVIHCRAGVGRTGQL-AAAMELN-----KSPNNLSVEDIVSDMRTSRNGkMVQ 217


                ....*
gi 15990529 263 TADQL 267
Cdd:cd14559 218 KDEQL 222
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 180-269 1.66e-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: 56.13  E-value: 1.66e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 180 PDFGVP--ESPASFLNFLFKVRESGslspehGPVVVHCSAGIGRSGTFcLAdtCLLLMdKRKDPSSVDIKKVllemRKFR 257
Cdd:cd14504  58 EDYTPPtlEQIDEFLDIVEEANAKN------EAVLVHCLAGKGRTGTM-LA--CYLVK-TGKISAVDAINEI----RRIR 123

                        90
                ....*....|..
gi 15990529 258 MGLIQTADQLRF 269
Cdd:cd14504 124 PGSIETSEQEKF 135
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 142-269 4.89e-09

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


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 54.96  E-value: 4.89e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 142 LTLISEDIKSYYTVRQLelenLTTQETREILHFHYTTwPDFGVPESPASFLN---FLFKVRESGslspehGPVVVHCSAG 218
Cdd:cd14505  48 VTLCTDGELEELGVPDL----LEQYQQAGITWHHLPI-PDGGVPSDIAQWQElleELLSALENG------KKVLIHCKGG 116

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 15990529 219 IGRSGTFCladTCLLLMDKRKDPSSVDIKKVllemRKFRMGLIQTADQLRF 269
Cdd:cd14505 117 LGRTGLIA---ACLLLELGDTLDPEQAIAAV----RALRPGAIQTPKQENF 160
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 204-269 4.51e-07

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: 48.11  E-value: 4.51e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15990529 204 LSPEHgPVVVHCSAGIGRSGTFCladTCLLLMDKRKDPssvdiKKVLLEMRKFR-MGLIQTADQLRF 269
Cdd:cd14494  53 EKPGE-PVLVHCKAGVGRTGTLV---ACYLVLLGGMSA-----EEAVRIVRLIRpGGIPQTIEQLDF 110
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 174-269 1.56e-05

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: 45.80  E-value: 1.56e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 174 FHYTTWPDFGVPeSPASFLN----FLFKVRESGSlspehgpVVVHCSAGIGRSGtfcLADTCLLLMDKRKDPSSVdIKKV 249
Cdd:cd14506  79 FYNFGWKDYGVP-SLTTILDivkvMAFALQEGGK-------VAVHCHAGLGRTG---VLIACYLVYALRMSADQA-IRLV 146

                        90       100
                ....*....|....*....|
gi 15990529 250 llemRKFRMGLIQTADQLRF 269
Cdd:cd14506 147 ----RSKRPNSIQTRGQVLC 162
DSP_MKP_classI cd14565
dual specificity phosphatase domain of class I mitogen-activated protein kinase phosphatase; ...
 173-228 5.26e-05

dual specificity phosphatase domain of class I 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 I MKPs consist of DUSP1/MKP-1, DUSP2 (PAC1), DUSP4/MKP-2 and DUSP5. They are all mitogen- and stress-inducible nuclear MKPs. 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: 350413 [Multi-domain]  Cd Length: 138  Bit Score: 42.76  E-value: 5.26e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15990529 173 HFHYTTWP--DFGVPESPASF---LNFLFKVRESGslspehGPVVVHCSAGIGRSGTFCLA 228
Cdd:cd14565  44 HFQYKSIPveDSHNADISSWFeeaIGFIDKVKASG------GRVLVHCQAGISRSATICLA 98
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 193-239 5.86e-05

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: 42.63  E-value: 5.86e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 15990529   193 NFLFKVRESGslspehGPVVVHCSAGIGRSGTFCLAdtclLLMDKRK 239
Cdd:pfam00782  60 EFIDDARQKG------GKVLVHCQAGISRSATLIIA----YLMKTRN 96
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 162-271 8.21e-05

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: 42.95  E-value: 8.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 162 NLTTQETREILHFHyTTWPDFGVPESPASFLNFLFKVRESG----SLSPEHgPVVVHCSAGIGRSGTFCladTCLLLMDK 237
Cdd:cd14497  47 NLSEEEYDDDSKFE-GRVLHYGFPDHHPPPLGLLLEIVDDIdswlSEDPNN-VAVVHCKAGKGRTGTVI---CAYLLYYG 121

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15990529 238 RKdpSSVDIKKVLLEMRKFRMGL--IQTADQLRFSY 271
Cdd:cd14497 122 QY--STADEALEYFAKKRFKEGLpgVTIPSQLRYLQ 155
DUSP14 cd14572
dual specificity protein phosphatase 14; dual specificity protein phosphatase 14 (DUSP14), ...
 173-228 9.16e-05

dual specificity protein phosphatase 14; dual specificity protein phosphatase 14 (DUSP14), also called mitogen-activated protein kinase (MAPK) phosphatase 6 (MKP-6) or MKP-1-like protein tyrosine phosphatase (MKP-L), 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. DUSP14 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. DUSP14 dephosphorylates JNK, ERK, and p38 in vitro. It also directly interacts and dephosphorylates TGF-beta-activated kinase 1 (TAK1)-binding protein 1 (TAB1) in T cells, and negatively regulates TCR signaling and immune responses.


Pssm-ID: 350420 [Multi-domain]  Cd Length: 150  Bit Score: 42.55  E-value: 9.16e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15990529 173 HFHYTTWPDFGVPESPASfLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLA 228
Cdd:cd14572  51 QFEYVKVPLADMPHAPIS-LYFDSVADKIHSVGRKHGATLVHCAAGVSRSATLCIA 105
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
207-239 1.16e-04

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 41.88  E-value: 1.16e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 15990529    207 EHGPVVVHCSAGIGRSGTFCLAdtclLLMDKRK 239
Cdd:smart00195  77 KGGKVLVHCQAGVSRSATLIIA----YLMKTRN 105
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 207-239 2.82e-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: 40.61  E-value: 2.82e-04
                        10        20        30
                ....*....|....*....|....*....|...
gi 15990529 207 EHGPVVVHCSAGIGRSGTFCLAdtclLLMDKRK 239
Cdd:cd14498  78 KGGKVLVHCQAGVSRSATIVIA----YLMKKYG 106
DUSP14-like cd14514
dual specificity protein phosphatases 14, 18, 21, 28 and similar proteins; This family is ...
 208-228 1.30e-03

dual specificity protein phosphatases 14, 18, 21, 28 and similar proteins; This family is composed of dual specificity protein phosphatase 14 (DUSP14, also known as MKP-6), 18 (DUSP18), 21 (DUSP21), 28 (DUSP28), and similar proteins. They function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48), and are atypical DUSPs. They contain the catalytic dual specificity phosphatase domain but lack the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. DUSP14 directly interacts and dephosphorylates TGF-beta-activated kinase 1 (TAK1)-binding protein 1 (TAB1) in T cells, and negatively regulates TCR signaling and immune responses. DUSP18 has been shown to interact and dephosphorylate SAPK/JNK, and may play a role in regulating the SAPK/JNK pathway. DUSP18 and DUSP21 target to opposing sides of the mitochondrial inner membrane. DUSP28 has been implicated in hepatocellular carcinoma progression and in migratory activity and drug resistance of pancreatic cancer cells.


Pssm-ID: 350364 [Multi-domain]  Cd Length: 133  Bit Score: 38.69  E-value: 1.30e-03
                        10        20
                ....*....|....*....|.
gi 15990529 208 HGPVVVHCSAGIGRSGTFCLA 228
Cdd:cd14514  77 GGRTLVHCVAGVSRSATLCLA 97
DSP_DUSP4 cd14640
dual specificity phosphatase domain of dual specificity protein phosphatase 4; Dual ...
 203-238 1.55e-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: 1.55e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 15990529 203 SLSPEHGPVVVHCSAGIGRSGTFCLAdtcLLLMDKR 238
Cdd:cd14640  73 SVKDCNGRVLVHCQAGISRSATICLA---YLMMKKR 105
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 162-269 2.57e-03

protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase/transmembrane phosphatase with tensin homology; Voltage-sensitive phosphatase (VSP) proteins comprise a family of phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. This family is conserved in deuterostomes; VSP was first identified as a sperm flagellar plasma membrane protein in Ciona intestinalis. Gene duplication events in primates resulted in the presence of paralogs, transmembrane phosphatase with tensin homology (TPTE) and TPTE2, that retain protein domain architecture but, in the case of TPTE, have lost catalytic activity. TPTE, also called cancer/testis antigen 44 (CT44), may play a role in the signal transduction pathways of the endocrine or spermatogenic function of the testis. TPTE2, also called TPTE and PTEN homologous inositol lipid phosphatase (TPIP), occurs in several differentially spliced forms; TPIP alpha displays phosphoinositide 3-phosphatase activity and is localized on the endoplasmic reticulum, while TPIP beta is cytosolic and lacks detectable phosphatase activity. VSP/TPTE proteins contain an N-terminal voltage sensor consisting of four transmembrane segments, a protein tyrosine phosphatase (PTP)-like phosphoinositide phosphatase catalytic domain, followed by a regulatory C2 domain.


Pssm-ID: 350360 [Multi-domain]  Cd Length: 177  Bit Score: 38.50  E-value: 2.57e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15990529 162 NLTTQETREILHFHYTT----WPDFGVPESPaSFLNFLFKVRESGSLSPEHgPVVVHCSAGIGRSGTFcladTCLLLMDK 237
Cdd:cd14510  60 NLCSERGYDPKYFHNRVervpIDDHNVPTLD-EMLSFTAEVREWMAADPKN-VVAIHCKGGKGRTGTM----VCAWLIYS 133

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15990529 238 RKDPSSVDIKKVLLEMR-------KFRMglIQTADQLRF 269
Cdd:cd14510 134 GQFESAKEALEYFGERRtdksvssKFQG--VETPSQSRY 170
DSP_DUSP2 cd14641
dual specificity phosphatase domain of dual specificity protein phosphatase 2; Dual ...
 192-228 3.04e-03

dual specificity phosphatase domain of dual specificity protein phosphatase 2; Dual specificity protein phosphatase 2 (DUSP2), also called dual specificity protein phosphatase PAC-1, functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other mitogen-activated protein kinase (MAPK) phosphatases (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. DUSP2 can preferentially dephosphorylate ERK1/2 and p38, but not JNK in vitro. It is predominantly expressed in hematopoietic tissues with high T-cell content, such as thymus, spleen, lymph nodes, peripheral blood and other organs such as the brain and liver. It has a critical and positive role in inflammatory responses. DUSP2 mRNA and protein are significantly reduced in most solid cancers including breast, colon, lung, ovary, kidney and prostate, and the suppression of DUSP2 is associated with tumorigenesis and malignancy. DUSP2 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: 350489 [Multi-domain]  Cd Length: 144  Bit Score: 37.92  E-value: 3.04e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 15990529 192 LNFLFKVRESGslspehGPVVVHCSAGIGRSGTFCLA 228
Cdd:cd14641  71 IDFIDSVKNSG------GRVLVHCQAGISRSATICLA 101
DSP_DUSP5 cd14639
dual specificity phosphatase domain of dual specificity protein phosphatase 5; Dual ...
 192-239 6.52e-03

dual specificity phosphatase domain of dual specificity protein phosphatase 5; Dual specificity protein phosphatase 5 (DUSP5) functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other mitogen-activated protein kinase (MAPK) phosphatases (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. DUSP5 preferentially dephosphorylates extracellular signal-regulated kinase (ERK), and is involved in ERK signaling and ERK-dependent inflammatory gene expression in adipocytes. It also plays a role in regulating pressure-dependent myogenic cerebral arterial constriction, which is crucial for the maintenance of constant cerebral blood flow to the brain. DUSP5 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: 350487 [Multi-domain]  Cd Length: 138  Bit Score: 36.82  E-value: 6.52e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 15990529 192 LNFLFKVRESGslspehGPVVVHCSAGIGRSGTFCLAdtclLLMDKRK 239
Cdd:cd14639  68 IDFIDCVRRAG------GKVLVHCEAGISRSPTICMA----YLMKTKR 105
DSP_MKP_classIII cd14568
dual specificity phosphatase domain of class III mitogen-activated protein kinase phosphatase; ...
 192-228 8.92e-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: 36.63  E-value: 8.92e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 15990529 192 LNFLFKVRESGslspehGPVVVHCSAGIGRSGTFCLA 228
Cdd:cd14568  69 VEFIEKARASN------KRVLVHCLAGISRSATIAIA 99
 
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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