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Conserved domains on  [gi|767903708|ref|XP_011539527|]
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tyrosine-protein phosphatase non-receptor type 22 isoform X9 [Homo sapiens]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 57-266 2.88e-155

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


The actual alignment was detected with superfamily member cd14602:

Pssm-ID: 475123 [Multi-domain]  Cd Length: 234  Bit Score: 450.06  E-value: 2.88e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  57 KNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGK 136
Cdd:cd14602    1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 137 ------------------------EAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQ 192
Cdd:cd14602   81 kkcerywaepgemqlefgpfsvtcEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQ 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767903708 193 EDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIREMRTQRPSLVQTQEQYELVYNAVLELF 266
Cdd:cd14602  161 EDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIELF 234
 
Name Accession Description Interval E-value
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 57-266 2.88e-155

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: 450.06  E-value: 2.88e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  57 KNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGK 136
Cdd:cd14602    1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 137 ------------------------EAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQ 192
Cdd:cd14602   81 kkcerywaepgemqlefgpfsvtcEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQ 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767903708 193 EDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIREMRTQRPSLVQTQEQYELVYNAVLELF 266
Cdd:cd14602  161 EDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIELF 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
24-264 7.09e-101

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 311.13  E-value: 7.09e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708    24 FANEFLKLKRQstkykADKTYPTTVAEKPKNIKKNRYKDILPYDYSRVELSLITsDEDSSYINANFIKGVYGPKAYIATQ 103
Cdd:smart00194   2 LEEEFEKLDRL-----KPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPP-GEGSDYINASYIDGPNGPKAYIATQ 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708   104 GPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKEA------------------------EKRKSDYIIRTLKVKF--NSE 157
Cdd:smart00194  76 GPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKcaqywpdeegepltygditvtlksVEKVDDYTIRTLEVTNtgCSE 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708   158 TRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIipeNFSVFSL 237
Cdd:smart00194 156 TRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGK---EVDIFEI 232

                          250       260
                   ....*....|....*....|....*..
gi 767903708   238 IREMRTQRPSLVQTQEQYELVYNAVLE 264
Cdd:smart00194 233 VKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
54-264 2.83e-92

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 287.60  E-value: 2.83e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708   54 NIKKNRYKDILPYDYSRVELSliTSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYE 133
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  134 MGKEA-------------------------EKRKSDYIIRTLKVKFN--SETRTIYQFHYKNWPDHDVPSSIDPILELIW 186
Cdd:pfam00102  79 KGREKcaqywpeeegesleygdftvtlkkeKEDEKDYTVRTLEVSNGgsEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767903708  187 DVR-CYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPEnfsVFSLIREMRTQRPSLVQTQEQYELVYNAVLE 264
Cdd:pfam00102 159 KVRkSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVD---IFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
13-256 4.94e-37

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 140.23  E-value: 4.94e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  13 EAQSKKITKEEFANEFLKLKRQSTKYKADKTYPTTVAEKPKNikknRYKDILPYDYSRVElslitsdEDSSYINANFIKg 92
Cdd:COG5599    5 NPIAIKSEEEKINSRLSTLTNELAPSHNDPQYLQNINGSPLN----RFRDIQPYKETALR-------ANLGYLNANYIQ- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  93 VYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGK--------------------EAEKRKSDYI-----I 147
Cdd:COG5599   73 VIGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISKpkvkmpvyfrqdgeygkyevSSELTESIQLrdgieA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 148 RTLKVKFNS---ETRTIYQFHYKNWPDHDVPSSiDPILELIWDVRCYQEDDSV---PICIHCSAGCGRTGVICAIDYTWM 221
Cdd:COG5599  153 RTYVLTIKGtgqKKIEIPVLHVKNWPDHGAISA-EALKNLADLIDKKEKIKDPdklLPVVHCRAGVGRTGTLIACLALSK 231

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 767903708 222 LLKDGIIPEnFSVFSLIREMRTQR-PSLVQTQEQYE 256
Cdd:COG5599  232 SINALVQIT-LSVEEIVIDMRTSRnGGMVQTSEQLD 266
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 44-267 5.25e-34

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 132.43  E-value: 5.25e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  44 YPTTVAEKPKNIKKNRYKDILPYDYSRVELSliTSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVL 123
Cdd:PHA02742  42 FSCNESLELKNMKKCRYPDAPCFDRNRVILK--IEDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVR 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 124 IIVMACMEYEMGKEA-------EKRKS----DYIIRTLKVK------------FNSETRT---IYQFHYKNWPDHDVPSS 177
Cdd:PHA02742 120 VIVMITKIMEDGKEAcypywmpHERGKathgEFKIKTKKIKsfrnyavtnlclTDTNTGAsldIKHFAYEDWPHGGLPRD 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 178 IDPILELIWDVRCYQEDDSV-----------PICIHCSAGCGRTGVICAIDYTWMLLKDGIIpenFSVFSLIREMRTQRP 246
Cdd:PHA02742 200 PNKFLDFVLAVREADLKADVdikgenivkepPILVHCSAGLDRAGAFCAIDICISKYNERAI---IPLLSIVRDLRKQRH 276

                        250       260
                 ....*....|....*....|.
gi 767903708 247 SLVQTQEQYELVYNAVLELFK 267
Cdd:PHA02742 277 NCLSLPQQYIFCYFIVLIFAK 297
 
Name Accession Description Interval E-value
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 57-266 2.88e-155

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: 450.06  E-value: 2.88e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  57 KNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGK 136
Cdd:cd14602    1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 137 ------------------------EAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQ 192
Cdd:cd14602   81 kkcerywaepgemqlefgpfsvtcEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQ 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767903708 193 EDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIREMRTQRPSLVQTQEQYELVYNAVLELF 266
Cdd:cd14602  161 EDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIELF 234
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 2-270 6.32e-148

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: 433.98  E-value: 6.32e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708   2 DQREILQKFLDEAQSKKIT----KEEFANEFLKLKRQSTKYKADKTYPTTVAEKPKNIKKNRYKDILPYDYSRVELSLIT 77
Cdd:cd14604    1 EQVEILKKFIERVQAMKSTdhngEDNFASDFMRLRRLSTKYRTEKIYPTATGEKEENVKKNRYKDILPFDHSRVKLTLKT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  78 SDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGK--------------------- 136
Cdd:cd14604   81 SSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRkkcerywplygeepmtfgpfr 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 137 ---EAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVI 213
Cdd:cd14604  161 iscEAEQARTDYFIRTLLLEFQNETRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAI 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767903708 214 CAIDYTWMLLKDGIIPENFSVFSLIREMRTQRPSLVQTQEQYELVYNAVLELFKRQM 270
Cdd:cd14604  241 CAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLFEKQL 297
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 84-260 3.10e-121

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: 361.36  E-value: 3.10e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGK------------------------EAE 139
Cdd:cd14542    1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKkkcerywpeegeeqlqfgpfkislEKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 140 KRKS-DYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDY 218
Cdd:cd14542   81 KRVGpDFLIRTLKVTFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRTGTICAIDY 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 767903708 219 TWMLLKDGIIPENFSVFSLIREMRTQRPSLVQTQEQYELVYN 260
Cdd:cd14542  161 VWNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 25-266 8.32e-111

catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein phosphatase non-receptor type 18 (PTPN18), also called brain-derived phosphatase, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. The N-terminal catalytic PTP domain of PTPN18 blocks lysosomal routing and delays the degradation of HER2 by dephosphorylation, and its C-terminal PEST domain promotes K48-linked HER2 ubiquitination and its destruction via the proteasome pathway.


Pssm-ID: 350451 [Multi-domain]  Cd Length: 266  Bit Score: 337.18  E-value: 8.32e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  25 ANEFLKLKRQSTKYKADKTYPTTVAEKPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQG 104
Cdd:cd14603    1 AGEFSEIRACSAAFKADYVCSTVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 105 PLSTTLLDFWRMIWEYSVLIIVMACMEYEMGK------------------------EAEKRKSDYIIRTLKVKFNSETRT 160
Cdd:cd14603   81 PLSHTVLDFWRMIWQYGVKVILMACREIEMGKkkcerywaqeqeplqtgpftitlvKEKRLNEEVILRTLKVTFQKESRS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 161 IYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIRE 240
Cdd:cd14603  161 VSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSIFDVVLE 240

                        250       260
                 ....*....|....*....|....*.
gi 767903708 241 MRTQRPSLVQTQEQYELVYNAVLELF 266
Cdd:cd14603  241 MRKQRPAAVQTEEQYEFLYHTVAQMF 266
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
24-264 7.09e-101

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 311.13  E-value: 7.09e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708    24 FANEFLKLKRQstkykADKTYPTTVAEKPKNIKKNRYKDILPYDYSRVELSLITsDEDSSYINANFIKGVYGPKAYIATQ 103
Cdd:smart00194   2 LEEEFEKLDRL-----KPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPP-GEGSDYINASYIDGPNGPKAYIATQ 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708   104 GPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKEA------------------------EKRKSDYIIRTLKVKF--NSE 157
Cdd:smart00194  76 GPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKcaqywpdeegepltygditvtlksVEKVDDYTIRTLEVTNtgCSE 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708   158 TRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIipeNFSVFSL 237
Cdd:smart00194 156 TRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGK---EVDIFEI 232

                          250       260
                   ....*....|....*....|....*..
gi 767903708   238 IREMRTQRPSLVQTQEQYELVYNAVLE 264
Cdd:smart00194 233 VKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
54-264 2.83e-92

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 287.60  E-value: 2.83e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708   54 NIKKNRYKDILPYDYSRVELSliTSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYE 133
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  134 MGKEA-------------------------EKRKSDYIIRTLKVKFN--SETRTIYQFHYKNWPDHDVPSSIDPILELIW 186
Cdd:pfam00102  79 KGREKcaqywpeeegesleygdftvtlkkeKEDEKDYTVRTLEVSNGgsEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767903708  187 DVR-CYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPEnfsVFSLIREMRTQRPSLVQTQEQYELVYNAVLE 264
Cdd:pfam00102 159 KVRkSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVD---IFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 84-259 5.54e-77

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: 246.43  E-value: 5.54e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKE------------------------AE 139
Cdd:cd00047    1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREkcerywpeeggkpleygditvtlvSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 140 KRKSDYIIRTLKVKF--NSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAID 217
Cdd:cd00047   81 EELSDYTIRTLELSPkgCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTFIAID 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 767903708 218 YTWMLLKDGiipENFSVFSLIREMRTQRPSLVQTQEQYELVY 259
Cdd:cd00047  161 ILLERLEAE---GEVDVFEIVKALRKQRPGMVQTLEQYEFIY 199
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 59-255 4.44e-63

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: 210.29  E-value: 4.44e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  59 RYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKE- 137
Cdd:cd14548    1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVk 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 138 ----------------------AEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDD 195
Cdd:cd14548   81 cdhywpfdqdpvyygditvtmlSESVLPDWTIREFKLERGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIKQE 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767903708 196 SVPICIHCSAGCGRTGVICAIDYtwmlLKDGIIPENF-SVFSLIREMRTQRPSLVQTQEQY 255
Cdd:cd14548  161 KGPTIVHCSAGVGRTGTFIALDR----LLQQIESEDYvDIFGIVYDLRKHRPLMVQTEAQY 217
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 51-259 3.01e-60

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: 204.14  E-value: 3.01e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  51 KPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACM 130
Cdd:cd14543   26 APANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVMTTR 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 131 EYEMGK---------EAEKR---------------KSDYIIRTLKVkFNSET---RTIYQFHYKNWPDHDVPSSIDPILE 183
Cdd:cd14543  106 VVERGRvkcgqywplEEGSSlrygdltvtnlsvenKEHYKKTTLEI-HNTETdesRQVTHFQFTSWPDFGVPSSAAALLD 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 184 LIWDVRCYQEdDSV--------------PICIHCSAGCGRTGVICAIDYTWMLLKD-GIIpenfSVFSLIREMRTQRPSL 248
Cdd:cd14543  185 FLGEVRQQQA-LAVkamgdrwkghppgpPIVVHCSAGIGRTGTFCTLDICLSQLEDvGTL----NVMQTVRRMRTQRAFS 259

                        250
                 ....*....|.
gi 767903708 249 VQTQEQYELVY 259
Cdd:cd14543  260 IQTPDQYYFCY 270
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 58-259 2.56e-56

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: 191.84  E-value: 2.56e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  58 NRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYG-PKAYIATQGPLSTTLLDFWRMIWEYSVLIIVM--------- 127
Cdd:cd14547    1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGeEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMitnlteake 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 128 ACMEY------------EMGKEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDV-RCYQED 194
Cdd:cd14547   81 KCAQYwpeeenetygdfEVTVQSVKETDGYTVRKLTLKYGGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVeEARQTE 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767903708 195 DSV-PICIHCSAGCGRTGVICAIDYTWMLLKdgiiPENF-SVFSLIREMRTQRPSLVQTQEQYELVY 259
Cdd:cd14547  161 PHRgPIVVHCSAGIGRTGCFIATSIGCQQLR----EEGVvDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 54-264 6.23e-56

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


Pssm-ID: 350401 [Multi-domain]  Cd Length: 238  Bit Score: 191.46  E-value: 6.23e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  54 NIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMacmeye 133
Cdd:cd14553    3 NKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVM------ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 134 MGKEAEKR--KSD--------------------------YIIRTLKVKFN--SETRTIYQFHYKNWPDHDVPSSIDPILE 183
Cdd:cd14553   77 MTKLEERSrvKCDqywptrgtetygliqvtlldtvelatYTVRTFALHKNgsSEKREVRQFQFTAWPDHGVPEHPTPFLA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 184 LIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYtwMLlkDGIIPEN-FSVFSLIREMRTQRPSLVQTQEQYELVYNAV 262
Cdd:cd14553  157 FLRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDS--ML--ERIKHEKtVDIYGHVTCLRAQRNYMVQTEDQYIFIHDAL 232


                 ..
gi 767903708 263 LE 264
Cdd:cd14553  233 LE 234
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 54-262 1.38e-55

catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) and type 6 (PTPN6) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 and PTPN6, are also called SH2 domain-containing tyrosine phosphatase 2 (SHP2) and 1 (SHP1), respectively. They contain two tandem SH2 domains: a catalytic PTP domain, and a C-terminal tail with regulatory properties. Although structurally similar, they have different localization and different roles in signal transduction. PTPN11/SHP2 is expressed ubiquitously and plays a positive role in cell signaling, leading to cell activation, while PTPN6/SHP1 expression is restricted mainly to hematopoietic and epithelial cells and functions as a negative regulator of signaling events.


Pssm-ID: 350392 [Multi-domain]  Cd Length: 251  Bit Score: 191.14  E-value: 1.38e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  54 NIKKNRYKDILPYDYSRVELSLITSDED-SSYINANFIK------GVYGP-KAYIATQGPLSTTLLDFWRMIWEYSVLII 125
Cdd:cd14544    1 NKGKNRYKNILPFDHTRVILKDRDPNVPgSDYINANYIRnenegpTTDENaKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 126 VMACMEYEMGKE-----------------------AEKRKSDYIIRTL---KVKFNSETRTIYQFHYKNWPDHDVPSSID 179
Cdd:cd14544   81 VMTTKEVERGKNkcvrywpdegmqkqygpyrvqnvSEHDTTDYTLRELqvsKLDQGDPIREIWHYQYLSWPDHGVPSDPG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 180 PILELIWDVRCYQE--DDSVPICIHCSAGCGRTGVICAIDytwMLL----KDGIIPEnFSVFSLIREMRTQRPSLVQTQE 253
Cdd:cd14544  161 GVLNFLEDVNQRQEslPHAGPIVVHCSAGIGRTGTFIVID---MLLdqikRKGLDCD-IDIQKTIQMVRSQRSGMVQTEA 236


                 ....*....
gi 767903708 254 QYELVYNAV 262
Cdd:cd14544  237 QYKFIYVAV 245
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 49-263 9.86e-55

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: 188.12  E-value: 9.86e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  49 AEKPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMA 128
Cdd:cd14554    1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 129 CMEYEMGKE----------------------AEKRKSDYIIRTLKVK--FNSETRTIYQFHYKNWPDHDVPSSIDPILEL 184
Cdd:cd14554   81 TKLREMGREkchqywpaersaryqyfvvdpmAEYNMPQYILREFKVTdaRDGQSRTVRQFQFTDWPEQGVPKSGEGFIDF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 185 IWDV-RCY-QEDDSVPICIHCSAGCGRTGVICAIDYTWMLLK-DGIIpenfSVFSLIREMRTQRPSLVQTQEQYELVYNA 261
Cdd:cd14554  161 IGQVhKTKeQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRyEGVV----DVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236


                 ..
gi 767903708 262 VL 263
Cdd:cd14554  237 AL 238
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 53-264 8.22e-54

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: 185.61  E-value: 8.22e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  53 KNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEY 132
Cdd:cd14630    2 ENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 133 EMGK----------------------EAEKRkSDYIIRTLKV--KFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDV 188
Cdd:cd14630   82 EVGRvkcvrywpddtevygdikvtliETEPL-AEYVIRTFTVqkKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVRQV 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767903708 189 RCYQEDDSVPICIHCSAGCGRTGVICAIDYTW-MLLKDGIIpenfSVFSLIREMRTQRPSLVQTQEQYELVYNAVLE 264
Cdd:cd14630  161 KFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLdMAENEGVV----DIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 84-259 1.70e-53

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: 183.99  E-value: 1.70e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  84 YINANFIK-GVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMG-------------------------KE 137
Cdd:cd18533    1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGrekcdqywpsgeyegeygdltvelvSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 138 AEKRKSDYIIRTLKVKF-NSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVR--CYQEDDSVPICIHCSAGCGRTGVIC 214
Cdd:cd18533   81 EENDDGGFIVREFELSKeDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRelNDSASLDPPIIVHCSAGVGRTGTFI 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767903708 215 AIDyTWM-LLKDGII---PENFS---VFSLIREMRTQRPSLVQTQEQYELVY 259
Cdd:cd18533  161 ALD-SLLdELKRGLSdsqDLEDSedpVYEIVNQLRKQRMSMVQTLRQYIFLY 211
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 58-265 1.75e-53

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: 184.71  E-value: 1.75e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  58 NRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMA--CMEYEMG 135
Cdd:cd14619    1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLtnCMEAGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 136 K---------------------EAEKRKSDYIIR--TLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCY- 191
Cdd:cd14619   81 KcehywpldytpctyghlrvtvVSEEVMENWTVRefLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQWl 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767903708 192 -QEDDSVPICIHCSAGCGRTGVICAIDYtwmLLKDGIIPENFSVFSLIREMRTQRPSLVQTQEQYELVYNAVLEL 265
Cdd:cd14619  161 dQTMSGGPTVVHCSAGVGRTGTLIALDV---LLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDF 232
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 45-263 1.06e-51

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: 180.08  E-value: 1.06e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  45 PTTVAEKPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLI 124
Cdd:cd14614    3 PHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 125 IVM----------ACMEY---------------EMGKEAEkrKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPS--S 177
Cdd:cd14614   83 IVMltqcnekrrvKCDHYwpfteepvaygditvEMLSEEE--QPDWAIREFRVSYADEVQDVMHFNYTAWPDHGVPTanA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 178 IDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGiipENFSVFSLIREMRTQRPSLVQTQEQYEL 257
Cdd:cd14614  161 AESILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDH---EFVDILGLVSEMRSYRMSMVQTEEQYIF 237


                 ....*.
gi 767903708 258 VYNAVL 263
Cdd:cd14614  238 IHQCVQ 243
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 84-255 4.43e-50

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


Pssm-ID: 350397 [Multi-domain]  Cd Length: 204  Bit Score: 174.08  E-value: 4.43e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVM----------ACMEY------------EMGKEAEKR 141
Cdd:cd14549    1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMitnlvergrrKCDQYwpkegtetygniQVTLLSTEV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 142 KSDYIIRTL--------KVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVI 213
Cdd:cd14549   81 LATYTVRTFslknlklkKVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTGTY 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 767903708 214 CAIDYTWMLLKD-GIIpenfSVFSLIREMRTQRPSLVQTQEQY 255
Cdd:cd14549  161 IVIDSMLQQIQDkGTV----NVFGFLKHIRTQRNYLVQTEEQY 199
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 31-264 3.54e-49

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: 174.08  E-value: 3.54e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  31 LKRQSTKYKADKTYPTTVAEKPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTL 110
Cdd:cd14633   17 FKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYHRPNHYIATQGPMQETI 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 111 LDFWRMIWEYSVLIIVMACMEYEMGK---------EAEKRK------------SDYIIRTLKVKFNS--ETRTIYQFHYK 167
Cdd:cd14633   97 YDFWRMVWHENTASIIMVTNLVEVGRvkcckywpdDTEIYKdikvtlietellAEYVIRTFAVEKRGvhEIREIRQFHFT 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 168 NWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTW-MLLKDGIIpenfSVFSLIREMRTQRP 246
Cdd:cd14633  177 GWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLdMAEREGVV----DIYNCVRELRSRRV 252

                        250
                 ....*....|....*...
gi 767903708 247 SLVQTQEQYELVYNAVLE 264
Cdd:cd14633  253 NMVQTEEQYVFIHDAILE 270
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 24-264 4.51e-49

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


Pssm-ID: 350505 [Multi-domain]  Cd Length: 274  Bit Score: 174.07  E-value: 4.51e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  24 FANEFLKLKRQStkykADKTYPTTVAEKPKNIKKNRYKDILPYDYSRVELSLITSDED--SSYINANFIKGVYGPKAYIA 101
Cdd:cd17667    1 FSEDFEEVQRCT----ADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGYNKAKAYIA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 102 TQGPLSTTLLDFWRMIWEYSVLIIVM----------ACMEY-------EMGKEAEKRKSDYI----------IRTLKVKF 154
Cdd:cd17667   77 TQGPLKSTFEDFWRMIWEQNTGIIVMitnlvekgrrKCDQYwptenseEYGNIIVTLKSTKIhacytvrrfsIRNTKVKK 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 155 NSE--------TRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDg 226
Cdd:cd17667  157 GQKgnpkgrqnERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKD- 235

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 767903708 227 iiPENFSVFSLIREMRTQRPSLVQTQEQYELVYNAVLE 264
Cdd:cd17667  236 --KSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 271
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 53-262 8.19e-48

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


Pssm-ID: 350453 [Multi-domain]  Cd Length: 253  Bit Score: 169.81  E-value: 8.19e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  53 KNIKKNRYKDILPYDYSRVELSLITSDED-SSYINANFIKGVYG--------PKAYIATQGPLSTTLLDFWRMIWEYSVL 123
Cdd:cd14605    1 ENKNKNRYKNILPFDHTRVVLHDGDPNEPvSDYINANIIMPEFEtkcnnskpKKSYIATQGCLQNTVNDFWRMVFQENSR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 124 IIVMACMEYEMGKEA-----------------------EKRKSDYIIRTLKV----KFNSEtRTIYQFHYKNWPDHDVPS 176
Cdd:cd14605   81 VIVMTTKEVERGKSKcvkywpdeyalkeygvmrvrnvkESAAHDYILRELKLskvgQGNTE-RTVWQYHFRTWPDHGVPS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 177 SIDPILELIWDVRCYQED--DSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIREMRTQRPSLVQTQEQ 254
Cdd:cd14605  160 DPGGVLDFLEEVHHKQESimDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVDCDIDVPKTIQMVRSQRSGMVQTEAQ 239


                 ....*...
gi 767903708 255 YELVYNAV 262
Cdd:cd14605  240 YRFIYMAV 247
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 14-264 4.72e-47

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: 169.14  E-value: 4.72e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  14 AQSKKITKEEFANEFLKLKRQSTKYKADKTYPTTV--AEKPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIK 91
Cdd:cd14628   10 AYIQKLTQIETGENVTGMELEFKRLASSKAHTSRFisANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFID 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  92 GVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKE----------------------AEKRKSDYIIRT 149
Cdd:cd14628   90 GYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREkchqywpaersaryqyfvvdpmAEYNMPQYILRE 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 150 LKVK--FNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQED--DSVPICIHCSAGCGRTGVICAIDYTWMLLK- 224
Cdd:cd14628  170 FKVTdaRDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSIVLERMRy 249

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 767903708 225 DGIIpenfSVFSLIREMRTQRPSLVQTQEQYELVYNAVLE 264
Cdd:cd14628  250 EGVV----DIFQTVKMLRTQRPAMVQTEDQYQFCYRAALE 285
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 58-255 5.26e-47

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: 166.53  E-value: 5.26e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  58 NRYKDILPYDYSRVELSLITSDEDSsYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVM---------- 127
Cdd:cd14615    1 NRYNNVLPYDISRVKLSVQSHSTDD-YINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMltkcveqgrt 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 128 ACMEYEMGKEA------------EKRKSDYIIRTLKVKF--NSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCY-- 191
Cdd:cd14615   80 KCEEYWPSKQKkdygditvtmtsEIVLPEWTIRDFTVKNaqTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREYmk 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767903708 192 QEDDSVPICIHCSAGCGRTGVICAIDYtwmLLKDGIIPENFSVFSLIREMRTQRPSLVQTQEQY 255
Cdd:cd14615  160 QNPPNSPILVHCSAGVGRTGTFIAIDR---LIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQY 220
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 52-259 9.99e-47

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: 166.55  E-value: 9.99e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  52 PKNIKKNRYKDILPYDYSRVEL-SLITSDEDSSYINANFIKGVYG-PKAYIATQGPLSTTLLDFWRMIWEYSVLIIVM-- 127
Cdd:cd14612   13 PGHASKDRYKTILPNPQSRVCLrRAGSQEEEGSYINANYIRGYDGkEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMit 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 128 -------ACMEYEMGKEAE-----------KRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVR 189
Cdd:cd14612   93 klkekkeKCVHYWPEKEGTygrfeirvqdmKECDGYTIRDLTIQLEEESRSVKHYWFSSWPDHQTPESAGPLLRLVAEVE 172

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767903708 190 CYQEDDSV--PICIHCSAGCGRTGVICAIDYTWMLLKDgiiPENFSVFSLIREMRTQRPSLVQTQEQYELVY 259
Cdd:cd14612  173 ESRQTAASpgPIVVHCSAGIGRTGCFIATSIGCQQLKD---TGKVDILGIVCQLRLDRGGMIQTSEQYQFLH 241
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 49-264 1.20e-46

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: 167.98  E-value: 1.20e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  49 AEKPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMA 128
Cdd:cd14629   48 ANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVML 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 129 CMEYEMGKE----------------------AEKRKSDYIIRTLKVK--FNSETRTIYQFHYKNWPDHDVPSSIDPILEL 184
Cdd:cd14629  128 TKLREMGREkchqywpaersaryqyfvvdpmAEYNMPQYILREFKVTdaRDGQSRTIRQFQFTDWPEQGVPKTGEGFIDF 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 185 IWDVRCYQED--DSVPICIHCSAGCGRTGVICAIDYTWMLLK-DGIIpenfSVFSLIREMRTQRPSLVQTQEQYELVYNA 261
Cdd:cd14629  208 IGQVHKTKEQfgQDGPITVHCSAGVGRTGVFITLSIVLERMRyEGVV----DMFQTVKTLRTQRPAMVQTEDQYQLCYRA 283


                 ...
gi 767903708 262 VLE 264
Cdd:cd14629  284 ALE 286
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 57-259 2.26e-46

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


Pssm-ID: 350393 [Multi-domain]  Cd Length: 231  Bit Score: 164.87  E-value: 2.26e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  57 KNRYKDILPYDYSRVELSLitSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVM--------- 127
Cdd:cd14545    1 LNRYRDRDPYDHDRSRVKL--KQGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMlnklmekgq 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 128 -ACMEY---EMGKE-------------AEKRKSDYIIRTLKV--KFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDV 188
Cdd:cd14545   79 iKCAQYwpqGEGNAmifedtglkvtllSEEDKSYYTVRTLELenLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQKV 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767903708 189 RCYQ--EDDSVPICIHCSAGCGRTGVICAIDyTWMLLKDGIIPENFSVFSLIREMRTQRPSLVQTQEQYELVY 259
Cdd:cd14545  159 RESGslSSDVGPPVVHCSAGIGRSGTFCLVD-TCLVLIEKGNPSSVDVKKVLLEMRKYRMGLIQTPDQLRFSY 230
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 49-264 4.45e-46

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: 166.06  E-value: 4.45e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  49 AEKPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMA 128
Cdd:cd14627   48 ANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVML 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 129 CMEYEMGKE----------------------AEKRKSDYIIRTLKVK--FNSETRTIYQFHYKNWPDHDVPSSIDPILEL 184
Cdd:cd14627  128 TKLREMGREkchqywpaersaryqyfvvdpmAEYNMPQYILREFKVTdaRDGQSRTVRQFQFTDWPEQGVPKSGEGFIDF 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 185 IWDVRCYQED--DSVPICIHCSAGCGRTGVICAIDYTWMLLK-DGIIpenfSVFSLIREMRTQRPSLVQTQEQYELVYNA 261
Cdd:cd14627  208 IGQVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSIVLERMRyEGVV----DIFQTVKMLRTQRPAMVQTEDEYQFCYQA 283


                 ...
gi 767903708 262 VLE 264
Cdd:cd14627  284 ALE 286
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 38-264 6.82e-46

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: 165.21  E-value: 6.82e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  38 YKADktyPTT--VAEKPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGvYGPK--AYIATQGPLSTTLLDF 113
Cdd:cd14609   27 YQAE---PNTcsTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIE-HDPRmpAYIATQGPLSHTIADF 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 114 WRMIWEYSVLIIVMACMEYEMGKEAEKRK-----------------------SDYIIRTLKVKF--NSETRTIYQFHYKN 168
Cdd:cd14609  103 WQMVWENGCTVIVMLTPLVEDGVKQCDRYwpdegsslyhiyevnlvsehiwcEDFLVRSFYLKNvqTQETRTLTQFHFLS 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 169 WPDHDVPSSIDPILELIWDV-RCYQeDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIipENFSVFSLIREMRTQRPS 247
Cdd:cd14609  183 WPAEGIPSSTRPLLDFRRKVnKCYR-GRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGV--KEIDIAATLEHVRDQRPG 259

                        250
                 ....*....|....*..
gi 767903708 248 LVQTQEQYELVYNAVLE 264
Cdd:cd14609  260 MVRTKDQFEFALTAVAE 276
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 53-263 1.92e-45

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: 162.31  E-value: 1.92e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  53 KNIKKNRYKDILPYDYSRVELSlitsdEDSSYINANFIKGVYGPK--AYIATQGPLSTTLLDFWRMIWEYSVLIIVMACM 130
Cdd:cd14597    2 ENRKKNRYKNILPYDTTRVPLG-----DEGGYINASFIKMPVGDEefVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 131 EYEMGK-------------------------EAEKRKSDYIIRTLKVK--FNSETRTIYQFHYKNWPDHDVPSSIDPILE 183
Cdd:cd14597   77 EVEGGKikcqrywpeilgkttmvdnrlqltlVRMQQLKNFVIRVLELEdiQTREVRHITHLNFTAWPDHDTPSQPEQLLT 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 184 LIWDVRCYQEddSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIipeNFSVFSLIREMRTQRPSLVQTQEQYELVYNAVL 263
Cdd:cd14597  157 FISYMRHIHK--SGPIITHCSAGIGRSGTLICIDVVLGLISKDL---DFDISDIVRTMRLQRHGMVQTEDQYIFCYQVIL 231
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 50-264 2.15e-45

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: 163.51  E-value: 2.15e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  50 EKPKNIKKNRYKDILPYDYSRVELSLITSD-EDSSYINANFIKG-VYG----PKAYIATQGPLSTTLLDFWRMIWEYSVL 123
Cdd:cd14606   14 QRPENKSKNRYKNILPFDHSRVILQGRDSNiPGSDYINANYVKNqLLGpdenAKTYIASQGCLEATVNDFWQMAWQENSR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 124 IIVMACMEYEMGKE-----------------------AEKRKSDYIIRTLKVKF---NSETRTIYQFHYKNWPDHDVPSS 177
Cdd:cd14606   94 VIVMTTREVEKGRNkcvpywpevgmqraygpysvtncGEHDTTEYKLRTLQVSPldnGELIREIWHYQYLSWPDHGVPSE 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 178 IDPILELIWDVRCYQED--DSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIREMRTQRPSLVQTQEQY 255
Cdd:cd14606  174 PGGVLSFLDQINQRQESlpHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLDCDIDIQKTIQMVRAQRSGMVQTEAQY 253


                 ....*....
gi 767903708 256 ELVYNAVLE 264
Cdd:cd14606  254 KFIYVAIAQ 262
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 52-266 2.25e-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: 163.11  E-value: 2.25e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  52 PKNIKKNRYKDILPYDYSRVelSLITSDED---SSYINANFIKGvYG--PKAYIATQGPLSTTLLDFWRMIWEYSVLIIV 126
Cdd:cd14613   23 PGLVRKNRYKTILPNPHSRV--CLTSPDQDdplSSYINANYIRG-YGgeEKVYIATQGPTVNTVGDFWRMVWQERSPIIV 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 127 M---------ACMEY-----------EMGKEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIW 186
Cdd:cd14613  100 MitnieemneKCTEYwpeeqvtyegiEITVKQVIHADDYRLRLITLKSGGEERGLKHYWYTSWPDQKTPDNAPPLLQLVQ 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 187 DV---RCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGiipenfSVFSLIR---EMRTQRPSLVQTQEQYELVYN 260
Cdd:cd14613  180 EVeeaRQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNE------GVVDILRttcQLRLDRGGMIQTCEQYQFVHH 253


                 ....*.
gi 767903708 261 aVLELF 266
Cdd:cd14613  254 -VLSLY 258
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 84-264 3.55e-45

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: 160.69  E-value: 3.55e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  84 YINANFIKGvYGPK--AYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKEAEKRK------------------- 142
Cdd:cd14546    1 YINASTIYD-HDPRnpAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYwpeegsevyhiyevhlvse 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 143 ----SDYIIRTLKVK--FNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDV-RCYQeDDSVPICIHCSAGCGRTGVICA 215
Cdd:cd14546   80 hiwcDDYLVRSFYLKnlQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVnKSYR-GRSCPIVVHCSDGAGRTGTYIL 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 767903708 216 IDYTWMLLKDGIipENFSVFSLIREMRTQRPSLVQTQEQYELVYNAVLE 264
Cdd:cd14546  159 IDMVLNRMAKGA--KEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 25-264 3.56e-45

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: 163.28  E-value: 3.56e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  25 ANEFLKLKRQSTKYKADKTYPTTVAEKPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQG 104
Cdd:cd14626   12 ANDGLKFSQEYESIDPGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGYRKQNAYIATQG 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 105 PLSTTLLDFWRMIWEYSVLIIVM----------ACMEYEMGKEAEK------------RKSDYIIRTLKVKFN--SETRT 160
Cdd:cd14626   92 PLPETLSDFWRMVWEQRTATIVMmtrleeksrvKCDQYWPIRGTETygmiqvtlldtvELATYSVRTFALYKNgsSEKRE 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 161 IYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDytwMLLKDGIIPENFSVFSLIRE 240
Cdd:cd14626  172 VRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVID---AMLERMKHEKTVDIYGHVTC 248

                        250       260
                 ....*....|....*....|....
gi 767903708 241 MRTQRPSLVQTQEQYELVYNAVLE 264
Cdd:cd14626  249 MRSQRNYMVQTEDQYIFIHEALLE 272
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 44-264 3.76e-45

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: 163.27  E-value: 3.76e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  44 YPTTVAEKPKNIKKNRYKDILPYDYSRVELSLitsdEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVL 123
Cdd:cd14608   15 FPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQ----EDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSR 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 124 IIVM----------ACMEYEMGKE----------------AEKRKSDYIIRTLKVK--FNSETRTIYQFHYKNWPDHDVP 175
Cdd:cd14608   91 GVVMlnrvmekgslKCAQYWPQKEekemifedtnlkltliSEDIKSYYTVRQLELEnlTTQETREILHFHYTTWPDFGVP 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 176 SSIDPILELIWDVRcyqEDDSV-----PICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIREMRTQRPSLVQ 250
Cdd:cd14608  171 ESPASFLNFLFKVR---ESGSLspehgPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQ 247

                        250
                 ....*....|....
gi 767903708 251 TQEQYELVYNAVLE 264
Cdd:cd14608  248 TADQLRFSYLAVIE 261
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 47-267 7.30e-45

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: 162.33  E-value: 7.30e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  47 TVAEKPKNIKKNRYKDILPYDYSRVELslitsDEDSSYINANFIK----GVYGPKAYIATQGPLSTTLLDFWRMIWEYSV 122
Cdd:cd14600   33 TCAKLPQNMDKNRYKDVLPYDATRVVL-----QGNEDYINASYVNmeipSANIVNKYIATQGPLPHTCAQFWQVVWEQKL 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 123 LIIVM----------ACMEY--------EMGK-----EAEKRKSDYIIRTLKVKfNSET---RTIYQFHYKNWPDHDVPS 176
Cdd:cd14600  108 SLIVMlttltergrtKCHQYwpdppdvmEYGGfrvqcHSEDCTIAYVFREMLLT-NTQTgeeRTVTHLQYVAWPDHGVPD 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 177 SIDPILELIWDVRCYQEdDSVPICIHCSAGCGRTGVICAIDyTWMLLkdgiIPENFSVFSL--IREMRTQRPSLVQTQEQ 254
Cdd:cd14600  187 DSSDFLEFVNYVRSKRV-ENEPVLVHCSAGIGRTGVLVTME-TAMCL----TERNQPVYPLdiVRKMRDQRAMMVQTSSQ 260

                        250
                 ....*....|...
gi 767903708 255 YELVYNAVLELFK 267
Cdd:cd14600  261 YKFVCEAILRVYE 273
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 57-260 1.31e-44

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: 159.70  E-value: 1.31e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  57 KNRYKDILPYDYSRVELSLITSDED-SSYINANFIKGVYG-PKAYIATQGPLSTTLLDFWRMIWEYSVLIIVM------- 127
Cdd:cd14611    2 KNRYKTILPNPHSRVCLKPKNSNDSlSTYINANYIRGYGGkEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMitklkek 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 128 --ACMEY-----------EMGKEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVrcyQED 194
Cdd:cd14611   82 neKCVLYwpekrgiygkvEVLVNSVKECDNYTIRNLTLKQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDV---EED 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767903708 195 -----DSVPICIHCSAGCGRTGVICAIDYTWMLLK-DGIIpenfSVFSLIREMRTQRPSLVQTQEQYELVYN 260
Cdd:cd14611  159 rlaspGRGPVVVHCSAGIGRTGCFIATTIGCQQLKeEGVV----DVLSIVCQLRVDRGGMVQTSEQYEFVHH 226
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 58-255 3.19e-44

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: 158.53  E-value: 3.19e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  58 NRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMG-- 135
Cdd:cd14616    1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGri 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 136 ----------------------KEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQE 193
Cdd:cd14616   81 rchqywpednkpvtvfgdivitKLMEDVQIDWTIRDLKIERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVRASRA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767903708 194 DDSVPICIHCSAGCGRTGVICAIDYTWMLLKDgiipENF-SVFSLIREMRTQRPSLVQTQEQY 255
Cdd:cd14616  161 HDNTPMIVHCSAGVGRTGVFIALDHLTQHIND----HDFvDIYGLVAELRSERMCMVQNLAQY 219
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 84-264 5.41e-44

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: 157.54  E-value: 5.41e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  84 YINANFIKGVYGPKA--YIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGK---------------------EAEK 140
Cdd:cd14538    1 YINASHIRIPVGGDTyhYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKvkchrywpdslnkplicggrlEVSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 141 RKS----DYIIRTLKVKFN--SETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQedDSVPICIHCSAGCGRTGVIC 214
Cdd:cd14538   81 EKYqslqDFVIRRISLRDKetGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIH--NSGPIVVHCSAGIGRTGVLI 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 767903708 215 AIDYTWMLLKDGIipeNFSVFSLIREMRTQRPSLVQTQEQYELVYNAVLE 264
Cdd:cd14538  159 TIDVALGLIERDL---PFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLE 205
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 38-264 1.28e-43

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: 159.07  E-value: 1.28e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  38 YKADKTyPTTVAEKPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGvYGPK--AYIATQGPLSTTLLDFWR 115
Cdd:cd14610   29 YQAEPN-ATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMD-HDPRnpAYIATQGPLPATVADFWQ 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 116 MIWEYSVLIIVM----------ACMEY------------EMGKEAEK-RKSDYIIRTLKVKF--NSETRTIYQFHYKNWP 170
Cdd:cd14610  107 MVWESGCVVIVMltplaengvkQCYHYwpdegsnlyhiyEVNLVSEHiWCEDFLVRSFYLKNlqTNETRTVTQFHFLSWN 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 171 DHDVPSSIDPILELIWDV-RCYQeDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGiiPENFSVFSLIREMRTQRPSLV 249
Cdd:cd14610  187 DQGVPASTRSLLDFRRKVnKCYR-GRSCPIIVHCSDGAGRSGTYILIDMVLNKMAKG--AKEIDIAATLEHLRDQRPGMV 263

                        250
                 ....*....|....*
gi 767903708 250 QTQEQYELVYNAVLE 264
Cdd:cd14610  264 QTKEQFEFALTAVAE 278
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 58-263 2.16e-43

catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type tyrosine-protein phosphatase V (PTPRV or R-PTP-V), also known as embryonic stem cell protein-tyrosine phosphatase (ES cell phosphatase) or osteotesticular protein-tyrosine phosphatase (OST-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRV is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. In rodents, it may play a role in the maintenance of pluripotency and may function in signaling pathways during bone remodeling. It is the only PTP whose function has been lost between rodent and human. The human OST-PTP gene is a pseudogene.


Pssm-ID: 350466 [Multi-domain]  Cd Length: 230  Bit Score: 156.64  E-value: 2.16e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  58 NRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKE 137
Cdd:cd14618    1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 138 -----------------------AEKRKSDYIIRTLKVKFNSE--TRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQ 192
Cdd:cd14618   81 lcdhywpsestpvsyghitvhllAQSSEDEWTRREFKLWHEDLrkERRVKHLHYTAWPDHGIPESTSSLMAFRELVREHV 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767903708 193 E--DDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPEnfsVFSLIREMRTQRPSLVQTQEQYELVYNAVL 263
Cdd:cd14618  161 QatKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVD---VFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 58-259 2.43e-43

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: 156.23  E-value: 2.43e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  58 NRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMA--CMEYEMG 135
Cdd:cd14617    1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVtqCVEKGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 136 K---------------------EAEKRKSDYIIRTLKVKFNSE---TRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCY 191
Cdd:cd14617   81 KcdhywpadqdslyygdlivqmLSESVLPEWTIREFKICSEEQldaPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVRDY 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767903708 192 --QEDDSVPICIHCSAGCGRTGVICAIDYTWMLL--KDGIipenfSVFSLIREMRTQRPSLVQTQEQYELVY 259
Cdd:cd14617  161 inRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLdsKDSV-----DIYGAVHDLRLHRVHMVQTECQYVYLH 227
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 59-264 1.23e-42

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: 154.43  E-value: 1.23e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  59 RYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVM----------A 128
Cdd:cd14623    1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMlteleergqeK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 129 CMEY--------------EMGKEAEKRKsdYIIRTLKVKFNSE--TRTIYQFHYKNWPDHDVPSSIDPILELIWDV-RCY 191
Cdd:cd14623   81 CAQYwpsdgsvsygditiELKKEEECES--YTVRDLLVTNTREnkSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVqKQQ 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767903708 192 QEDDSVPICIHCSAGCGRTGVICAIDYTWMLLK-DGIIpenfSVFSLIREMRTQRPSLVQTQEQYELVYNAVLE 264
Cdd:cd14623  159 QQSGNHPITVHCSAGAGRTGTFCALSTVLERVKaEGIL----DVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 25-264 3.08e-42

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


Pssm-ID: 350473 [Multi-domain]  Cd Length: 282  Bit Score: 155.25  E-value: 3.08e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  25 ANEFLKLKRQSTKYKADKTYPTTVAEKPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQG 104
Cdd:cd14625   18 ANDNLKLSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINANYIDGYRKQNAYIATQG 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 105 PLSTTLLDFWRMIWEYSVLIIVM----------ACMEYEMGKEAEK------------RKSDYIIRTLKVKFN--SETRT 160
Cdd:cd14625   98 PLPETFGDFWRMVWEQRSATVVMmtkleeksriKCDQYWPSRGTETygmiqvtlldtiELATFCVRTFSLHKNgsSEKRE 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 161 IYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDytwmLLKDGIIPE-NFSVFSLIR 239
Cdd:cd14625  178 VRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVID----AMLERIKHEkTVDIYGHVT 253

                        250       260
                 ....*....|....*....|....*
gi 767903708 240 EMRTQRPSLVQTQEQYELVYNAVLE 264
Cdd:cd14625  254 LMRSQRNYMVQTEDQYSFIHDALLE 278
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 84-267 3.21e-42

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: 152.48  E-value: 3.21e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  84 YINANF----IKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVM----------ACMEY--EMGKE---------- 137
Cdd:cd14541    2 YINANYvnmeIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMlttlvergrvKCHQYwpDLGETmqfgnlqitc 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 138 -AEKRKSDYIIRTLKVK--FNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVIC 214
Cdd:cd14541   82 vSEEVTPSFAFREFILTntNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGIGRTGVLI 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767903708 215 AIDyTWMLLkdgiIPENFSVFSL--IREMRTQRPSLVQTQEQYELVYNAVLELFK 267
Cdd:cd14541  162 TME-TAMCL----IEANEPVYPLdiVRTMRDQRAMLIQTPSQYRFVCEAILRVYE 211
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 84-262 8.42e-42

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: 151.27  E-value: 8.42e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVM----------ACMEY--------------EMGKEAE 139
Cdd:cd14552    1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMlteikersqnKCAQYwpedgsvssgditvELKDQTD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 140 KRksDYIIRTLKVKFNSE--TRTIYQFHYKNWPDHDVPSSIDPILELIWDV-RCYQEDDSVPICIHCSAGCGRTGVICAI 216
Cdd:cd14552   81 YE--DYTLRDFLVTKGKGgsTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVqKQQQQSGNHPITVHCSAGAGRTGTFCAL 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 767903708 217 DYTWMLLK-DGIIpenfSVFSLIREMRTQRPSLVQTQEQYELVYNAV 262
Cdd:cd14552  159 STVLERVKaEGVL----DVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 34-267 4.12e-41

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: 152.07  E-value: 4.12e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  34 QSTKYKADKTYptTVAEKPKNIKKNRYKDILPYDYSRVELsLITSDEDSSYINANFIKGVYGPKA--YIATQGPLSTTLL 111
Cdd:cd14599   20 QIPKKKADGVF--TTATLPENAERNRIREVVPYEENRVEL-VPTKENNTGYINASHIKVTVGGEEwhYIATQGPLPHTCH 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 112 DFWRMIWEYSVLIIVMACMEYEMGKEAEKR-----------------------KSD---YIIRTLKVK--FNSETRTIYQ 163
Cdd:cd14599   97 DFWQMVWEQGVNVIAMVTAEEEGGRSKSHRywpklgskhssatygkfkvttkfRTDsgcYATTGLKVKhlLSGQERTVWH 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 164 FHYKNWPDHDVPSSID---PILELIWDVRCY-------QEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGiipENFS 233
Cdd:cd14599  177 LQYTDWPDHGCPEEVQgflSYLEEIQSVRRHtnsmldsTKNCNPPIVVHCSAGVGRTGVVILTELMIGCLEHN---EKVE 253

                        250       260       270
                 ....*....|....*....|....*....|....
gi 767903708 234 VFSLIREMRTQRPSLVQTQEQYELVYNAVLELFK 267
Cdd:cd14599  254 VPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 84-264 4.47e-41

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: 149.30  E-value: 4.47e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGK----------------------EAEKR 141
Cdd:cd14555    1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRvkcsrywpddtevygdikvtlvETEPL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 142 kSDYIIRTLKV--KFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYT 219
Cdd:cd14555   81 -AEYVVRTFALerRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYIVIDIM 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 767903708 220 W-MLLKDGIIpenfSVFSLIREMRTQRPSLVQTQEQYELVYNAVLE 264
Cdd:cd14555  160 LdMAEREGVV----DIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 25-264 7.99e-41

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: 151.04  E-value: 7.99e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  25 ANEFLKLKRQSTKYKADKTYPTTVAEKPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQG 104
Cdd:cd14624   18 ANDNLKFSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINANYIDGYRKQNAYIATQG 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 105 PLSTTLLDFWRMIWEYSVLIIVM----------ACMEYEMGKEAEKRK------------SDYIIRTLKVKFN--SETRT 160
Cdd:cd14624   98 ALPETFGDFWRMIWEQRSATVVMmtkleersrvKCDQYWPSRGTETYGliqvtlldtvelATYCVRTFALYKNgsSEKRE 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 161 IYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDgiiPENFSVFSLIRE 240
Cdd:cd14624  178 VRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKH---EKTVDIYGHVTL 254

                        250       260
                 ....*....|....*....|....
gi 767903708 241 MRTQRPSLVQTQEQYELVYNAVLE 264
Cdd:cd14624  255 MRAQRNYMVQTEDQYIFIHDALLE 278
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 84-259 4.32e-40

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


Pssm-ID: 350406 [Multi-domain]  Cd Length: 203  Bit Score: 146.38  E-value: 4.32e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVM----------ACMEY---------EMG---KEAEKR 141
Cdd:cd14558    1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMltelkegdqeQCAQYwgdekktygDIEvelKDTEKS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 142 kSDYIIRTLKVKF--NSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDD------SVPICIHCSAGCGRTGVI 213
Cdd:cd14558   81 -PTYTVRVFEITHlkRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKnskhgrSVPIVVHCSDGSSRTGIF 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 767903708 214 CAIdytWMLLKDGIIPENFSVFSLIREMRTQRPSLVQTQEQYELVY 259
Cdd:cd14558  160 CAL---WNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 70-264 1.62e-39

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


Pssm-ID: 350479 [Multi-domain]  Cd Length: 218  Bit Score: 145.16  E-value: 1.62e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  70 RVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGK---------EAE- 139
Cdd:cd14631    1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRvkcykywpdDTEv 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 140 -----------KRKSDYIIRTLKVK---FNsETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSA 205
Cdd:cd14631   81 ygdfkvtcvemEPLAEYVVRTFTLErrgYN-EIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSA 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 206 GCGRTGVICAIDYTW-MLLKDGIIpenfSVFSLIREMRTQRPSLVQTQEQYELVYNAVLE 264
Cdd:cd14631  160 GAGRTGCYIVIDIMLdMAEREGVV----DIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 84-263 3.12e-39

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: 144.35  E-value: 3.12e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGkeaeKRKSD------------------- 144
Cdd:cd17668    1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKG----RRKCDqywpadgseeygnflvtqk 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 145 -------YIIRTLKV----------KFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGC 207
Cdd:cd17668   77 svqvlayYTVRNFTLrntkikkgsqKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGV 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767903708 208 GRTGVICAIDytwMLLKDGIIPENFSVFSLIREMRTQRPSLVQTQEQYELVYNAVL 263
Cdd:cd17668  157 GRTGTYIVLD---SMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 26-262 1.56e-38

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: 143.95  E-value: 1.56e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  26 NEFLKLKRQSTKYkadktyPTTVAEKPKNIKKNRYKDILPYDYSRVELSlitsDEDSSYINANFIKGVYGPKAYIATQGP 105
Cdd:cd14607    2 PLYLEIRNESHDY------PHRVAKYPENRNRNRYRDVSPYDHSRVKLQ----NTENDYINASLVVIEEAQRSYILTQGP 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 106 LSTTLLDFWRMIWEYSVLIIVM----------ACMEYEMGKE----------------AEKRKSDYIIRTLKVK-FNS-E 157
Cdd:cd14607   72 LPNTCCHFWLMVWQQKTKAVVMlnrivekdsvKCAQYWPTDEeevlsfketgfsvkllSEDVKSYYTVHLLQLEnINSgE 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 158 TRTIYQFHYKNWPDHDVPSSIDPILELIWDVRcyqEDDSV-----PICIHCSAGCGRTGVICAIDyTWMLLKDGIIPENF 232
Cdd:cd14607  152 TRTISHFHYTTWPDFGVPESPASFLNFLFKVR---ESGSLspehgPAVVHCSAGIGRSGTFSLVD-TCLVLMEKKDPDSV 227

                        250       260       270
                 ....*....|....*....|....*....|
gi 767903708 233 SVFSLIREMRTQRPSLVQTQEQYELVYNAV 262
Cdd:cd14607  228 DIKQVLLDMRKYRMGLIQTPDQLRFSYMAV 257
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 60-264 2.54e-38

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: 142.39  E-value: 2.54e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  60 YKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVM----------AC 129
Cdd:cd14620    1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMltnlkerkeeKC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 130 MEY------------EMGKEAEKRKSDYIIRTLKVKFNSE-----TRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQ 192
Cdd:cd14620   81 YQYwpdqgcwtygniRVAVEDCVVLVDYTIRKFCIQPQLPdgckaPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKSVN 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767903708 193 EDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDgiiPENFSVFSLIREMRTQRPSLVQTQEQYELVYNAVLE 264
Cdd:cd14620  161 PVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHA---EQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 49-264 8.03e-38

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: 143.24  E-value: 8.03e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  49 AEKPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMA 128
Cdd:cd14621   47 ASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMV 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 129 ----------CMEY------------EMGKEAEKRKSDYIIRTL------KVKFNSETRTIYQFHYKNWPDHDVPSSIDP 180
Cdd:cd14621  127 tnlkerkeckCAQYwpdqgcwtygniRVSVEDVTVLVDYTVRKFciqqvgDVTNKKPQRLITQFHFTSWPDFGVPFTPIG 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 181 ILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDgiiPENFSVFSLIREMRTQRPSLVQTQEQYELVYN 260
Cdd:cd14621  207 MLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHA---ERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQ 283


                 ....
gi 767903708 261 AVLE 264
Cdd:cd14621  284 ALLE 287
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 84-264 1.66e-37

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


Pssm-ID: 350388 [Multi-domain]  Cd Length: 219  Bit Score: 139.51  E-value: 1.66e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  84 YINANFIKGVYGPKA--YIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKE------------------------ 137
Cdd:cd14540    1 YINASHITATVGGKQrfYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREkcfrywptlggehdaltfgeykvs 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 138 AEKRKSD--YIIRTLKVKFNSE--TRTIYQFHYKNWPDHDVPSSIDPILELIWDV-----RCYQEDD----SVPICIHCS 204
Cdd:cd14540   81 TKFSVSSgcYTTTGLRVKHTLSgqSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEInsvrrHTNQDVAghnrNPPTLVHCS 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 205 AGCGRTGVICAIDYTWMLLKDGIIPEnfsVFSLIREMRTQRPSLVQTQEQYELVYNAVLE 264
Cdd:cd14540  161 AGVGRTGVVILADLMLYCLDHNEELD---IPRVLALLRHQRMLLVQTLAQYKFVYNVLIQ 217
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
160-264 3.84e-37

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 134.41  E-value: 3.84e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708   160 TIYQFHYKNWPDHDVPSSIDPILELIWDVR--CYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIipENFSVFSL 237
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKknLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEA--GEVDIFDT 78

                           90       100
                   ....*....|....*....|....*..
gi 767903708   238 IREMRTQRPSLVQTQEQYELVYNAVLE 264
Cdd:smart00404  79 VKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 160-264 3.84e-37

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


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 134.41  E-value: 3.84e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708   160 TIYQFHYKNWPDHDVPSSIDPILELIWDVR--CYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIipENFSVFSL 237
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKknLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEA--GEVDIFDT 78

                           90       100
                   ....*....|....*....|....*..
gi 767903708   238 IREMRTQRPSLVQTQEQYELVYNAVLE 264
Cdd:smart00012  79 VKELRSQRPGMVQTEEQYLFLYRALLE 105
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
13-256 4.94e-37

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 140.23  E-value: 4.94e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  13 EAQSKKITKEEFANEFLKLKRQSTKYKADKTYPTTVAEKPKNikknRYKDILPYDYSRVElslitsdEDSSYINANFIKg 92
Cdd:COG5599    5 NPIAIKSEEEKINSRLSTLTNELAPSHNDPQYLQNINGSPLN----RFRDIQPYKETALR-------ANLGYLNANYIQ- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  93 VYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGK--------------------EAEKRKSDYI-----I 147
Cdd:COG5599   73 VIGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISKpkvkmpvyfrqdgeygkyevSSELTESIQLrdgieA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 148 RTLKVKFNS---ETRTIYQFHYKNWPDHDVPSSiDPILELIWDVRCYQEDDSV---PICIHCSAGCGRTGVICAIDYTWM 221
Cdd:COG5599  153 RTYVLTIKGtgqKKIEIPVLHVKNWPDHGAISA-EALKNLADLIDKKEKIKDPdklLPVVHCRAGVGRTGTLIACLALSK 231

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 767903708 222 LLKDGIIPEnFSVFSLIREMRTQR-PSLVQTQEQYE 256
Cdd:COG5599  232 SINALVQIT-LSVEEIVIDMRTSRnGGMVQTSEQLD 266
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 84-267 4.11e-36

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: 135.26  E-value: 4.11e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  84 YINANFIKGVYGPKA--YIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGK------------------------E 137
Cdd:cd14596    1 YINASYITMPVGEEElfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKvkchrywpetlqepmelenyqlrlE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 138 AEKRKSDYIIRTLKV--KFNSETRTIYQFHYKNWPDHDVPSSIDPILELIwdvrCYQED--DSVPICIHCSAGCGRTGVI 213
Cdd:cd14596   81 NYQALQYFIIRIIKLveKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFI----CYMRKvhNTGPIVVHCSAGIGRAGVL 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767903708 214 CAIDYTWMLLKDGIipeNFSVFSLIREMRTQRPSLVQTQEQYELVYNAVLELFK 267
Cdd:cd14596  157 ICVDVLLSLIEKDL---SFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 84-262 8.28e-36

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: 134.36  E-value: 8.28e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVM----------ACMEY-------EMGKEAEKRKSDYI 146
Cdd:cd14622    2 YINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMltelqereqeKCVQYwpsegsvTHGEITIEIKNDTL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 147 -----IRTLKVKFNSE--TRTIYQFHYKNWPDHDVPSSIDPILELIWDV-RCYQEDDSVPICIHCSAGCGRTGVICAIDY 218
Cdd:cd14622   82 letisIRDFLVTYNQEkqTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVqKQQQQTGNHPIVVHCSAGAGRTGTFIALSN 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 767903708 219 TWMLLK-DGIIpenfSVFSLIREMRTQRPSLVQTQEQYELVYNAV 262
Cdd:cd14622  162 ILERVKaEGLL----DVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 84-259 4.92e-35

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: 131.87  E-value: 4.92e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMA----------CMEY----EMGKEA----------E 139
Cdd:cd14557    1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVtrceegnrnkCAQYwpsmEEGSRAfgdvvvkineE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 140 KRKSDYIIRTLKVKFNSET---RTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAI 216
Cdd:cd14557   81 KICPDYIIRKLNINNKKEKgsgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYIGI 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 767903708 217 DytwmLLKDGIIPEN-FSVFSLIREMRTQRPSLVQTQEQYELVY 259
Cdd:cd14557  161 D----AMLEGLEAEGrVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 44-267 5.25e-34

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 132.43  E-value: 5.25e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  44 YPTTVAEKPKNIKKNRYKDILPYDYSRVELSliTSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVL 123
Cdd:PHA02742  42 FSCNESLELKNMKKCRYPDAPCFDRNRVILK--IEDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVR 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 124 IIVMACMEYEMGKEA-------EKRKS----DYIIRTLKVK------------FNSETRT---IYQFHYKNWPDHDVPSS 177
Cdd:PHA02742 120 VIVMITKIMEDGKEAcypywmpHERGKathgEFKIKTKKIKsfrnyavtnlclTDTNTGAsldIKHFAYEDWPHGGLPRD 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 178 IDPILELIWDVRCYQEDDSV-----------PICIHCSAGCGRTGVICAIDYTWMLLKDGIIpenFSVFSLIREMRTQRP 246
Cdd:PHA02742 200 PNKFLDFVLAVREADLKADVdikgenivkepPILVHCSAGLDRAGAFCAIDICISKYNERAI---IPLLSIVRDLRKQRH 276

                        250       260
                 ....*....|....*....|.
gi 767903708 247 SLVQTQEQYELVYNAVLELFK 267
Cdd:PHA02742 277 NCLSLPQQYIFCYFIVLIFAK 297
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 50-279 1.19e-33

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 131.66  E-value: 1.19e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  50 EKPKNIKKNRYKDILPYDYSRVELSlITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVM-- 127
Cdd:PHA02747  47 EKPENQPKNRYWDIPCWDHNRVILD-SGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMlt 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 128 ---------ACMEY-EMGKEAEKRKSDYIIRTLKV---------------KFNSETRTIYQFHYKNWPDHDVPSSIDPIL 182
Cdd:PHA02747 126 ptkgtngeeKCYQYwCLNEDGNIDMEDFRIETLKTsvrakyiltlieitdKILKDSRKISHFQCSEWFEDETPSDHPDFI 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 183 ELIWDV--------RCYQEDDSV--PICIHCSAGCGRTGVICAIDytwMLLKDGIIPENFSVFSLIREMRTQRPSLVQTQ 252
Cdd:PHA02747 206 KFIKIIdinrkksgKLFNPKDALlcPIVVHCSDGVGKTGIFCAVD---ICLNQLVKRKAICLAKTAEKIREQRHAGIMNF 282

                        250       260       270
                 ....*....|....*....|....*....|
gi 767903708 253 EQYELV---YNAVLELFKRQMDVIRDKHSG 279
Cdd:PHA02747 283 DDYLFIqpgYEVLHYFLSKIKAIDKIKFCG 312
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 84-264 2.65e-33

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: 127.09  E-value: 2.65e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGK---------EAE------------KRK 142
Cdd:cd14632    1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRvkcskywpdDSDtygdikitllktETL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 143 SDYIIRTLKVKFN--SETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTW 220
Cdd:cd14632   81 AEYSVRTFALERRgySARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYIVLDVML 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 767903708 221 -MLLKDGIIpenfSVFSLIREMRTQRPSLVQTQEQYELVYNAVLE 264
Cdd:cd14632  161 dMAECEGVV----DIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 84-259 3.06e-33

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: 127.11  E-value: 3.06e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  84 YINANFIKGV--YGPKaYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKE-----------------------A 138
Cdd:cd14539    1 YINASLIEDLtpYCPR-FIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQkvhrywptergqalvygaitvslQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 139 EKRKSDYII-RTLKVKFN--SETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCY---QEDDSVPICIHCSAGCGRTGV 212
Cdd:cd14539   80 SVRTTPTHVeRIISIQHKdtRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHylqQRSLQTPIVVHCSSGVGRTGA 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 767903708 213 ICAIdYTWM--LLKDGIIPEnfsVFSLIREMRTQRPSLVQTQEQYELVY 259
Cdd:cd14539  160 FCLL-YAAVqeIEAGNGIPD---LPQLVRKMRQQRKYMLQEKEHLKFCY 204
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 84-259 4.13e-33

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: 126.37  E-value: 4.13e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVM---------ACMEY--EMGKEA----------EKRK 142
Cdd:cd14556    1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMlnqldpkdqSCPQYwpDEGSGTygpiqvefvsTTID 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 143 SDYIIRTLKV----KFNSETRTIYQFHYKNWPDH-DVPSSIDPILELIWDVRCYQED-DSVPICIHCSAGCGRTGVICAI 216
Cdd:cd14556   81 EDVISRIFRLqnttRPQEGYRMVQQFQFLGWPRDrDTPPSKRALLKLLSEVEKWQEQsGEGPIVVHCLNGVGRSGVFCAI 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 767903708 217 DYTWMLLKDgiipEN-FSVFSLIREMRTQRPSLVQTQEQYELVY 259
Cdd:cd14556  161 SSVCERIKV----ENvVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 84-267 9.57e-33

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


Pssm-ID: 350449 [Multi-domain]  Cd Length: 212  Bit Score: 125.83  E-value: 9.57e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  84 YINANFIKGVYGPKA----YIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGK----------------------- 136
Cdd:cd14601    2 YINANYINMEIPSSSiinrYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRvkchqywpepsgsssyggfqvtc 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 137 EAEKRKSDYIIR--TLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVIC 214
Cdd:cd14601   82 HSEEGNPAYVFRemTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTGVLI 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767903708 215 AIDyTWMLLKDGiipeNFSVFSL--IREMRTQRPSLVQTQEQYELVYNAVLELFK 267
Cdd:cd14601  162 TME-TAMCLIEC----NQPVYPLdiVRTMRDQRAMMIQTPSQYRFVCEAILKVYE 211
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 51-262 1.20e-31

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 125.91  E-value: 1.20e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  51 KPKNIKKNRYKDILPYDYSRVELS------------------LITS-DEDSSYINANFIKGVYGPKAYIATQGPLSTTLL 111
Cdd:PHA02746  48 KKENLKKNRFHDIPCWDHSRVVINaheslkmfdvgdsdgkkiEVTSeDNAENYIHANFVDGFKEANKFICAQGPKEDTSE 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 112 DFWRMIWEYSVLIIV---------MACMEYEMG-KEAEKRKSDYIIRTLKV---------------KFNSETRTIYQFHY 166
Cdd:PHA02746 128 DFFKLISEHESQVIVsltdiddddEKCFELWTKeEDSELAFGRFVAKILDIieelsftktrlmitdKISDTSREIHHFWF 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 167 KNWPDHDVPSSIDPILELIWDVRCYQ-------EDDSV---PICIHCSAGCGRTGVICAIDYTWMLLKDgiiPENFSVFS 236
Cdd:PHA02746 208 PDWPDNGIPTGMAEFLELINKVNEEQaelikqaDNDPQtlgPIVVHCSAGIGRAGTFCAIDNALEQLEK---EKEVCLGE 284

                        250       260
                 ....*....|....*....|....*.
gi 767903708 237 LIREMRTQRPSLVQTQEQYELVYNAV 262
Cdd:PHA02746 285 IVLKIRKQRHSSVFLPEQYAFCYKAL 310
PHA02738 PHA02738
hypothetical protein; Provisional
 33-262 2.36e-31

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 125.04  E-value: 2.36e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  33 RQSTKYKADKTYPTTVAEKpKNIKKNRYKDILPYDYSRVELSliTSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLD 112
Cdd:PHA02738  29 REHQKVISEKVDGTFNAEK-KNRKLNRYLDAVCFDHSRVILP--AERNRGDYINANYVDGFEYKKKFICGQAPTRQTCYD 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 113 FWRMIWEYSVLIIVMACMEYEMGKE------------------------AEKRKSDYIIRTLKVKFNSE-TRTIYQFHYK 167
Cdd:PHA02738 106 FYRMLWMEHVQIIVMLCKKKENGREkcfpywsdveqgsirfgkfkitttQVETHPHYVKSTLLLTDGTSaTQTVTHFNFT 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 168 NWPDHDVPSSIDPILELIWDVRCYQED-------------DSVPICIHCSAGCGRTGVICAIDYTWMLLKDGiipENFSV 234
Cdd:PHA02738 186 AWPDHDVPKNTSEFLNFVLEVRQCQKElaqeslqighnrlQPPPIVVHCNAGLGRTPCYCVVDISISRFDAC---ATVSI 262

                        250       260
                 ....*....|....*....|....*...
gi 767903708 235 FSLIREMRTQRPSLVQTQEQYELVYNAV 262
Cdd:PHA02738 263 PSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 84-267 1.03e-30

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: 120.47  E-value: 1.03e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  84 YINANFIKGVYGPKA--YIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKEAEKR-------------------- 141
Cdd:cd14598    1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRywprlgsrhntvtygrfkit 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 142 ---KSD---YIIRTLKVK--FNSETRTIYQFHYKNWPDHDVPSSID---PILELIWDVRCYQEDDS------VPICIHCS 204
Cdd:cd14598   81 trfRTDsgcYATTGLKIKhlLTGQERTVWHLQYTDWPEHGCPEDLKgflSYLEEIQSVRRHTNSTIdpkspnPPVLVHCS 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767903708 205 AGCGRTGVICAIDYTWMLLKDGiipENFSVFSLIREMRTQRPSLVQTQEQYELVYNAVLELFK 267
Cdd:cd14598  161 AGVGRTGVVILSEIMIACLEHN---EMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 84-260 1.50e-30

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: 119.49  E-value: 1.50e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  84 YINANFIKG---VYGPKaYIATQGPLSTTLLDFWRMIWEYSVLIIVM-----------ACMEYEMGKEAEKRK------- 142
Cdd:cd17658    1 YINASLVETpasESLPK-FIATQGPLPHTFEDFWEMVIQQRCPVIIMltrlvdnystaKCADYFPAEENESREfgrisvt 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 143 ------SDYII--RTLKVKFNS---ETRTIYQFHYKNWPDHDVPSSIDPILELIwdVRCYQEDDSV-PICIHCSAGCGRT 210
Cdd:cd17658   80 nkklkhSQHSItlRVLEVQYIEseePPLSVLHIQYPEWPDHGVPKDTRSVRELL--KRLYGIPPSAgPIVVHCSAGIGRT 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 767903708 211 GVICAIDYTWMLLKDGIIpENFSVFSLIREMRTQRPSLVQTQEQYELVYN 260
Cdd:cd17658  158 GAYCTIHNTIRRILEGDM-SAVDLSKTVRKFRSQRIGMVQTQDQYIFCYA 206
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 84-259 4.83e-29

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: 115.01  E-value: 4.83e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKE---------AEKRKS----------- 143
Cdd:cd14551    1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKkcsqywpdqGCWTYGnlrvrvedtvv 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 144 --DYIIRTLKV-KFNSET-----RTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICA 215
Cdd:cd14551   81 lvDYTTRKFCIqKVNRGIgekrvRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTGTFIV 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 767903708 216 IDYTW-MLLKDGIIpenfSVFSLIREMRTQRPSLVQTQEQYELVY 259
Cdd:cd14551  161 IDAMLdMMHAEGKV----DVFGFVSRIRQQRSQMVQTDMQYVFIY 201
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 84-264 1.90e-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: 95.86  E-value: 1.90e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVM--------ACMEYeMGKEAEKR-------------K 142
Cdd:cd14636    1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMlnevdlaqGCPQY-WPEEGMLRygpiqvecmscsmD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 143 SDYIIRTLKVKFNSETRTIY----QFHYKNWPDH-DVPSSIDPILELIWDVRCYQED----DSVPIcIHCSAGCGRTGVI 213
Cdd:cd14636   80 CDVISRIFRICNLTRPQEGYlmvqQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEEcdegEGRTI-IHCLNGGGRSGMF 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767903708 214 CAIDYTWMLLKDGIIPEnfsVFSLIREMRTQRPSLVQTQEQYELVYNAVLE 264
Cdd:cd14636  159 CAISIVCEMIKRQNVVD---VFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 84-264 1.35e-21

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: 93.55  E-value: 1.35e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMA--------CMEYEMGKE------------AEKRKS 143
Cdd:cd14634    1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLnemdaaqlCMQYWPEKTsccygpiqvefvSADIDE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 144 DYIIRTLKV----KFNSETRTIYQFHYKNWPDH-DVPSSIDPILELIWDVRCYQED---DSVPICIHCSAGCGRTGVICA 215
Cdd:cd14634   81 DIISRIFRIcnmaRPQDGYRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQydgREGRTVVHCLNGGGRSGTFCA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 767903708 216 I-DYTWMLLKDGIIpenfSVFSLIREMRTQRPSLVQTQEQYELVYNAVLE 264
Cdd:cd14634  161 IcSVCEMIQQQNII----DVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 84-264 1.22e-18

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: 85.12  E-value: 1.22e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVM--------ACMEY--EMGKE----------AEKRKS 143
Cdd:cd14635    1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMlndvdpaqLCPQYwpENGVHrhgpiqvefvSADLEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 144 DYIIRTLKVkFNSET-----RTIYQFHYKNWPDH-DVPSSIDPILELIWDVRCYQED---DSVPICIHCSAGCGRTGVIC 214
Cdd:cd14635   81 DIISRIFRI-YNAARpqdgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEyngGEGRTVVHCLNGGGRSGTFC 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 767903708 215 AIDYTWMLLKDgiiPENFSVFSLIREMRTQRPSLVQTQEQYELVYNAVLE 264
Cdd:cd14635  160 AISIVCEMLRH---QRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 84-264 1.70e-17

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: 81.88  E-value: 1.70e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVM-----------ACMEY--EMGKE----------AEK 140
Cdd:cd14637    1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMlnqlnqsnsawPCLQYwpEPGLQqygpmevefvSGS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 141 RKSDYIIRTLKVK----FNSETRTIYQFHYKNW-PDHDVPSSIDPILELIWDVRCYQEDDSV-PICIHCSAGCGRTGVIC 214
Cdd:cd14637   81 ADEDIVTRLFRVQnitrLQEGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQRESGEgRTVVHCLNGGGRSGTYC 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767903708 215 AIDytwmLLKDGIIPENF-SVFSLIREMRTQRPSLVQTQEQYELVYNAVLE 264
Cdd:cd14637  161 ASA----MILEMIRCHNIvDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 84-260 2.28e-17

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


Pssm-ID: 350398 [Multi-domain]  Cd Length: 200  Bit Score: 81.21  E-value: 2.28e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVM---------------------ACMEYEMGKEAEKRK 142
Cdd:cd14550    1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMltdnelnedepiywptkekplECETFKVTLSGEDHS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 143 S----------DYIIRTLKVKFNSETRtiyQFHYKNWPDHDVPssIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGV 212
Cdd:cd14550   81 ClsneirlivrDFILESTQDDYVLEVR---QFQCPSWPNPCSP--IHTVFELINTVQEWAQQRDGPIVVHDRYGGVQAAT 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 767903708 213 ICAidytWMLLKDGIIPEN-FSVFSLIREMRTQRPSLVQTQEQYELVYN 260
Cdd:cd14550  156 FCA----LTTLHQQLEHESsVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 84-263 6.89e-17

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: 79.72  E-value: 6.89e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMA----------------------CMEYE-------- 133
Cdd:cd17670    1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdnqglaedefvywpsreesmnCEAFTvtliskdr 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 134 --MGKEAEKRKSDYIIRTLKVKFNSETRtiyQFHYKNWPDHDVPssIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTG 211
Cdd:cd17670   81 lcLSNEEQIIIHDFILEATQDDYVLEVR---HFQCPKWPNPDAP--ISSTFELINVIKEEALTRDGPTIVHDEFGAVSAG 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767903708 212 VICAIDYTWMLLKDGIIPENFSVFSLIREMrtqRPSLVQTQEQYELVYNAVL 263
Cdd:cd17670  156 TLCALTTLSQQLENENAVDVYQVAKMINLM---RPGVFTDIEQYQFLYKAML 204
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 84-263 1.86e-16

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: 78.50  E-value: 1.86e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  84 YINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVM----------------------ACMEYEMGKEAEKR 141
Cdd:cd17669    1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMlpdgqnmaedefvywpnkdepiNCETFKVTLIAEEH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 142 K----------SDYIIRTLKVKFNSETRtiyQFHYKNWPDHDVPssIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTG 211
Cdd:cd17669   81 KclsneekliiQDFILEATQDDYVLEVR---HFQCPKWPNPDSP--ISKTFELISIIKEEAANRDGPMIVHDEHGGVTAG 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767903708 212 VICAIdYTWMllkDGIIPEN-FSVFSLIREMRTQRPSLVQTQEQYELVYNAVL 263
Cdd:cd17669  156 TFCAL-TTLM---HQLEKENsVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 58-257 8.79e-13

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: 68.58  E-value: 8.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  58 NRYKDIlpydYSRVELSlitsdeDSSYINANFIKgVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIV-------MACM 130
Cdd:cd14559    1 NRFTNI----QTRVSTP------VGKNLNANRVQ-IGNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVvlasnkdIQRK 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 131 ---EY--------EMGKEAEKRKSDYIIR-------TLKVKFNSETRTIYQFHYKNWPDHDVPSSID------------- 179
Cdd:cd14559   70 glpPYfrqsgtygSVTVKSKKTGKDELVDglkadmyNLKITDGNKTITIPVVHVTNWPDHTAISSEGlkeladlvnksae 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 180 ---PILELIWDVRCYQEDDSVPIcIHCSAGCGRTGVICAIdytwMLLKDGiiPENFSVFSLIREMRTQRPS-LVQTQEQY 255
Cdd:cd14559  150 ekrNFYKSKGSSAINDKNKLLPV-IHCRAGVGRTGQLAAA----MELNKS--PNNLSVEDIVSDMRTSRNGkMVQKDEQL 222


                 ..
gi 767903708 256 EL 257
Cdd:cd14559  223 DT 224
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 96-260 9.68e-12

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: 62.37  E-value: 9.68e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  96 PKAYIATQGPLSTtLLDFWRMIWEYSVLIIVMACmeyemgkeaekrksdyiirtlkvkfnsetrtiyqfhyknwpDHDVp 175
Cdd:cd14494    6 PLRLIAGALPLSP-LEADSRFLKQLGVTTIVDLT-----------------------------------------LAMV- 42

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 176 ssiDPILELIWDvrcyQEDDSVPICIHCSAGCGRTGVICAIdytWMLLKDGiipenFSVFSLIREMRTQRPS-LVQTQEQ 254
Cdd:cd14494   43 ---DRFLEVLDQ----AEKPGEPVLVHCKAGVGRTGTLVAC---YLVLLGG-----MSAEEAVRIVRLIRPGgIPQTIEQ 107


                 ....*.
gi 767903708 255 YELVYN 260
Cdd:cd14494  108 LDFLIK 113
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
169-259 1.18e-07

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 51.51  E-value: 1.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 169 WPDHDVPS--SIDPILELIWdvRCYQEDDSVpiCIHCSAGCGRTGVICAidytWMLLKDGIIPENfsvfsLIREMRTQRP 246
Cdd:COG2453   55 IPDFGAPDdeQLQEAVDFID--EALREGKKV--LVHCRGGIGRTGTVAA----AYLVLLGLSAEE-----ALARVRAARP 121

                         90
                 ....*....|...
gi 767903708 247 SLVQTQEQYELVY 259
Cdd:COG2453  122 GAVETPAQRAFLE 134
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 49-274 1.34e-06

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 50.74  E-value: 1.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708  49 AEKPKNIKKNRYKD------ILPYDYSRVELSlitsdEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSV 122
Cdd:PHA02740  42 ANKACAQAENKAKDenlalhITRLLHRRIKLF-----NDEKVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKV 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 123 LIIVMAC--------MEYEMGKEAEKRKSD-YIIRTLKV----KFN----------SETRTIYQFHYKNWP----DHDVP 175
Cdd:PHA02740 117 QIIVLISrhadkkcfNQFWSLKEGCVITSDkFQIETLEIiikpHFNltllsltdkfGQAQKISHFQYTAWPadgfSHDPD 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 176 SSID---PILELIWDVRCYQEDDSV-PICIHCSAGCGRTGVICAIDYTWMLL-KDGIIpenfSVFSLIREMRTQRPSLVQ 250
Cdd:PHA02740 197 AFIDffcNIDDLCADLEKHKADGKIaPIIIDCIDGISSSAVFCVFDICATEFdKTGML----SIANALKKVRQKKYGCMN 272

                        250       260
                 ....*....|....*....|....
gi 767903708 251 TQEQYELVYNAVLELFKRQMDVIR 274
Cdd:PHA02740 273 CLDDYVFCYHLIAAYLKEKFDILK 296
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 170-259 2.64e-06

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


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 48.03  E-value: 2.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 170 PDHDVPSSIDPILELIWDVR-CYQEDDSVpiCIHCSAGCGRTGVICAidYTWMLLKDGIIPEnfsvfSLIREMRTQRPSL 248
Cdd:cd14505   81 PDGGVPSDIAQWQELLEELLsALENGKKV--LIHCKGGLGRTGLIAA--CLLLELGDTLDPE-----QAIAAVRALRPGA 151

                         90
                 ....*....|.
gi 767903708 249 VQTQEQYELVY 259
Cdd:cd14505  152 IQTPKQENFLH 162
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 161-258 5.65e-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: 45.03  E-value: 5.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 161 IYQFHYkNWPDHDVPSsidpiLELIWD---VRCYQEDDSVPICIHCSAGCGRTGVICAidyTWMLLKDGIIPENfsvfsL 237
Cdd:cd14506   77 IYFYNF-GWKDYGVPS-----LTTILDivkVMAFALQEGGKVAVHCHAGLGRTGVLIA---CYLVYALRMSADQ-----A 142

                         90       100
                 ....*....|....*....|.
gi 767903708 238 IREMRTQRPSLVQTQEQYELV 258
Cdd:cd14506  143 IRLVRSKRPNSIQTRGQVLCV 163
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 163-215 8.93e-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: 43.34  E-value: 8.93e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767903708 163 QFHYKNWPDHDVPSsidpiLELIWDVrCY------QEDDSVPICIHCSAGCGRTGVICA 215
Cdd:cd14497   62 RVLHYGFPDHHPPP-----LGLLLEI-VDdidswlSEDPNNVAVVHCKAGKGRTGTVIC 114
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 198-258 1.07e-04

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: 43.03  E-value: 1.07e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767903708 198 PICIHCSAGCGRTGVI--CAIDYTWMLlkDGIipenfsvfSLIREMRTQRPSLVQTQEQYELV 258
Cdd:cd14504   84 AVLVHCLAGKGRTGTMlaCYLVKTGKI--SAV--------DAINEIRRIRPGSIETSEQEKFV 136
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 170-258 5.72e-04

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: 41.58  E-value: 5.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903708 170 PDHDVPSsIDPILELIWDVRCY-QEDDSVPICIHCSAGCGRTG-VICAidytWmLLKDGIIPENFSVFSLIREMRTqRPS 247
Cdd:cd14510   82 DDHNVPT-LDEMLSFTAEVREWmAADPKNVVAIHCKGGKGRTGtMVCA----W-LIYSGQFESAKEALEYFGERRT-DKS 154

                         90
                 ....*....|....*..
gi 767903708 248 L------VQTQEQYELV 258
Cdd:cd14510  155 VsskfqgVETPSQSRYV 171
PFA-DSP_Oca2 cd17661
atypical dual specificity phosphatases similar to oxidant-induced cell-cycle arrest protein 2; ...
 155-216 4.59e-03

atypical dual specificity phosphatases similar to oxidant-induced cell-cycle arrest protein 2; Oxidant-induced cell-cycle arrest protein 2 (Oca2) is an atypical dual specificity phosphatase of unknown function. It has been identified as a putative negative regulator acting on cell wall integrity and mating MAPK pathways in yeast. It belongs to a group of atypical DSPs present in plants, fungi, kinetoplastids, and slime molds called plant and fungi atypical dual-specificity phosphatases (PFA-DSPs). Oca2 may be an inactive DSP-like protein as it lacks the CxxxxxR catalytic motif.


Pssm-ID: 350499 [Multi-domain]  Cd Length: 146  Bit Score: 38.15  E-value: 4.59e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767903708 155 NSETRTIYQFHYKNWPDHDVP---SSIDPILELIWDVRCYqeddsvPICIHCSAGCGRTGVICAI 216
Cdd:cd17661   53 QSQGIELYYFDFSSSSEPFTEedqERMEQALKLLLDKRNY------PILVHSNKGKHRVGVLVGI 111
PTP_PTEN cd14509
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ...
 164-215 6.36e-03

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


Pssm-ID: 350359 [Multi-domain]  Cd Length: 158  Bit Score: 37.95  E-value: 6.36e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767903708 164 FHYK--NWP--DHDVPSsIDPILELIWDVRCY-QEDDSVPICIHCSAGCGRTGV-ICA 215
Cdd:cd14509   58 FNGRvaEYPfdDHNPPP-LELIKPFCEDVDEWlKEDEKNVAAVHCKAGKGRTGVmICC 114
Oca4 COG2365
Protein tyrosine/serine phosphatase Oca4 [Signal transduction mechanisms];
165-216 8.87e-03

Protein tyrosine/serine phosphatase Oca4 [Signal transduction mechanisms];


Pssm-ID: 441932 [Multi-domain]  Cd Length: 248  Bit Score: 38.79  E-value: 8.87e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767903708 165 HYKNWPDHDVPSSIDPILELIwdvrcyQEDDSVPICIHCSAGCGRTGVICAI 216
Cdd:COG2365  108 LYRAFVDPDAADAYRAAFRAL------ADAENGPVLFHCTAGKDRTGVAAAL 153
 
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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