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Conserved domains on  [gi|320541922|ref|NP_001188574|]
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protein tyrosine phosphatase Meg2, isoform H [Drosophila melanogaster]

Protein Classification

protein-tyrosine phosphatase family protein; phosphatase PAP2/dual specificity phosphatase family protein( domain architecture ID 12998429)

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| bifunctional phosphatase PAP2/dual specificity phosphatase (DSP) family protein containing a C-terminal DSP domain that may dephosphorylate phosphotyrosine, phosphoserine, and phosphothreonine residues in target proteins, and an N-terminal phosphatase PAP2 domain that may be a histidine phosphatase that catalyzes the dephosphorylation of phospholipids

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 200-470 0e+00

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: 551.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 200 GRHGLIKEYADIRNRAPEGTFLHARMRANLTKNRYTDVLCYDHSRVVLAHEDGDEPSDYINANFVDGYKQKNAYISTQGP 279
Cdd:cd14543    1 QKRGIYEEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 280 LPKTSQDFWRMIWEQHCLVIVMTTRVMERGRVKCGQYWEPTEESSLEFGDYHVRTISVECNEDYMVASLELRNIKTDEIR 359
Cdd:cd14543   81 LPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDESR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 360 NVSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQAQLVQGLGDTWAGHPRGPPIVVHCSAGIGRTGTFITLDICISRLEDV 439
Cdd:cd14543  161 QVTHFQFTSWPDFGVPSSAAALLDFLGEVRQQQALAVKAMGDRWKGHPPGPPIVVHCSAGIGRTGTFCTLDICLSQLEDV 240

                        250       260       270
                 ....*....|....*....|....*....|.
gi 320541922 440 GTADIRGTVEKIRSQRAYSIQMPDQYVFCHL 470
Cdd:cd14543  241 GTLNVMQTVRRMRTQRAFSIQTPDQYYFCYK 271
 
Name Accession Description Interval E-value
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 200-470 0e+00

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: 551.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 200 GRHGLIKEYADIRNRAPEGTFLHARMRANLTKNRYTDVLCYDHSRVVLAHEDGDEPSDYINANFVDGYKQKNAYISTQGP 279
Cdd:cd14543    1 QKRGIYEEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 280 LPKTSQDFWRMIWEQHCLVIVMTTRVMERGRVKCGQYWEPTEESSLEFGDYHVRTISVECNEDYMVASLELRNIKTDEIR 359
Cdd:cd14543   81 LPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDESR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 360 NVSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQAQLVQGLGDTWAGHPRGPPIVVHCSAGIGRTGTFITLDICISRLEDV 439
Cdd:cd14543  161 QVTHFQFTSWPDFGVPSSAAALLDFLGEVRQQQALAVKAMGDRWKGHPPGPPIVVHCSAGIGRTGTFCTLDICLSQLEDV 240

                        250       260       270
                 ....*....|....*....|....*....|.
gi 320541922 440 GTADIRGTVEKIRSQRAYSIQMPDQYVFCHL 470
Cdd:cd14543  241 GTLNVMQTVRRMRTQRAFSIQTPDQYYFCYK 271
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
228-474 1.00e-119

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 350.77  E-value: 1.00e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922  228 NLTKNRYTDVLCYDHSRVVLAHEDGdePSDYINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVME 307
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGDPG--PSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922  308 RGRVKCGQYWEPTEESSLEFGDYHVRTISVE-CNEDYMVASLELRNIKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQ 386
Cdd:pfam00102  79 KGREKCAQYWPEEEGESLEYGDFTVTLKKEKeDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922  387 KVREKQaqlvqglgdtwaGHPRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYV 466
Cdd:pfam00102 159 KVRKSS------------LDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYI 226


                  ....*...
gi 320541922  467 FCHLALIE 474
Cdd:pfam00102 227 FLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
203-474 1.80e-118

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 348.49  E-value: 1.80e-118
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922   203 GLIKEYADI-RNRAPEGTFLHARMRANLTKNRYTDVLCYDHSRVVLAHEDGdEPSDYINANFVDGYKQKNAYISTQGPLP 281
Cdd:smart00194   1 GLEEEFEKLdRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPG-EGSDYINASYIDGPNGPKAYIATQGPLP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922   282 KTSQDFWRMIWEQHCLVIVMTTRVMERGRVKCGQYWEPTEESSLEFGDYHVRTISVECNEDYMVASLELRNIKTDEIRNV 361
Cdd:smart00194  80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTV 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922   362 SHWQFTSWPDYGVPSSAMAMLNFLQKVREKQAQLvqglgdtwaghprGPPIVVHCSAGIGRTGTFITLDICISRLEDVGT 441
Cdd:smart00194 160 THYHYTNWPDHGVPESPESILDLIRAVRKSQSTS-------------TGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKE 226

                          250       260       270
                   ....*....|....*....|....*....|...
gi 320541922   442 ADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIE 474
Cdd:smart00194 227 VDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
PHA02738 PHA02738
hypothetical protein; Provisional
 206-475 3.14e-77

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 244.83  E-value: 3.14e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 206 KEYADIRNRAPEGTFLHARMRANLtkNRYTDVLCYDHSRVVLAHEDGDepSDYINANFVDGYKQKNAYISTQGPLPKTSQ 285
Cdd:PHA02738  29 REHQKVISEKVDGTFNAEKKNRKL--NRYLDAVCFDHSRVILPAERNR--GDYINANYVDGFEYKKKFICGQAPTRQTCY 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 286 DFWRMIWEQHCLVIVMTTRVMERGRVKCGQYWEPTEESSLEFGDYHVRTISVECNEDYMVASLELRNiKTDEIRNVSHWQ 365
Cdd:PHA02738 105 DFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGSIRFGKFKITTTQVETHPHYVKSTLLLTD-GTSATQTVTHFN 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 366 FTSWPDYGVPSSAMAMLNFLQKVREKQAQLVQglGDTWAGHPRG--PPIVVHCSAGIGRTGTFITLDICISRLEDVGTAD 443
Cdd:PHA02738 184 FTAWPDHDVPKNTSEFLNFVLEVRQCQKELAQ--ESLQIGHNRLqpPPIVVHCNAGLGRTPCYCVVDISISRFDACATVS 261

                        250       260       270
                 ....*....|....*....|....*....|..
gi 320541922 444 IRGTVEKIRSQRAYSIQMPDQYVFCHLALIEY 475
Cdd:PHA02738 262 IPSIVSSIRNQRYYSLFIPFQYFFCYRAVKRY 293
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
228-480 4.90e-33

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 126.74  E-value: 4.90e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 228 NLTKNRYTDVLCYDHSRVvlahedgDEPSDYINANFVDGyKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVME 307
Cdd:COG5599   42 GSPLNRFRDIQPYKETAL-------RANLGYLNANYIQV-IGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDE 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 308 --RGRVKCGQYWEPTeesslefGDYHVRTISVE------CNEDYMVASLELRNIKTD-EIRNVSHWQFTSWPDYGVPSSA 378
Cdd:COG5599  114 isKPKVKMPVYFRQD-------GEYGKYEVSSEltesiqLRDGIEARTYVLTIKGTGqKKIEIPVLHVKNWPDHGAISAE 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 379 mAMLNFLQKVREKQaqlvqglgdTWAGHPRGPPiVVHCSAGIGRTGTFItLDICISRLEDVGTaDIRGTVEKI----RSQ 454
Cdd:COG5599  187 -ALKNLADLIDKKE---------KIKDPDKLLP-VVHCRAGVGRTGTLI-ACLALSKSINALV-QITLSVEEIvidmRTS 253

                        250       260
                 ....*....|....*....|....*..
gi 320541922 455 RAYSI-QMPDQYVFchlaLIEYAYSRG 480
Cdd:COG5599  254 RNGGMvQTSEQLDV----LVKLAEQQI 276
 
Name Accession Description Interval E-value
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 200-470 0e+00

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: 551.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 200 GRHGLIKEYADIRNRAPEGTFLHARMRANLTKNRYTDVLCYDHSRVVLAHEDGDEPSDYINANFVDGYKQKNAYISTQGP 279
Cdd:cd14543    1 QKRGIYEEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 280 LPKTSQDFWRMIWEQHCLVIVMTTRVMERGRVKCGQYWEPTEESSLEFGDYHVRTISVECNEDYMVASLELRNIKTDEIR 359
Cdd:cd14543   81 LPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDESR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 360 NVSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQAQLVQGLGDTWAGHPRGPPIVVHCSAGIGRTGTFITLDICISRLEDV 439
Cdd:cd14543  161 QVTHFQFTSWPDFGVPSSAAALLDFLGEVRQQQALAVKAMGDRWKGHPPGPPIVVHCSAGIGRTGTFCTLDICLSQLEDV 240

                        250       260       270
                 ....*....|....*....|....*....|.
gi 320541922 440 GTADIRGTVEKIRSQRAYSIQMPDQYVFCHL 470
Cdd:cd14543  241 GTLNVMQTVRRMRTQRAFSIQTPDQYYFCYK 271
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
228-474 1.00e-119

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 350.77  E-value: 1.00e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922  228 NLTKNRYTDVLCYDHSRVVLAHEDGdePSDYINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVME 307
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGDPG--PSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922  308 RGRVKCGQYWEPTEESSLEFGDYHVRTISVE-CNEDYMVASLELRNIKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQ 386
Cdd:pfam00102  79 KGREKCAQYWPEEEGESLEYGDFTVTLKKEKeDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922  387 KVREKQaqlvqglgdtwaGHPRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYV 466
Cdd:pfam00102 159 KVRKSS------------LDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYI 226


                  ....*...
gi 320541922  467 FCHLALIE 474
Cdd:pfam00102 227 FLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
203-474 1.80e-118

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 348.49  E-value: 1.80e-118
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922   203 GLIKEYADI-RNRAPEGTFLHARMRANLTKNRYTDVLCYDHSRVVLAHEDGdEPSDYINANFVDGYKQKNAYISTQGPLP 281
Cdd:smart00194   1 GLEEEFEKLdRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPG-EGSDYINASYIDGPNGPKAYIATQGPLP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922   282 KTSQDFWRMIWEQHCLVIVMTTRVMERGRVKCGQYWEPTEESSLEFGDYHVRTISVECNEDYMVASLELRNIKTDEIRNV 361
Cdd:smart00194  80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTV 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922   362 SHWQFTSWPDYGVPSSAMAMLNFLQKVREKQAQLvqglgdtwaghprGPPIVVHCSAGIGRTGTFITLDICISRLEDVGT 441
Cdd:smart00194 160 THYHYTNWPDHGVPESPESILDLIRAVRKSQSTS-------------TGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKE 226

                          250       260       270
                   ....*....|....*....|....*....|...
gi 320541922   442 ADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIE 474
Cdd:smart00194 227 VDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 258-469 1.13e-93

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: 282.64  E-value: 1.13e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 258 YINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVMERGRVKCGQYWEPTEESSLEFGDYHVRTISV 337
Cdd:cd00047    1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYGDITVTLVSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 338 ECNEDYMVASLELRNIKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQAQlvqglgdtwaghpRGPPIVVHCS 417
Cdd:cd00047   81 EELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARK-------------PNGPIVVHCS 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 320541922 418 AGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCH 469
Cdd:cd00047  148 AGVGRTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIY 199
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 227-474 3.84e-91

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: 277.74  E-value: 3.84e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 227 ANLTKNRYTDVLCYDHSRVVLAHEDGDEPSDYINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVM 306
Cdd:cd14553    2 VNKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 307 ERGRVKCGQYWePTEESSlEFGDYHVrTIsVECNE--DYMVASLELRNIKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNF 384
Cdd:cd14553   82 ERSRVKCDQYW-PTRGTE-TYGLIQV-TL-LDTVElaTYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAF 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 385 LQKVRekqaqlvqglgdtwAGHPR-GPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPD 463
Cdd:cd14553  158 LRRVK--------------ACNPPdAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTED 223

                        250
                 ....*....|.
gi 320541922 464 QYVFCHLALIE 474
Cdd:cd14553  224 QYIFIHDALLE 234
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 233-469 3.26e-84

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: 259.21  E-value: 3.26e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 233 RYTDVLCYDHSRVVLAHEDGDEPSDYINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVMERGRVK 312
Cdd:cd14548    1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 313 CGQYWePTEESSLEFGDYHVRTISVECNEDYMVASLELRNIktDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREkq 392
Cdd:cd14548   81 CDHYW-PFDQDPVYYGDITVTMLSESVLPDWTIREFKLERG--DEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRD-- 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 320541922 393 aqlvqglgdtWAGHPRGPPIvVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCH 469
Cdd:cd14548  156 ----------YIKQEKGPTI-VHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 206-476 3.17e-78

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: 246.10  E-value: 3.17e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 206 KEYADIrNRAPEGTFLHARMRANLTKNRYTDVLCYDHSRVVLAHEDGDEPSDYINANFVDGYKQKNAYISTQGPLPKTSQ 285
Cdd:cd14626   20 QEYESI-DPGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGYRKQNAYIATQGPLPETLS 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 286 DFWRMIWEQHCLVIVMTTRVMERGRVKCGQYWePTEESSlEFGDYHVRTISVECNEDYMVASLELRNIKTDEIRNVSHWQ 365
Cdd:cd14626   99 DFWRMVWEQRTATIVMMTRLEEKSRVKCDQYW-PIRGTE-TYGMIQVTLLDTVELATYSVRTFALYKNGSSEKREVRQFQ 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 366 FTSWPDYGVPSSAMAMLNFLQKVREkqaqlvqglgdtwAGHPRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIR 445
Cdd:cd14626  177 FMAWPDHGVPEYPTPILAFLRRVKA-------------CNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIY 243

                        250       260       270
                 ....*....|....*....|....*....|.
gi 320541922 446 GTVEKIRSQRAYSIQMPDQYVFCHLALIEYA 476
Cdd:cd14626  244 GHVTCMRSQRNYMVQTEDQYIFIHEALLEAA 274
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 258-469 7.70e-78

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: 242.26  E-value: 7.70e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 258 YINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVMERGRVKCGQYWePTEEsSLEFGDYHVRTISV 337
Cdd:cd14549    1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYW-PKEG-TETYGNIQVTLLST 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 338 ECNEDYMVASLELRNIK------TDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVrekqaqlvqglgdTWAGHPRGPP 411
Cdd:cd14549   79 EVLATYTVRTFSLKNLKlkkvkgRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKS-------------SAANPPGAGP 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 320541922 412 IVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCH 469
Cdd:cd14549  146 IVVHCSAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 231-470 1.69e-77

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: 242.30  E-value: 1.69e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 231 KNRYTDVLCYDHSRVVLAHEDGDepSDYINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVMERGR 310
Cdd:cd14545    1 LNRYRDRDPYDHDRSRVKLKQGD--NDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 311 VKCGQYW--EPTEESSLEFGDYHVRTISVECNEDYMVASLELRNIKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKV 388
Cdd:cd14545   79 IKCAQYWpqGEGNAMIFEDTGLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQKV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 389 REkQAQLVQGLGdtwaghprgpPIVVHCSAGIGRTGTFITLDICISRLE--DVGTADIRGTVEKIRSQRAYSIQMPDQYV 466
Cdd:cd14545  159 RE-SGSLSSDVG----------PPVVHCSAGIGRSGTFCLVDTCLVLIEkgNPSSVDVKKVLLEMRKYRMGLIQTPDQLR 227


                 ....
gi 320541922 467 FCHL 470
Cdd:cd14545  228 FSYL 231
PHA02738 PHA02738
hypothetical protein; Provisional
 206-475 3.14e-77

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 244.83  E-value: 3.14e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 206 KEYADIRNRAPEGTFLHARMRANLtkNRYTDVLCYDHSRVVLAHEDGDepSDYINANFVDGYKQKNAYISTQGPLPKTSQ 285
Cdd:PHA02738  29 REHQKVISEKVDGTFNAEKKNRKL--NRYLDAVCFDHSRVILPAERNR--GDYINANYVDGFEYKKKFICGQAPTRQTCY 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 286 DFWRMIWEQHCLVIVMTTRVMERGRVKCGQYWEPTEESSLEFGDYHVRTISVECNEDYMVASLELRNiKTDEIRNVSHWQ 365
Cdd:PHA02738 105 DFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGSIRFGKFKITTTQVETHPHYVKSTLLLTD-GTSATQTVTHFN 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 366 FTSWPDYGVPSSAMAMLNFLQKVREKQAQLVQglGDTWAGHPRG--PPIVVHCSAGIGRTGTFITLDICISRLEDVGTAD 443
Cdd:PHA02738 184 FTAWPDHDVPKNTSEFLNFVLEVRQCQKELAQ--ESLQIGHNRLqpPPIVVHCNAGLGRTPCYCVVDISISRFDACATVS 261

                        250       260       270
                 ....*....|....*....|....*....|..
gi 320541922 444 IRGTVEKIRSQRAYSIQMPDQYVFCHLALIEY 475
Cdd:PHA02738 262 IPSIVSSIRNQRYYSLFIPFQYFFCYRAVKRY 293
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 232-467 3.64e-76

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: 238.95  E-value: 3.64e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 232 NRYTDVLCYDHSRVVLAHEdGDEPSDYINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVMERGRV 311
Cdd:cd14615    1 NRYNNVLPYDISRVKLSVQ-SHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 312 KCGQYWePTEEsSLEFGDYHVRTISVECNEDYMVASLELRNIKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREK 391
Cdd:cd14615   80 KCEEYW-PSKQ-KKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREY 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 320541922 392 QAQlvqglgdtwagHPRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVF 467
Cdd:cd14615  158 MKQ-----------NPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVF 222
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 223-471 5.86e-76

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: 238.58  E-value: 5.86e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 223 ARMRANLTKNRYTDVLCYDHSRVVLAHEDGDEPSDYINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMT 302
Cdd:cd14554    1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 303 TRVMERGRVKCGQYWePTEESSlEFGDYHVRTISVECNEDYMVASLELRNIKTDEIRNVSHWQFTSWPDYGVPSSAMAML 382
Cdd:cd14554   81 TKLREMGREKCHQYW-PAERSA-RYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFI 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 383 NFLQKVREKQAQLVQglgdtwaghprGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMP 462
Cdd:cd14554  159 DFIGQVHKTKEQFGQ-----------EGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTE 227


                 ....*....
gi 320541922 463 DQYVFCHLA 471
Cdd:cd14554  228 DQYQFCYRA 236
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 228-475 4.97e-75

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: 236.59  E-value: 4.97e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 228 NLTKNRYTDVLCYDHSRVVLAHEDGDEP-SDYINANFV-------DGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVI 299
Cdd:cd14544    1 NKGKNRYKNILPFDHTRVILKDRDPNVPgSDYINANYIrnenegpTTDENAKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 300 VMTTRVMERGRVKCGQYWePTEESSLEFGDYHVRTISVECNEDYMVASLELRNIK-TDEIRNVSHWQFTSWPDYGVPSSA 378
Cdd:cd14544   81 VMTTKEVERGKNKCVRYW-PDEGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDqGDPIREIWHYQYLSWPDHGVPSDP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 379 MAMLNFLQKVREKQAQLvqglgdtwaghPRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTA---DIRGTVEKIRSQR 455
Cdd:cd14544  160 GGVLNFLEDVNQRQESL-----------PHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLDcdiDIQKTIQMVRSQR 228

                        250       260
                 ....*....|....*....|
gi 320541922 456 AYSIQMPDQYVFCHLALIEY 475
Cdd:cd14544  229 SGMVQTEAQYKFIYVAVAQY 248
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 208-476 3.23e-74

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: 235.69  E-value: 3.23e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 208 YADIRNRAPEGTFLHARMRANLTKNRYTDVLCYDHSRVVLAHEDgdepSDYINANFVDGYKQKNAYISTQGPLPKTSQDF 287
Cdd:cd14608    5 YQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQED----NDYINASLIKMEEAQRSYILTQGPLPNTCGHF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 288 WRMIWEQHCLVIVMTTRVMERGRVKCGQYWEPTEESSLEFGDYHVR--TISVECNEDYMVASLELRNIKTDEIRNVSHWQ 365
Cdd:cd14608   81 WEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKltLISEDIKSYYTVRQLELENLTTQETREILHFH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 366 FTSWPDYGVPSSAMAMLNFLQKVREKQAQlvqglgdtwagHPRGPPIVVHCSAGIGRTGTFITLDICI---SRLEDVGTA 442
Cdd:cd14608  161 YTTWPDFGVPESPASFLNFLFKVRESGSL-----------SPEHGPVVVHCSAGIGRSGTFCLADTCLllmDKRKDPSSV 229

                        250       260       270
                 ....*....|....*....|....*....|....
gi 320541922 443 DIRGTVEKIRSQRAYSIQMPDQYVFCHLALIEYA 476
Cdd:cd14608  230 DIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEGA 263
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 222-474 9.39e-74

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: 234.16  E-value: 9.39e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 222 HARMRANLTKNRYTDVLCYDHSRVVLAHEDGDEP--SDYINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVI 299
Cdd:cd17667   21 HSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGII 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 300 VMTTRVMERGRVKCGQYWePTEESSlEFGDYHVRTISVECNEDYMVASLELRNIKTDEI-----------RNVSHWQFTS 368
Cdd:cd17667  101 VMITNLVEKGRRKCDQYW-PTENSE-EYGNIIVTLKSTKIHACYTVRRFSIRNTKVKKGqkgnpkgrqneRTVIQYHYTQ 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 369 WPDYGVPSSAMAMLNFlqkVREKQAqlvqglgdtwAGHPRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTV 448
Cdd:cd17667  179 WPDMGVPEYALPVLTF---VRRSSA----------ARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFL 245

                        250       260
                 ....*....|....*....|....*.
gi 320541922 449 EKIRSQRAYSIQMPDQYVFCHLALIE 474
Cdd:cd17667  246 KHIRTQRNYLVQTEEQYIFIHDALLE 271
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 186-474 2.30e-73

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: 233.45  E-value: 2.30e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 186 PKPIDQI---VQMVKQRGRHGLIKEYADIrNRAPEGTFLHARMRANLTKNRYTDVLCYDHSRVVLAHEDGDEPSDYINAN 262
Cdd:cd14625    3 PIPISELaehTERLKANDNLKLSQEYESI-DPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINAN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 263 FVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVMERGRVKCGQYW-----------EPTEESSLEFGDYH 331
Cdd:cd14625   82 YIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWpsrgtetygmiQVTLLDTIELATFC 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 332 VRTISVECNedymvaslelrniKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREkqaqlvqglgdtwAGHPRGPP 411
Cdd:cd14625  162 VRTFSLHKN-------------GSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKT-------------CNPPDAGP 215

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 320541922 412 IVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIE 474
Cdd:cd14625  216 IVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLE 278
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 232-469 1.17e-72

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: 229.59  E-value: 1.17e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 232 NRYTDVLCYDHSRVVLAHEDGDEPSDYINANFVDGYKQKN-AYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVMERgR 310
Cdd:cd14547    1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGEEkAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA-K 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 311 VKCGQYWePTEESSlEFGDYHVRTISVECNEDYMVASLELRNikTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVRE 390
Cdd:cd14547   80 EKCAQYW-PEEENE-TYGDFEVTVQSVKETDGYTVRKLTLKY--GGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEE 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 391 -KQAQlvqglgdtwaghPRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCH 469
Cdd:cd14547  156 aRQTE------------PHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 186-474 3.69e-72

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: 230.77  E-value: 3.69e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 186 PKPIDQI---VQMVKQRGRHGLIKEYADIrNRAPEGTFLHARMRANLTKNRYTDVLCYDHSRVVLAHEDGDEPSDYINAN 262
Cdd:cd14624    3 PIPILELadhIERLKANDNLKFSQEYESI-DPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINAN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 263 FVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVMERGRVKCGQYWePTEESSLEfGDYHVRTISVECNED 342
Cdd:cd14624   82 YIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYW-PSRGTETY-GLIQVTLLDTVELAT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 343 YMVASLELRNIKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREkqaqlvqglgdtwAGHPRGPPIVVHCSAGIGR 422
Cdd:cd14624  160 YCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKT-------------CNPPDAGPMVVHCSAGVGR 226

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 320541922 423 TGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIE 474
Cdd:cd14624  227 TGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLE 278
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 208-472 6.41e-72

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: 229.08  E-value: 6.41e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 208 YADIRNRAPEGTFLHARMRANLTKNRYTDVLCYDHSRVVLAHEDgdepSDYINANFVDGYKQKNAYISTQGPLPKTSQDF 287
Cdd:cd14607    4 YLEIRNESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNTE----NDYINASLVVIEEAQRSYILTQGPLPNTCCHF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 288 WRMIWEQHCLVIVMTTRVMERGRVKCGQYWEPTEESSLEFGD--YHVRTISVECNEDYMVASLELRNIKTDEIRNVSHWQ 365
Cdd:cd14607   80 WLMVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSFKEtgFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFH 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 366 FTSWPDYGVPSSAMAMLNFLQKVREKQAqlvqgLGdtwaghPRGPPIVVHCSAGIGRTGTFITLDICISRLE--DVGTAD 443
Cdd:cd14607  160 YTTWPDFGVPESPASFLNFLFKVRESGS-----LS------PEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEkkDPDSVD 228

                        250       260
                 ....*....|....*....|....*....
gi 320541922 444 IRGTVEKIRSQRAYSIQMPDQYVFCHLAL 472
Cdd:cd14607  229 IKQVLLDMRKYRMGLIQTPDQLRFSYMAV 257
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 232-469 2.45e-71

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: 226.69  E-value: 2.45e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 232 NRYTDVLCYDHSRVVLAHEDGDEPSDYINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVMERGRV 311
Cdd:cd14619    1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 312 KCGQYWePTEESSLEFGDYHVRTISVECNEDYMVASLELRNIKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREK 391
Cdd:cd14619   81 KCEHYW-PLDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQW 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 320541922 392 QAQLVQGlgdtwaghprGPPiVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCH 469
Cdd:cd14619  160 LDQTMSG----------GPT-VVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLH 226
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 232-473 1.09e-70

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: 224.82  E-value: 1.09e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 232 NRYTDVLCYDHSRVVLAHEDGDEPSDYINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVMERGRV 311
Cdd:cd14618    1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 312 KCGQYWePTEESSLEFGDYHVRTISVECNEDYMVASLELRNIKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREk 391
Cdd:cd14618   81 LCDHYW-PSESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVRE- 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 392 QAQLVQGLGdtwaghprgpPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLA 471
Cdd:cd14618  159 HVQATKGKG----------PTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSC 228


                 ..
gi 320541922 472 LI 473
Cdd:cd14618  229 IL 230
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 207-472 2.76e-70

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 227.22  E-value: 2.76e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 207 EYADIRNRAPEGTFLHARMRANLTKNRYTDVLCYDHSRVVL-AHE----------DG--------DEPSDYINANFVDGY 267
Cdd:PHA02746  30 EHAEVMDIPIRGTTNHFLKKENLKKNRFHDIPCWDHSRVVInAHEslkmfdvgdsDGkkievtseDNAENYIHANFVDGF 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 268 KQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVmERGRVKCGQYWEPTEESSLEFGDYHVRTISVECNEDYMVAS 347
Cdd:PHA02746 110 KEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTDI-DDDDEKCFELWTKEEDSELAFGRFVAKILDIIEELSFTKTR 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 348 LELRNIKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQAQLVQglgdTWAGHPRGP-PIVVHCSAGIGRTGTF 426
Cdd:PHA02746 189 LMITDKISDTSREIHHFWFPDWPDNGIPTGMAEFLELINKVNEEQAELIK----QADNDPQTLgPIVVHCSAGIGRAGTF 264

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 320541922 427 ITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLAL 472
Cdd:PHA02746 265 CAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 228-476 3.65e-70

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 226.04  E-value: 3.65e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 228 NLTKNRYTDVLCYDHSRVVLAHEDGDepSDYINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVME 307
Cdd:PHA02742  52 NMKKCRYPDAPCFDRNRVILKIEDGG--DDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIME 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 308 RGRVKCGQYWEPTEESSLEFGDYHVRTISVECNEDYMVASLELRNIKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQK 387
Cdd:PHA02742 130 DGKEACYPYWMPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFVLA 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 388 VREkqAQLVQGLGDTWAGHPRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVF 467
Cdd:PHA02742 210 VRE--ADLKADVDIKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIF 287


                 ....*....
gi 320541922 468 CHLALIEYA 476
Cdd:PHA02742 288 CYFIVLIFA 296
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 223-469 1.05e-69

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: 222.84  E-value: 1.05e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 223 ARMRANLTKNRYTDVLCYDHSRVVLAHEDGDEPSDYINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMT 302
Cdd:cd14614    7 ADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVML 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 303 TRVMERGRVKCGQYWEPTEEsSLEFGDYHVRTISVECNEDYMVAslELRNIKTDEIRNVSHWQFTSWPDYGVPS--SAMA 380
Cdd:cd14614   87 TQCNEKRRVKCDHYWPFTEE-PVAYGDITVEMLSEEEQPDWAIR--EFRVSYADEVQDVMHFNYTAWPDHGVPTanAAES 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 381 MLNFLQKVREKQAQlvqglgdtwaghpRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQ 460
Cdd:cd14614  164 ILQFVQMVRQQAVK-------------SKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQ 230


                 ....*....
gi 320541922 461 MPDQYVFCH 469
Cdd:cd14614  231 TEEQYIFIH 239
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 257-467 2.88e-69

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: 220.28  E-value: 2.88e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 257 DYINANFVD----GYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVMERGRVKCGQYWePTEESSLEFGDYHV 332
Cdd:cd14541    1 DYINANYVNmeipGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYW-PDLGETMQFGNLQI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 333 RTISVECNEDYMVASLELRNIKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQAQLVqglgdtwaghprgPPI 412
Cdd:cd14541   80 TCVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMV-------------EPT 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 320541922 413 VVHCSAGIGRTGTFITLD--IC-ISRLEDVGTADIrgtVEKIRSQRAYSIQMPDQYVF 467
Cdd:cd14541  147 VVHCSAGIGRTGVLITMEtaMClIEANEPVYPLDI---VRTMRDQRAMLIQTPSQYRF 201
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 228-474 4.51e-69

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: 221.05  E-value: 4.51e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 228 NLTKNRYTDVLCYDHSRVVLAHEDGDEPSDYINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVME 307
Cdd:cd14630    3 NRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 308 RGRVKCGQYWEPTEESsleFGDYHVRTISVECNEDYMVASLELRNIKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQK 387
Cdd:cd14630   83 VGRVKCVRYWPDDTEV---YGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVRQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 388 VRekqaqlvqglgdtWAGHPRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVF 467
Cdd:cd14630  160 VK-------------FLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVF 226


                 ....*..
gi 320541922 468 CHLALIE 474
Cdd:cd14630  227 VHDAILE 233
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 189-475 3.85e-68

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: 220.37  E-value: 3.85e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 189 IDQIVQMvkQRGRH--GLIKEYADIRN-RAPEGTFLHARMRANLTKNRYTDVLCYDHSRVVLAHEDGDEPSDYINANFVD 265
Cdd:cd14627   13 IQKLAQV--EVGEHvtGMELEFKRLANsKAHTSRFISANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFID 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 266 GYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVMERGRVKCGQYWePTEESSLEfgDYHVRTISVECN-EDYM 344
Cdd:cd14627   91 GYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYW-PAERSARY--QYFVVDPMAEYNmPQYI 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 345 VASLELRNIKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQAQLVQglgdtwaghprGPPIVVHCSAGIGRTG 424
Cdd:cd14627  168 LREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQ-----------DGPISVHCSAGVGRTG 236

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 320541922 425 TFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIEY 475
Cdd:cd14627  237 VFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEY 287
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 234-474 4.82e-68

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: 217.89  E-value: 4.82e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 234 YTDVLCYDHSRVVLAHEDGDEPSDYINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVMERGRVKC 313
Cdd:cd14620    1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 314 GQYWepTEESSLEFGDYHVRTISVECNEDYMVASLELRNIKTDEI---RNVSHWQFTSWPDYGVPSSAMAMLNFLQKVRE 390
Cdd:cd14620   81 YQYW--PDQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDGCkapRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKS 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 391 kqaqlvqgLGDTWAGhprgpPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHL 470
Cdd:cd14620  159 --------VNPVHAG-----PIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQ 225


                 ....
gi 320541922 471 ALIE 474
Cdd:cd14620  226 ALLE 229
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 228-475 5.04e-68

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: 218.73  E-value: 5.04e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 228 NLTKNRYTDVLCYDHSRVVLAHEDGDEP-SDYINANFV--------DGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLV 298
Cdd:cd14605    2 NKNKNRYKNILPFDHTRVVLHDGDPNEPvSDYINANIImpefetkcNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 299 IVMTTRVMERGRVKCGQYWePTEESSLEFGDYHVRTISVECNEDYMVASLELRNI-KTDEIRNVSHWQFTSWPDYGVPSS 377
Cdd:cd14605   82 IVMTTKEVERGKSKCVKYW-PDEYALKEYGVMRVRNVKESAAHDYILRELKLSKVgQGNTERTVWQYHFRTWPDHGVPSD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 378 AMAMLNFLQKVREKQAQLVQglgdtwAGhprgpPIVVHCSAGIGRTGTFITLDICISRLEDVGT---ADIRGTVEKIRSQ 454
Cdd:cd14605  161 PGGVLDFLEEVHHKQESIMD------AG-----PVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQ 229

                        250       260
                 ....*....|....*....|.
gi 320541922 455 RAYSIQMPDQYVFCHLALIEY 475
Cdd:cd14605  230 RSGMVQTEAQYRFIYMAVQHY 250
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 206-474 6.55e-68

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: 218.93  E-value: 6.55e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 206 KEYADIRNRAP----EGTFLH--ARMRANLTKNRYTDVLCYDHSRVVLAHEDGDEPSDYINANFVDGYKQKNAYISTQGP 279
Cdd:cd14603    2 GEFSEIRACSAafkaDYVCSTvaGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 280 LPKTSQDFWRMIWEQHCLVIVMTTRVMERGRVKCGQYWePTEESSLEFGDYHVRTISVE-CNEDYMVASLELRniKTDEI 358
Cdd:cd14603   82 LSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYW-AQEQEPLQTGPFTITLVKEKrLNEEVILRTLKVT--FQKES 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 359 RNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQAqlvqglgdtwaghpRGP-PIVVHCSAGIGRTGTFITLDIcISRL- 436
Cdd:cd14603  159 RSVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQG--------------SGPePLCVHCSAGCGRTGVICTVDY-VRQLl 223

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 320541922 437 ------EDVGTADIrgtVEKIRSQRAYSIQMPDQYVFCHLALIE 474
Cdd:cd14603  224 ltqripPDFSIFDV---VLEMRKQRPAAVQTEEQYEFLYHTVAQ 264
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 232-470 5.97e-67

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: 215.17  E-value: 5.97e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 232 NRYTDVLCYDHSRVVLAHEDGDEPSDYINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVMERGRV 311
Cdd:cd14617    1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 312 KCGQYWePTEESSLEFGDYHVRTISVECNEDYMVASLELRN-IKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVRe 390
Cdd:cd14617   81 KCDHYW-PADQDSLYYGDLIVQMLSESVLPEWTIREFKICSeEQLDAPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVR- 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 391 kqaqlvqglgDTWAGHPRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHL 470
Cdd:cd14617  159 ----------DYINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 189-475 1.07e-66

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: 216.52  E-value: 1.07e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 189 IDQIVQMVKQRGRHGLIKEYADI-RNRAPEGTFLHARMRANLTKNRYTDVLCYDHSRVVLAHEDGDEPSDYINANFVDGY 267
Cdd:cd14628   12 IQKLTQIETGENVTGMELEFKRLaSSKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIDGY 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 268 KQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVMERGRVKCGQYWePTEESSLEfgDYHVRTISVECN-EDYMVA 346
Cdd:cd14628   92 RQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYW-PAERSARY--QYFVVDPMAEYNmPQYILR 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 347 SLELRNIKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQAQLVQglgdtwaghprGPPIVVHCSAGIGRTGTF 426
Cdd:cd14628  169 EFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQ-----------DGPISVHCSAGVGRTGVF 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 320541922 427 ITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIEY 475
Cdd:cd14628  238 ITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEY 286
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 223-467 4.55e-66

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: 214.33  E-value: 4.55e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 223 ARMRANLTKNRYTDVLCYDHSRVVLaheDGDEpsDYINANFVD----GYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLV 298
Cdd:cd14600   35 AKLPQNMDKNRYKDVLPYDATRVVL---QGNE--DYINASYVNmeipSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSL 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 299 IVMTTRVMERGRVKCGQYWePTEESSLEFGDYHVRTISVECNEDYMVASLELRNIKTDEIRNVSHWQFTSWPDYGVPSSA 378
Cdd:cd14600  110 IVMLTTLTERGRTKCHQYW-PDPPDVMEYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTVTHLQYVAWPDHGVPDDS 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 379 MAMLNFLQKVREKQAQLVqglgdtwaghprgpPIVVHCSAGIGRTGTFITLD--IC-ISRLEDVGTADIrgtVEKIRSQR 455
Cdd:cd14600  189 SDFLEFVNYVRSKRVENE--------------PVLVHCSAGIGRTGVLVTMEtaMClTERNQPVYPLDI---VRKMRDQR 251

                        250
                 ....*....|..
gi 320541922 456 AYSIQMPDQYVF 467
Cdd:cd14600  252 AMMVQTSSQYKF 263
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 213-475 8.76e-66

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: 214.20  E-value: 8.76e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 213 NRAPEGTFLHARMRANLTKNRYTDVLCYDHSRVVLAHEDGDEPSDYINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIW 292
Cdd:cd14629   38 SKAHTSRFISANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLW 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 293 EQHCLVIVMTTRVMERGRVKCGQYWePTEESSLEfgDYHVRTISVECN-EDYMVASLELRNIKTDEIRNVSHWQFTSWPD 371
Cdd:cd14629  118 EHNSTIVVMLTKLREMGREKCHQYW-PAERSARY--QYFVVDPMAEYNmPQYILREFKVTDARDGQSRTIRQFQFTDWPE 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 372 YGVPSSAMAMLNFLQKVREKQAQLVQglgdtwaghprGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKI 451
Cdd:cd14629  195 QGVPKTGEGFIDFIGQVHKTKEQFGQ-----------DGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTL 263

                        250       260
                 ....*....|....*....|....
gi 320541922 452 RSQRAYSIQMPDQYVFCHLALIEY 475
Cdd:cd14629  264 RTQRPAMVQTEDQYQLCYRAALEY 287
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 258-474 1.16e-65

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: 211.08  E-value: 1.16e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 258 YINANFV--DGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVMERGRVKCGQYW-EPTEESSLEFGDYHVRT 334
Cdd:cd14538    1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWpDSLNKPLICGGRLEVSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 335 ISVECNEDYMVASLELRNIKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREkqaqlvqgLGDTWaghprgpPIVV 414
Cdd:cd14538   81 EKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRR--------IHNSG-------PIVV 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 415 HCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIE 474
Cdd:cd14538  146 HCSAGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLE 205
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 216-474 9.69e-65

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: 211.45  E-value: 9.69e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 216 PEGTFLhARMRANLTKNRYTDVLCYDHSRVVLAHEDGDEPSDYINANFVDGYKQKN-AYISTQGPLPKTSQDFWRMIWEQ 294
Cdd:cd14610   33 PNATNV-AQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMDHDPRNpAYIATQGPLPATVADFWQMVWES 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 295 HCLVIVMTTRVMERGRVKCGQYWePTEESSLeFGDYHVRTIS--VECnEDYMVASLELRNIKTDEIRNVSHWQFTSWPDY 372
Cdd:cd14610  112 GCVVIVMLTPLAENGVKQCYHYW-PDEGSNL-YHIYEVNLVSehIWC-EDFLVRSFYLKNLQTNETRTVTQFHFLSWNDQ 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 373 GVPSSAMAMLNFLQKVREkqaqlvqglgdTWAGhpRGPPIVVHCSAGIGRTGTFITLDICISRL-EDVGTADIRGTVEKI 451
Cdd:cd14610  189 GVPASTRSLLDFRRKVNK-----------CYRG--RSCPIIVHCSDGAGRSGTYILIDMVLNKMaKGAKEIDIAATLEHL 255

                        250       260
                 ....*....|....*....|...
gi 320541922 452 RSQRAYSIQMPDQYVFCHLALIE 474
Cdd:cd14610  256 RDQRPGMVQTKEQFEFALTAVAE 278
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 228-475 1.65e-64

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: 210.12  E-value: 1.65e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 228 NLTKNRYTDVLCYDHSRVVLAHEDGDEP-SDYINANFV------DGYKQKNaYISTQGPLPKTSQDFWRMIWEQHCLVIV 300
Cdd:cd14606   18 NKSKNRYKNILPFDHSRVILQGRDSNIPgSDYINANYVknqllgPDENAKT-YIASQGCLEATVNDFWQMAWQENSRVIV 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 301 MTTRVMERGRVKCGQYWePTEESSLEFGDYHVRTISVECNEDYMVASLELRNI-KTDEIRNVSHWQFTSWPDYGVPSSAM 379
Cdd:cd14606   97 MTTREVEKGRNKCVPYW-PEVGMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLdNGELIREIWHYQYLSWPDHGVPSEPG 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 380 AMLNFLQKVREKQAQLvqglgdtwaghPRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGT---ADIRGTVEKIRSQRA 456
Cdd:cd14606  176 GVLSFLDQINQRQESL-----------PHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRS 244

                        250
                 ....*....|....*....
gi 320541922 457 YSIQMPDQYVFCHLALIEY 475
Cdd:cd14606  245 GMVQTEAQYKFIYVAIAQF 263
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 223-474 2.88e-64

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: 209.51  E-value: 2.88e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 223 ARMRANLTKNRYTDVLCYDHSRVVLAHEDGDEPSDYINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMT 302
Cdd:cd14633   35 AKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMV 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 303 TRVMERGRVKCGQYWEPTEESsleFGDYHVRTISVECNEDYMVASLELRNIKTDEIRNVSHWQFTSWPDYGVPSSAMAML 382
Cdd:cd14633  115 TNLVEVGRVKCCKYWPDDTEI---YKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLL 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 383 NFLQKVREKQAqlvqglgdtwaghPRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMP 462
Cdd:cd14633  192 GFVRQVKSKSP-------------PNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTE 258

                        250
                 ....*....|..
gi 320541922 463 DQYVFCHLALIE 474
Cdd:cd14633  259 EQYVFIHDAILE 270
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 258-473 9.07e-64

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: 205.98  E-value: 9.07e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 258 YINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVMERGRVKCGQYWePTEESSlEFGDYHVRTISV 337
Cdd:cd17668    1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYW-PADGSE-EYGNFLVTQKSV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 338 ECNEDYMVASLELRNIKTDE--------IRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQAQLVQglgdtwaghprg 409
Cdd:cd17668   79 QVLAYYTVRNFTLRNTKIKKgsqkgrpsGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVG------------ 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 320541922 410 pPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALI 473
Cdd:cd17668  147 -PVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 203-467 9.48e-64

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 209.47  E-value: 9.48e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 203 GLIK-EYADIRNRAPEGTFLHARMRANLTKNRYTDVLCYDHSRVVLAHEDGdEPSDYINANFVDGYKQKNAYISTQGPLP 281
Cdd:PHA02747  25 GIIRdEHHQIILKPFDGLIANFEKPENQPKNRYWDIPCWDHNRVILDSGGG-STSDYIHANWIDGFEDDKKFIATQGPFA 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 282 KTSQDFWRMIWEQHCLVIVMTTRVME-RGRVKCGQYWEPTEESSLEFGDYHVRTISVECNEDYMVASLELRNIKTDEIRN 360
Cdd:PHA02747 104 ETCADFWKAVWQEHCSIIVMLTPTKGtNGEEKCYQYWCLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRK 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 361 VSHWQFTSWPDYGVPSSA---MAMLNFLQKVREKQAQLVQGLGDTWAghprgpPIVVHCSAGIGRTGTFITLDICISRLE 437
Cdd:PHA02747 184 ISHFQCSEWFEDETPSDHpdfIKFIKIIDINRKKSGKLFNPKDALLC------PIVVHCSDGVGKTGIFCAVDICLNQLV 257

                        250       260       270
                 ....*....|....*....|....*....|
gi 320541922 438 DVGTADIRGTVEKIRSQRAYSIQMPDQYVF 467
Cdd:PHA02747 258 KRKAICLAKTAEKIREQRHAGIMNFDDYLF 287
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 199-474 1.05e-63

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: 208.35  E-value: 1.05e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 199 RGRHGLIKEY-ADIRNRAPEGTFLHARMRANLTKNRYTDVLCYDHSRVVLAHEDGDEPSDYINAN-FVDGYKQKNAYIST 276
Cdd:cd14609   12 RNRDRLAKEWqALCAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASpIIEHDPRMPAYIAT 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 277 QGPLPKTSQDFWRMIWEQHCLVIVMTTRVMERGRVKCGQYWePTEESSLeFGDYHVRTIS--VECnEDYMVASLELRNIK 354
Cdd:cd14609   92 QGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYW-PDEGSSL-YHIYEVNLVSehIWC-EDFLVRSFYLKNVQ 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 355 TDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREkqaqlvqglgdTWAGhpRGPPIVVHCSAGIGRTGTFITLDICIS 434
Cdd:cd14609  169 TQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNK-----------CYRG--RSCPIIVHCSDGAGRTGTYILIDMVLN 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 320541922 435 RL-EDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIE 474
Cdd:cd14609  236 RMaKGVKEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAE 276
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 258-476 2.39e-63

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: 205.38  E-value: 2.39e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 258 YINANFVD---GYKQKNaYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVMERGRVKCGQYWE--PTEESSLEFGDYHV 332
Cdd:cd14540    1 YINASHITatvGGKQRF-YIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPtlGGEHDALTFGEYKV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 333 RTISVECNEDYMVASLELRNIKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQAQLVQglgdTWAGHPRGPPI 412
Cdd:cd14540   80 STKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSVRRHTNQ----DVAGHNRNPPT 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 320541922 413 VVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIEYA 476
Cdd:cd14540  156 LVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 258-474 4.94e-63

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: 204.00  E-value: 4.94e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 258 YINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVMERGRVKCGQYWEPTEESsleFGDYHVRTISV 337
Cdd:cd14555    1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEV---YGDIKVTLVET 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 338 ECNEDYMVASLELRNIKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQAqlvqglgdtwaghPRGPPIVVHCS 417
Cdd:cd14555   78 EPLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNP-------------PSAGPIVVHCS 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 320541922 418 AGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIE 474
Cdd:cd14555  145 AGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 258-469 6.98e-63

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: 204.02  E-value: 6.98e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 258 YINANFVD-GYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVMERGRVKCGQYWePTEESSLEFGDYHVRTIS 336
Cdd:cd18533    1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYW-PSGEYEGEYGDLTVELVS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 337 VECNED--YMVASLELRNiKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQAQlvqglgdtwagHPRGPPIVV 414
Cdd:cd18533   80 EEENDDggFIVREFELSK-EDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDS-----------ASLDPPIIV 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 320541922 415 HCSAGIGRTGTFITLDICISRLEDVGTAD---------IRGTVEKIRSQRAYSIQMPDQYVFCH 469
Cdd:cd18533  148 HCSAGVGRTGTFIALDSLLDELKRGLSDSqdledsedpVYEIVNQLRKQRMSMVQTLRQYIFLY 211
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 186-475 3.09e-62

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: 205.26  E-value: 3.09e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 186 PKPIDQIVQMVKQR--GRHGLIKEYADIRNRAP-EGTFLHARMRANLTKNRYTDVLCYDHSRVVLAHEDGDEPSDYINAN 262
Cdd:cd14621    7 PLPVDKLEEEINRRmaDDNKLFREEFNALPACPiQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINAS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 263 FVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVMERGRVKCGQYWepTEESSLEFGDYHVRTISVECNED 342
Cdd:cd14621   87 FINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYW--PDQGCWTYGNIRVSVEDVTVLVD 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 343 YMVASLELRNI----KTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQAQlvqglgdtWAGhprgpPIVVHCSA 418
Cdd:cd14621  165 YTVRKFCIQQVgdvtNKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQ--------YAG-----AIVVHCSA 231

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 320541922 419 GIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIEY 475
Cdd:cd14621  232 GVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEH 288
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 258-472 2.44e-61

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: 199.42  E-value: 2.44e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 258 YINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVMERGRVKCGQYWepTEESSLEFGDYHVRTISV 337
Cdd:cd14552    1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYW--PEDGSVSSGDITVELKDQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 338 ECNEDYMVASLELRNIKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQAQLVQGlgdtwaghprgpPIVVHCS 417
Cdd:cd14552   79 TDYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSGNH------------PITVHCS 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 320541922 418 AGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLAL 472
Cdd:cd14552  147 AGAGRTGTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 258-469 2.92e-61

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: 199.28  E-value: 2.92e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 258 YINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVMERGRVKCGQYWEPTEESSLEFGDYHVRTISV 337
Cdd:cd14557    1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKINEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 338 ECNEDYMVASLELRNIKTD-EIRNVSHWQFTSWPDYGVPSSAmamlNFLQKVREKqaqlVQGLGDTWAGhprgpPIVVHC 416
Cdd:cd14557   81 KICPDYIIRKLNINNKKEKgSGREVTHIQFTSWPDHGVPEDP----HLLLKLRRR----VNAFNNFFSG-----PIVVHC 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 320541922 417 SAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCH 469
Cdd:cd14557  148 SAGVGRTGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 244-474 8.65e-61

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: 198.71  E-value: 8.65e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 244 RVVLAHEDGDEPSDYINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVMERGRVKCGQYWEPTEES 323
Cdd:cd14631    1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTEV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 324 sleFGDYHVRTISVECNEDYMVASLELRNIKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVRekqaqlvqglgdtW 403
Cdd:cd14631   81 ---YGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVK-------------L 144

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 320541922 404 AGHPRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIE 474
Cdd:cd14631  145 SNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 233-474 9.40e-61

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: 199.12  E-value: 9.40e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 233 RYTDVLCYDHSRVVLAHEDGDEPSDYINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVMERGRVK 312
Cdd:cd14623    1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 313 CGQYWePTeESSLEFGDYHVRTISVECNEDYMVASLELRNIKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQ 392
Cdd:cd14623   81 CAQYW-PS-DGSVSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQ 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 393 AQlvqglgdtwAGHprgPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLAL 472
Cdd:cd14623  159 QQ---------SGN---HPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVV 226


                 ..
gi 320541922 473 IE 474
Cdd:cd14623  227 QE 228
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 232-469 7.18e-60

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: 196.67  E-value: 7.18e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 232 NRYTDVLCYDHSRVVLAHEDGDEPSDYINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVMERGRV 311
Cdd:cd14616    1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 312 KCGQYWEPTEESSLEFGDYHVRTISVECNEDYMVASLELRniKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREK 391
Cdd:cd14616   81 RCHQYWPEDNKPVTVFGDIVITKLMEDVQIDWTIRDLKIE--RHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVRAS 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 320541922 392 QAQlvqglgdtwaghpRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCH 469
Cdd:cd14616  159 RAH-------------DNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 230-475 1.18e-59

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: 196.60  E-value: 1.18e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 230 TKNRYTDVLCYDHSRVVLAHEDG-DEPSDYINANFVDGYKQK-NAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVME 307
Cdd:cd14612   17 SKDRYKTILPNPQSRVCLRRAGSqEEEGSYINANYIRGYDGKeKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKE 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 308 RgRVKCGQYWePTEESSleFGDYHVRTISV-ECNEdYMVASLELRNikTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQ 386
Cdd:cd14612   97 K-KEKCVHYW-PEKEGT--YGRFEIRVQDMkECDG-YTIRDLTIQL--EEESRSVKHYWFSSWPDHQTPESAGPLLRLVA 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 387 KVREKQAQlvqglgdtwAGHPrgPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYV 466
Cdd:cd14612  170 EVEESRQT---------AASP--GPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQ 238


                 ....*....
gi 320541922 467 FCHLALIEY 475
Cdd:cd14612  239 FLHHTLALY 247
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 258-467 1.92e-59

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: 194.75  E-value: 1.92e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 258 YINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVMERGRVKCGQYWEPTEESSleFGDYHVRTISV 337
Cdd:cd14551    1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWT--YGNLRVRVEDT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 338 ECNEDYMVASLELRNIKTD----EIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREkqaqlvqglgdtwAGHPRGPPIV 413
Cdd:cd14551   79 VVLVDYTTRKFCIQKVNRGigekRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKS-------------ANPPRAGPIV 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 320541922 414 VHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVF 467
Cdd:cd14551  146 VHCSAGVGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVF 199
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 228-472 3.90e-59

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: 197.08  E-value: 3.90e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 228 NLTKNRYTDVLCYDHSRVVLAHEDGDEPSDYINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVME 307
Cdd:cd14604   57 NVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFE 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 308 RGRVKCGQYWEPTEESSLEFGDYHVRTISVECNEDYMVASL--ELRNiktdEIRNVSHWQFTSWPDYGVPSSAMAMLNFL 385
Cdd:cd14604  137 MGRKKCERYWPLYGEEPMTFGPFRISCEAEQARTDYFIRTLllEFQN----ETRRLYQFHYVNWPDHDVPSSFDSILDMI 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 386 QKVREKQAQlvqglgdtwaghpRGPPIVVHCSAGIGRTGTFITLDICISRL------EDVGTADIrgtVEKIRSQRAYSI 459
Cdd:cd14604  213 SLMRKYQEH-------------EDVPICIHCSAGCGRTGAICAIDYTWNLLkagkipEEFNVFNL---IQEMRTQRHSAV 276

                        250
                 ....*....|...
gi 320541922 460 QMPDQYVFCHLAL 472
Cdd:cd14604  277 QTKEQYELVHRAI 289
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 258-474 7.08e-59

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: 193.34  E-value: 7.08e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 258 YINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVMERGRVKCGQYWEPTEESsleFGDYHVRTISV 337
Cdd:cd14632    1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDT---YGDIKITLLKT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 338 ECNEDYMVASLELRNIKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQAqlvqglgdtwaghPRGPPIVVHCS 417
Cdd:cd14632   78 ETLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTP-------------PDAGPVVVHCS 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 320541922 418 AGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIE 474
Cdd:cd14632  145 AGAGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 258-474 3.93e-58

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: 191.50  E-value: 3.93e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 258 YINANFVDGYKQKN-AYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVMERGRVKCGQYWePTEESSLeFGDYHVRTIS 336
Cdd:cd14546    1 YINASTIYDHDPRNpAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYW-PEEGSEV-YHIYEVHLVS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 337 VEC-NEDYMVASLELRNIKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQaqlvqglgdtwagHPRGPPIVVH 415
Cdd:cd14546   79 EHIwCDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSY-------------RGRSCPIVVH 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 416 CSAGIGRTGTFITLDICISRL-EDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIE 474
Cdd:cd14546  146 CSDGAGRTGTYILIDMVLNRMaKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 231-475 5.22e-58

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: 192.77  E-value: 5.22e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 231 KNRYTDVLCYDHSRVVLAHEDGDEP-SDYINANFVDGY-KQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVMER 308
Cdd:cd14613   28 KNRYKTILPNPHSRVCLTSPDQDDPlSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 309 GRvKCGQYWEpteESSLEFGDYHVRTISVECNEDYmvaSLELRNIKTD-EIRNVSHWQFTSWPDYGVPSSAMAMLNFLQK 387
Cdd:cd14613  108 NE-KCTEYWP---EEQVTYEGIEITVKQVIHADDY---RLRLITLKSGgEERGLKHYWYTSWPDQKTPDNAPPLLQLVQE 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 388 VREKQAQlvqglgdtwaGHPRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVF 467
Cdd:cd14613  181 VEEARQQ----------AEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQF 250


                 ....*...
gi 320541922 468 CHLALIEY 475
Cdd:cd14613  251 VHHVLSLY 258
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 226-469 2.31e-57

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: 190.43  E-value: 2.31e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 226 RANLTKNRYTDVLCYDHSRVVLAHEDGdepsdYINANFVD---GyKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMT 302
Cdd:cd14597    1 KENRKKNRYKNILPYDTTRVPLGDEGG-----YINASFIKmpvG-DEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMM 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 303 TRVMERGRVKCGQYWEPTEESSLEFGD-YHVRTISVECNEDYMVASLELRNIKTDEIRNVSHWQFTSWPDYGVPSSAMAM 381
Cdd:cd14597   75 TQEVEGGKIKCQRYWPEILGKTTMVDNrLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 382 LNFLQKVREKqaqlvqglgdtwagHPRGpPIVVHCSAGIGRTGTFITLDIC---ISRLEDVgtaDIRGTVEKIRSQRAYS 458
Cdd:cd14597  155 LTFISYMRHI--------------HKSG-PIITHCSAGIGRSGTLICIDVVlglISKDLDF---DISDIVRTMRLQRHGM 216

                        250
                 ....*....|.
gi 320541922 459 IQMPDQYVFCH 469
Cdd:cd14597  217 VQTEDQYIFCY 227
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 257-475 3.48e-57

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: 188.68  E-value: 3.48e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 257 DYINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVMERGRVKCGQYWePTeESSLEFGDyhvrtIS 336
Cdd:cd14622    1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYW-PS-EGSVTHGE-----IT 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 337 VECNEDYMVASLELRNI-----KTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQAQLvqglgdtwAGHprgpP 411
Cdd:cd14622   74 IEIKNDTLLETISIRDFlvtynQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQT--------GNH----P 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 320541922 412 IVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIEY 475
Cdd:cd14622  142 IVVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 231-474 7.28e-57

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: 188.90  E-value: 7.28e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 231 KNRYTDVLCYDHSRVVLAHEDGDEPSDYINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVMERGR 310
Cdd:cd14602    1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 311 VKCGQYWEPTEESSLEFGDYHVRTISVECNEDYMVASLELRNIKtdEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVRE 390
Cdd:cd14602   81 KKCERYWAEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNS--ETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRC 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 391 KQaqlvqglgdtwagHPRGPPIVVHCSAGIGRTGTFITLDICISRLED---VGTADIRGTVEKIRSQRAYSIQMPDQYVF 467
Cdd:cd14602  159 YQ-------------EDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDgiiPENFSVFSLIQEMRTQRPSLVQTKEQYEL 225


                 ....*..
gi 320541922 468 CHLALIE 474
Cdd:cd14602  226 VYNAVIE 232
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 257-475 1.28e-56

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


Pssm-ID: 350449 [Multi-domain]  Cd Length: 212  Bit Score: 187.46  E-value: 1.28e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 257 DYINANFVD----GYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVMERGRVKCGQYWePTEESSLEFGDYHV 332
Cdd:cd14601    1 DYINANYINmeipSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYW-PEPSGSSSYGGFQV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 333 RTISVECNEDYMVASLELRNIKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQaqlvqglgdtwAGHPRgpPI 412
Cdd:cd14601   80 TCHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKR-----------AGKDE--PV 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 320541922 413 VVHCSAGIGRTGTFITLDICISRLE---DVGTADIrgtVEKIRSQRAYSIQMPDQYVF-CHLALIEY 475
Cdd:cd14601  147 VVHCSAGIGRTGVLITMETAMCLIEcnqPVYPLDI---VRTMRDQRAMMIQTPSQYRFvCEAILKVY 210
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 258-474 4.50e-55

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: 183.41  E-value: 4.50e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 258 YINANFVDGY--KQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVMERGRVKCGQYWEPTEESSLEFGDYHVRTI 335
Cdd:cd14596    1 YINASYITMPvgEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLRLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 336 SVECNEDYMVASLELRNIKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVRekqaqlvqglgdtwAGHPRGpPIVVH 415
Cdd:cd14596   81 NYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMR--------------KVHNTG-PIVVH 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 320541922 416 CSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIE 474
Cdd:cd14596  146 CSAGIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLE 204
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 258-469 9.60e-54

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: 179.54  E-value: 9.60e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 258 YINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVMERGRVKCGQYWEPTEESSLEFGDYHVRTISV 337
Cdd:cd14542    1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLQFGPFKISLEKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 338 E-CNEDYMVASLELRniKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQAQlvqglgdtwaghpRGPPIVVHC 416
Cdd:cd14542   81 KrVGPDFLIRTLKVT--FQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGS-------------EDVPICVHC 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 320541922 417 SAGIGRTGTFITLDICISRL------EDVGTADIrgtVEKIRSQRAYSIQMPDQYVFCH 469
Cdd:cd14542  146 SAGCGRTGTICAIDYVWNLLktgkipEEFSLFDL---VREMRKQRPAMVQTKEQYELVY 201
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 207-475 5.27e-53

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: 180.58  E-value: 5.27e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 207 EYADIRNRAPEGTFLHARMRANLTKNRYTDVLCYDHSRVVLAhEDGDEPSDYINANF----VDGykQKNAYISTQGPLPK 282
Cdd:cd14599   17 EYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELV-PTKENNTGYINASHikvtVGG--EEWHYIATQGPLPH 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 283 TSQDFWRMIWEQHCLVIVMTTRVMERGRVKCGQYWEP--TEESSLEFGDYHVRTISVECNEDYMVASLELRNIKTDEIRN 360
Cdd:cd14599   94 TCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKlgSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERT 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 361 VSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQAQLVQGLGDTWAGHprgPPIVVHCSAGIGRTGTFITLDICISRLEDVG 440
Cdd:cd14599  174 VWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTNSMLDSTKNCN---PPIVVHCSAGVGRTGVVILTELMIGCLEHNE 250

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 320541922 441 TADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIEY 475
Cdd:cd14599  251 KVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQF 285
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 230-469 2.01e-52

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: 177.03  E-value: 2.01e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 230 TKNRYTDVLCYDHSRVVLAHEDGDEP-SDYINANFVDGYK-QKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVME 307
Cdd:cd14611    1 TKNRYKTILPNPHSRVCLKPKNSNDSlSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 308 RGRvKCGQYWEpteESSLEFGDYHVRTISVECNEDYMVASLELRNikTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQK 387
Cdd:cd14611   81 KNE-KCVLYWP---EKRGIYGKVEVLVNSVKECDNYTIRNLTLKQ--GSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLD 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 388 VREKQAQlvqglgdtWAGhpRGPpIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVF 467
Cdd:cd14611  155 VEEDRLA--------SPG--RGP-VVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEF 223


                 ..
gi 320541922 468 CH 469
Cdd:cd14611  224 VH 225
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 258-469 1.02e-51

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: 174.57  E-value: 1.02e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 258 YINANFVDGYKQKN--AYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVMERGR-VKCGQYWEPTEESSLEFGDYHVRT 334
Cdd:cd17658    1 YINASLVETPASESlpKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYStAKCADYFPAEENESREFGRISVTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 335 ISVECNEDymvaSLELRNIKTDEI------RNVSHWQFTSWPDYGVPSSAMAmlnflqkVREkqaqLVQGLgdtWAGHPR 408
Cdd:cd17658   81 KKLKHSQH----SITLRVLEVQYIeseeppLSVLHIQYPEWPDHGVPKDTRS-------VRE----LLKRL---YGIPPS 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 320541922 409 GPPIVVHCSAGIGRTGTFITLDICISR--LEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCH 469
Cdd:cd17658  143 AGPIVVHCSAGIGRTGAYCTIHNTIRRilEGDMSAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 258-469 4.66e-50

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: 169.88  E-value: 4.66e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 258 YINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVMERGRVKCGQYWEPTEESsleFGDYHVRTISV 337
Cdd:cd14558    1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKT---YGDIEVELKDT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 338 ECNEDYMVASLELRNIKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQaqlvqglGDTWAGHPRGPPIVVHCS 417
Cdd:cd14558   78 EKSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKL-------PYKNSKHGRSVPIVVHCS 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 320541922 418 AGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCH 469
Cdd:cd14558  151 DGSSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 258-469 3.01e-46

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: 159.86  E-value: 3.01e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 258 YINANFVDGYKQKNA-YISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVMERGRVKCGQYWePTEE-SSLEFGDYHVRTI 335
Cdd:cd14539    1 YINASLIEDLTPYCPrFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYW-PTERgQALVYGAITVSLQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 336 SVECNEDYMVASLELRNIKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREK-QAQlvqglgdtwagHPRGPPIVV 414
Cdd:cd14539   80 SVRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHyLQQ-----------RSLQTPIVV 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 320541922 415 HCSAGIGRTGTFITLDICISRLE-DVGTADIRGTVEKIRSQRAYSIQMPDQYVFCH 469
Cdd:cd14539  149 HCSSGVGRTGAFCLLYAAVQEIEaGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCY 204
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 258-469 1.08e-43

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: 152.95  E-value: 1.08e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 258 YINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRvMERGRVKCGQYWepTEESSLEFGDYHVRTISV 337
Cdd:cd14556    1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQ-LDPKDQSCPQYW--PDEGSGTYGPIQVEFVST 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 338 ECNEDYMVASLELRNIKTDE--IRNVSHWQFTSWPDYG-VPSSAMAMLNFLQKVREKQAQLVQGlgdtwaghprgpPIVV 414
Cdd:cd14556   78 TIDEDVISRIFRLQNTTRPQegYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKWQEQSGEG------------PIVV 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 320541922 415 HCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCH 469
Cdd:cd14556  146 HCLNGVGRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 258-475 2.73e-40

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: 144.73  E-value: 2.73e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 258 YINANFVD---GYKQKNaYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVMERGRVKCGQYWE--PTEESSLEFGDYHV 332
Cdd:cd14598    1 YINASHIKvtvGGKEWD-YIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrlGSRHNTVTYGRFKI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 333 ----RTISVeCnedYMVASLELRNIKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVrekqaQLVQGLGDTwAGHPR 408
Cdd:cd14598   80 ttrfRTDSG-C---YATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEI-----QSVRRHTNS-TIDPK 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 320541922 409 GP--PIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIEY 475
Cdd:cd14598  150 SPnpPVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQF 218
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
361-474 3.41e-36

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 129.79  E-value: 3.41e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922   361 VSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQAQlvqglgdtwagHPRGPPIVVHCSAGIGRTGTFITLDICISRLED-V 439
Cdd:smart00404   2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQ-----------SESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAeA 70

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 320541922   440 GTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIE 474
Cdd:smart00404  71 GEVDIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 361-474 3.41e-36

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: 129.79  E-value: 3.41e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922   361 VSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQAQlvqglgdtwagHPRGPPIVVHCSAGIGRTGTFITLDICISRLED-V 439
Cdd:smart00012   2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQ-----------SESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAeA 70

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 320541922   440 GTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIE 474
Cdd:smart00012  71 GEVDIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 258-474 3.97e-33

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: 124.75  E-value: 3.97e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 258 YINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRvMERGRVkCGQYWepTEESSLEFGDYHVRTISV 337
Cdd:cd14634    1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNE-MDAAQL-CMQYW--PEKTSCCYGPIQVEFVSA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 338 ECNEDYMVASLELRNIK--TDEIRNVSHWQFTSWPDY-GVPSSAMAMLNFLQKVREKQAQLVQGLGDTwaghprgppiVV 414
Cdd:cd14634   77 DIDEDIISRIFRICNMArpQDGYRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQYDGREGRT----------VV 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 415 HCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIE 474
Cdd:cd14634  147 HCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
228-480 4.90e-33

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 126.74  E-value: 4.90e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 228 NLTKNRYTDVLCYDHSRVvlahedgDEPSDYINANFVDGyKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVME 307
Cdd:COG5599   42 GSPLNRFRDIQPYKETAL-------RANLGYLNANYIQV-IGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDE 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 308 --RGRVKCGQYWEPTeesslefGDYHVRTISVE------CNEDYMVASLELRNIKTD-EIRNVSHWQFTSWPDYGVPSSA 378
Cdd:COG5599  114 isKPKVKMPVYFRQD-------GEYGKYEVSSEltesiqLRDGIEARTYVLTIKGTGqKKIEIPVLHVKNWPDHGAISAE 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 379 mAMLNFLQKVREKQaqlvqglgdTWAGHPRGPPiVVHCSAGIGRTGTFItLDICISRLEDVGTaDIRGTVEKI----RSQ 454
Cdd:COG5599  187 -ALKNLADLIDKKE---------KIKDPDKLLP-VVHCRAGVGRTGTLI-ACLALSKSINALV-QITLSVEEIvidmRTS 253

                        250       260
                 ....*....|....*....|....*..
gi 320541922 455 RAYSI-QMPDQYVFchlaLIEYAYSRG 480
Cdd:COG5599  254 RNGGMvQTSEQLDV----LVKLAEQQI 276
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 258-474 5.19e-31

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: 119.02  E-value: 5.19e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 258 YINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVmERGRVkCGQYWepTEESSLEFGDYHVRTISV 337
Cdd:cd14635    1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDV-DPAQL-CPQYW--PENGVHRHGPIQVEFVSA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 338 ECNEDYMVASLELRNIK--TDEIRNVSHWQFTSWPDY-GVPSSAMAMLNFLQKVREKQAQLVQGLGDTwaghprgppiVV 414
Cdd:cd14635   77 DLEEDIISRIFRIYNAArpQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEYNGGEGRT----------VV 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 415 HCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIE 474
Cdd:cd14635  147 HCLNGGGRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 258-467 1.13e-30

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: 117.81  E-value: 1.13e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 258 YINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVMERGrvKCGQYWePTEESSLEFGDYHVR---- 333
Cdd:cd14550    1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYW-PTKEKPLECETFKVTlsge 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 334 -TISVECNEDYMVASLELRNIKTDEIRNVSHWQFTSWPDYGVPSSamAMLNFLQKVREKQAQlvqglgdtwaghpRGPPI 412
Cdd:cd14550   78 dHSCLSNEIRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIH--TVFELINTVQEWAQQ-------------RDGPI 142

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 320541922 413 VVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVF 467
Cdd:cd14550  143 VVHDRYGGVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQF 197
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 258-469 1.31e-28

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: 112.43  E-value: 1.31e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 258 YINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRV-MERGrvkCGQYWepTEESSLEFGDYHVRTIS 336
Cdd:cd14636    1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVdLAQG---CPQYW--PEEGMLRYGPIQVECMS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 337 VECNEDYMVASLELRNIKTDE--IRNVSHWQFTSWPDY-GVPSSAMAMLNFLQKVREKQAQLVQGLGDTwaghprgppiV 413
Cdd:cd14636   76 CSMDCDVISRIFRICNLTRPQegYLMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEECDEGEGRT----------I 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 320541922 414 VHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCH 469
Cdd:cd14636  146 IHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCY 201
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 204-475 8.19e-28

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 112.75  E-value: 8.19e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 204 LIKEYADIRNRAPEGtflhARMRANLTKNRYTD------VLCYDHSRVVLAHEDgdepsDYINANFVDGYKQKNAYISTQ 277
Cdd:PHA02740  27 IIKEYRAIVPEHEDE----ANKACAQAENKAKDenlalhITRLLHRRIKLFNDE-----KVLDARFVDGYDFEQKFICII 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 278 GPLPKTSQDFWRMIWEQHCLVIVMTTRVMERgrvKC-GQYWEPTEESSLEFGDYHVRTISVECNEDYMVASLELRNIKTD 356
Cdd:PHA02740  98 NLCEDACDKFLQALSDNKVQIIVLISRHADK---KCfNQFWSLKEGCVITSDKFQIETLEIIIKPHFNLTLLSLTDKFGQ 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 357 EiRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQAQLVQGLGDTWAGhprgpPIVVHCSAGIGRTGTFITLDICISRL 436
Cdd:PHA02740 175 A-QKISHFQYTAWPADGFSHDPDAFIDFFCNIDDLCADLEKHKADGKIA-----PIIIDCIDGISSSAVFCVFDICATEF 248

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 320541922 437 EDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIEY 475
Cdd:PHA02740 249 DKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLIAAY 287
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 258-474 1.98e-25

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: 103.45  E-value: 1.98e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 258 YINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVMERGRV-KCGQYWepTEESSLEFGDYHVRTIS 336
Cdd:cd14637    1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYW--PEPGLQQYGPMEVEFVS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 337 VECNEDYMVASLELRNIK--TDEIRNVSHWQFTSWPDY-GVPSSAMAMLNFLQKVREKQAQlvQGLGDTwaghprgppiV 413
Cdd:cd14637   79 GSADEDIVTRLFRVQNITrlQEGHLMVRHFQFLRWSAYrDTPDSKKAFLHLLASVEKWQRE--SGEGRT----------V 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 320541922 414 VHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIE 474
Cdd:cd14637  147 VHCLNGGGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 258-473 1.81e-22

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: 95.06  E-value: 1.81e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 258 YINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVMERGRVKCgQYWePTEESSLEFGDYHVRTISV 337
Cdd:cd17669    1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYW-PNKDEPINCETFKVTLIAE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 338 EC-----NEDYMVASLELRNIKTDEIRNVSHWQFTSWPDYGVPSSamAMLNFLQKVREKQAQlvqglgdtwaghpRGPPI 412
Cdd:cd17669   79 EHkclsnEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPIS--KTFELISIIKEEAAN-------------RDGPM 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 320541922 413 VVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALI 473
Cdd:cd17669  144 IVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 258-473 1.00e-21

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


Pssm-ID: 350508 [Multi-domain]  Cd Length: 205  Bit Score: 93.20  E-value: 1.00e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 258 YINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVM---TTRVMERGRVkcgqYWePTEESSLEFGDYHVRT 334
Cdd:cd17670    1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMlpdNQGLAEDEFV----YW-PSREESMNCEAFTVTL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 335 ISVE--C---NEDYMVASLELRNIKTDEIRNVSHWQFTSWPDYGVP-SSAMAMLNFLqkvreKQAQLVqglgdtwaghpR 408
Cdd:cd17670   76 ISKDrlClsnEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPiSSTFELINVI-----KEEALT-----------R 139

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 320541922 409 GPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALI 473
Cdd:cd17670  140 DGPTIVHDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 408-469 3.00e-09

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: 54.66  E-value: 3.00e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 320541922 408 RGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTAdirgtVEKIRSQR-AYSIQMPDQYVFCH 469
Cdd:cd14494   55 PGEPVLVHCKAGVGRTGTLVACYLVLLGGMSAEEA-----VRIVRLIRpGGIPQTIEQLDFLI 112
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
369-467 6.09e-08

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 51.51  E-value: 6.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 369 WPDYGVPSsamamlnflqkvrekQAQLVQGLGDTWAGHPRGPPIVVHCSAGIGRTGTFItldICISRLEDVGTADIrgtV 448
Cdd:COG2453   55 IPDFGAPD---------------DEQLQEAVDFIDEALREGKKVLVHCRGGIGRTGTVA---AAYLVLLGLSAEEA---L 113

                         90
                 ....*....|....*....
gi 320541922 449 EKIRSQRAYSIQMPDQYVF 467
Cdd:COG2453  114 ARVRAARPGAVETPAQRAF 132
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 259-427 5.37e-07

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: 50.48  E-value: 5.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 259 INANFVDgYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVMERGRVKCGQYWEPTEEssleFGDYHV---RTI 335
Cdd:cd14559   18 LNANRVQ-IGNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYFRQSGT----YGSVTVkskKTG 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 336 SVECNEDYMVASLELrNIKTDEIR-NVSHWQFTSWPDYG-VPSSAMAML-NFLQKVREKQAQLVQGLGDTWAGHPRGPPI 412
Cdd:cd14559   93 KDELVDGLKADMYNL-KITDGNKTiTIPVVHVTNWPDHTaISSEGLKELaDLVNKSAEEKRNFYKSKGSSAINDKNKLLP 171

                        170
                 ....*....|....*
gi 320541922 413 VVHCSAGIGRTGTFI 427
Cdd:cd14559  172 VIHCRAGVGRTGQLA 186
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 312-469 3.44e-05

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: 44.18  E-value: 3.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 312 KCGQYWEPTEESSLEFGDYHVRTISVECNEDymvaslELRNIKTDEIRN-VSHWQFTSW----PDYGVPSSamamLNFLQ 386
Cdd:cd14505   24 KFKDHRRDLQADLEELKDQGVDDVVTLCTDG------ELEELGVPDLLEqYQQAGITWHhlpiPDGGVPSD----IAQWQ 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 387 KVREkqaQLVQGLGDtwaghprGPPIVVHCSAGIGRTGTfitldICISRLEDVG-TADIRGTVEKIRSQRAYSIQMPDQY 465
Cdd:cd14505   94 ELLE---ELLSALEN-------GKKVLIHCKGGLGRTGL-----IAACLLLELGdTLDPEQAIAAVRALRPGAIQTPKQE 158


                 ....
gi 320541922 466 VFCH 469
Cdd:cd14505  159 NFLH 162
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 359-469 1.13e-04

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: 43.49  E-value: 1.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 359 RNVSHWQFtSWPDYGVPSsamamLNFLQKVREKQAQLVQGLGDtwaghprgppIVVHCSAGIGRTGTFITldiCI-SRLE 437
Cdd:cd14506   75 AGIYFYNF-GWKDYGVPS-----LTTILDIVKVMAFALQEGGK----------VAVHCHAGLGRTGVLIA---CYlVYAL 135

                         90       100       110
                 ....*....|....*....|....*....|..
gi 320541922 438 DVGTADirgTVEKIRSQRAYSIQMPDQYVFCH 469
Cdd:cd14506  136 RMSADQ---AIRLVRSKRPNSIQTRGQVLCVR 164
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 370-464 3.14e-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: 41.11  E-value: 3.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320541922 370 PDYGVPSSAMaMLNFLQKVREKQAqlvqglgdtwaghpRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTAdirgtVE 449
Cdd:cd14504   58 EDYTPPTLEQ-IDEFLDIVEEANA--------------KNEAVLVHCLAGKGRTGTMLACYLVKTGKISAVDA-----IN 117

                         90
                 ....*....|....*
gi 320541922 450 KIRSQRAYSIQMPDQ 464
Cdd:cd14504  118 EIRRIRPGSIETSEQ 132
 
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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