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Conserved domains on  [gi|767962407|ref|XP_011537907|]
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tyrosine-protein phosphatase non-receptor type 20 isoform X1 [Homo sapiens]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 208-414 8.29e-142

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


The actual alignment was detected with superfamily member cd14596:

Pssm-ID: 475123 [Multi-domain]  Cd Length: 207  Bit Score: 402.59  E-value: 8.29e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 208 YINASYIRIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLE 287
Cdd:cd14596    1 YINASYITMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLRLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 288 NYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSHLTGPMVVHCSAGIGRTGVFLCVD 367
Cdd:cd14596   81 NYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNTGPIVVHCSAGIGRAGVLICVD 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 767962407 368 VVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEVLR 414
Cdd:cd14596  161 VLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207
 
Name Accession Description Interval E-value
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 208-414 8.29e-142

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: 402.59  E-value: 8.29e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 208 YINASYIRIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLE 287
Cdd:cd14596    1 YINASYITMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLRLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 288 NYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSHLTGPMVVHCSAGIGRTGVFLCVD 367
Cdd:cd14596   81 NYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNTGPIVVHCSAGIGRAGVLICVD 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 767962407 368 VVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEVLR 414
Cdd:cd14596  161 VLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
159-411 4.93e-112

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 329.23  E-value: 4.93e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407   159 IMQEFMAL-ELKNLPGEFNSGNQPSNREKNRYRDILPYDSTRVPL----GKSKDYINASYIRIVNCGEEYfyIATQGPLL 233
Cdd:smart00194   2 LEEEFEKLdRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLkpppGEGSDYINASYIDGPNGPKAY--IATQGPLP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407   234 STIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSV 313
Cdd:smart00194  80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTV 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407   314 KQLQFTKWPDHGTPASADSFIKYIRYARK--SHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQ 391
Cdd:smart00194 160 THYHYTNWPDHGVPESPESILDLIRAVRKsqSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQ 239

                          250       260
                   ....*....|....*....|
gi 767962407   392 RSGMVQTKEQYHFCYDIVLE 411
Cdd:smart00194 240 RPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
183-411 2.32e-108

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 318.80  E-value: 2.32e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407  183 NREKNRYRDILPYDSTRVPLGKSK---DYINASYIRIVNcgEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIE 259
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGDPgpsDYINASYIDGYK--KPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407  260 GGIIKCYHYWPISLKKPLELKHFRVFLENY-QILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIR 338
Cdd:pfam00102  79 KGREKCAQYWPEEEGESLEYGDFTVTLKKEkEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767962407  339 YARKSHL---TGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 411
Cdd:pfam00102 159 KVRKSSLdgrSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
179-418 1.75e-48

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 166.42  E-value: 1.75e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 179 NQPSNREKNRYRDILPYDSTRVplGKSKDYINASYIRIvncGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREI 258
Cdd:COG5599   38 QNINGSPLNRFRDIQPYKETAL--RANLGYLNANYIQV---IGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDD 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 259 EGG--IIKCYHYWPIS---LKKPLELKHfrvfLENYQILQYFIIRMFQVVEKSTG-TSHSVKQLQFTKWPDHGTPaSADS 332
Cdd:COG5599  113 EISkpKVKMPVYFRQDgeyGKYEVSSEL----TESIQLRDGIEARTYVLTIKGTGqKKIEIPVLHVKNWPDHGAI-SAEA 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 333 FIKYIRYARKSHLT-----GPMVVHCSAGIGRTGVFLCVDVVFCAI--VKNCSFNIMDIVAQMREQR-SGMVQTKEQYHF 404
Cdd:COG5599  188 LKNLADLIDKKEKIkdpdkLLPVVHCRAGVGRTGTLIACLALSKSInaLVQITLSVEEIVIDMRTSRnGGMVQTSEQLDV 267

                        250
                 ....*....|....
gi 767962407 405 CYDIVLEVLRKLLT 418
Cdd:COG5599  268 LVKLAEQQIRPLLR 281
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 159-420 1.86e-46

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 162.09  E-value: 1.86e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 159 IMQEFMALELKNLPGEFNSGNQPSNREKNRYRDILPYDSTRVPL----GKSKDYINASYIRIVNcgEEYFYIATQGPLLS 234
Cdd:PHA02747  27 IRDEHHQIILKPFDGLIANFEKPENQPKNRYWDIPCWDHNRVILdsggGSTSDYIHANWIDGFE--DDKKFIATQGPFAE 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 235 TIDDFWQMVLENNSNVIAMIT-REIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSV 313
Cdd:PHA02747 105 TCADFWKAVWQEHCSIIVMLTpTKGTNGEEKCYQYWCLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKI 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 314 KQLQFTKWPDHGTPASADSFIKYIR------------YARKSHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNI 381
Cdd:PHA02747 185 SHFQCSEWFEDETPSDHPDFIKFIKiidinrkksgklFNPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICL 264

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 767962407 382 MDIVAQMREQRSGMVQTKEQYHF---CYDIVLEVLRKLLTLD 420
Cdd:PHA02747 265 AKTAEKIREQRHAGIMNFDDYLFiqpGYEVLHYFLSKIKAID 306
 
Name Accession Description Interval E-value
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 208-414 8.29e-142

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: 402.59  E-value: 8.29e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 208 YINASYIRIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLE 287
Cdd:cd14596    1 YINASYITMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLRLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 288 NYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSHLTGPMVVHCSAGIGRTGVFLCVD 367
Cdd:cd14596   81 NYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNTGPIVVHCSAGIGRAGVLICVD 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 767962407 368 VVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEVLR 414
Cdd:cd14596  161 VLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 208-413 1.93e-137

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: 391.74  E-value: 1.93e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 208 YINASYIRIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPL-ELKHFRVFL 286
Cdd:cd14538    1 YINASHIRIPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKPLiCGGRLEVSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 287 ENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSHLTGPMVVHCSAGIGRTGVFLCV 366
Cdd:cd14538   81 EKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIHNSGPIVVHCSAGIGRTGVLITI 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 767962407 367 DVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEVL 413
Cdd:cd14538  161 DVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
159-411 4.93e-112

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 329.23  E-value: 4.93e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407   159 IMQEFMAL-ELKNLPGEFNSGNQPSNREKNRYRDILPYDSTRVPL----GKSKDYINASYIRIVNCGEEYfyIATQGPLL 233
Cdd:smart00194   2 LEEEFEKLdRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLkpppGEGSDYINASYIDGPNGPKAY--IATQGPLP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407   234 STIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSV 313
Cdd:smart00194  80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTV 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407   314 KQLQFTKWPDHGTPASADSFIKYIRYARK--SHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQ 391
Cdd:smart00194 160 THYHYTNWPDHGVPESPESILDLIRAVRKsqSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQ 239

                          250       260
                   ....*....|....*....|
gi 767962407   392 RSGMVQTKEQYHFCYDIVLE 411
Cdd:smart00194 240 RPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
183-411 2.32e-108

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 318.80  E-value: 2.32e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407  183 NREKNRYRDILPYDSTRVPLGKSK---DYINASYIRIVNcgEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIE 259
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGDPgpsDYINASYIDGYK--KPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407  260 GGIIKCYHYWPISLKKPLELKHFRVFLENY-QILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIR 338
Cdd:pfam00102  79 KGREKCAQYWPEEEGESLEYGDFTVTLKKEkEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767962407  339 YARKSHL---TGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 411
Cdd:pfam00102 159 KVRKSSLdgrSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 183-413 6.68e-100

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: 297.51  E-value: 6.68e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 183 NREKNRYRDILPYDSTRVPLGKSKDYINASYIRIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGI 262
Cdd:cd14597    3 NRKKNRYKNILPYDTTRVPLGDEGGYINASFIKMPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQEVEGGK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 263 IKCYHYWPISLKKPLEL-KHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYAR 341
Cdd:cd14597   83 IKCQRYWPEILGKTTMVdNRLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLLTFISYMR 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767962407 342 KSHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEVL 413
Cdd:cd14597  163 HIHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVILYVL 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 208-407 1.47e-86

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: 261.84  E-value: 1.47e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 208 YINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLE 287
Cdd:cd00047    1 YINASYIDGYRGPKEY--IATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYGDITVTLV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 288 NYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKS--HLTGPMVVHCSAGIGRTGVFLC 365
Cdd:cd00047   79 SEEELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEarKPNGPIVVHCSAGVGRTGTFIA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 767962407 366 VDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYD 407
Cdd:cd00047  159 IDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 159-406 1.05e-73

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: 231.48  E-value: 1.05e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 159 IMQEFMALELKNLPGEFNSGNQPSNREKNRYRDILPYDSTRVPLGK-----SKDYINASYIrivncgEEY----FYIATQ 229
Cdd:cd14543    5 IYEEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKrngdeRTDYINANFM------DGYkqknAYIATQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 230 GPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGT 309
Cdd:cd14543   79 GPLPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 310 SHSVKQLQFTKWPDHGTPASADSFIKYIRYAR--------------KSHLTG-PMVVHCSAGIGRTGVFLCVDVVFCAIV 374
Cdd:cd14543  159 SRQVTHFQFTSWPDFGVPSSAAALLDFLGEVRqqqalavkamgdrwKGHPPGpPIVVHCSAGIGRTGTFCTLDICLSQLE 238

                        250       260       270
                 ....*....|....*....|....*....|..
gi 767962407 375 KNCSFNIMDIVAQMREQRSGMVQTKEQYHFCY 406
Cdd:cd14543  239 DVGTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 188-404 1.51e-71

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: 224.16  E-value: 1.51e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 188 RYRDILPYDSTRVPLGKS-----KDYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGI 262
Cdd:cd14548    1 RYTNILPYDHSRVKLIPIneeegSDYINANYIPGYNSPREF--IATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 263 IKCYHYWPISlKKPLELKHFRVFLENYQILQYFIIRMFQVveKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARK 342
Cdd:cd14548   79 VKCDHYWPFD-QDPVYYGDITVTMLSESVLPDWTIREFKL--ERGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRD 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767962407 343 S--HLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHF 404
Cdd:cd14548  156 YikQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIF 219
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 208-407 3.08e-70

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: 220.58  E-value: 3.08e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 208 YINASYIrIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPiSLKKPLELKHFRV-FL 286
Cdd:cd18533    1 YINASYI-TLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWP-SGEYEGEYGDLTVeLV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 287 ENYQI-LQYFIIRMFQVVeKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARK----SHLTGPMVVHCSAGIGRTG 361
Cdd:cd18533   79 SEEENdDGGFIVREFELS-KEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRElndsASLDPPIIVHCSAGVGRTG 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767962407 362 VFLCVDVVF---------CAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYD 407
Cdd:cd18533  158 TFIALDSLLdelkrglsdSQDLEDSEDPVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 179-406 1.67e-68

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: 217.01  E-value: 1.67e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 179 NQPSNREKNRYRDILPYDSTRVPLG-----KSKDYINASYIRivncGEEY--FYIATQGPLLSTIDDFWQMVLENNSNVI 251
Cdd:cd14554    2 NLPCNKFKNRLVNILPYESTRVCLQpirgvEGSDYINASFID----GYRQrgAYIATQGPLAETTEDFWRMLWEHNSTII 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 252 AMITREIEGGIIKCYHYWPisLKKPLELKHFRVF-LENYQILQYfIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASA 330
Cdd:cd14554   78 VMLTKLREMGREKCHQYWP--AERSARYQYFVVDpMAEYNMPQY-ILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSG 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 331 DSFIKYIRYARKSH----LTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCY 406
Cdd:cd14554  155 EGFIDFIGQVHKTKeqfgQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCY 234
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 180-415 6.91e-67

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: 6.91e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 180 QPSNREKNRYRDILPYDSTRVPLGKSKDYINASYIRI----VNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMIT 255
Cdd:cd14600   37 LPQNMDKNRYKDVLPYDATRVVLQGNEDYINASYVNMeipsANIVNKY--IATQGPLPHTCAQFWQVVWEQKLSLIVMLT 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 256 REIEGGIIKCYHYWPiSLKKPLELKHFRVFL--ENYQILqyFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSF 333
Cdd:cd14600  115 TLTERGRTKCHQYWP-DPPDVMEYGGFRVQChsEDCTIA--YVFREMLLTNTQTGEERTVTHLQYVAWPDHGVPDDSSDF 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 334 IKYIRYARKSHLTG-PMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEV 412
Cdd:cd14600  192 LEFVNYVRSKRVENePVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAILRV 271


                 ...
gi 767962407 413 LRK 415
Cdd:cd14600  272 YEE 274
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 183-411 9.57e-67

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: 212.64  E-value: 9.57e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 183 NREKNRYRDILPYDSTRVPLGKSK-----DYINASYI---RIVNCgeeyfYIATQGPLLSTIDDFWQMVLENNSNVIAMI 254
Cdd:cd14553    3 NKPKNRYANVIAYDHSRVILQPIEgvpgsDYINANYCdgyRKQNA-----YIATQGPLPETFGDFWRMVWEQRSATIVMM 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 255 TREIEGGIIKCYHYWPISLKKPLELKHfrVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFI 334
Cdd:cd14553   78 TKLEERSRVKCDQYWPTRGTETYGLIQ--VTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFL 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767962407 335 KYIRYARKSHL--TGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 411
Cdd:cd14553  156 AFLRRVKACNPpdAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLE 234
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 186-406 3.08e-66

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: 211.10  E-value: 3.08e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 186 KNRYRDILPYDSTRVPL---GKSKDYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGI 262
Cdd:cd14545    1 LNRYRDRDPYDHDRSRVklkQGDNDYINASLVEVEEAKRSY--ILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 263 IKCYHYWPISLKKPLELKH--FRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYA 340
Cdd:cd14545   79 IKCAQYWPQGEGNAMIFEDtgLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQKV 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767962407 341 RKSHL----TGPMVVHCSAGIGRTGVFLCVDVVFCAIVKN--CSFNIMDIVAQMREQRSGMVQTKEQYHFCY 406
Cdd:cd14545  159 RESGSlssdVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGnpSSVDVKKVLLEMRKYRMGLIQTPDQLRFSY 230
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 176-412 7.24e-66

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: 211.22  E-value: 7.24e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 176 NSGNQPSNREKNRYRDILPYDSTRVPL------GKSkDYINASYIRIVNcgEEYFYIATQGPLLSTIDDFWQMVLENNSN 249
Cdd:cd14603   23 VAGGRKENVKKNRYKDILPYDQTRVILsllqeeGHS-DYINANFIKGVD--GSRAYIATQGPLSHTVLDFWRMIWQYGVK 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 250 VIAMITREIEGGIIKCYHYWPiSLKKPLELKHFRV-FLENYQILQYFIIRMFQVVEKStgTSHSVKQLQFTKWPDHGTPA 328
Cdd:cd14603  100 VILMACREIEMGKKKCERYWA-QEQEPLQTGPFTItLVKEKRLNEEVILRTLKVTFQK--ESRSVSHFQYMAWPDHGIPD 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 329 SADSFIKYIRYARKSHLTG--PMVVHCSAGIGRTGVFLCVDVVFCAIVKNC---SFNIMDIVAQMREQRSGMVQTKEQYH 403
Cdd:cd14603  177 SPDCMLAMIELARRLQGSGpePLCVHCSAGCGRTGVICTVDYVRQLLLTQRippDFSIFDVVLEMRKQRPAAVQTEEQYE 256


                 ....*....
gi 767962407 404 FCYDIVLEV 412
Cdd:cd14603  257 FLYHTVAQM 265
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 183-406 4.61e-65

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: 208.47  E-value: 4.61e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 183 NREKNRYRDILPYDSTRVPLG------KSKDYINASYIRIVNCGEEYF-----YIATQGPLLSTIDDFWQMVLENNSNVI 251
Cdd:cd14544    1 NKGKNRYKNILPFDHTRVILKdrdpnvPGSDYINANYIRNENEGPTTDenaktYIATQGCLENTVSDFWSMVWQENSRVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 252 AMITREIEGGIIKCYHYWPISLKKPlELKHFRVFLENYQILQYFIIRMFQVVEKSTGTS-HSVKQLQFTKWPDHGTPASA 330
Cdd:cd14544   81 VMTTKEVERGKNKCVRYWPDEGMQK-QYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDPiREIWHYQYLSWPDHGVPSDP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 331 D---SFIKYIRYaRKSHL--TGPMVVHCSAGIGRTGVFLCVDVVFCAIVKN---CSFNIMDIVAQMREQRSGMVQTKEQY 402
Cdd:cd14544  160 GgvlNFLEDVNQ-RQESLphAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKgldCDIDIQKTIQMVRSQRSGMVQTEAQY 238


                 ....
gi 767962407 403 HFCY 406
Cdd:cd14544  239 KFIY 242
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 187-404 7.84e-65

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: 207.25  E-value: 7.84e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 187 NRYRDILPYDSTRVPLGKSKD-----YINASYIRIVNcGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGG 261
Cdd:cd14547    1 NRYKTILPNEHSRVCLPSVDDdplssYINANYIRGYD-GEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 262 iIKCYHYWPIslKKPLELKHFRVFLENYQILQYFIIRmfQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIR--- 338
Cdd:cd14547   80 -EKCAQYWPE--EENETYGDFEVTVQSVKETDGYTVR--KLTLKYGGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQeve 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767962407 339 -YARKSHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHF 404
Cdd:cd14547  155 eARQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEF 221
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 208-413 1.01e-62

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: 201.53  E-value: 1.01e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 208 YINASYIRIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKK--PLELKHFRVF 285
Cdd:cd14540    1 YINASHITATVGGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEhdALTFGEYKVS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 286 LENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYAR--KSHLTG---------PMVVHCS 354
Cdd:cd14540   81 TKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINsvRRHTNQdvaghnrnpPTLVHCS 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767962407 355 AGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEVL 413
Cdd:cd14540  161 AGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 187-413 1.31e-62

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: 201.66  E-value: 1.31e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 187 NRYRDILPYDSTRVPLGKSK-----DYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGG 261
Cdd:cd14619    1 NRFRNVLPYDWSRVPLKPIHeepgsDYINANYMPGYWSSQEF--IATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 262 IIKCYHYWPISlKKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYAR 341
Cdd:cd14619   79 RVKCEHYWPLD-YTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLR 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767962407 342 K---SHL-TGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEVL 413
Cdd:cd14619  158 QwldQTMsGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 148-414 1.46e-62

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: 203.30  E-value: 1.46e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 148 KILEEKTAAYDIMQEFMALELKNLPGEFNSGNQPSNREKNRYRDILPYDSTRVPLGKSKD----YINASYIRIVNCGEEY 223
Cdd:cd14599    3 KTLERKLEEGMVFTEYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVPTKEnntgYINASHIKVTVGGEEW 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 224 FYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPislkkPLELKHFRVFLENYQILQYF-------I 296
Cdd:cd14599   83 HYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWP-----KLGSKHSSATYGKFKVTTKFrtdsgcyA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 297 IRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKY---IRYARK---------SHLTGPMVVHCSAGIGRTGVFL 364
Cdd:cd14599  158 TTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEEVQGFLSYleeIQSVRRhtnsmldstKNCNPPIVVHCSAGVGRTGVVI 237

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 767962407 365 CVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEVLR 414
Cdd:cd14599  238 LTELMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 164-413 7.22e-62

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: 201.89  E-value: 7.22e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 164 MALELKNLP------GEFNSGNQPSNREKNRYRDILPYDSTRVPLG-----KSKDYINASYIRivNCGEEYFYIATQGPL 232
Cdd:cd14627   28 MELEFKRLAnskahtSRFISANLPCNKFKNRLVNIMPYETTRVCLQpirgvEGSDYINASFID--GYRQQKAYIATQGPL 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 233 LSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPIslKKPLELKHFRVF-LENYQILQYfIIRMFQVVEKSTGTSH 311
Cdd:cd14627  106 AETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPA--ERSARYQYFVVDpMAEYNMPQY-ILREFKVTDARDGQSR 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 312 SVKQLQFTKWPDHGTPASADSFIKYIRYARKSH----LTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQ 387
Cdd:cd14627  183 TVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKeqfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKM 262

                        250       260
                 ....*....|....*....|....*.
gi 767962407 388 MREQRSGMVQTKEQYHFCYDIVLEVL 413
Cdd:cd14627  263 LRTQRPAMVQTEDEYQFCYQAALEYL 288
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 187-406 1.19e-60

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: 196.68  E-value: 1.19e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 187 NRYRDILPYDSTRVPLGK-----SKDYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGG 261
Cdd:cd14617    1 NRYNNILPYDSTRVKLSNvdddpCSDYINASYIPGNNFRREY--IATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 262 IIKCYHYWPISlKKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHS-VKQLQFTKWPDHGTPASADSFIKYIR-- 338
Cdd:cd14617   79 RVKCDHYWPAD-QDSLYYGDLIVQMLSESVLPEWTIREFKICSEEQLDAPRlVRHFHYTVWPDHGVPETTQSLIQFVRtv 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 339 --YARKSHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCY 406
Cdd:cd14617  158 rdYINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 164-413 7.82e-60

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: 196.49  E-value: 7.82e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 164 MALELKNLPG------EFNSGNQPSNREKNRYRDILPYDSTRVPLG-----KSKDYINASYIRivNCGEEYFYIATQGPL 232
Cdd:cd14628   27 MELEFKRLASskahtsRFISANLPCNKFKNRLVNIMPYESTRVCLQpirgvEGSDYINASFID--GYRQQKAYIATQGPL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 233 LSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPIslKKPLELKHFRVF-LENYQILQYfIIRMFQVVEKSTGTSH 311
Cdd:cd14628  105 AETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPA--ERSARYQYFVVDpMAEYNMPQY-ILREFKVTDARDGQSR 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 312 SVKQLQFTKWPDHGTPASADSFIKYIRYARKSH----LTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQ 387
Cdd:cd14628  182 TVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKeqfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKM 261

                        250       260
                 ....*....|....*....|....*.
gi 767962407 388 MREQRSGMVQTKEQYHFCYDIVLEVL 413
Cdd:cd14628  262 LRTQRPAMVQTEDQYQFCYRAALEYL 287
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 208-407 1.25e-59

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: 192.95  E-value: 1.25e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 208 YINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPisLKKPLELKHFRVFLE 287
Cdd:cd14549    1 YINANYVDGYNKARAY--IATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWP--KEGTETYGNIQVTLL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 288 NYQILQYFIIRMFQV------VEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIR--YARKSHLTGPMVVHCSAGIGR 359
Cdd:cd14549   77 STEVLATYTVRTFSLknlklkKVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRksSAANPPGAGPIVVHCSAGVGR 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 767962407 360 TGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYD 407
Cdd:cd14549  157 TGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 207-412 4.15e-59

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: 191.77  E-value: 4.15e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 207 DYINASYIR-------IVNcgeeyFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPiSLKKPLEL 279
Cdd:cd14541    1 DYINANYVNmeipgsgIVN-----RYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWP-DLGETMQF 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 280 KHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSHLTG--PMVVHCSAGI 357
Cdd:cd14541   75 GNLQITCVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMvePTVVHCSAGI 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767962407 358 GRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEV 412
Cdd:cd14541  155 GRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRV 209
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 164-413 1.87e-57

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: 190.32  E-value: 1.87e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 164 MALELKNLPG------EFNSGNQPSNREKNRYRDILPYDSTRVPLG-----KSKDYINASYIRivNCGEEYFYIATQGPL 232
Cdd:cd14629   28 MELEFKLLANskahtsRFISANLPCNKFKNRLVNIMPYELTRVCLQpirgvEGSDYINASFID--GYRQQKAYIATQGPL 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 233 LSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPIslKKPLELKHFRVF-LENYQILQYfIIRMFQVVEKSTGTSH 311
Cdd:cd14629  106 AETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPA--ERSARYQYFVVDpMAEYNMPQY-ILREFKVTDARDGQSR 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 312 SVKQLQFTKWPDHGTPASADSFIKYIRYARKSH----LTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQ 387
Cdd:cd14629  183 TIRQFQFTDWPEQGVPKTGEGFIDFIGQVHKTKeqfgQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKT 262

                        250       260
                 ....*....|....*....|....*.
gi 767962407 388 MREQRSGMVQTKEQYHFCYDIVLEVL 413
Cdd:cd14629  263 LRTQRPAMVQTEDQYQLCYRAALEYL 288
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 187-404 5.50e-57

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: 186.95  E-value: 5.50e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 187 NRYRDILPYDSTRVPLG----KSKDYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGI 262
Cdd:cd14615    1 NRYNNVLPYDISRVKLSvqshSTDDYINANYMPGYNSKKEF--IAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 263 IKCYHYWPISLKKplELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYiRYARK 342
Cdd:cd14615   79 TKCEEYWPSKQKK--DYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINF-RHLVR 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767962407 343 SHLT-----GPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHF 404
Cdd:cd14615  156 EYMKqnppnSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVF 222
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 177-410 6.23e-57

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: 187.40  E-value: 6.23e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 177 SGNQPSNREKNRYRDILPYDSTRVPL-----GKSKDYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVI 251
Cdd:cd14614    6 AADLPVNRCKNRYTNILPYDFSRVKLvsmheEEGSDYINANYIPGYNSPQEY--IATQGPLPETRNDFWKMVLQQKSQII 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 252 AMITREIEGGIIKCYHYWPISlKKPLELKHFRVFLENYQILQYFIIRMFQVveKSTGTSHSVKQLQFTKWPDHGTPA--S 329
Cdd:cd14614   84 VMLTQCNEKRRVKCDHYWPFT-EEPVAYGDITVEMLSEEEQPDWAIREFRV--SYADEVQDVMHFNYTAWPDHGVPTanA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 330 ADSFIKYIRYARKSHLT--GPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYD 407
Cdd:cd14614  161 AESILQFVQMVRQQAVKskGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 240


                 ...
gi 767962407 408 IVL 410
Cdd:cd14614  241 CVQ 243
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 179-413 1.48e-56

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: 187.55  E-value: 1.48e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 179 NQPSNREKNRYRDILPYDSTRVPL-------GKSKDYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVI 251
Cdd:cd17667   23 NHPDNKHKNRYINILAYDHSRVKLrplpgkdSKHSDYINANYVDGYNKAKAY--IATQGPLKSTFEDFWRMIWEQNTGII 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 252 AMITREIEGGIIKCYHYWPISLKKplELKHFRVFLENYQILQYFIIRMFQVVE-----------KSTGTSHSVKQLQFTK 320
Cdd:cd17667  101 VMITNLVEKGRRKCDQYWPTENSE--EYGNIIVTLKSTKIHACYTVRRFSIRNtkvkkgqkgnpKGRQNERTVIQYHYTQ 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 321 WPDHGTPASADSFIKYIRY---ARKSHLtGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQ 397
Cdd:cd17667  179 WPDMGVPEYALPVLTFVRRssaARTPEM-GPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQ 257

                        250
                 ....*....|....*.
gi 767962407 398 TKEQYHFCYDIVLEVL 413
Cdd:cd17667  258 TEEQYIFIHDALLEAI 273
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 176-417 1.76e-56

catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein phosphatase non-receptor type 12 (PTPN12), also called PTP-PEST or protein-tyrosine phosphatase G1 (PTPG1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling. It regulates various physiological processes, including cell migration, immune response, and neuronal activity, by dephosphorylating multiple substrates including HER2, FAK, PYK2, PSTPIP, WASP, p130Cas, paxillin, Shc, catenin, c-Abl, ArgBP2, p190RhoGAP, RhoGDI, cell adhesion kinase beta, and Rho GTPase.


Pssm-ID: 350452 [Multi-domain]  Cd Length: 297  Bit Score: 187.83  E-value: 1.76e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 176 NSGNQPSNREKNRYRDILPYDSTRVPL-----GKSKDYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNV 250
Cdd:cd14604   50 ATGEKEENVKKNRYKDILPFDHSRVKLtlktsSQDSDYINANFIKGVYGPKAY--IATQGPLANTVIDFWRMIWEYNVAI 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 251 IAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVveKSTGTSHSVKQLQFTKWPDHGTPASA 330
Cdd:cd14604  128 IVMACREFEMGRKKCERYWPLYGEEPMTFGPFRISCEAEQARTDYFIRTLLL--EFQNETRRLYQFHYVNWPDHDVPSSF 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 331 DSFIKYIRYARK--SHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNC---SFNIMDIVAQMREQRSGMVQTKEQYHFC 405
Cdd:cd14604  206 DSILDMISLMRKyqEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKipeEFNVFNLIQEMRTQRHSAVQTKEQYELV 285

                        250
                 ....*....|..
gi 767962407 406 YDIVLEVLRKLL 417
Cdd:cd14604  286 HRAIAQLFEKQL 297
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 183-406 2.00e-56

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: 186.38  E-value: 2.00e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 183 NREKNRYRDILPYDSTRV------PLGKSKDYINASYI------RIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNV 250
Cdd:cd14605    2 NKNKNRYKNILPFDHTRVvlhdgdPNEPVSDYINANIImpefetKCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 251 IAMITREIEGGIIKCYHYWP--ISLKkplELKHFRVFLENYQILQYFIIRMFQVVEKSTG-TSHSVKQLQFTKWPDHGTP 327
Cdd:cd14605   82 IVMTTKEVERGKSKCVKYWPdeYALK---EYGVMRVRNVKESAAHDYILRELKLSKVGQGnTERTVWQYHFRTWPDHGVP 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 328 ASAD---SFIKYIRYARKSHL-TGPMVVHCSAGIGRTGVFLCVDVVFCAIVK---NCSFNIMDIVAQMREQRSGMVQTKE 400
Cdd:cd14605  159 SDPGgvlDFLEEVHHKQESIMdAGPVVVHCSAGIGRTGTFIVIDILIDIIREkgvDCDIDVPKTIQMVRSQRSGMVQTEA 238


                 ....*.
gi 767962407 401 QYHFCY 406
Cdd:cd14605  239 QYRFIY 244
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 181-406 2.45e-56

catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein phosphatase non-receptor type 7 (PTPN7), also called hematopoietic protein-tyrosine phosphatase (HePTP) or LC-PTP. belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN7/HePTP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. PTPN7/HePTP is found exclusively in the white blood cells in bone marrow, thymus, spleen, lymph nodes and all myeloid and lymphoid cell lines. It negatively regulates T-cell activation and proliferation, and is often dysregulated in the preleukemic disorder myelodysplastic syndrome, as well as in acute myelogenous leukemia.


Pssm-ID: 350460 [Multi-domain]  Cd Length: 247  Bit Score: 185.81  E-value: 2.45e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 181 PSNREKNRYRDILPYDSTRVPLGKSK------DYINASYIRIVNcGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMI 254
Cdd:cd14612   13 PGHASKDRYKTILPNPQSRVCLRRAGsqeeegSYINANYIRGYD-GKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMI 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 255 TREIEGGiIKCYHYWPislKKPLELKHFRVFLENYQILQYFIIRmfQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFI 334
Cdd:cd14612   92 TKLKEKK-EKCVHYWP---EKEGTYGRFEIRVQDMKECDGYTIR--DLTIQLEEESRSVKHYWFSSWPDHQTPESAGPLL 165

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767962407 335 KYIRYARKSHLT----GPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCY 406
Cdd:cd14612  166 RLVAEVEESRQTaaspGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLH 241
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 181-411 7.69e-56

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: 185.61  E-value: 7.69e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 181 PSNREKNRYRDILPYDSTRVPLGKS-KDYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIE 259
Cdd:cd14608   23 PKNKNRNRYRDVSPFDHSRIKLHQEdNDYINASLIKMEEAQRSY--ILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVME 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 260 GGIIKCYHYWPISLKKPL--ELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYI 337
Cdd:cd14608  101 KGSLKCAQYWPQKEEKEMifEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFL 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 338 RYARKSHLT----GPMVVHCSAGIGRTGVFLCVDVVFCAIVKN---CSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVL 410
Cdd:cd14608  181 FKVRESGSLspehGPVVVHCSAGIGRSGTFCLADTCLLLMDKRkdpSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVI 260


                 .
gi 767962407 411 E 411
Cdd:cd14608  261 E 261
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 208-406 6.23e-55

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: 180.70  E-value: 6.23e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 208 YINASYIRIVNcgEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLE 287
Cdd:cd14542    1 YINANFIKGVS--GSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLQFGPFKISLE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 288 NYQILQY-FIIRMFQVveKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARK--SHLTGPMVVHCSAGIGRTGVFL 364
Cdd:cd14542   79 KEKRVGPdFLIRTLKV--TFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDyqGSEDVPICVHCSAGCGRTGTIC 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 767962407 365 CVDVVFCAI---VKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCY 406
Cdd:cd14542  157 AIDYVWNLLktgKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVY 201
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 166-406 1.25e-54

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: 181.70  E-value: 1.25e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 166 LELKNLPGE--FNSGNQPSNREKNRYRDILPYDSTRVPLGKSK-DYINASYIRIVNCgeEYFYIATQGPLLSTIDDFWQM 242
Cdd:cd14607    5 LEIRNESHDypHRVAKYPENRNRNRYRDVSPYDHSRVKLQNTEnDYINASLVVIEEA--QRSYILTQGPLPNTCCHFWLM 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 243 VLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKH--FRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTK 320
Cdd:cd14607   83 VWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSFKEtgFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYTT 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 321 WPDHGTPASADSFIKYIRYARKSHL----TGPMVVHCSAGIGRTGVFLCVD--VVFCAIVKNCSFNIMDIVAQMREQRSG 394
Cdd:cd14607  163 WPDFGVPESPASFLNFLFKVRESGSlspeHGPAVVHCSAGIGRSGTFSLVDtcLVLMEKKDPDSVDIKQVLLDMRKYRMG 242

                        250
                 ....*....|..
gi 767962407 395 MVQTKEQYHFCY 406
Cdd:cd14607  243 LIQTPDQLRFSY 254
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 186-412 3.31e-54

catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), also called lymphoid phosphatase (LyP), PEST-domain phosphatase (PEP), or hematopoietic cell protein-tyrosine phosphatase 70Z-PEP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. Mutations in the PTPN22 gene are associated with multiple connective tissue and autoimmune diseases including type 1 diabetes mellitus, rheumatoid arthritis, and systemic lupus erythematosus. PTPN22 contains an N-terminal catalytic PTP domain and four proline-rich regions at the C-terminus.


Pssm-ID: 350450 [Multi-domain]  Cd Length: 234  Bit Score: 180.04  E-value: 3.31e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 186 KNRYRDILPYDSTRVPLG-----KSKDYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEG 260
Cdd:cd14602    1 KNRYKDILPYDHSRVELSlitsdEDSDYINANFIKGVYGPRAY--IATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEM 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 261 GIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVveKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYA 340
Cdd:cd14602   79 GKKKCERYWAEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKV--KFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDV 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767962407 341 R--KSHLTGPMVVHCSAGIGRTGVFLCVDVVFC----AIVKNCsFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEV 412
Cdd:cd14602  157 RcyQEDDSVPICIHCSAGCGRTGVICAIDYTWMllkdGIIPEN-FSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIEL 233
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 183-411 1.61e-53

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: 178.30  E-value: 1.61e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 183 NREKNRYRDILPYDSTRVPL-----GKSKDYINASYIRIVNcgEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITRE 257
Cdd:cd14630    3 NRNKNRYGNIISYDHSRVRLqlldgDPHSDYINANYIDGYH--RPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 258 IEGGIIKCYHYWPISLKKPLELKhfrVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYI 337
Cdd:cd14630   81 VEVGRVKCVRYWPDDTEVYGDIK---VTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFV 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767962407 338 RYAR--KSHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 411
Cdd:cd14630  158 RQVKflNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 178-411 7.47e-53

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: 177.38  E-value: 7.47e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 178 GNQPSNREKNRYRDILPYDSTRVPLGKS------KDYINASYIR---IVNCGEEYFYIATQGPLLSTIDDFWQMVLENNS 248
Cdd:cd14606   13 GQRPENKSKNRYKNILPFDHSRVILQGRdsnipgSDYINANYVKnqlLGPDENAKTYIASQGCLEATVNDFWQMAWQENS 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 249 NVIAMITREIEGGIIKCYHYWPiSLKKPLELKHFRVFLENYQILQYFIIRMFQV-VEKSTGTSHSVKQLQFTKWPDHGTP 327
Cdd:cd14606   93 RVIVMTTREVEKGRNKCVPYWP-EVGMQRAYGPYSVTNCGEHDTTEYKLRTLQVsPLDNGELIREIWHYQYLSWPDHGVP 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 328 ASAD---SFIKYIRYARKS-HLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVK---NCSFNIMDIVAQMREQRSGMVQTKE 400
Cdd:cd14606  172 SEPGgvlSFLDQINQRQESlPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTkglDCDIDIQKTIQMVRAQRSGMVQTEA 251

                        250
                 ....*....|.
gi 767962407 401 QYHFCYDIVLE 411
Cdd:cd14606  252 QYKFIYVAIAQ 262
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 161-411 5.14e-52

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: 175.61  E-value: 5.14e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 161 QEFMALElknlPGE---FNSGNQPSNREKNRYRDILPYDSTRVPLGK-----SKDYINASYIRivNCGEEYFYIATQGPL 232
Cdd:cd14626   20 QEYESID----PGQqftWENSNLEVNKPKNRYANVIAYDHSRVILTSvdgvpGSDYINANYID--GYRKQNAYIATQGPL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 233 LSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELkhFRVFLENYQILQYFIIRMFQVVEKSTGTSHS 312
Cdd:cd14626   94 PETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTETYGM--IQVTLLDTVELATYSVRTFALYKNGSSEKRE 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 313 VKQLQFTKWPDHGTPASADSFIKYIRYARKSHL--TGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMRE 390
Cdd:cd14626  172 VRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPpdAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRS 251

                        250       260
                 ....*....|....*....|.
gi 767962407 391 QRSGMVQTKEQYHFCYDIVLE 411
Cdd:cd14626  252 QRNYMVQTEDQYIFIHEALLE 272
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 172-411 5.67e-52

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: 175.63  E-value: 5.67e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 172 PGEFNSGNQPSNREKNRYRDILPYDSTRVPLG-----KSKDYINASYIrIVNCGEEYFYIATQGPLLSTIDDFWQMVLEN 246
Cdd:cd14610   33 PNATNVAQREENVQKNRSLAVLPYDHSRIILKaenshSHSDYINASPI-MDHDPRNPAYIATQGPLPATVADFWQMVWES 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 247 NSNVIAMITREIEGGIIKCYHYWPislKKPLELKH-FRVFLENYQI-LQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDH 324
Cdd:cd14610  112 GCVVIVMLTPLAENGVKQCYHYWP---DEGSNLYHiYEVNLVSEHIwCEDFLVRSFYLKNLQTNETRTVTQFHFLSWNDQ 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 325 GTPASADSFIKYIRYARKSH--LTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNC-SFNIMDIVAQMREQRSGMVQTKEQ 401
Cdd:cd14610  189 GVPASTRSLLDFRRKVNKCYrgRSCPIIVHCSDGAGRSGTYILIDMVLNKMAKGAkEIDIAATLEHLRDQRPGMVQTKEQ 268

                        250
                 ....*....|
gi 767962407 402 YHFCYDIVLE 411
Cdd:cd14610  269 FEFALTAVAE 278
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 175-411 1.37e-51

catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350481 [Multi-domain]  Cd Length: 273  Bit Score: 174.46  E-value: 1.37e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 175 FNSGNQPSNREKNRYRDILPYDSTRVPL-----GKSKDYINASYIRIVNcgEEYFYIATQGPLLSTIDDFWQMVLENNSN 249
Cdd:cd14633   32 WDSAKKDENRMKNRYGNIIAYDHSRVRLqpiegETSSDYINGNYIDGYH--RPNHYIATQGPMQETIYDFWRMVWHENTA 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 250 VIAMITREIEGGIIKCYHYWPISLKKpleLKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPAS 329
Cdd:cd14633  110 SIIMVTNLVEVGRVKCCKYWPDDTEI---YKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYH 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 330 ADSFIKYIRY--ARKSHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYD 407
Cdd:cd14633  187 ATGLLGFVRQvkSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHD 266


                 ....
gi 767962407 408 IVLE 411
Cdd:cd14633  267 AILE 270
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 208-407 2.03e-51

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: 171.80  E-value: 2.03e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 208 YINASYIrivncgEEYF-----YIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHF 282
Cdd:cd14539    1 YINASLI------EDLTpycprFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQALVYGAI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 283 RVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIR-----YARKSHLTGPMVVHCSAGI 357
Cdd:cd14539   75 TVSLQSVRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEevhshYLQQRSLQTPIVVHCSSGV 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767962407 358 GRTGVFlCvdVVFCAIVK----NCSFNIMDIVAQMREQRSGMVQTKEQYHFCYD 407
Cdd:cd14539  155 GRTGAF-C--LLYAAVQEieagNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 186-406 2.07e-51

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: 172.41  E-value: 2.07e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 186 KNRYRDILPYDSTRVPLgKSKD-------YINASYIRIVNcGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREI 258
Cdd:cd14611    2 KNRYKTILPNPHSRVCL-KPKNsndslstYINANYIRGYG-GKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 259 EGGIiKCYHYWPislKKPLELKHFRVFLENYQILQYFIIRmfQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKY-- 336
Cdd:cd14611   80 EKNE-KCVLYWP---EKRGIYGKVEVLVNSVKECDNYTIR--NLTLKQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLml 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767962407 337 -IRYARKSHLT-GPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCY 406
Cdd:cd14611  154 dVEEDRLASPGrGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 207-415 3.15e-51

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: 171.67  E-value: 3.15e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 207 DYINASYI--RIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPiSLKKPLELKHFRV 284
Cdd:cd14601    1 DYINANYInmEIPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWP-EPSGSSSYGGFQV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 285 FLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYAR--KSHLTGPMVVHCSAGIGRTGV 362
Cdd:cd14601   80 TCHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRnkRAGKDEPVVVHCSAGIGRTGV 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767962407 363 FLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEVLRK 415
Cdd:cd14601  160 LITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVYEE 212
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 187-410 1.78e-50

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: 170.12  E-value: 1.78e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 187 NRYRDILPYDSTRVPLGK-----SKDYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGG 261
Cdd:cd14618    1 NRYPHVLPYDHSRVRLSQlggepHSDYINANFIPGYTSPQEF--IATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 262 IIKCYHYWPISLkKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYAR 341
Cdd:cd14618   79 RVLCDHYWPSES-TPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVR 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767962407 342 K----SHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVL 410
Cdd:cd14618  158 EhvqaTKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 161-413 4.45e-50

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: 170.66  E-value: 4.45e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 161 QEFMALElknlPGE---FNSGNQPSNREKNRYRDILPYDSTRVPLGK-----SKDYINASYIRivNCGEEYFYIATQGPL 232
Cdd:cd14625   26 QEYESID----PGQqftWEHSNLEVNKPKNRYANVIAYDHSRVILQPiegimGSDYINANYID--GYRKQNAYIATQGPL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 233 LSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPislKKPLELKHF-RVFLENYQILQYFIIRMFQVVEKSTGTSH 311
Cdd:cd14625  100 PETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWP---SRGTETYGMiQVTLLDTIELATFCVRTFSLHKNGSSEKR 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 312 SVKQLQFTKWPDHGTPASADSFIKYIRYARKSHL--TGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMR 389
Cdd:cd14625  177 EVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPpdAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMR 256

                        250       260
                 ....*....|....*....|....
gi 767962407 390 EQRSGMVQTKEQYHFCYDIVLEVL 413
Cdd:cd14625  257 SQRNYMVQTEDQYSFIHDALLEAV 280
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 208-411 2.93e-49

catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The type II (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350403 [Multi-domain]  Cd Length: 204  Bit Score: 166.25  E-value: 2.93e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 208 YINASYIRIVNcgEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKpleLKHFRVFLE 287
Cdd:cd14555    1 YINANYIDGYH--RPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEV---YGDIKVTLV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 288 NYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSH--LTGPMVVHCSAGIGRTGVFLC 365
Cdd:cd14555   76 ETEPLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNppSAGPIVVHCSAGAGRTGCYIV 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 767962407 366 VDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 411
Cdd:cd14555  156 IDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 208-406 3.48e-49

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: 166.10  E-value: 3.48e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 208 YINASYIRIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEG-GIIKCYHYWPISLKKPLELKHFRVFL 286
Cdd:cd17658    1 YINASLVETPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNySTAKCADYFPAEENESREFGRISVTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 287 ENYQILQYFI-IRMFQVVE-KSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRyaRKSHL---TGPMVVHCSAGIGRTG 361
Cdd:cd17658   81 KKLKHSQHSItLRVLEVQYiESEEPPLSVLHIQYPEWPDHGVPKDTRSVRELLK--RLYGIppsAGPIVVHCSAGIGRTG 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 767962407 362 VFLCVDVVFCAIVKN--CSFNIMDIVAQMREQRSGMVQTKEQYHFCY 406
Cdd:cd17658  159 AYCTIHNTIRRILEGdmSAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 161-413 5.92e-49

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: 167.99  E-value: 5.92e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 161 QEFMALElknlPGE---FNSGNQPSNREKNRYRDILPYDSTRVPLGK-----SKDYINASYIRivNCGEEYFYIATQGPL 232
Cdd:cd14624   26 QEYESID----PGQqftWEHSNLEVNKPKNRYANVIAYDHSRVLLSAiegipGSDYINANYID--GYRKQNAYIATQGAL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 233 LSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELkhFRVFLENYQILQYFIIRMFQVVEKSTGTSHS 312
Cdd:cd14624  100 PETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTETYGL--IQVTLLDTVELATYCVRTFALYKNGSSEKRE 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 313 VKQLQFTKWPDHGTPASADSFIKYIRYARKSHL--TGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMRE 390
Cdd:cd14624  178 VRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPpdAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRA 257

                        250       260
                 ....*....|....*....|...
gi 767962407 391 QRSGMVQTKEQYHFCYDIVLEVL 413
Cdd:cd14624  258 QRNYMVQTEDQYIFIHDALLEAV 280
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 208-407 8.49e-49

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: 165.15  E-value: 8.49e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 208 YINASYIRIVNcgEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPisLKKPLELKHFRVFLE 287
Cdd:cd17668    1 YINANYVDGYN--KPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWP--ADGSEEYGNFLVTQK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 288 NYQILQYFIIRMFQV--------VEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYAR--KSHLTGPMVVHCSAGI 357
Cdd:cd17668   77 SVQVLAYYTVRNFTLrntkikkgSQKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASyaKRHAVGPVVVHCSAGV 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 767962407 358 GRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYD 407
Cdd:cd17668  157 GRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHD 206
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 189-411 8.98e-49

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: 165.50  E-value: 8.98e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 189 YRDILPYDSTRVPL-----GKSKDYINASYIRivNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGII 263
Cdd:cd14620    1 YPNILPYDHSRVILsqldgIPCSDYINASYID--GYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 264 KCYHYWPIslKKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHS---VKQLQFTKWPDHG---TPASADSFIKYI 337
Cdd:cd14620   79 KCYQYWPD--QGCWTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDGCKAprlVTQLHFTSWPDFGvpfTPIGMLKFLKKV 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767962407 338 RYARKSHlTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 411
Cdd:cd14620  157 KSVNPVH-AGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
179-418 1.75e-48

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 166.42  E-value: 1.75e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 179 NQPSNREKNRYRDILPYDSTRVplGKSKDYINASYIRIvncGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREI 258
Cdd:COG5599   38 QNINGSPLNRFRDIQPYKETAL--RANLGYLNANYIQV---IGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDD 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 259 EGG--IIKCYHYWPIS---LKKPLELKHfrvfLENYQILQYFIIRMFQVVEKSTG-TSHSVKQLQFTKWPDHGTPaSADS 332
Cdd:COG5599  113 EISkpKVKMPVYFRQDgeyGKYEVSSEL----TESIQLRDGIEARTYVLTIKGTGqKKIEIPVLHVKNWPDHGAI-SAEA 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 333 FIKYIRYARKSHLT-----GPMVVHCSAGIGRTGVFLCVDVVFCAI--VKNCSFNIMDIVAQMREQR-SGMVQTKEQYHF 404
Cdd:COG5599  188 LKNLADLIDKKEKIkdpdkLLPVVHCRAGVGRTGTLIACLALSKSInaLVQITLSVEEIVIDMRTSRnGGMVQTSEQLDV 267

                        250
                 ....*....|....
gi 767962407 405 CYDIVLEVLRKLLT 418
Cdd:COG5599  268 LVKLAEQQIRPLLR 281
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 172-411 2.35e-48

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: 166.37  E-value: 2.35e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 172 PGEFNSGNQPSNREKNRYRDILPYDSTRVPLG-----KSKDYINASYIrIVNCGEEYFYIATQGPLLSTIDDFWQMVLEN 246
Cdd:cd14609   31 PNTCSTAQGEANVKKNRNPDFVPYDHARIKLKaesnpSRSDYINASPI-IEHDPRMPAYIATQGPLSHTIADFWQMVWEN 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 247 NSNVIAMITREIEGGIIKCYHYWPislKKPLELKH-FRVFLENYQI-LQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDH 324
Cdd:cd14609  110 GCTVIVMLTPLVEDGVKQCDRYWP---DEGSSLYHiYEVNLVSEHIwCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAE 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 325 GTPASADSFIKYIRYARKSH--LTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNC-SFNIMDIVAQMREQRSGMVQTKEQ 401
Cdd:cd14609  187 GIPSSTRPLLDFRRKVNKCYrgRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGVkEIDIAATLEHVRDQRPGMVRTKDQ 266

                        250
                 ....*....|
gi 767962407 402 YHFCYDIVLE 411
Cdd:cd14609  267 FEFALTAVAE 276
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 187-404 2.42e-48

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: 164.31  E-value: 2.42e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 187 NRYRDILPYDSTRVPL-----GKSKDYINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGG 261
Cdd:cd14616    1 NRFPNIKPYNNNRVKLiadagVPGSDYINASYISGYLCPNEF--IATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 262 IIKCYHYWPISlKKPLElkhfrVF--------LENYQIlqYFIIRMFQvVEKStGTSHSVKQLQFTKWPDHGTPASADSF 333
Cdd:cd14616   79 RIRCHQYWPED-NKPVT-----VFgdivitklMEDVQI--DWTIRDLK-IERH-GDYMMVRQCNFTSWPEHGVPESSAPL 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767962407 334 IKYIRYAR--KSHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHF 404
Cdd:cd14616  149 IHFVKLVRasRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIF 221
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 208-414 2.93e-47

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: 161.30  E-value: 2.93e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 208 YINASYIRIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPislkkPLELKHFRVFLE 287
Cdd:cd14598    1 YINASHIKVTVGGKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWP-----RLGSRHNTVTYG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 288 NYQILQYF-------IIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKY---IRYARKsHLTG---------P 348
Cdd:cd14598   76 RFKITTRFrtdsgcyATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYleeIQSVRR-HTNStidpkspnpP 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767962407 349 MVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEVLR 414
Cdd:cd14598  155 VLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 159-420 1.86e-46

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 162.09  E-value: 1.86e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 159 IMQEFMALELKNLPGEFNSGNQPSNREKNRYRDILPYDSTRVPL----GKSKDYINASYIRIVNcgEEYFYIATQGPLLS 234
Cdd:PHA02747  27 IRDEHHQIILKPFDGLIANFEKPENQPKNRYWDIPCWDHNRVILdsggGSTSDYIHANWIDGFE--DDKKFIATQGPFAE 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 235 TIDDFWQMVLENNSNVIAMIT-REIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSV 313
Cdd:PHA02747 105 TCADFWKAVWQEHCSIIVMLTpTKGTNGEEKCYQYWCLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKI 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 314 KQLQFTKWPDHGTPASADSFIKYIR------------YARKSHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNI 381
Cdd:PHA02747 185 SHFQCSEWFEDETPSDHPDFIKFIKiidinrkksgklFNPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICL 264

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 767962407 382 MDIVAQMREQRSGMVQTKEQYHF---CYDIVLEVLRKLLTLD 420
Cdd:PHA02747 265 AKTAEKIREQRHAGIMNFDDYLFiqpGYEVLHYFLSKIKAID 306
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 208-411 3.02e-46

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: 158.38  E-value: 3.02e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 208 YINASYIrIVNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPislKKPLELKH-FRVFL 286
Cdd:cd14546    1 YINASTI-YDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWP---EEGSEVYHiYEVHL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 287 ENYQIL-QYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSH--LTGPMVVHCSAGIGRTGVF 363
Cdd:cd14546   77 VSEHIWcDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYrgRSCPIVVHCSDGAGRTGTY 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767962407 364 LCVDVVFCAIVKncSFNIMDIVA---QMREQRSGMVQTKEQYHFCYDIVLE 411
Cdd:cd14546  157 ILIDMVLNRMAK--GAKEIDIAAtleHLRDQRPGMVKTKDQFEFVLTAVAE 205
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 161-411 3.25e-46

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: 160.96  E-value: 3.25e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 161 QEFMALELKNLPGEFNSGNQPSNREKNRYRDILPYDSTRVPLGK-----SKDYINASYIRivNCGEEYFYIATQGPLLST 235
Cdd:cd14621   30 EEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPvegvpDSDYINASFIN--GYQEKNKFIAAQGPKEET 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 236 IDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPIslKKPLELKHFRVFLENYQILQYFIIRMF--QVVEKSTGTSHS- 312
Cdd:cd14621  108 VNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPD--QGCWTYGNIRVSVEDVTVLVDYTVRKFciQQVGDVTNKKPQr 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 313 -VKQLQFTKWPDHGTPASADSFIKYIRYARKSH--LTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMR 389
Cdd:cd14621  186 lITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNpqYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIR 265

                        250       260
                 ....*....|....*....|..
gi 767962407 390 EQRSGMVQTKEQYHFCYDIVLE 411
Cdd:cd14621  266 AQRCQMVQTDMQYVFIYQALLE 287
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 205-411 3.51e-46

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: 158.65  E-value: 3.51e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 205 SKDYINASYIRivNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPislkKPLEL-KHFR 283
Cdd:cd14631   12 SSDYINANYID--GYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP----DDTEVyGDFK 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 284 VFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSH--LTGPMVVHCSAGIGRTG 361
Cdd:cd14631   86 VTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNppSAGPIVVHCSAGAGRTG 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 767962407 362 VFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 411
Cdd:cd14631  166 CYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 208-409 6.43e-46

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350400 [Multi-domain]  Cd Length: 202  Bit Score: 157.43  E-value: 6.43e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 208 YINASYIRIVNcgEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPIslKKPLELKHFRVFLE 287
Cdd:cd14552    1 YINASFIDGYR--QKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPE--DGSVSSGDITVELK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 288 NYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSHL---TGPMVVHCSAGIGRTGVFL 364
Cdd:cd14552   77 DQTDYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQqsgNHPITVHCSAGAGRTGTFC 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 767962407 365 CVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIV 409
Cdd:cd14552  157 ALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 186-409 1.23e-45

catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein phosphatase non-receptor type 5 (PTPN5), also called striatum-enriched protein-tyrosine phosphatase (STEP) or neural-specific PTP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN5/STEP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. It is a CNS-enriched protein that regulates key signaling proteins required for synaptic strengthening, as well as NMDA and AMPA receptor trafficking. PTPN5 is implicated in multiple neurologic and neuropsychiatric disorders, such as Alzheimer's disease, Parkinson's disease, schizophrenia, and fragile X syndrome.


Pssm-ID: 350461 [Multi-domain]  Cd Length: 258  Bit Score: 158.49  E-value: 1.23e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 186 KNRYRDILPYDSTRVPLgKSKD-------YINASYIRIVNcGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITrEI 258
Cdd:cd14613   28 KNRYKTILPNPHSRVCL-TSPDqddplssYINANYIRGYG-GEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMIT-NI 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 259 EGGIIKCYHYWP----------ISLKKPLELKHFRvflenyqilqyfiIRMFQVveKSTGTSHSVKQLQFTKWPDHGTPA 328
Cdd:cd14613  105 EEMNEKCTEYWPeeqvtyegieITVKQVIHADDYR-------------LRLITL--KSGGEERGLKHYWYTSWPDQKTPD 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 329 SADSFIKYIR-------YARKSHltGPMVVHCSAGIGRTGVFLCVDVVfCAIVKNCS-FNIMDIVAQMREQRSGMVQTKE 400
Cdd:cd14613  170 NAPPLLQLVQeveearqQAEPNC--GPVIVHCSAGIGRTGCFIATSIC-CKQLRNEGvVDILRTTCQLRLDRGGMIQTCE 246


                 ....*....
gi 767962407 401 QYHFCYDIV 409
Cdd:cd14613  247 QYQFVHHVL 255
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 208-411 1.22e-44

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


Pssm-ID: 350480 [Multi-domain]  Cd Length: 205  Bit Score: 154.05  E-value: 1.22e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 208 YINASYIRIVNcgEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKhfrVFLE 287
Cdd:cd14632    1 YINANYIDGYH--RSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDTYGDIK---ITLL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 288 NYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSHL--TGPMVVHCSAGIGRTGVFLC 365
Cdd:cd14632   76 KTETLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPpdAGPVVVHCSAGAGRTGCYIV 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 767962407 366 VDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 411
Cdd:cd14632  156 LDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 144-411 1.48e-44

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 157.09  E-value: 1.48e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 144 KDCLKILEEKTAAYDIMQEFMALELKNLPGEFNSGNQPSNREKNRYRDILPYDSTRVPLGKSK---DYINASYIRIVNCG 220
Cdd:PHA02742  13 KNCEQLIEESNLAEILKEEHEHIMQEIVAFSCNESLELKNMKKCRYPDAPCFDRNRVILKIEDggdDFINASYVDGHNAK 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 221 EEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFIIRMF 300
Cdd:PHA02742  93 GRF--ICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYWMPHERGKATHGEFKIKTKKIKSFRNYAVTNL 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 301 QVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSHLTG-------------PMVVHCSAGIGRTGVFLCVD 367
Cdd:PHA02742 171 CLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFVLAVREADLKAdvdikgenivkepPILVHCSAGLDRAGAFCAID 250

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 767962407 368 VVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 411
Cdd:PHA02742 251 ICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCYFIVLI 294
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 208-402 4.02e-44

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: 152.67  E-value: 4.02e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 208 YINASYIRivNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLE 287
Cdd:cd14557    1 YINASYID--GFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKIN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 288 NYQILQYFIIRMFQVV-EKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRY--ARKSHLTGPMVVHCSAGIGRTGVFL 364
Cdd:cd14557   79 EEKICPDYIIRKLNINnKKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRvnAFNNFFSGPIVVHCSAGVGRTGTYI 158

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 767962407 365 CVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQY 402
Cdd:cd14557  159 GIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQY 196
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 208-407 7.23e-43

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: 149.08  E-value: 7.23e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 208 YINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKhfrVFLE 287
Cdd:cd14558    1 YINASFIDGYWGPKSL--IATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKTYGDIE---VELK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 288 NYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYAR--------KSHLTGPMVVHCSAGIGR 359
Cdd:cd14558   76 DTEKSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKqklpyknsKHGRSVPIVVHCSDGSSR 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 360 TGvflcvdvVFCAIvkncsFNIMD------------IVAQMREQRSGMVQTKEQYHFCYD 407
Cdd:cd14558  156 TG-------IFCAL-----WNLLEsaetekvvdvfqVVKALRKQRPGMVSTLEQYQFLYD 203
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 208-406 1.05e-41

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: 146.21  E-value: 1.05e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 208 YINASYIRivNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKplELKHFRVFLE 287
Cdd:cd14551    1 YINASYID--GYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCW--TYGNLRVRVE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 288 NYQILQYFIIRMFQVVEKSTGTSHS----VKQLQFTKWPDHGTPASADSFIKYIRYArKSHLT---GPMVVHCSAGIGRT 360
Cdd:cd14551   77 DTVVLVDYTTRKFCIQKVNRGIGEKrvrlVTQFHFTSWPDFGVPFTPIGMLKFLKKV-KSANPpraGPIVVHCSAGVGRT 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 767962407 361 GVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCY 406
Cdd:cd14551  156 GTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 207-409 1.43e-40

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: 143.22  E-value: 1.43e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 207 DYINASYIRivNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPIslKKPLELKHFRVFL 286
Cdd:cd14622    1 DYINASFID--GYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPS--EGSVTHGEITIEI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 287 ENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARKSHL-TG--PMVVHCSAGIGRTGVF 363
Cdd:cd14622   77 KNDTLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQqTGnhPIVVHCSAGAGRTGTF 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 767962407 364 LCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIV 409
Cdd:cd14622  157 IALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 188-411 4.21e-39

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: 140.18  E-value: 4.21e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 188 RYRDILPYDSTRV--PLGKSK---DYINASYIRivNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGI 262
Cdd:cd14623    1 RVLQIIPYEFNRViiPVKRGEentDYVNASFID--GYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 263 IKCYHYWPISlkKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARK 342
Cdd:cd14623   79 EKCAQYWPSD--GSVSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQK 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767962407 343 SHLTG---PMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 411
Cdd:cd14623  157 QQQQSgnhPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
312-411 1.04e-36

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 129.79  E-value: 1.04e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407   312 SVKQLQFTKWPDHGTPASADSFIKYIRYARKSH----LTGPMVVHCSAGIGRTGVFLCVDVVfCAIVKNCS--FNIMDIV 385
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLnqseSSGPVVVHCSAGVGRTGTFVAIDIL-LQQLEAEAgeVDIFDTV 79

                           90       100
                   ....*....|....*....|....*.
gi 767962407   386 AQMREQRSGMVQTKEQYHFCYDIVLE 411
Cdd:smart00404  80 KELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 312-411 1.04e-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: 1.04e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407   312 SVKQLQFTKWPDHGTPASADSFIKYIRYARKSH----LTGPMVVHCSAGIGRTGVFLCVDVVfCAIVKNCS--FNIMDIV 385
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLnqseSSGPVVVHCSAGVGRTGTFVAIDIL-LQQLEAEAgeVDIFDTV 79

                           90       100
                   ....*....|....*....|....*.
gi 767962407   386 AQMREQRSGMVQTKEQYHFCYDIVLE 411
Cdd:smart00012  80 KELRSQRPGMVQTEEQYLFLYRALLE 105
PHA02738 PHA02738
hypothetical protein; Provisional
 138-409 1.36e-36

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 136.21  E-value: 1.36e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 138 HEQTAIKDCLKILEEKTAAYDIMQEFMALELKNLPGEFNSgnQPSNREKNRYRDILPYDSTRVPLGKSK---DYINASYI 214
Cdd:PHA02738   6 FRELKYAEFLALMEKSDCEEVITREHQKVISEKVDGTFNA--EKKNRKLNRYLDAVCFDHSRVILPAERnrgDYINANYV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 215 RivncGEEYF--YIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQIL 292
Cdd:PHA02738  84 D----GFEYKkkFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGSIRFGKFKITTTQVETH 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 293 QYFIIRMFQVVEkSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYAR---------------KSHLTGPMVVHCSAGI 357
Cdd:PHA02738 160 PHYVKSTLLLTD-GTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRqcqkelaqeslqighNRLQPPPIVVHCNAGL 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767962407 358 GRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIV 409
Cdd:PHA02738 239 GRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 134-413 1.28e-34

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 130.92  E-value: 1.28e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 134 IFNFHEQT-AIKDCLKILEEKTAAYDImqefmalelkNLPGEFNSGNQPSNREKNRYRDILPYDSTRVPLGK-------- 204
Cdd:PHA02746  11 AFDFFDKTnHAKFCEFVLLEHAEVMDI----------PIRGTTNHFLKKENLKKNRFHDIPCWDHSRVVINAheslkmfd 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 205 ------------SKD----YINASYIRivNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITrEIEGGIIKCYHY 268
Cdd:PHA02746  81 vgdsdgkkievtSEDnaenYIHANFVD--GFKEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLT-DIDDDDEKCFEL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 269 WpiSLKKPLELKHFRVFLENYQILQ--YFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASADSFIKYIRYARK---- 342
Cdd:PHA02746 158 W--TKEEDSELAFGRFVAKILDIIEelSFTKTRLMITDKISDTSREIHHFWFPDWPDNGIPTGMAEFLELINKVNEeqae 235

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767962407 343 --------SHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLEVL 413
Cdd:PHA02746 236 likqadndPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKALKYAI 314
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 208-407 8.50e-34

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: 125.21  E-value: 8.50e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 208 YINASYIrivncgEEY----FYIATQGPLLSTIDDFWQMVLENNSNVIAMITrEIEGGIIKCYHYWPIslKKPLELKHFR 283
Cdd:cd14556    1 YINAALL------DSYkqpaAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLN-QLDPKDQSCPQYWPD--EGSGTYGPIQ 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 284 VFLENYQILQYFIIRMFQVVE--KSTGTSHSVKQLQFTKWPDHG-TPASADSFIKYIRYARK---SHLTGPMVVHCSAGI 357
Cdd:cd14556   72 VEFVSTTIDEDVISRIFRLQNttRPQEGYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKwqeQSGEGPIVVHCLNGV 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 767962407 358 GRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYD 407
Cdd:cd14556  152 GRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 208-411 4.56e-24

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: 98.94  E-value: 4.56e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 208 YINASYIRivNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITrEIEGGIIkCYHYWPisLKKPLELKHFRVFLE 287
Cdd:cd14634    1 YINAALMD--SHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLN-EMDAAQL-CMQYWP--EKTSCCYGPIQVEFV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 288 NYQILQYFIIRMFQV--VEKSTGTSHSVKQLQFTKWPDH-GTPASADSFIKYIRYARKSHLT-----GPMVVHCSAGIGR 359
Cdd:cd14634   75 SADIDEDIISRIFRIcnMARPQDGYRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQydgreGRTVVHCLNGGGR 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767962407 360 TGVFlcvdvvfCAIVKNCSF----NIMDI---VAQMREQRSGMVQTKEQYHFCYDIVLE 411
Cdd:cd14634  155 SGTF-------CAICSVCEMiqqqNIIDVfhtVKTLRNNKSNMVETLEQYKFVYEVALE 206
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 208-406 5.88e-23

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: 95.85  E-value: 5.88e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 208 YINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGiiKCYHYWPISlKKPLELKHFRVFL- 286
Cdd:cd14550    1 YINASYLQGYRRSNEF--IITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTK-EKPLECETFKVTLs 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 287 ---------ENYQILQYFIIRMFQ---VVEkstgtshsVKQLQFTKWPDHGTPASadSFIKYIRYARKSHLT--GPMVVH 352
Cdd:cd14550   76 gedhsclsnEIRLIVRDFILESTQddyVLE--------VRQFQCPSWPNPCSPIH--TVFELINTVQEWAQQrdGPIVVH 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767962407 353 -----CSAGigrtgvflcvdvVFCAI------VKNCsfNIMDI--VAQMREQ-RSGMVQTKEQYHFCY 406
Cdd:cd14550  146 dryggVQAA------------TFCALttlhqqLEHE--SSVDVyqVAKLYHLmRPGVFTSKEDYQFLY 199
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 208-411 1.75e-22

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: 94.75  E-value: 1.75e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 208 YINASYIRivNCGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITrEIEGGIIkCYHYWP---ISLKKPLELKHFRV 284
Cdd:cd14635    1 YINAALMD--SYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLN-DVDPAQL-CPQYWPengVHRHGPIQVEFVSA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 285 FLENYQILQYFiiRMFQVVEKSTGTsHSVKQLQFTKWPDH-GTPASADSFIKYIRYARKSHLT-----GPMVVHCSAGIG 358
Cdd:cd14635   77 DLEEDIISRIF--RIYNAARPQDGY-RMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEynggeGRTVVHCLNGGG 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767962407 359 RTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 411
Cdd:cd14635  154 RSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 208-411 2.16e-21

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: 91.51  E-value: 2.16e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 208 YINA----SYIRIVNcgeeyfYIATQGPLLSTIDDFWQMVLENNSNVIAMITR-EIEGGIIKCYHYWP---ISLKKPLEL 279
Cdd:cd14637    1 YINAaltdSYTRSAA------FIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQlNQSNSAWPCLQYWPepgLQQYGPMEV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 280 KHFRVFLEnyqilQYFIIRMFQV--VEKSTGTSHSVKQLQFTKW-PDHGTPASADSFIKYI----RYARKSHlTGPMVVH 352
Cdd:cd14637   75 EFVSGSAD-----EDIVTRLFRVqnITRLQEGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLasveKWQRESG-EGRTVVH 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767962407 353 CSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 411
Cdd:cd14637  149 CLNGGGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 208-411 9.39e-21

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: 89.70  E-value: 9.39e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 208 YINASYIRIVNcgEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMITR-EIEGGiikCYHYWP---ISLKKPLELKHFR 283
Cdd:cd14636    1 YINAALMDSYR--QPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEvDLAQG---CPQYWPeegMLRYGPIQVECMS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 284 VFLENYQILQYFiiRMFQVVEKSTGTShSVKQLQFTKWPDH-GTPASADSFIKYIRYARK-----SHLTGPMVVHCSAGI 357
Cdd:cd14636   76 CSMDCDVISRIF--RICNLTRPQEGYL-MVQQFQYLGWASHrEVPGSKRSFLKLILQVEKwqeecDEGEGRTIIHCLNGG 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767962407 358 GRTGVFLCVDVVfCAIVKNCsfNIMDI---VAQMREQRSGMVQTKEQYHFCYDIVLE 411
Cdd:cd14636  153 GRSGMFCAISIV-CEMIKRQ--NVVDVfhaVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 208-410 1.02e-20

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: 89.67  E-value: 1.02e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 208 YINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITREIEGGIIKCYhYWPiSLKKPLELKHFRVFL- 286
Cdd:cd17669    1 YINASYIMGYYQSNEF--IITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWP-NKDEPINCETFKVTLi 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 287 ---------ENYQILQYFIIRMFQ---VVEkstgtshsVKQLQFTKWPDHGTPASADSFIKYIRYARKSHLTGPMVVHCS 354
Cdd:cd17669   77 aeehkclsnEEKLIIQDFILEATQddyVLE--------VRHFQCPKWPNPDSPISKTFELISIIKEEAANRDGPMIVHDE 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767962407 355 AGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVL 410
Cdd:cd17669  149 HGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 187-402 5.77e-20

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: 87.84  E-value: 5.77e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 187 NRYRDIlpydSTRVPLGKSKDyINASYIRIvncGEEYFYIATQGPLLSTIDDFWQMVLENNSNVIAMIT--REIEGGIIK 264
Cdd:cd14559    1 NRFTNI----QTRVSTPVGKN-LNANRVQI---GNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLAsnKDIQRKGLP 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 265 CY-----HYWPISLKKPLELKhfrvflenYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHgTPASADSFIK---Y 336
Cdd:cd14559   73 PYfrqsgTYGSVTVKSKKTGK--------DELVDGLKADMYNLKITDGNKTITIPVVHVTNWPDH-TAISSEGLKEladL 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 337 IRYARKSHLTGPM---------------VVHCSAGIGRTGVFLCvdvVFCAIVKNCSFNIMDIVAQMREQRSG-MVQTKE 400
Cdd:cd14559  144 VNKSAEEKRNFYKskgssaindknkllpVIHCRAGVGRTGQLAA---AMELNKSPNNLSVEDIVSDMRTSRNGkMVQKDE 220


                 ..
gi 767962407 401 QY 402
Cdd:cd14559  221 QL 222
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 159-409 7.04e-18

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 83.48  E-value: 7.04e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 159 IMQEFMALelknLPGEFNSGNQPSNREKNRYRD------ILPYDSTRVPLGKSKDYINASYIRIVNcgEEYFYIATQGPL 232
Cdd:PHA02740  27 IIKEYRAI----VPEHEDEANKACAQAENKAKDenlalhITRLLHRRIKLFNDEKVLDARFVDGYD--FEQKFICIINLC 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 233 LSTIDDFWQMVLENNSNVIAMITREIEGgiiKCYH-YWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVVEKStGTSH 311
Cdd:PHA02740 101 EDACDKFLQALSDNKVQIIVLISRHADK---KCFNqFWSLKEGCVITSDKFQIETLEIIIKPHFNLTLLSLTDKF-GQAQ 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 312 SVKQLQFTKWPDHGTPASADSFIKY----------IRYARKSHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNI 381
Cdd:PHA02740 177 KISHFQYTAWPADGFSHDPDAFIDFfcniddlcadLEKHKADGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSI 256

                        250       260
                 ....*....|....*....|....*...
gi 767962407 382 MDIVAQMREQRSGMVQTKEQYHFCYDIV 409
Cdd:PHA02740 257 ANALKKVRQKKYGCMNCLDDYVFCYHLI 284
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 208-410 1.53e-16

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: 77.80  E-value: 1.53e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 208 YINASYIRIVNCGEEYfyIATQGPLLSTIDDFWQMVLENNSNVIAMITrEIEGGIIKCYHYWPiSLKKPLELKHFRVFLE 287
Cdd:cd17670    1 YINASYIMGYYRSNEF--IITQHPLPHTTKDFWRMIWDHNAQIIVMLP-DNQGLAEDEFVYWP-SREESMNCEAFTVTLI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 288 NYQIL-----QYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHGTPASadSFIKYIRYARKSHLT--GPMVVHCSAGIGRT 360
Cdd:cd17670   77 SKDRLclsneEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPIS--STFELINVIKEEALTrdGPTIVHDEFGAVSA 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 767962407 361 GVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVL 410
Cdd:cd17670  155 GTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
321-404 7.69e-10

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 56.90  E-value: 7.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 321 WPDHGTP--ASADSFIKYIRYARKSHltGPMVVHCSAGIGRTGVFL-CVdvvfcAIVKNCSFNimDIVAQMREQRSGMVQ 397
Cdd:COG2453   55 IPDFGAPddEQLQEAVDFIDEALREG--KKVLVHCRGGIGRTGTVAaAY-----LVLLGLSAE--EALARVRAARPGAVE 125


                 ....*..
gi 767962407 398 TKEQYHF 404
Cdd:COG2453  126 TPAQRAF 132
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 347-407 9.35e-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: 53.12  E-value: 9.35e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767962407 347 GPMVVHCSAGIGRTGVFLCvdvvfCAIVKNCSFNIMDIVAQMREQR-SGMVQTKEQYHFCYD 407
Cdd:cd14494   57 EPVLVHCKAGVGRTGTLVA-----CYLVLLGGMSAEEAVRIVRLIRpGGIPQTIEQLDFLIK 113
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 331-404 2.07e-08

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: 52.66  E-value: 2.07e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767962407 331 DSFIKYIRYARKSHLtgPMVVHCSAGIGRTGVFLCvdvvfCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHF 404
Cdd:cd14504   69 DEFLDIVEEANAKNE--AVLVHCLAGKGRTGTMLA-----CYLVKTGKISAVDAINEIRRIRPGSIETSEQEKF 135
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 315-404 1.92e-05

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 44.63  E-value: 1.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 315 QLQFTKWP--DHGTPASA--DSFIKYIR--YARKSHLTGPMVVHCSAGIGRTGVFLCVdvvfcAIVKNCSFNIMDIVAQM 388
Cdd:PTZ00242  61 GIEVHDWPfdDGAPPPKAviDNWLRLLDqeFAKQSTPPETIAVHCVAGLGRAPILVAL-----ALVEYGGMEPLDAVGFV 135

                         90
                 ....*....|....*.
gi 767962407 389 REQRSGMVQTKeQYHF 404
Cdd:PTZ00242 136 REKRKGAINQT-QLQF 150
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 321-401 2.48e-05

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


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 45.03  E-value: 2.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767962407 321 WPDHGTPASA---DSfIKYIRYARKshLTGPMVVHCSAGIGRTGVflcvdVVFCAIVKNCSFNIMDIVAQMREQRSGMVQ 397
Cdd:cd14506   84 WKDYGVPSLTtilDI-VKVMAFALQ--EGGKVAVHCHAGLGRTGV-----LIACYLVYALRMSADQAIRLVRSKRPNSIQ 155


                 ....
gi 767962407 398 TKEQ 401
Cdd:cd14506  156 TRGQ 159
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 350-407 2.78e-04

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: 41.09  E-value: 2.78e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767962407 350 VVHCSAGIGRTGVFL-CVdvvfcAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYD 407
Cdd:cd14505  110 LIHCKGGLGRTGLIAaCL-----LLELGDTLDPEQAIAAVRALRPGAIQTPKQENFLHQ 163
 
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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