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Conserved domains on  [gi|1207734383|ref|NP_001339455|]
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tyrosine-protein phosphatase non-receptor type 20 isoform 12 [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 ...
 1-173 1.22e-112

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: 319.00  E-value: 1.22e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKW 80
Cdd:cd14596    35 MVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLRLENYQALQYFIIRIIKLVEKETGENRLIKHLQFTTW 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  81 PDHGTPASADSFIKYIRYARKSHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQ 160
Cdd:cd14596   115 PDHGTPQSSDQLVKFICYMRKVHNTGPIVVHCSAGIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQ 194

                         170
                  ....*....|...
gi 1207734383 161 YHFCYDIVLEVLR 173
Cdd:cd14596   195 YLFCYKVVLEVLQ 207
 
Name Accession Description Interval E-value
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 1-173 1.22e-112

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: 319.00  E-value: 1.22e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKW 80
Cdd:cd14596    35 MVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLRLENYQALQYFIIRIIKLVEKETGENRLIKHLQFTTW 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  81 PDHGTPASADSFIKYIRYARKSHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQ 160
Cdd:cd14596   115 PDHGTPQSSDQLVKFICYMRKVHNTGPIVVHCSAGIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQ 194

                         170
                  ....*....|...
gi 1207734383 161 YHFCYDIVLEVLR 173
Cdd:cd14596   195 YLFCYKVVLEVLQ 207
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1-170 7.58e-71

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 214.83  E-value: 7.58e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383    1 MVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKW 80
Cdd:smart00194  88 MVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTVTHYHYTNW 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   81 PDHGTPASADSFIKYIRYARK--SHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTK 158
Cdd:smart00194 168 PDHGVPESPESILDLIRAVRKsqSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQRPGMVQTE 247

                          170
                   ....*....|..
gi 1207734383  159 EQYHFCYDIVLE 170
Cdd:smart00194 248 EQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1-170 2.81e-70

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 212.49  E-value: 2.81e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLENY-QILQYFIIRMFQVVEKSTGTSHSVKQLQFTK 79
Cdd:pfam00102  61 MVWEEKVTIIVMLTELEEKGREKCAQYWPEEEGESLEYGDFTVTLKKEkEDEKDYTVRTLEVSNGGSEETRTVKHFHYTG 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  80 WPDHGTPASADSFIKYIRYARKSHL---TGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQ 156
Cdd:pfam00102 141 WPDHGVPESPNSLLDLLRKVRKSSLdgrSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQ 220

                         170
                  ....*....|....
gi 1207734383 157 TKEQYHFCYDIVLE 170
Cdd:pfam00102 221 TLEQYIFLYDAILE 234
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 1-179 1.64e-28

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 107.39  E-value: 1.64e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMIT-REIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTK 79
Cdd:PHA02747  112 AVWQEHCSIIVMLTpTKGTNGEEKCYQYWCLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKISHFQCSE 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  80 WPDHGTPASADSFIKYIR------------YARKSHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQM 147
Cdd:PHA02747  192 WFEDETPSDHPDFIKFIKiidinrkksgklFNPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKI 271

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1207734383 148 REQRSGMVQTKEQYHF---CYDIVLEVLRKLLTLD 179
Cdd:PHA02747  272 REQRHAGIMNFDDYLFiqpGYEVLHYFLSKIKAID 306
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
1-177 3.81e-27

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 103.25  E-value: 3.81e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGG--IIKCYHYWPIS---LKKPLELKHfrvfLENYQILQYFIIRMFQVVEKSTG-TSHSVKQ 74
Cdd:COG5599    96 MLFDNNTPVLVVLASDDEISkpKVKMPVYFRQDgeyGKYEVSSEL----TESIQLRDGIEARTYVLTIKGTGqKKIEIPV 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  75 LQFTKWPDHGTPaSADSFIKYIRYARKSHLT-----GPMVVHCSAGIGRTGVFLCVDVVFCAI--VKNCSFNIMDIVAQM 147
Cdd:COG5599   172 LHVKNWPDHGAI-SAEALKNLADLIDKKEKIkdpdkLLPVVHCRAGVGRTGTLIACLALSKSInaLVQITLSVEEIVIDM 250

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1207734383 148 REQR-SGMVQTKEQYHFCYDIVLEVLRKLLT 177
Cdd:COG5599   251 RTSRnGGMVQTSEQLDVLVKLAEQQIRPLLR 281
 
Name Accession Description Interval E-value
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 1-173 1.22e-112

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: 319.00  E-value: 1.22e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKW 80
Cdd:cd14596    35 MVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLRLENYQALQYFIIRIIKLVEKETGENRLIKHLQFTTW 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  81 PDHGTPASADSFIKYIRYARKSHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQ 160
Cdd:cd14596   115 PDHGTPQSSDQLVKFICYMRKVHNTGPIVVHCSAGIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQ 194

                         170
                  ....*....|...
gi 1207734383 161 YHFCYDIVLEVLR 173
Cdd:cd14596   195 YLFCYKVVLEVLQ 207
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 1-172 1.75e-107

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: 305.84  E-value: 1.75e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPL-ELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTK 79
Cdd:cd14538    35 MVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKPLiCGGRLEVSLEKYQSLQDFVIRRISLRDKETGEVHHITHLNFTT 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  80 WPDHGTPASADSFIKYIRYARKSHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKE 159
Cdd:cd14538   115 WPDHGTPQSADPLLRFIRYMRRIHNSGPIVVHCSAGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKD 194

                         170
                  ....*....|...
gi 1207734383 160 QYHFCYDIVLEVL 172
Cdd:cd14538   195 QYIFCYKACLEVL 207
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1-170 7.58e-71

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 214.83  E-value: 7.58e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383    1 MVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKW 80
Cdd:smart00194  88 MVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTVTHYHYTNW 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   81 PDHGTPASADSFIKYIRYARK--SHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTK 158
Cdd:smart00194 168 PDHGVPESPESILDLIRAVRKsqSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQRPGMVQTE 247

                          170
                   ....*....|..
gi 1207734383  159 EQYHFCYDIVLE 170
Cdd:smart00194 248 EQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1-170 2.81e-70

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 212.49  E-value: 2.81e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLENY-QILQYFIIRMFQVVEKSTGTSHSVKQLQFTK 79
Cdd:pfam00102  61 MVWEEKVTIIVMLTELEEKGREKCAQYWPEEEGESLEYGDFTVTLKKEkEDEKDYTVRTLEVSNGGSEETRTVKHFHYTG 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  80 WPDHGTPASADSFIKYIRYARKSHL---TGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQ 156
Cdd:pfam00102 141 WPDHGVPESPNSLLDLLRKVRKSSLdgrSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQ 220

                         170
                  ....*....|....
gi 1207734383 157 TKEQYHFCYDIVLE 170
Cdd:pfam00102 221 TLEQYIFLYDAILE 234
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 1-172 3.49e-65

catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein phosphatase non-receptor type 13 (PTPN13, also known as PTPL1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN13 is an important regulator of tumor aggressiveness. It regulates breast cancer cell aggressiveness through direct inactivation of Src kinase. In hepatocellular carcinoma, PTPN13 is a tumor suppressor. PTPN13 contains a FERM domain, five PDZ domains, and a C-terminal catalytic PTP domain. With its PDZ domains, PTPN13 has numerous interacting partners that can actively participate in the regulation of its phosphatase activity or can permit direct or indirect recruitment of tyrosine phosphorylated substrates. Its FERM domain is necessary for localization to the membrane.


Pssm-ID: 350445 [Multi-domain]  Cd Length: 234  Bit Score: 199.67  E-value: 3.49e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLEL-KHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTK 79
Cdd:cd14597    62 MVWEQKSTVIAMMTQEVEGGKIKCQRYWPEILGKTTMVdNRLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTA 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  80 WPDHGTPASADSFIKYIRYARKSHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKE 159
Cdd:cd14597   142 WPDHDTPSQPEQLLTFISYMRHIHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTED 221

                         170
                  ....*....|...
gi 1207734383 160 QYHFCYDIVLEVL 172
Cdd:cd14597   222 QYIFCYQVILYVL 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 1-166 1.08e-64

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: 197.12  E-value: 1.08e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKW 80
Cdd:cd00047    33 MVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYGDITVTLVSEEELSDYTIRTLELSPKGCSESREVTHLHYTGW 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  81 PDHGTPASADSFIKYIRYARKS--HLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTK 158
Cdd:cd00047   113 PDHGVPSSPEDLLALVRRVRKEarKPNGPIVVHCSAGVGRTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTL 192


                  ....*...
gi 1207734383 159 EQYHFCYD 166
Cdd:cd00047   193 EQYEFIYE 200
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 1-166 3.26e-51

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: 163.19  E-value: 3.26e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPiSLKKPLELKHFRV-FLENYQI-LQYFIIRMFQVVeKSTGTSHSVKQLQFT 78
Cdd:cd18533    34 MIWQNNVGVIVMLTPLVENGREKCDQYWP-SGEYEGEYGDLTVeLVSEEENdDGGFIVREFELS-KEDGKVKKVYHIQYK 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  79 KWPDHGTPASADSFIKYIRYARK----SHLTGPMVVHCSAGIGRTGVFLCVDVVF---------CAIVKNCSFNIMDIVA 145
Cdd:cd18533   112 SWPDFGVPDSPEDLLTLIKLKRElndsASLDPPIIVHCSAGVGRTGTFIALDSLLdelkrglsdSQDLEDSEDPVYEIVN 191

                         170       180
                  ....*....|....*....|.
gi 1207734383 146 QMREQRSGMVQTKEQYHFCYD 166
Cdd:cd18533   192 QLRKQRMSMVQTLRQYIFLYD 212
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 1-163 4.58e-46

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: 150.58  E-value: 4.58e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISlKKPLELKHFRVFLENYQILQYFIIRMFQVveKSTGTSHSVKQLQFTKW 80
Cdd:cd14548    58 MVWEQNSHTIVMLTQCMEKGRVKCDHYWPFD-QDPVYYGDITVTMLSESVLPDWTIREFKL--ERGDEVRSVRQFHFTAW 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  81 PDHGTPASADSFIKYIRYARKS--HLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTK 158
Cdd:cd14548   135 PDHGVPEAPDSLLRFVRLVRDYikQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTE 214


                  ....*
gi 1207734383 159 EQYHF 163
Cdd:cd14548   215 AQYIF 219
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 1-165 6.59e-46

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: 150.75  E-value: 6.59e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPisLKKPLELKHFRVF-LENYQILQYfIIRMFQVVEKSTGTSHSVKQLQFTK 79
Cdd:cd14554    68 MLWEHNSTIIVMLTKLREMGREKCHQYWP--AERSARYQYFVVDpMAEYNMPQY-ILREFKVTDARDGQSRTVRQFQFTD 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  80 WPDHGTPASADSFIKYIRYARKSH----LTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMV 155
Cdd:cd14554   145 WPEQGVPKSGEGFIDFIGQVHKTKeqfgQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMV 224

                         170
                  ....*....|
gi 1207734383 156 QTKEQYHFCY 165
Cdd:cd14554   225 QTEDQYQFCY 234
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 1-165 4.41e-45

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: 148.31  E-value: 4.41e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKH--FRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFT 78
Cdd:cd14545    58 MVWEQNSKAVIMLNKLMEKGQIKCAQYWPQGEGNAMIFEDtgLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYT 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  79 KWPDHGTPASADSFIKYIRYARKSHL----TGPMVVHCSAGIGRTGVFLCVDVVFCAIVKN--CSFNIMDIVAQMREQRS 152
Cdd:cd14545   138 TWPDFGVPESPAAFLNFLQKVRESGSlssdVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGnpSSVDVKKVLLEMRKYRM 217

                         170
                  ....*....|...
gi 1207734383 153 GMVQTKEQYHFCY 165
Cdd:cd14545   218 GLIQTPDQLRFSY 230
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 1-170 1.07e-44

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: 147.54  E-value: 1.07e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHfrVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKW 80
Cdd:cd14553    65 MVWEQRSATIVMMTKLEERSRVKCDQYWPTRGTETYGLIQ--VTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAW 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  81 PDHGTPASADSFIKYIRYARKSHL--TGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTK 158
Cdd:cd14553   143 PDHGVPEHPTPFLAFLRRVKACNPpdAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTE 222

                         170
                  ....*....|..
gi 1207734383 159 EQYHFCYDIVLE 170
Cdd:cd14553   223 DQYIFIHDALLE 234
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 1-165 2.29e-44

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: 147.51  E-value: 2.29e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKW 80
Cdd:cd14543    91 MVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDESRQVTHFQFTSW 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  81 PDHGTPASADSFIKYIRYAR--------------KSHLTG-PMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVA 145
Cdd:cd14543   171 PDFGVPSSAAALLDFLGEVRqqqalavkamgdrwKGHPPGpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVR 250

                         170       180
                  ....*....|....*....|
gi 1207734383 146 QMREQRSGMVQTKEQYHFCY 165
Cdd:cd14543   251 RMRTQRAFSIQTPDQYYFCY 270
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 1-166 5.96e-44

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: 144.42  E-value: 5.96e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPisLKKPLELKHFRVFLENYQILQYFIIRMFQV------VEKSTGTSHSVKQ 74
Cdd:cd14549    33 MVWEQNSAIIVMITNLVERGRRKCDQYWP--KEGTETYGNIQVTLLSTEVLATYTVRTFSLknlklkKVKGRSSERVVYQ 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  75 LQFTKWPDHGTPASADSFIKYIR--YARKSHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRS 152
Cdd:cd14549   111 YHYTQWPDHGVPDYTLPVLSFVRksSAANPPGAGPIVVHCSAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRN 190

                         170
                  ....*....|....
gi 1207734383 153 GMVQTKEQYHFCYD 166
Cdd:cd14549   191 YLVQTEEQYIFIHD 204
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1-172 1.02e-43

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: 144.52  E-value: 1.02e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISLKK--PLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFT 78
Cdd:cd14540    35 MVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEhdALTFGEYKVSTKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYT 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  79 KWPDHGTPASADSFIKYIRYAR--KSHLTG---------PMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQM 147
Cdd:cd14540   115 DWPDHGCPEDVSGFLDFLEEINsvRRHTNQdvaghnrnpPTLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALL 194

                         170       180
                  ....*....|....*....|....*
gi 1207734383 148 REQRSGMVQTKEQYHFCYDIVLEVL 172
Cdd:cd14540   195 RHQRMLLVQTLAQYKFVYNVLIQYL 219
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1-171 1.52e-42

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3) and type 4 (PTPN4) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 and PTPN4 are large modular proteins containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses.


Pssm-ID: 350389 [Multi-domain]  Cd Length: 212  Bit Score: 141.31  E-value: 1.52e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPiSLKKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKW 80
Cdd:cd14541    38 MVWEQKSTLIVMLTTLVERGRVKCHQYWP-DLGETMQFGNLQITCVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAW 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  81 PDHGTPASADSFIKYIRYARKSHLTG--PMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTK 158
Cdd:cd14541   117 PDHGVPDDSSDFLDFVKRVRQNRVGMvePTVVHCSAGIGRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTP 196

                         170
                  ....*....|...
gi 1207734383 159 EQYHFCYDIVLEV 171
Cdd:cd14541   197 SQYRFVCEAILRV 209
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 1-172 1.49e-41

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: 141.02  E-value: 1.49e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPIslKKPLELKHFRVF-LENYQILQYfIIRMFQVVEKSTGTSHSVKQLQFTK 79
Cdd:cd14627   115 MLWENNSTIVVMLTKLREMGREKCHQYWPA--ERSARYQYFVVDpMAEYNMPQY-ILREFKVTDARDGQSRTVRQFQFTD 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  80 WPDHGTPASADSFIKYIRYARKSH----LTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMV 155
Cdd:cd14627   192 WPEQGVPKSGEGFIDFIGQVHKTKeqfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMV 271

                         170
                  ....*....|....*..
gi 1207734383 156 QTKEQYHFCYDIVLEVL 172
Cdd:cd14627   272 QTEDEYQFCYQAALEYL 288
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 1-165 2.02e-41

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: 137.94  E-value: 2.02e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQILQY-FIIRMFQVveKSTGTSHSVKQLQFTK 79
Cdd:cd14542    33 MIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLQFGPFKISLEKEKRVGPdFLIRTLKV--TFQKESRTVYQFHYTA 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  80 WPDHGTPASADSFIKYIRYARK--SHLTGPMVVHCSAGIGRTGVFLCVDVVFCAI---VKNCSFNIMDIVAQMREQRSGM 154
Cdd:cd14542   111 WPDHGVPSSVDPILDLVRLVRDyqGSEDVPICVHCSAGCGRTGTICAIDYVWNLLktgKIPEEFSLFDLVREMRKQRPAM 190

                         170
                  ....*....|.
gi 1207734383 155 VQTKEQYHFCY 165
Cdd:cd14542   191 VQTKEQYELVY 201
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 1-172 3.95e-41

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: 138.10  E-value: 3.95e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISlKKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKW 80
Cdd:cd14619    59 MIWEQQSSTIVMLTNCMEAGRVKCEHYWPLD-YTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAW 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  81 PDHGTPASADSFIKYIRYARK---SHL-TGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQ 156
Cdd:cd14619   138 PDHGVPSSTDTLLAFRRLLRQwldQTMsGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQ 217

                         170
                  ....*....|....*.
gi 1207734383 157 TKEQYHFCYDIVLEVL 172
Cdd:cd14619   218 TESQYVFLHQCILDFL 233
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 1-174 2.02e-40

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: 137.67  E-value: 2.02e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPiSLKKPLELKHFRVFL--ENYQILqyFIIRMFQVVEKSTGTSHSVKQLQFT 78
Cdd:cd14600   101 VVWEQKLSLIVMLTTLTERGRTKCHQYWP-DPPDVMEYGGFRVQChsEDCTIA--YVFREMLLTNTQTGEERTVTHLQYV 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  79 KWPDHGTPASADSFIKYIRYARKSHLTG-PMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQT 157
Cdd:cd14600   178 AWPDHGVPDDSSDFLEFVNYVRSKRVENePVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQT 257

                         170
                  ....*....|....*..
gi 1207734383 158 KEQYHFCYDIVLEVLRK 174
Cdd:cd14600   258 SSQYKFVCEAILRVYEE 274
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 1-166 6.22e-40

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: 134.43  E-value: 6.22e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKW 80
Cdd:cd14539    34 MVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQALVYGAITVSLQSVRTTPTHVERIISIQHKDTRLSRSVVHLQFTTW 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  81 PDHGTPASADSFIKYIR-----YARKSHLTGPMVVHCSAGIGRTGVFlCvdVVFCAIVK----NCSFNIMDIVAQMREQR 151
Cdd:cd14539   114 PELGLPDSPNPLLRFIEevhshYLQQRSLQTPIVVHCSSGVGRTGAF-C--LLYAAVQEieagNGIPDLPQLVRKMRQQR 190

                         170
                  ....*....|....*
gi 1207734383 152 SGMVQTKEQYHFCYD 166
Cdd:cd14539   191 KYMLQEKEHLKFCYE 205
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 1-172 1.75e-39

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


Pssm-ID: 350476 [Multi-domain]  Cd Length: 292  Bit Score: 135.63  E-value: 1.75e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPIslKKPLELKHFRVF-LENYQILQYfIIRMFQVVEKSTGTSHSVKQLQFTK 79
Cdd:cd14628   114 MLWEHNSTIVVMLTKLREMGREKCHQYWPA--ERSARYQYFVVDpMAEYNMPQY-ILREFKVTDARDGQSRTVRQFQFTD 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  80 WPDHGTPASADSFIKYIRYARKSH----LTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMV 155
Cdd:cd14628   191 WPEQGVPKSGEGFIDFIGQVHKTKeqfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMV 270

                         170
                  ....*....|....*..
gi 1207734383 156 QTKEQYHFCYDIVLEVL 172
Cdd:cd14628   271 QTEDQYQFCYRAALEYL 287
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 1-172 2.06e-39

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


Pssm-ID: 350477 [Multi-domain]  Cd Length: 291  Bit Score: 135.62  E-value: 2.06e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPIslKKPLELKHFRVF-LENYQILQYfIIRMFQVVEKSTGTSHSVKQLQFTK 79
Cdd:cd14629   115 MLWEHNSTIVVMLTKLREMGREKCHQYWPA--ERSARYQYFVVDpMAEYNMPQY-ILREFKVTDARDGQSRTIRQFQFTD 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  80 WPDHGTPASADSFIKYIRYARKSH----LTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMV 155
Cdd:cd14629   192 WPEQGVPKTGEGFIDFIGQVHKTKeqfgQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMV 271

                         170
                  ....*....|....*..
gi 1207734383 156 QTKEQYHFCYDIVLEVL 172
Cdd:cd14629   272 QTEDQYQLCYRAALEYL 288
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 1-171 1.14e-38

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: 133.03  E-value: 1.14e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPiSLKKPLELKHFRV-FLENYQILQYFIIRMFQVVEKSTgtSHSVKQLQFTK 79
Cdd:cd14603    92 MIWQYGVKVILMACREIEMGKKKCERYWA-QEQEPLQTGPFTItLVKEKRLNEEVILRTLKVTFQKE--SRSVSHFQYMA 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  80 WPDHGTPASADSFIKYIRYARKSHLTG--PMVVHCSAGIGRTGVFLCVDVVFCAIVKNC---SFNIMDIVAQMREQRSGM 154
Cdd:cd14603   169 WPDHGIPDSPDCMLAMIELARRLQGSGpePLCVHCSAGCGRTGVICTVDYVRQLLLTQRippDFSIFDVVLEMRKQRPAA 248

                         170
                  ....*....|....*..
gi 1207734383 155 VQTKEQYHFCYDIVLEV 171
Cdd:cd14603   249 VQTEEQYEFLYHTVAQM 265
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 1-163 1.48e-38

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: 131.36  E-value: 1.48e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIiKCYHYWPIslKKPLELKHFRVFLENYQILQYFIIRmfQVVEKSTGTSHSVKQLQFTKW 80
Cdd:cd14547    60 MVWQEKTPIIVMITNLTEAKE-KCAQYWPE--EENETYGDFEVTVQSVKETDGYTVR--KLTLKYGGEKRYLKHYWYTSW 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  81 PDHGTPASADSFIKYIR----YARKSHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQ 156
Cdd:cd14547   135 PDHKTPEAAQPLLSLVQeveeARQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQ 214


                  ....*..
gi 1207734383 157 TKEQYHF 163
Cdd:cd14547   215 TAEQYEF 221
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 1-165 2.82e-38

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: 131.43  E-value: 2.82e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPlELKHFRVFLENYQILQYFIIRMFQVVEKSTGTS-HSVKQLQFTK 79
Cdd:cd14544    71 MVWQENSRVIVMTTKEVERGKNKCVRYWPDEGMQK-QYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDPiREIWHYQYLS 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  80 WPDHGTPASAD---SFIKYIRYaRKSHL--TGPMVVHCSAGIGRTGVFLCVDVVFCAIVKN---CSFNIMDIVAQMREQR 151
Cdd:cd14544   150 WPDHGVPSDPGgvlNFLEDVNQ-RQESLphAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKgldCDIDIQKTIQMVRSQR 228

                         170
                  ....*....|....
gi 1207734383 152 SGMVQTKEQYHFCY 165
Cdd:cd14544   229 SGMVQTEAQYKFIY 242
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 1-170 3.80e-38

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: 129.65  E-value: 3.80e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISLKKpleLKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKW 80
Cdd:cd14555    33 MVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEV---YGDIKVTLVETEPLAEYVVRTFALERRGYHEIREVRQFHFTGW 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  81 PDHGTPASADSFIKYIRYARKSH--LTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTK 158
Cdd:cd14555   110 PDHGVPYHATGLLGFIRRVKASNppSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTE 189

                         170
                  ....*....|..
gi 1207734383 159 EQYHFCYDIVLE 170
Cdd:cd14555   190 EQYIFIHDAILE 201
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 1-174 1.10e-37

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: 128.91  E-value: 1.10e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPiSLKKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKW 80
Cdd:cd14601    38 MTWEQGSSMVVMLTTQVERGRVKCHQYWP-EPSGSSSYGGFQVTCHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAW 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  81 PDHGTPASADSFIKYIRYAR--KSHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTK 158
Cdd:cd14601   117 PDHGVPDDSSDFLDFVCLVRnkRAGKDEPVVVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTP 196

                         170
                  ....*....|....*.
gi 1207734383 159 EQYHFCYDIVLEVLRK 174
Cdd:cd14601   197 SQYRFVCEAILKVYEE 212
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 1-165 3.14e-37

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: 128.11  E-value: 3.14e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISlKKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHS-VKQLQFTK 79
Cdd:cd14617    59 MVWEQNVHNIVMVTQCVEKGRVKCDHYWPAD-QDSLYYGDLIVQMLSESVLPEWTIREFKICSEEQLDAPRlVRHFHYTV 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  80 WPDHGTPASADSFIKYIR----YARKSHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMV 155
Cdd:cd14617   138 WPDHGVPETTQSLIQFVRtvrdYINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMV 217

                         170
                  ....*....|
gi 1207734383 156 QTKEQYHFCY 165
Cdd:cd14617   218 QTECQYVYLH 227
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 1-165 1.04e-36

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: 127.44  E-value: 1.04e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWP--ISLKkplELKHFRVFLENYQILQYFIIRMFQVVEKSTG-TSHSVKQLQF 77
Cdd:cd14605    73 MVFQENSRVIVMTTKEVERGKSKCVKYWPdeYALK---EYGVMRVRNVKESAAHDYILRELKLSKVGQGnTERTVWQYHF 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  78 TKWPDHGTPASAD---SFIKYIRYARKSHL-TGPMVVHCSAGIGRTGVFLCVDVVFCAIVK---NCSFNIMDIVAQMREQ 150
Cdd:cd14605   150 RTWPDHGVPSDPGgvlDFLEEVHHKQESIMdAGPVVVHCSAGIGRTGTFIVIDILIDIIREkgvDCDIDVPKTIQMVRSQ 229

                         170
                  ....*....|....*
gi 1207734383 151 RSGMVQTKEQYHFCY 165
Cdd:cd14605   230 RSGMVQTEAQYRFIY 244
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 1-166 1.23e-36

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: 125.86  E-value: 1.23e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPisLKKPLELKHFRVFLENYQILQYFIIRMFQV--------VEKSTGTSHSV 72
Cdd:cd17668    33 MIWEHNVEVIVMITNLVEKGRRKCDQYWP--ADGSEEYGNFLVTQKSVQVLAYYTVRNFTLrntkikkgSQKGRPSGRVV 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  73 KQLQFTKWPDHGTPASADSFIKYIRYAR--KSHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQ 150
Cdd:cd17668   111 TQYHYTQWPDMGVPEYTLPVLTFVRKASyaKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQ 190

                         170
                  ....*....|....*.
gi 1207734383 151 RSGMVQTKEQYHFCYD 166
Cdd:cd17668   191 RNYLVQTEEQYVFIHD 206
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 1-163 3.22e-36

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: 125.70  E-value: 3.22e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISLKKplELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKW 80
Cdd:cd14615    58 MVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQKK--DYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSW 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  81 PDHGTPASADSFIKYiRYARKSHLT-----GPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMV 155
Cdd:cd14615   136 PDHGVPETTDLLINF-RHLVREYMKqnppnSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMV 214


                  ....*...
gi 1207734383 156 QTKEQYHF 163
Cdd:cd14615   215 QTEDQYVF 222
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 1-170 4.14e-36

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: 124.78  E-value: 4.14e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKhfrVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKW 80
Cdd:cd14632    33 MVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDTYGDIK---ITLLKTETLAEYSVRTFALERRGYSARHEVKQFHFTSW 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  81 PDHGTPASADSFIKYIRYARKSHL--TGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTK 158
Cdd:cd14632   110 PEHGVPYHATGLLAFIRRVKASTPpdAGPVVVHCSAGAGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTE 189

                         170
                  ....*....|..
gi 1207734383 159 EQYHFCYDIVLE 170
Cdd:cd14632   190 EQYIFIHDAILE 201
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 1-170 1.18e-35

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: 125.52  E-value: 1.18e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPL--ELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFT 78
Cdd:cd14608    83 MVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMifEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYT 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  79 KWPDHGTPASADSFIKYIRYARKSHLT----GPMVVHCSAGIGRTGVFLCVDVVFCAIVKN---CSFNIMDIVAQMREQR 151
Cdd:cd14608   163 TWPDFGVPESPASFLNFLFKVRESGSLspehGPVVVHCSAGIGRSGTFCLADTCLLLMDKRkdpSSVDIKKVLLEMRKFR 242

                         170
                  ....*....|....*....
gi 1207734383 152 SGMVQTKEQYHFCYDIVLE 170
Cdd:cd14608   243 MGLIQTADQLRFSYLAVIE 261
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 1-170 1.50e-35

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: 123.98  E-value: 1.50e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKhfrVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKW 80
Cdd:cd14630    65 MIWQENSASVVMVTNLVEVGRVKCVRYWPDDTEVYGDIK---VTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSW 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  81 PDHGTPASADSFIKYIRYAR--KSHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTK 158
Cdd:cd14630   142 PDHGVPCYATGLLGFVRQVKflNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTE 221

                         170
                  ....*....|..
gi 1207734383 159 EQYHFCYDIVLE 170
Cdd:cd14630   222 EQYVFVHDAILE 233
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 1-165 1.80e-35

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: 124.31  E-value: 1.80e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKH--FRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFT 78
Cdd:cd14607    82 MVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSFKEtgFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYT 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  79 KWPDHGTPASADSFIKYIRYARKSHL----TGPMVVHCSAGIGRTGVFLCVD--VVFCAIVKNCSFNIMDIVAQMREQRS 152
Cdd:cd14607   162 TWPDFGVPESPASFLNFLFKVRESGSlspeHGPAVVHCSAGIGRSGTFSLVDtcLVLMEKKDPDSVDIKQVLLDMRKYRM 241

                         170
                  ....*....|...
gi 1207734383 153 GMVQTKEQYHFCY 165
Cdd:cd14607   242 GLIQTPDQLRFSY 254
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 1-170 2.37e-35

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: 123.21  E-value: 2.37e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPislkKPLEL-KHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTK 79
Cdd:cd14631    47 MIWQEQSACIVMVTNLVEVGRVKCYKYWP----DDTEVyGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTG 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  80 WPDHGTPASADSFIKYIRYARKSH--LTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQT 157
Cdd:cd14631   123 WPDHGVPYHATGLLSFIRRVKLSNppSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQT 202

                         170
                  ....*....|...
gi 1207734383 158 KEQYHFCYDIVLE 170
Cdd:cd14631   203 EEQYIFIHDAILE 215
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
71-170 7.42e-35

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 118.23  E-value: 7.42e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   71 SVKQLQFTKWPDHGTPASADSFIKYIRYARKSH----LTGPMVVHCSAGIGRTGVFLCVDVVfCAIVKNCS--FNIMDIV 144
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLnqseSSGPVVVHCSAGVGRTGTFVAIDIL-LQQLEAEAgeVDIFDTV 79

                           90       100
                   ....*....|....*....|....*.
gi 1207734383  145 AQMREQRSGMVQTKEQYHFCYDIVLE 170
Cdd:smart00404  80 KELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 71-170 7.42e-35

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: 118.23  E-value: 7.42e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   71 SVKQLQFTKWPDHGTPASADSFIKYIRYARKSH----LTGPMVVHCSAGIGRTGVFLCVDVVfCAIVKNCS--FNIMDIV 144
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLnqseSSGPVVVHCSAGVGRTGTFVAIDIL-LQQLEAEAgeVDIFDTV 79

                           90       100
                   ....*....|....*....|....*.
gi 1207734383  145 AQMREQRSGMVQTKEQYHFCYDIVLE 170
Cdd:smart00012  80 KELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 1-172 7.93e-35

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: 123.28  E-value: 7.93e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPislKKPLELKHF-RVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTK 79
Cdd:cd14625   109 MVWEQRSATVVMMTKLEEKSRIKCDQYWP---SRGTETYGMiQVTLLDTIELATFCVRTFSLHKNGSSEKREVRQFQFTA 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  80 WPDHGTPASADSFIKYIRYARKSHL--TGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQT 157
Cdd:cd14625   186 WPDHGVPEYPTPFLAFLRRVKTCNPpdAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQT 265

                         170
                  ....*....|....*
gi 1207734383 158 KEQYHFCYDIVLEVL 172
Cdd:cd14625   266 EDQYSFIHDALLEAV 280
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 1-170 1.11e-34

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: 122.84  E-value: 1.11e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISLKKpleLKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKW 80
Cdd:cd14633   102 MVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEI---YKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGW 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  81 PDHGTPASADSFIKYIRY--ARKSHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTK 158
Cdd:cd14633   179 PDHGVPYHATGLLGFVRQvkSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTE 258

                         170
                  ....*....|..
gi 1207734383 159 EQYHFCYDIVLE 170
Cdd:cd14633   259 EQYVFIHDAILE 270
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 1-172 3.40e-34

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: 121.76  E-value: 3.40e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELkhFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKW 80
Cdd:cd14624   109 MIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTETYGL--IQVTLLDTVELATYCVRTFALYKNGSSEKREVRQFQFTAW 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  81 PDHGTPASADSFIKYIRYARKSHL--TGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTK 158
Cdd:cd14624   187 PDHGVPEHPTPFLAFLRRVKTCNPpdAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTE 266

                         170
                  ....*....|....
gi 1207734383 159 EQYHFCYDIVLEVL 172
Cdd:cd14624   267 DQYIFIHDALLEAV 280
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 1-165 5.35e-34

protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis thaliana protein tyrosine phosphatase 1 (AtPTP1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. AtPTP1 dephosphorylates and inhibits MAP kinase 6 (MPK6) in non-oxidative stress conditions. Together with MAP kinase phosphatase 1 (MKP1) it expresses salicylic acid (SA) and camalexin biosynthesis, and therefore, modulating defense response.


Pssm-ID: 350496 [Multi-domain]  Cd Length: 206  Bit Score: 119.11  E-value: 5.35e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEG-GIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFI-IRMFQVVE-KSTGTSHSVKQLQF 77
Cdd:cd17658    35 MVIQQRCPVIIMLTRLVDNySTAKCADYFPAEENESREFGRISVTNKKLKHSQHSItLRVLEVQYiESEEPPLSVLHIQY 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  78 TKWPDHGTPASADSFIKYIRyaRKSHL---TGPMVVHCSAGIGRTGVFLCVDVVFCAIVKN--CSFNIMDIVAQMREQRS 152
Cdd:cd17658   115 PEWPDHGVPKDTRSVRELLK--RLYGIppsAGPIVVHCSAGIGRTGAYCTIHNTIRRILEGdmSAVDLSKTVRKFRSQRI 192

                         170
                  ....*....|...
gi 1207734383 153 GMVQTKEQYHFCY 165
Cdd:cd17658   193 GMVQTQDQYIFCY 205
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 1-176 9.48e-34

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: 120.81  E-value: 9.48e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVveKSTGTSHSVKQLQFTKW 80
Cdd:cd14604   119 MIWEYNVAIIVMACREFEMGRKKCERYWPLYGEEPMTFGPFRISCEAEQARTDYFIRTLLL--EFQNETRRLYQFHYVNW 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  81 PDHGTPASADSFIKYIRYARK--SHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNC---SFNIMDIVAQMREQRSGMV 155
Cdd:cd14604   197 PDHDVPSSFDSILDMISLMRKyqEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKipeEFNVFNLIQEMRTQRHSAV 276

                         170       180
                  ....*....|....*....|.
gi 1207734383 156 QTKEQYHFCYDIVLEVLRKLL 176
Cdd:cd14604   277 QTKEQYELVHRAIAQLFEKQL 297
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 1-170 1.99e-33

PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type tyrosine-protein phosphatase N2 (PTPRN2 or R-PTP-N2), also called islet cell autoantigen-related protein (IAR), ICAAR, phogrin, or IA-2beta, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. It is mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells. It may function as a phosphatidylinositol phosphatase to regulate insulin secretion. It is also required for normal accumulation of the neurotransmitters norepinephrine, dopamine and serotonin in the brain.


Pssm-ID: 350458 [Multi-domain]  Cd Length: 283  Bit Score: 119.78  E-value: 1.99e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPislKKPLELKH-FRVFLENYQI-LQYFIIRMFQVVEKSTGTSHSVKQLQFT 78
Cdd:cd14610   107 MVWESGCVVIVMLTPLAENGVKQCYHYWP---DEGSNLYHiYEVNLVSEHIwCEDFLVRSFYLKNLQTNETRTVTQFHFL 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  79 KWPDHGTPASADSFIKYIRYARKSH--LTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNC-SFNIMDIVAQMREQRSGMV 155
Cdd:cd14610   184 SWNDQGVPASTRSLLDFRRKVNKCYrgRSCPIIVHCSDGAGRSGTYILIDMVLNKMAKGAkEIDIAATLEHLRDQRPGMV 263

                         170
                  ....*....|....*
gi 1207734383 156 QTKEQYHFCYDIVLE 170
Cdd:cd14610   264 QTKEQFEFALTAVAE 278
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 1-172 2.26e-33

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: 119.37  E-value: 2.26e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISLKKplELKHFRVFLENYQILQYFIIRMFQVVE-----------KSTGTS 69
Cdd:cd17667    91 MIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSE--EYGNIIVTLKSTKIHACYTVRRFSIRNtkvkkgqkgnpKGRQNE 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  70 HSVKQLQFTKWPDHGTPASADSFIKYIRY---ARKSHLtGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQ 146
Cdd:cd17667   169 RTVIQYHYTQWPDMGVPEYALPVLTFVRRssaARTPEM-GPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKH 247

                         170       180
                  ....*....|....*....|....*.
gi 1207734383 147 MREQRSGMVQTKEQYHFCYDIVLEVL 172
Cdd:cd17667   248 IRTQRNYLVQTEEQYIFIHDALLEAI 273
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 1-170 2.90e-33

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: 119.37  E-value: 2.90e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELkhFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKW 80
Cdd:cd14626   103 MVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTETYGM--IQVTLLDTVELATYSVRTFALYKNGSSEKREVRQFQFMAW 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  81 PDHGTPASADSFIKYIRYARKSHL--TGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTK 158
Cdd:cd14626   181 PDHGVPEYPTPILAFLRRVKACNPpdAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTE 260

                         170
                  ....*....|..
gi 1207734383 159 EQYHFCYDIVLE 170
Cdd:cd14626   261 DQYIFIHEALLE 272
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 1-171 3.61e-33

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: 117.63  E-value: 3.61e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVveKSTGTSHSVKQLQFTKW 80
Cdd:cd14602    60 MIWEYSVLIIVMACMEFEMGKKKCERYWAEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKV--KFNSETRTIYQFHYKNW 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  81 PDHGTPASADSFIKYIRYAR--KSHLTGPMVVHCSAGIGRTGVFLCVDVVFC----AIVKNCsFNIMDIVAQMREQRSGM 154
Cdd:cd14602   138 PDHDVPSSIDPILELIWDVRcyQEDDSVPICIHCSAGCGRTGVICAIDYTWMllkdGIIPEN-FSVFSLIQEMRTQRPSL 216

                         170
                  ....*....|....*..
gi 1207734383 155 VQTKEQYHFCYDIVLEV 171
Cdd:cd14602   217 VQTKEQYELVYNAVIEL 233
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 1-169 4.50e-33

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: 117.68  E-value: 4.50e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISlKKPLELKHFRVFLENYQILQYFIIRMFQVveKSTGTSHSVKQLQFTKW 80
Cdd:cd14614    74 MVLQQKSQIIVMLTQCNEKRRVKCDHYWPFT-EEPVAYGDITVEMLSEEEQPDWAIREFRV--SYADEVQDVMHFNYTAW 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  81 PDHGTPA--SADSFIKYIRYARKSHLT--GPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQ 156
Cdd:cd14614   151 PDHGVPTanAAESILQFVQMVRQQAVKskGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQ 230

                         170
                  ....*....|...
gi 1207734383 157 TKEQYHFCYDIVL 169
Cdd:cd14614   231 TEEQYIFIHQCVQ 243
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 1-170 5.61e-33

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: 116.39  E-value: 5.61e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPislKKPLELKH-FRVFLENYQIL-QYFIIRMFQVVEKSTGTSHSVKQLQFT 78
Cdd:cd14546    34 MIWEQGCVVIVMLTRLQENGVKQCARYWP---EEGSEVYHiYEVHLVSEHIWcDDYLVRSFYLKNLQTSETRTVTQFHFL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  79 KWPDHGTPASADSFIKYIRYARKSH--LTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKncSFNIMDIVA---QMREQRSG 153
Cdd:cd14546   111 SWPDEGIPASAKPLLEFRRKVNKSYrgRSCPIVVHCSDGAGRTGTYILIDMVLNRMAK--GAKEIDIAAtleHLRDQRPG 188

                         170
                  ....*....|....*..
gi 1207734383 154 MVQTKEQYHFCYDIVLE 170
Cdd:cd14546   189 MVKTKDQFEFVLTAVAE 205
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 1-168 9.62e-33

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: 115.83  E-value: 9.62e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPIslKKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKW 80
Cdd:cd14552    33 MIWEWKSCSIVMLTEIKERSQNKCAQYWPE--DGSVSSGDITVELKDQTDYEDYTLRDFLVTKGKGGSTRTVRQFHFHGW 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  81 PDHGTPASADSFIKYIRYARKSHL---TGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQT 157
Cdd:cd14552   111 PEVGIPDNGKGMIDLIAAVQKQQQqsgNHPITVHCSAGAGRTGTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQT 190

                         170
                  ....*....|.
gi 1207734383 158 KEQYHFCYDIV 168
Cdd:cd14552   191 LEQYEFCYKVV 201
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 1-170 1.18e-32

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: 116.19  E-value: 1.18e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPIslKKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHS---VKQLQF 77
Cdd:cd14620    57 MVWEQKSATIVMLTNLKERKEEKCYQYWPD--QGCWTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDGCKAprlVTQLHF 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  78 TKWPDHG---TPASADSFIKYIRYARKSHlTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGM 154
Cdd:cd14620   135 TSWPDFGvpfTPIGMLKFLKKVKSVNPVH-AGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQM 213

                         170
                  ....*....|....*.
gi 1207734383 155 VQTKEQYHFCYDIVLE 170
Cdd:cd14620   214 VQTDMQYSFIYQALLE 229
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 1-165 2.66e-32

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: 116.09  E-value: 2.66e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIiKCYHYWPislKKPLELKHFRVFLENYQILQYFIIRmfQVVEKSTGTSHSVKQLQFTKW 80
Cdd:cd14612    79 MVWQEECPIIVMITKLKEKKE-KCVHYWP---EKEGTYGRFEIRVQDMKECDGYTIR--DLTIQLEEESRSVKHYWFSSW 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  81 PDHGTPASADSFIKYIRYARKSHLT----GPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQ 156
Cdd:cd14612   153 PDHQTPESAGPLLRLVAEVEESRQTaaspGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQ 232


                  ....*....
gi 1207734383 157 TKEQYHFCY 165
Cdd:cd14612   233 TSEQYQFLH 241
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 1-161 7.63e-32

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: 113.38  E-value: 7.63e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVV-EKSTGTSHSVKQLQFTK 79
Cdd:cd14557    33 MIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKINEEKICPDYIIRKLNINnKKEKGSGREVTHIQFTS 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  80 WPDHGTPASADSFIKYIRY--ARKSHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQT 157
Cdd:cd14557   113 WPDHGVPEDPHLLLKLRRRvnAFNNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQV 192


                  ....
gi 1207734383 158 KEQY 161
Cdd:cd14557   193 EAQY 196
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 1-173 1.05e-31

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: 115.48  E-value: 1.05e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPislkkPLELKHFRVFLENYQILQYF-------IIRMFQVVEKSTGTSHSVK 73
Cdd:cd14599   101 MVWEQGVNVIAMVTAEEEGGRSKSHRYWP-----KLGSKHSSATYGKFKVTTKFrtdsgcyATTGLKVKHLLSGQERTVW 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  74 QLQFTKWPDHGTPASADSFIKY---IRYARK---------SHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIM 141
Cdd:cd14599   176 HLQYTDWPDHGCPEEVQGFLSYleeIQSVRRhtnsmldstKNCNPPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVP 255

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1207734383 142 DIVAQMREQRSGMVQTKEQYHFCYDIVLEVLR 173
Cdd:cd14599   256 VMLRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 1-169 3.14e-31

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: 112.73  E-value: 3.14e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISLKkPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKW 80
Cdd:cd14618    59 LVWEQQVCNIIMLTVGMENGRVLCDHYWPSEST-PVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAW 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  81 PDHGTPASADSFIKYIRYARK----SHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQ 156
Cdd:cd14618   138 PDHGIPESTSSLMAFRELVREhvqaTKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQ 217

                         170
                  ....*....|...
gi 1207734383 157 TKEQYHFCYDIVL 169
Cdd:cd14618   218 TLSQYIFLHSCIL 230
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 1-170 5.12e-31

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: 113.05  E-value: 5.12e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPiSLKKPLELKHFRVFLENYQILQYFIIRMFQV-VEKSTGTSHSVKQLQFTK 79
Cdd:cd14606    86 MAWQENSRVIVMTTREVEKGRNKCVPYWP-EVGMQRAYGPYSVTNCGEHDTTEYKLRTLQVsPLDNGELIREIWHYQYLS 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  80 WPDHGTPASAD---SFIKYIRYARKS-HLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVK---NCSFNIMDIVAQMREQRS 152
Cdd:cd14606   165 WPDHGVPSEPGgvlSFLDQINQRQESlPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTkglDCDIDIQKTIQMVRAQRS 244

                         170
                  ....*....|....*...
gi 1207734383 153 GMVQTKEQYHFCYDIVLE 170
Cdd:cd14606   245 GMVQTEAQYKFIYVAIAQ 262
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 1-165 1.14e-30

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: 111.16  E-value: 1.14e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIiKCYHYWPislKKPLELKHFRVFLENYQILQYFIIRmfQVVEKSTGTSHSVKQLQFTKW 80
Cdd:cd14611    63 MVWQEDSPVIVMITKLKEKNE-KCVLYWP---EKRGIYGKVEVLVNSVKECDNYTIR--NLTLKQGSQSRSVKHYWYTSW 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  81 PDHGTPASADSFIKY---IRYARKSHLT-GPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQ 156
Cdd:cd14611   137 PDHKTPDSAQPLLQLmldVEEDRLASPGrGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQ 216


                  ....*....
gi 1207734383 157 TKEQYHFCY 165
Cdd:cd14611   217 TSEQYEFVH 225
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 1-163 3.81e-30

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: 109.61  E-value: 3.81e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISlKKPLElkhfrVF--------LENYQIlqYFIIRMFQVvEKStGTSHSV 72
Cdd:cd14616    59 MVWETRAKTIVMLTQCFEKGRIRCHQYWPED-NKPVT-----VFgdivitklMEDVQI--DWTIRDLKI-ERH-GDYMMV 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  73 KQLQFTKWPDHGTPASADSFIKYIRYAR--KSHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQ 150
Cdd:cd14616   129 RQCNFTSWPEHGVPESSAPLIHFVKLVRasRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSE 208

                         170
                  ....*....|...
gi 1207734383 151 RSGMVQTKEQYHF 163
Cdd:cd14616   209 RMCMVQNLAQYIF 221
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 1-173 4.36e-30

catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21), also called protein-tyrosine phosphatase D1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN21 is a component of a multivalent scaffold complex nucleated by focal adhesion kinase (FAK) at specific intracellular sites. It promotes cytoskeleton events that induce cell adhesion and migration by modulating Src-FAK signaling. It can also selectively associate with and stimulate Tec family kinases and modulate Stat3 activation. Human PTPN21 may also play a pathologic role in gastrointestinal tract tumorigenesis. PTPN21 contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350446 [Multi-domain]  Cd Length: 220  Bit Score: 109.68  E-value: 4.36e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPislkkPLELKHFRVFLENYQILQYF-------IIRMFQVVEKSTGTSHSVK 73
Cdd:cd14598    35 MVWEQGVAIIAMVTAEEEGGREKSFRYWP-----RLGSRHNTVTYGRFKITTRFrtdsgcyATTGLKIKHLLTGQERTVW 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  74 QLQFTKWPDHGTPASADSFIKY---IRYARKsHLTG---------PMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIM 141
Cdd:cd14598   110 HLQYTDWPEHGCPEDLKGFLSYleeIQSVRR-HTNStidpkspnpPVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIP 188

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1207734383 142 DIVAQMREQRSGMVQTKEQYHFCYDIVLEVLR 173
Cdd:cd14598   189 RVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 1-165 8.75e-30

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: 108.08  E-value: 8.75e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISLKKplELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHS----VKQLQ 76
Cdd:cd14551    33 MIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCW--TYGNLRVRVEDTVVLVDYTTRKFCIQKVNRGIGEKrvrlVTQFH 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  77 FTKWPDHGTPASADSFIKYIRYArKSHLT---GPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSG 153
Cdd:cd14551   111 FTSWPDFGVPFTPIGMLKFLKKV-KSANPpraGPIVVHCSAGVGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQ 189

                         170
                  ....*....|..
gi 1207734383 154 MVQTKEQYHFCY 165
Cdd:cd14551   190 MVQTDMQYVFIY 201
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 1-166 7.82e-29

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: 105.55  E-value: 7.82e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKhfrVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKW 80
Cdd:cd14558    33 MIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKTYGDIE---VELKDTEKSPTYTVRVFEITHLKRKDSRTVYQYQYHKW 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  81 PDHGTPASADSFIKYIRYAR--------KSHLTGPMVVHCSAGIGRTGVFlcvdvvfCAIvkncsFNIMD---------- 142
Cdd:cd14558   110 KGEELPEKPKDLVDMIKSIKqklpyknsKHGRSVPIVVHCSDGSSRTGIF-------CAL-----WNLLEsaetekvvdv 177

                         170       180
                  ....*....|....*....|....*.
gi 1207734383 143 --IVAQMREQRSGMVQTKEQYHFCYD 166
Cdd:cd14558   178 fqVVKALRKQRPGMVSTLEQYQFLYD 203
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 1-170 1.39e-28

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: 107.05  E-value: 1.39e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPislKKPLELKH-FRVFLENYQI-LQYFIIRMFQVVEKSTGTSHSVKQLQFT 78
Cdd:cd14609   105 MVWENGCTVIVMLTPLVEDGVKQCDRYWP---DEGSSLYHiYEVNLVSEHIwCEDFLVRSFYLKNVQTQETRTLTQFHFL 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  79 KWPDHGTPASADSFIKYIRYARKSHL--TGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNC-SFNIMDIVAQMREQRSGMV 155
Cdd:cd14609   182 SWPAEGIPSSTRPLLDFRRKVNKCYRgrSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGVkEIDIAATLEHVRDQRPGMV 261

                         170
                  ....*....|....*
gi 1207734383 156 QTKEQYHFCYDIVLE 170
Cdd:cd14609   262 RTKDQFEFALTAVAE 276
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 1-179 1.64e-28

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 107.39  E-value: 1.64e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMIT-REIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTK 79
Cdd:PHA02747  112 AVWQEHCSIIVMLTpTKGTNGEEKCYQYWCLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKISHFQCSE 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  80 WPDHGTPASADSFIKYIR------------YARKSHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQM 147
Cdd:PHA02747  192 WFEDETPSDHPDFIKFIKiidinrkksgklFNPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKI 271

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1207734383 148 REQRSGMVQTKEQYHF---CYDIVLEVLRKLLTLD 179
Cdd:PHA02747  272 REQRHAGIMNFDDYLFiqpGYEVLHYFLSKIKAID 306
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 1-168 6.66e-28

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: 103.55  E-value: 6.66e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPIslKKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKW 80
Cdd:cd14622    34 MVWEWKCHTIVMLTELQEREQEKCVQYWPS--EGSVTHGEITIEIKNDTLLETISIRDFLVTYNQEKQTRLVRQFHFHGW 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  81 PDHGTPASADSFIKYIRYARKSHL-TG--PMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQT 157
Cdd:cd14622   112 PEIGIPAEGKGMIDLIAAVQKQQQqTGnhPIVVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQT 191

                         170
                  ....*....|.
gi 1207734383 158 KEQYHFCYDIV 168
Cdd:cd14622   192 LEQYEFCYRVV 202
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 1-170 2.76e-27

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 104.31  E-value: 2.76e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKW 80
Cdd:PHA02742  112 AIFQDQVRVIVMITKIMEDGKEACYPYWMPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFAYEDW 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  81 PDHGTPASADSFIKYIRYARKSHLTG-------------PMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQM 147
Cdd:PHA02742  192 PHGGLPRDPNKFLDFVLAVREADLKAdvdikgenivkepPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDL 271

                         170       180
                  ....*....|....*....|...
gi 1207734383 148 REQRSGMVQTKEQYHFCYDIVLE 170
Cdd:PHA02742  272 RKQRHNCLSLPQQYIFCYFIVLI 294
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
1-177 3.81e-27

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 103.25  E-value: 3.81e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGG--IIKCYHYWPIS---LKKPLELKHfrvfLENYQILQYFIIRMFQVVEKSTG-TSHSVKQ 74
Cdd:COG5599    96 MLFDNNTPVLVVLASDDEISkpKVKMPVYFRQDgeyGKYEVSSEL----TESIQLRDGIEARTYVLTIKGTGqKKIEIPV 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  75 LQFTKWPDHGTPaSADSFIKYIRYARKSHLT-----GPMVVHCSAGIGRTGVFLCVDVVFCAI--VKNCSFNIMDIVAQM 147
Cdd:COG5599   172 LHVKNWPDHGAI-SAEALKNLADLIDKKEKIkdpdkLLPVVHCRAGVGRTGTLIACLALSKSInaLVQITLSVEEIVIDM 250

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1207734383 148 REQR-SGMVQTKEQYHFCYDIVLEVLRKLLT 177
Cdd:COG5599   251 RTSRnGGMVQTSEQLDVLVKLAEQQIRPLLR 281
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 1-170 5.57e-27

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: 103.18  E-value: 5.57e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPIslKKPLELKHFRVFLENYQILQYFIIRMF--QVVEKSTGTSHS--VKQLQ 76
Cdd:cd14621   114 MIWEQNTATIVMVTNLKERKECKCAQYWPD--QGCWTYGNIRVSVEDVTVLVDYTVRKFciQQVGDVTNKKPQrlITQFH 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  77 FTKWPDHGTPASADSFIKYIRYARKSH--LTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGM 154
Cdd:cd14621   192 FTSWPDFGVPFTPIGMLKFLKKVKNCNpqYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQM 271

                         170
                  ....*....|....*.
gi 1207734383 155 VQTKEQYHFCYDIVLE 170
Cdd:cd14621   272 VQTDMQYVFIYQALLE 287
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 1-170 2.60e-26

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: 99.73  E-value: 2.60e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISlkKPLELKHFRVFLENYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKW 80
Cdd:cd14623    58 MIWEWKSCSIVMLTELEERGQEKCAQYWPSD--GSVSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGW 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  81 PDHGTPASADSFIKYIRYARKSHLTG---PMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQT 157
Cdd:cd14623   136 PEVGIPSDGKGMINIIAAVQKQQQQSgnhPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQT 215

                         170
                  ....*....|...
gi 1207734383 158 KEQYHFCYDIVLE 170
Cdd:cd14623   216 LEQYEFCYKVVQE 228
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 1-168 5.56e-25

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: 97.24  E-value: 5.56e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITrEIEGGIIKCYHYWP----------ISLKKPLELKHFRvflenyqilqyfiIRMFQVveKSTGTSH 70
Cdd:cd14613    89 MVWQERSPIIVMIT-NIEEMNEKCTEYWPeeqvtyegieITVKQVIHADDYR-------------LRLITL--KSGGEER 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  71 SVKQLQFTKWPDHGTPASADSFIKYIR-------YARKSHltGPMVVHCSAGIGRTGVFLCVDVVfCAIVKNCS-FNIMD 142
Cdd:cd14613   153 GLKHYWYTSWPDQKTPDNAPPLLQLVQeveearqQAEPNC--GPVIVHCSAGIGRTGCFIATSIC-CKQLRNEGvVDILR 229

                         170       180
                  ....*....|....*....|....*.
gi 1207734383 143 IVAQMREQRSGMVQTKEQYHFCYDIV 168
Cdd:cd14613   230 TTCQLRLDRGGMIQTCEQYQFVHHVL 255
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 1-172 2.36e-24

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 96.64  E-value: 2.36e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITrEIEGGIIKCYHYWpiSLKKPLELKHFRVFLENYQILQ--YFIIRMFQVVEKSTGTSHSVKQLQFT 78
Cdd:PHA02746  132 LISEHESQVIVSLT-DIDDDDEKCFELW--TKEEDSELAFGRFVAKILDIIEelSFTKTRLMITDKISDTSREIHHFWFP 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  79 KWPDHGTPASADSFIKYIRYARK------------SHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQ 146
Cdd:PHA02746  209 DWPDNGIPTGMAEFLELINKVNEeqaelikqadndPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLK 288

                         170       180
                  ....*....|....*....|....*.
gi 1207734383 147 MREQRSGMVQTKEQYHFCYDIVLEVL 172
Cdd:PHA02746  289 IRKQRHSSVFLPEQYAFCYKALKYAI 314
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 1-166 1.06e-23

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: 92.47  E-value: 1.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITrEIEGGIIKCYHYWPIslKKPLELKHFRVFLENYQILQYFIIRMFQVVE--KSTGTSHSVKQLQFT 78
Cdd:cd14556    33 LVYDYGCTSIVMLN-QLDPKDQSCPQYWPD--EGSGTYGPIQVEFVSTTIDEDVISRIFRLQNttRPQEGYRMVQQFQFL 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  79 KWPDHG-TPASADSFIKYIRYARK---SHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGM 154
Cdd:cd14556   110 GWPRDRdTPPSKRALLKLLSEVEKwqeQSGEGPIVVHCLNGVGRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNM 189

                         170
                  ....*....|..
gi 1207734383 155 VQTKEQYHFCYD 166
Cdd:cd14556   190 VETEEQYKFCYD 201
PHA02738 PHA02738
hypothetical protein; Provisional
 1-168 6.41e-22

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 89.98  E-value: 6.41e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYHYWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVVEkSTGTSHSVKQLQFTKW 80
Cdd:PHA02738  109 MLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGSIRFGKFKITTTQVETHPHYVKSTLLLTD-GTSATQTVTHFNFTAW 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  81 PDHGTPASADSFIKYIRYAR---------------KSHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVA 145
Cdd:PHA02738  188 PDHDVPKNTSEFLNFVLEVRqcqkelaqeslqighNRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVS 267

                         170       180
                  ....*....|....*....|...
gi 1207734383 146 QMREQRSGMVQTKEQYHFCYDIV 168
Cdd:PHA02738  268 SIRNQRYYSLFIPFQYFFCYRAV 290
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 1-170 2.43e-17

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: 75.83  E-value: 2.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITrEIEGGIIkCYHYWPisLKKPLELKHFRVFLENYQILQYFIIRMFQV--VEKSTGTSHSVKQLQFT 78
Cdd:cd14634    33 LVFDYNCSSVVMLN-EMDAAQL-CMQYWP--EKTSCCYGPIQVEFVSADIDEDIISRIFRIcnMARPQDGYRIVQHLQYI 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  79 KWPDH-GTPASADSFIKYIRYARKSHLT-----GPMVVHCSAGIGRTGVFlcvdvvfCAIVKNCSF----NIMDI---VA 145
Cdd:cd14634   109 GWPAYrDTPPSKRSILKVVRRLEKWQEQydgreGRTVVHCLNGGGRSGTF-------CAICSVCEMiqqqNIIDVfhtVK 181

                         170       180
                  ....*....|....*....|....*
gi 1207734383 146 QMREQRSGMVQTKEQYHFCYDIVLE 170
Cdd:cd14634   182 TLRNNKSNMVETLEQYKFVYEVALE 206
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 24-170 2.43e-16

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: 73.18  E-value: 2.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  24 CYHYWP---ISLKKPLELKHFRVFLENYQILQYFiiRMFQVVEKSTGTsHSVKQLQFTKWPDH-GTPASADSFIKYIRYA 99
Cdd:cd14635    54 CPQYWPengVHRHGPIQVEFVSADLEEDIISRIF--RIYNAARPQDGY-RMVQQFQFLGWPMYrDTPVSKRSFLKLIRQV 130

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207734383 100 RKSHLT-----GPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 170
Cdd:cd14635   131 DKWQEEynggeGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 24-170 1.54e-15

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: 71.09  E-value: 1.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  24 CYHYWP---ISLKKPLELKHFRVFLEnyqilQYFIIRMFQV--VEKSTGTSHSVKQLQFTKW-PDHGTPASADSFIKYI- 96
Cdd:cd14637    57 CLQYWPepgLQQYGPMEVEFVSGSAD-----EDIVTRLFRVqnITRLQEGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLa 131

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207734383  97 ---RYARKSHlTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYDIVLE 170
Cdd:cd14637   132 sveKWQRESG-EGRTVVHCLNGGGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 72-170 2.50e-15

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: 70.44  E-value: 2.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  72 VKQLQFTKWPDH-GTPASADSFIKYIRYARK-----SHLTGPMVVHCSAGIGRTGVFLCVDVVfCAIVKNCsfNIMDI-- 143
Cdd:cd14636   102 VQQFQYLGWASHrEVPGSKRSFLKLILQVEKwqeecDEGEGRTIIHCLNGGGRSGMFCAISIV-CEMIKRQ--NVVDVfh 178

                          90       100
                  ....*....|....*....|....*...
gi 1207734383 144 -VAQMREQRSGMVQTKEQYHFCYDIVLE 170
Cdd:cd14636   179 aVKTLRNSKPNMVETPEQYRFCYDVALE 206
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 47-161 1.15e-14

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


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 68.97  E-value: 1.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  47 NYQILQYFIIRMFQVVEKSTGTSHSVKQLQFTKWPDHgTPASADSFIK---YIRYARKSHLTGPM--------------- 108
Cdd:cd14559    93 KDELVDGLKADMYNLKITDGNKTITIPVVHVTNWPDH-TAISSEGLKEladLVNKSAEEKRNFYKskgssaindknkllp 171

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1207734383 109 VVHCSAGIGRTGVFLCvdvVFCAIVKNCSFNIMDIVAQMREQRSG-MVQTKEQY 161
Cdd:cd14559   172 VIHCRAGVGRTGQLAA---AMELNKSPNNLSVEDIVSDMRTSRNGkMVQKDEQL 222
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
80-163 9.42e-11

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 56.90  E-value: 9.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  80 WPDHGTP--ASADSFIKYIRYARKSHltGPMVVHCSAGIGRTGVFL-CVdvvfcAIVKNCSFNimDIVAQMREQRSGMVQ 156
Cdd:COG2453    55 IPDFGAPddEQLQEAVDFIDEALREG--KKVLVHCRGGIGRTGTVAaAY-----LVLLGLSAE--EALARVRAARPGAVE 125


                  ....*..
gi 1207734383 157 TKEQYHF 163
Cdd:COG2453   126 TPAQRAF 132
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 1-168 2.57e-10

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 57.67  E-value: 2.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGgiiKCYH-YWPISLKKPLELKHFRVFLENYQILQYFIIRMFQVVEKStGTSHSVKQLQFTK 79
Cdd:PHA02740  110 ALSDNKVQIIVLISRHADK---KCFNqFWSLKEGCVITSDKFQIETLEIIIKPHFNLTLLSLTDKF-GQAQKISHFQYTA 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  80 WPDHGTPASADSFIKY----------IRYARKSHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMRE 149
Cdd:PHA02740  186 WPADGFSHDPDAFIDFfcniddlcadLEKHKADGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQ 265

                         170
                  ....*....|....*....
gi 1207734383 150 QRSGMVQTKEQYHFCYDIV 168
Cdd:PHA02740  266 KKYGCMNCLDDYVFCYHLI 284
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 1-165 1.08e-09

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: 55.02  E-value: 1.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGiiKCYHYWPISlKKPLELKHFRVFL----------ENYQILQYFIIRMFQ---VVEkstg 67
Cdd:cd14550    33 MIWDHNSQTIVMLTDNELNE--DEPIYWPTK-EKPLECETFKVTLsgedhsclsnEIRLIVRDFILESTQddyVLE---- 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  68 tshsVKQLQFTKWPDHGTPASadSFIKYIRYARKSHLT--GPMVVH-----CSAGigrtgvflcvdvVFCAI------VK 134
Cdd:cd14550   106 ----VRQFQCPSWPNPCSPIH--TVFELINTVQEWAQQrdGPIVVHdryggVQAA------------TFCALttlhqqLE 167

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1207734383 135 NCsfNIMDI--VAQMREQ-RSGMVQTKEQYHFCY 165
Cdd:cd14550   168 HE--SSVDVyqVAKLYHLmRPGVFTSKEDYQFLY 199
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 1-169 1.82e-09

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: 54.61  E-value: 1.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITREIEGGIIKCYhYWPiSLKKPLELKHFRVFL----------ENYQILQYFIIRMFQ---VVEkstg 67
Cdd:cd17669    33 MIWDHNAQLIVMLPDGQNMAEDEFV-YWP-NKDEPINCETFKVTLiaeehkclsnEEKLIIQDFILEATQddyVLE---- 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  68 tshsVKQLQFTKWPDHGTPASADSFIKYIRYARKSHLTGPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQM 147
Cdd:cd17669   107 ----VRHFQCPKWPNPDSPISKTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMI 182

                         170       180
                  ....*....|....*....|..
gi 1207734383 148 REQRSGMVQTKEQYHFCYDIVL 169
Cdd:cd17669   183 NLMRPGVFTDIEQYQFLYKAIL 204
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 90-163 1.07e-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: 51.51  E-value: 1.07e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207734383  90 DSFIKYIRYARKSHLtgPMVVHCSAGIGRTGVFLCvdvvfCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHF 163
Cdd:cd14504    69 DEFLDIVEEANAKNE--AVLVHCLAGKGRTGTMLA-----CYLVKTGKISAVDAINEIRRIRPGSIETSEQEKF 135
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 106-166 4.61e-08

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


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 48.89  E-value: 4.61e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207734383 106 GPMVVHCSAGIGRTGVFLCvdvvfCAIVKNCSFNIMDIVAQMREQR-SGMVQTKEQYHFCYD 166
Cdd:cd14494    57 EPVLVHCKAGVGRTGTLVA-----CYLVLLGGMSAEEAVRIVRLIRpGGIPQTIEQLDFLIK 113
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 1-169 1.65e-07

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: 49.29  E-value: 1.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383   1 MVLENNSNVIAMITrEIEGGIIKCYHYWPiSLKKPLELKHFRVFLENYQIL-----QYFIIRMFQVVEKSTGTSHSVKQL 75
Cdd:cd17670    33 MIWDHNAQIIVMLP-DNQGLAEDEFVYWP-SREESMNCEAFTVTLISKDRLclsneEQIIIHDFILEATQDDYVLEVRHF 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  76 QFTKWPDHGTPASadSFIKYIRYARKSHLT--GPMVVHCSAGIGRTGVFLCVDVVFCAIVKNCSFNIMDIVAQMREQRSG 153
Cdd:cd17670   111 QCPKWPNPDAPIS--STFELINVIKEEALTrdGPTIVHDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPG 188

                         170
                  ....*....|....*.
gi 1207734383 154 MVQTKEQYHFCYDIVL 169
Cdd:cd17670   189 VFTDIEQYQFLYKAML 204
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 74-163 6.04e-06

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 44.24  E-value: 6.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  74 QLQFTKWP--DHGTPASA--DSFIKYIR--YARKSHLTGPMVVHCSAGIGRTGVFLCVdvvfcAIVKNCSFNIMDIVAQM 147
Cdd:PTZ00242   61 GIEVHDWPfdDGAPPPKAviDNWLRLLDqeFAKQSTPPETIAVHCVAGLGRAPILVAL-----ALVEYGGMEPLDAVGFV 135

                          90
                  ....*....|....*.
gi 1207734383 148 REQRSGMVQTKeQYHF 163
Cdd:PTZ00242  136 REKRKGAINQT-QLQF 150
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 80-160 1.95e-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: 43.11  E-value: 1.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  80 WPDHGTPASAD--SFIKYIRYARKshLTGPMVVHCSAGIGRTGVflcvdVVFCAIVKNCSFNIMDIVAQMREQRSGMVQT 157
Cdd:cd14506    84 WKDYGVPSLTTilDIVKVMAFALQ--EGGKVAVHCHAGLGRTGV-----LIACYLVYALRMSADQAIRLVRSKRPNSIQT 156


                  ...
gi 1207734383 158 KEQ 160
Cdd:cd14506   157 RGQ 159
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 109-166 7.20e-05

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


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 41.09  E-value: 7.20e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1207734383 109 VVHCSAGIGRTGVFL-CVdvvfcAIVKNCSFNIMDIVAQMREQRSGMVQTKEQYHFCYD 166
Cdd:cd14505   110 LIHCKGGLGRTGLIAaCL-----LLELGDTLDPEQAIAAVRALRPGAIQTPKQENFLHQ 163
PTPLP-like cd14495
Protein tyrosine phosphatase-like domains of phytases and similar domains; This subfamily ...
 79-149 5.45e-03

Protein tyrosine phosphatase-like domains of phytases and similar domains; This subfamily contains the tandem protein tyrosine phosphatase (PTP)-like domains of protein tyrosine phosphatase-like phytases (PTPLPs) and similar domains including the PTP domain of Pseudomonas syringae tyrosine-protein phosphatase hopPtoD2. PTPLPs, also known as cysteine phytases, are one of four known classes of phytases, enzymes that degrade phytate (inositol hexakisphosphate [InsP(6)]) to less-phosphorylated myo-inositol derivatives. Phytate is the most abundant cellular inositol phosphate and plays important roles in a broad scope of cellular processes, including DNA repair, RNA processing and export, development, apoptosis, and pathogenicity. PTPLPs adopt a PTP fold, including the active-site signature sequence (CX5R(S/T)) and utilize a classical PTP reaction mechanism. However, these enzymes display no catalytic activity against classical PTP substrates due to several unique structural features that confer specificity for myo-inositol polyphosphates.


Pssm-ID: 350345  Cd Length: 278  Bit Score: 36.20  E-value: 5.45e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207734383  79 KWPDhgtPASADSFIKYIRYARKShltGPMVVHCSAGIGRTGVFLcvdvVFCAIVKN---CSFNimDIVAQMRE 149
Cdd:cd14495   166 VWPD---DEEIDAFVAFYRSLPAD---AWLHFHCRAGKGRTTTFM----VMYDMLKNpkdVSFD--DIIARQYL 227
PTP-IVa1 cd18537
protein tyrosine phosphatase type IVA 1; Protein tyrosine phosphatase type IVA 1 (PTP-IVa1), ...
 44-159 7.37e-03

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


Pssm-ID: 350513 [Multi-domain]  Cd Length: 167  Bit Score: 35.43  E-value: 7.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207734383  44 FLEnyQILQYFIIRMFQVVEKSTGTSHSVKQ-LQFTKWP-DHGTPAS---ADSFIKYIRYARKSHLTGPMVVHCSAGIGR 118
Cdd:cd18537    33 FIE--ELKKYGVTTVVRVCEATYDTTLVEKEgIQVLDWPfDDGAPPSnqiVDDWLNLLKVKFREEPGCCIAVHCVAGLGR 110

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1207734383 119 TGVFLCVDVVfcaivkNCSFNIMDIVAQMREQRSGMVQTKE 159
Cdd:cd18537   111 APVLVALALI------ECGMKYEDAVQFIRQKRRGAFNSKQ 145
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 106-163 8.48e-03

C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division control protein 14 (CDC14) family is highly conserved in all eukaryotes, although the roles of its members seem to have diverged during evolution. Yeast Cdc14, the best characterized member of this family, is a dual-specificity phosphatase that plays key roles in cell cycle control. It preferentially dephosphorylates cyclin-dependent kinase (CDK) targets, which makes it the main antagonist of CDK in the cell. Cdc14 functions at the end of mitosis and it triggers the events that completely eliminates the activity of CDK and other mitotic kinases. It is also involved in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint, and in chromosome segregation. Cdc14 phosphatases also function in DNA replication, DNA damage checkpoint, and DNA repair. Vertebrates may contain more than one Cdc14 homolog; humans have three (CDC14A, CDC14B, and CDC14C). CDC14 family proteins contain a highly conserved N-terminal pseudophosphatase domain that contributes to substrate specificity and a C-terminal catalytic dual-specificity phosphatase domain with the PTP signature motif.


Pssm-ID: 350349 [Multi-domain]  Cd Length: 174  Bit Score: 35.12  E-value: 8.48e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1207734383 106 GPMVVHCSAGIGRTGVFLCvdvvfCAIVKNCSFNIMDIVAQMREQRSGMVQTKEQyHF 163
Cdd:cd14499   110 GAIAVHCKAGLGRTGTLIA-----CYLMKHYGFTAREAIAWLRICRPGSVIGPQQ-QF 161
 
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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