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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 438148     1 WKSCSIVMLTELEERGQEKCAQYWPSDGLVSYGDITVELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIP 80
Cdd:cd14623  62 WKSCSIVMLTELEERGQEKCAQYWPSDGSVSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIP 141

                        90       100
                ....*....|....*....|....*.
gi 438148    81 SDGKGMINIIAAVQKQQQQSGNHPIT 106
Cdd:cd14623 142 SDGKGMINIIAAVQKQQQQSGNHPIT 167

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).

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 438148     1 WKSCSIVMLTELEERGQEKCAQYWPSDGLVSYGDITVELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIP 80
Cdd:cd14623  62 WKSCSIVMLTELEERGQEKCAQYWPSDGSVSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIP 141

                        90       100
                ....*....|....*....|....*.
gi 438148    81 SDGKGMINIIAAVQKQQQQSGNHPIT 106
Cdd:cd14623 142 SDGKGMINIIAAVQKQQQQSGNHPIT 167

Protein tyrosine phosphatase, catalytic domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 438148        2 KSCSIVMLTELEERGQEKCAQYWPSDGLVS--YGDITVELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGI 79
Cdd:smart00194  93 KVTVIVMLTELVEKGREKCAQYWPDEEGEPltYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTVTHYHYTNWPDHGV 172

                           90       100
                   ....*....|....*....|....*.
gi 438148       80 PSDGKGMINIIAAVqKQQQQSGNHPI 105
Cdd:smart00194 173 PESPESILDLIRAV-RKSQSTSTGPI 197

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).

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 438148     1 WKSCSIVMLTELEERGQEKCAQYWPSDGLVSYGDITVELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIP 80
Cdd:cd14623  62 WKSCSIVMLTELEERGQEKCAQYWPSDGSVSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIP 141

                        90       100
                ....*....|....*....|....*.
gi 438148    81 SDGKGMINIIAAVQKQQQQSGNHPIT 106
Cdd:cd14623 142 SDGKGMINIIAAVQKQQQQSGNHPIT 167

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).

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 438148     1 WKSCSIVMLTELEERGQEKCAQYWPSDGLVSYGDITVELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIP 80
Cdd:cd14622  38 WKCHTIVMLTELQEREQEKCVQYWPSEGSVTHGEITIEIKNDTLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIP 117

                        90       100
                ....*....|....*....|....*.
gi 438148    81 SDGKGMINIIAAVQKQQQQSGNHPIT 106
Cdd:cd14622 118 AEGKGMIDLIAAVQKQQQQTGNHPIV 143

Protein tyrosine phosphatase, catalytic domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 438148        2 KSCSIVMLTELEERGQEKCAQYWPSDGLVS--YGDITVELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGI 79
Cdd:smart00194  93 KVTVIVMLTELVEKGREKCAQYWPDEEGEPltYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTVTHYHYTNWPDHGV 172

                           90       100
                   ....*....|....*....|....*.
gi 438148       80 PSDGKGMINIIAAVqKQQQQSGNHPI 105
Cdd:smart00194 173 PESPESILDLIRAV-RKSQSTSTGPI 197

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).

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 438148     1 WKSCS--IVMLTELEERGQEKCAQYWPSDGLVSYGDITVELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVG 78
Cdd:cd14554  70 WEHNStiIVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQG 149

                        90       100
                ....*....|....*....|....*....
gi 438148    79 IPSDGKGMINIIAAVQKQQQQSGNH-PIT 106
Cdd:cd14554 150 VPKSGEGFIDFIGQVHKTKEQFGQEgPIT 178

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).

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 438148     2 KSCSIVMLTELEERGQEKCAQYWPSDGLVSYGDITVELKKEEECESYTVRDLLVTNTRENKS------RQIRQFHFHGWP 75
Cdd:cd14549  38 NSAIIVMITNLVERGRRKCDQYWPKEGTETYGNIQVTLLSTEVLATYTVRTFSLKNLKLKKVkgrsseRVVYQYHYTQWP 117

                        90       100
                ....*....|....*....|
gi 438148    76 EVGIPSDgkgMINIIAAVQK 95
Cdd:cd14549 118 DHGVPDY---TLPVLSFVRK 134

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 438148     2 KSCSIVMLTELEERGQEKCAQYWPSDGL-VSYGDITVELKKEEECESYTVRDLLVTntRENKSRQIRQFHFHGWPEVGIP 80
Cdd:cd14548  63 NSHTIVMLTQCMEKGRVKCDHYWPFDQDpVYYGDITVTMLSESVLPDWTIREFKLE--RGDEVRSVRQFHFTAWPDHGVP 140

                        90       100
                ....*....|....*....|....*
gi 438148    81 SDGKGMINIIAAVQKQQQQSGNHPI 105
Cdd:cd14548 141 EAPDSLLRFVRLVRDYIKQEKGPTI 165

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 438148     6 IVMLTELEERGQEKCAQYWPSDGLVS--YGDITVELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDG 83
Cdd:cd14543 100 IVMTTRVVERGRVKCGQYWPLEEGSSlrYGDLTVTNLSVENKEHYKKTTLEIHNTETDESRQVTHFQFTSWPDFGVPSSA 179

                        90
                ....*....|....*..
gi 438148    84 KGMINIIAAVQKQQQQS 100
Cdd:cd14543 180 AALLDFLGEVRQQQALA 196

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 438148     3 SCSIVMLTELEERGQEKCAQYWPSDGLVSYGDITVELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSD 82
Cdd:cd14628 120 STIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKS 199

                        90       100
                ....*....|....*....|....*
gi 438148    83 GKGMINIIAAVQKQQQQSG-NHPIT 106
Cdd:cd14628 200 GEGFIDFIGQVHKTKEQFGqDGPIS 224

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 438148     6 IVMLTELEERGQEKCAQYWPSDGLVS-YGDITVELKKEEECE--SYTVRDLLVTNTrENKSRQIRQFHFHGWPEVGIPSD 82
Cdd:cd18533  43 IVMLTPLVENGREKCDQYWPSGEYEGeYGDLTVELVSEEENDdgGFIVREFELSKE-DGKVKKVYHIQYKSWPDFGVPDS 121

                        90       100
                ....*....|....*....|..
gi 438148    83 GKGMINIIAAVQKQQQQSGNHP 104
Cdd:cd18533 122 PEDLLTLIKLKRELNDSASLDP 143

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 438148     2 KSCSIVMLTELEERGQEKCAQYWPSDGL-VSYGDITVELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIP 80
Cdd:cd14619  64 QSSTIVMLTNCMEAGRVKCEHYWPLDYTpCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVP 143

                .
gi 438148    81 S 81
Cdd:cd14619 144 S 144

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 438148     2 KSCSIVMLTELEERGQEKCAQYWPS----DGLVSYGDITVELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEV 77
Cdd:cd14545  63 NSKAVIMLNKLMEKGQIKCAQYWPQgegnAMIFEDTGLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDF 142

                        90
                ....*....|....*.
gi 438148    78 GIPSDGKGMINIIAAV 93
Cdd:cd14545 143 GVPESPAAFLNFLQKV 158

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 438148     6 IVMLTELEERGQEKCAQYWPSDGLV-SYGDITVELKKEEECESYTVRDLLVTNTRE-NKSRQIRQFHFHGWPEVGIPSDG 83
Cdd:cd14544  80 IVMTTKEVERGKNKCVRYWPDEGMQkQYGPYRVQNVSEHDTTDYTLRELQVSKLDQgDPIREIWHYQYLSWPDHGVPSDP 159

                        90       100
                ....*....|....*....|.
gi 438148    84 KGMINIIAAVQkQQQQSGNHP 104
Cdd:cd14544 160 GGVLNFLEDVN-QRQESLPHA 179

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 438148     2 KSCSIVMLTELEERGQEKCAQYWPSDGLVSYGDITVELKKEEE-CESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIP 80
Cdd:cd14546  39 GCVVIVMLTRLQENGVKQCARYWPEEGSEVYHIYEVHLVSEHIwCDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIP 118

                        90
                ....*....|....*
gi 438148    81 SDGKGMINIIAAVQK 95
Cdd:cd14546 119 ASAKPLLEFRRKVNK 133

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 438148     2 KSCSIVMLTELEERGQEKCAQYWPS--DGLVSYGDITVELKKEEECESYTVRDLLVTNTRENKS-RQIRQFHFHGWPEVG 78
Cdd:cd14557  38 KSTVIVMVTRCEEGNRNKCAQYWPSmeEGSRAFGDVVVKINEEKICPDYIIRKLNINNKKEKGSgREVTHIQFTSWPDHG 117

                ....
gi 438148    79 IPSD 82
Cdd:cd14557 118 VPED 121

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 438148     3 SCSIVMLTELEERGQEkCAQYWPSDGLVSYGDITVELKKEEECESYTVRDLLVTNTR--ENKSRQIRQFHFHGWPEVGIP 80
Cdd:cd14556  39 CTSIVMLNQLDPKDQS-CPQYWPDEGSGTYGPIQVEFVSTTIDEDVISRIFRLQNTTrpQEGYRMVQQFQFLGWPRDRDT 117

                        90       100
                ....*....|....*....|....*..
gi 438148    81 SDGKG-MINIIAAVQKQQQQSGNHPIT 106
Cdd:cd14556 118 PPSKRaLLKLLSEVEKWQEQSGEGPIV 144

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 438148     6 IVMLTELEERGQEKCAQYWPSD-GLVSYGDITVELKKEEECESYTVRDLLVTNTRE-NKSRQIRQFHFHGWPEVGIPSDG 83
Cdd:cd14605  82 IVMTTKEVERGKSKCVKYWPDEyALKEYGVMRVRNVKESAAHDYILRELKLSKVGQgNTERTVWQYHFRTWPDHGVPSDP 161

                        90       100
                ....*....|....*....|...
gi 438148    84 KGMINIIAAVQ-KQQQQSGNHPI 105
Cdd:cd14605 162 GGVLDFLEEVHhKQESIMDAGPV 184

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).

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 438148     6 IVMLTELEERGQEKCAQYWPSDGLVSYGDITVELKKEEECESYTVRDLLVTNTRENKSRQ--------IRQFHFHGWPEV 77
Cdd:cd17668  42 IVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQVLAYYTVRNFTLRNTKIKKGSQkgrpsgrvVTQYHYTQWPDM 121

                ...
gi 438148    78 GIP 80
Cdd:cd17668 122 GVP 124

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).

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 438148     2 KSCSIVMLTELEERGQEKCAQYWPSDGLVSYGDITVELKKEEECESYTVRDLLVTNTRENKS---RQIRQFHFHGWPEVG 78
Cdd:cd14620  62 KSATIVMLTNLKERKEEKCYQYWPDQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDGCkapRLVTQLHFTSWPDFG 141

                        90
                ....*....|....*.
gi 438148    79 IPSDGKGMINIIAAVQ 94
Cdd:cd14620 142 VPFTPIGMLKFLKKVK 157

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 438148     2 KSCSIVMLTELEERGQEKCAQYWPSDGLV-SYGDITVELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIP 80
Cdd:cd14600 106 KLSLIVMLTTLTERGRTKCHQYWPDPPDVmEYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTVTHLQYVAWPDHGVP 185

                        90       100
                ....*....|....*....|
gi 438148    81 SDGKGMINIIAAVQKQQQQS 100
Cdd:cd14600 186 DDSSDFLEFVNYVRSKRVEN 205

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 438148     1 WKS-CS-IVMLTELEERGQEKCAQYWPSDGLVSYGDITVELKKEE-ECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEV 77
Cdd:cd14610 109 WESgCVvIVMLTPLAENGVKQCYHYWPDEGSNLYHIYEVNLVSEHiWCEDFLVRSFYLKNLQTNETRTVTQFHFLSWNDQ 188

                        90
                ....*....|....*...
gi 438148    78 GIPSDGKGMINIIAAVQK 95
Cdd:cd14610 189 GVPASTRSLLDFRRKVNK 206

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 438148     1 WKS-CS-IVMLTELEERGQEKCAQYWPSDGLVSYGDITVELKKEE-ECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEV 77
Cdd:cd14609 107 WENgCTvIVMLTPLVEDGVKQCDRYWPDEGSSLYHIYEVNLVSEHiWCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAE 186

                        90
                ....*....|....*...
gi 438148    78 GIPSDGKGMINIIAAVQK 95
Cdd:cd14609 187 GIPSSTRPLLDFRRKVNK 204

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).

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 438148     2 KSCSIVMLTELEERGQEKCAQYWPSDGLVSYGDITVELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIP 80
Cdd:cd14625 114 RSATVVMMTKLEEKSRIKCDQYWPSRGTETYGMIQVTLLDTIELATFCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVP 192

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 438148     6 IVMLTELEERgQEKCAQYWPSDGlVSYGDITVELKKEEECESYTVRDLLVtnTRENKSRQIRQFHFHGWPEVGIPSDGKG 85
Cdd:cd14612  88 IVMITKLKEK-KEKCVHYWPEKE-GTYGRFEIRVQDMKECDGYTIRDLTI--QLEEESRSVKHYWFSSWPDHQTPESAGP 163

                        90
                ....*....|....*..
gi 438148    86 MINIIAAVQKQQQQSGN 102
Cdd:cd14612 164 LLRLVAEVEESRQTAAS 180

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 438148     4 CSIVMLTELEERGQEKCAQYWPSDGL-VSYGDITVELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSD 82
Cdd:cd14618  66 CNIIMLTVGMENGRVLCDHYWPSESTpVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPES 145

                        90       100
                ....*....|....*....|....
gi 438148    83 GKGMINIIAAVQKQQQQS-GNHPI 105
Cdd:cd14618 146 TSSLMAFRELVREHVQATkGKGPT 169

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 438148     2 KSCSIVMLTELEERGQEKCAQYWP-SDGLVSYGDITVELKKEEECESYTVRDLLVTNTREnkSRQIRQFHFHGWPEVGIP 80
Cdd:cd14614  79 KSQIIVMLTQCNEKRRVKCDHYWPfTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADE--VQDVMHFNYTAWPDHGVP 156

                        90       100
                ....*....|....*....|....
gi 438148    81 SdGKGMINIIAAVQKQQQQSGNHP 104
Cdd:cd14614 157 T-ANAAESILQFVQMVRQQAVKSK 179

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 438148     5 SIVMLTELEERGQEKCAQYWPSDG--LVSYGDITVELKKEEECESYTVRDLLVtnTRENKSRQIRQFHFHGWPEVGIPSD 82
Cdd:cd14616  67 TIVMLTQCFEKGRIRCHQYWPEDNkpVTVFGDIVITKLMEDVQIDWTIRDLKI--ERHGDYMMVRQCNFTSWPEHGVPES 144

                        90       100
                ....*....|....*....|...
gi 438148    83 GKGMINIIAAVQKQQQQSgNHPI 105
Cdd:cd14616 145 SAPLIHFVKLVRASRAHD-NTPM 166

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 438148     6 IVMLTELEERGQEKCAQYWPSDG----LVSYGDITVELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPS 81
Cdd:cd14540  44 VVMVTAEEEGGREKCFRYWPTLGgehdALTFGEYKVSTKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPE 123

                        90
                ....*....|...
gi 438148    82 DGKGMINIIAAVQ 94
Cdd:cd14540 124 DVSGFLDFLEEIN 136

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 438148     6 IVMLTELEERGQEKCAQYWP--SDGLVSYGDITVELKKEEECESYTVRDLLVTntRENKSRQIRQFHFHGWPEVGIPSDG 83
Cdd:cd14604 128 IVMACREFEMGRKKCERYWPlyGEEPMTFGPFRISCEAEQARTDYFIRTLLLE--FQNETRRLYQFHYVNWPDHDVPSSF 205

                        90
                ....*....|....*.
gi 438148    84 KGMINIIAAVQKQQQQ 99
Cdd:cd14604 206 DSILDMISLMRKYQEH 221