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
                  ....*....|....*....|....*...
gi 2462518462  78 IMQEFMFNIMDIVAQMREQRSGMVQTKE 105
Cdd:cd14596   166 IEKDLSFNIKDIVREMRQQRYGMIQTKD 193

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.

                          10        20
                  ....*....|....*....|....*...
gi 2462518462  78 IMQEFMFNIMDIVAQMREQRSGMVQTKE 105
Cdd:cd14596   166 IEKDLSFNIKDIVREMRQQRYGMIQTKD 193

Protein-tyrosine phosphatase;

                          10        20        30
                  ....*....|....*....|....*....|...
gi 2462518462  73 TAAYDIMQEFMFNIMDIVAQMREQRSGMVQTKE 105
Cdd:pfam00102 191 IALQQLEAEGEVDIFQIVKELRSQRPGMVQTLE 223

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.

                          10        20
                  ....*....|....*....|....*...
gi 2462518462  78 IMQEFMFNIMDIVAQMREQRSGMVQTKE 105
Cdd:cd14596   166 IEKDLSFNIKDIVREMRQQRYGMIQTKD 193

Protein tyrosine phosphatase, catalytic domain;

                           10        20
                   ....*....|....*....|....*...
gi 2462518462   78 IMQEFMFNIMDIVAQMREQRSGMVQTKE 105
Cdd:smart00194 221 LEAGKEVDIFEIVKELRSQRPGMVQTEE 248

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.

                          10        20
                  ....*....|....*....|....*...
gi 2462518462  78 IMQEFMFNIMDIVAQMREQRSGMVQTKE 105
Cdd:cd00047   166 LEAEGEVDVFEIVKALRKQRPGMVQTLE 193

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.

                           10        20
                   ....*....|....*....|..
gi 2462518462   84 FNIMDIVAQMREQRSGMVQTKE 105
Cdd:smart00012  73 VDIFDTVKELRSQRPGMVQTEE 94

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.

                          10        20
                  ....*....|....*....|....*...
gi 2462518462  78 IMQEFMFNIMDIVAQMREQRSGMVQTKE 105
Cdd:cd14597   194 ISKDLDFDISDIVRTMRLQRHGMVQTED 221

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.

                          10        20
                  ....*....|....*....|....*.
gi 2462518462  80 QEFMFNIMDIVAQMREQRSGMVQTKE 105
Cdd:cd14547   192 EEGVVDVLGIVCQLRLDRGGMVQTAE 217