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Enzyme Name | UniProtKB | KEGG |
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| P10586 |
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Protein name | Receptor-type tyrosine-protein phosphatase F | protein-tyrosine-phosphatasephosphotyrosine phosphatasephosphoprotein phosphatase (phosphotyrosine)phosphotyrosine histone phosphataseprotein phosphotyrosine phosphatasetyrosylprotein phosphatasephosphotyrosine protein phosphatasephosphotyrosylprotein phosphatasetyrosine O-phosphate phosphatasePPT-phosphatasePTPase[phosphotyrosine]protein phosphatasePTP-phosphatase |
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Synonyms | EC 3.1.3.48Leukocyte common antigen relatedLAR |
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RefSeq | NP_002831.2 (Protein) NM_002840.3 (DNA/RNA sequence) NP_569707.2 (Protein) NM_130440.2 (DNA/RNA sequence)
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Pfam | PF00041 (fn3) PF07679 (I-set) PF00102 (Y_phosphatase) [Graphical view]
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UniProtKB:Accession Number | P10586 |
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Entry name | PTPRF_HUMAN |
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Activity | Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate. |
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Subunit | Interacts with GRIP1 (By similarity). Interacts with PPFIA1, PPFIA2 and PPFIA3. |
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Subcellular location | Membrane, Single-pass type I membrane protein. |
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Cofactor |
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Compound table: links to PDB-related databases & PoSSuM |
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| Substrates | Products |
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KEGG-id | C00001 | C01167 | C00009 | C00585 |
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Compound | H2O | Protein tyrosine phosphate | Orthophosphate | Protein tyrosine |
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Type | H2O | aromatic ring (only carbon atom),peptide/protein,phosphate group/phosphate ion | phosphate group/phosphate ion | aromatic ring (only carbon atom),peptide/protein |
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ChEBI | 15377
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| 26078
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PubChem | 22247451 962
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| 1004 22486802
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| | | | | | | | | | | |
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1larA01 |  |  |  |  |  |  |  | | Unbound | Unbound | Unbound |
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1larB01 |  |  |  |  |  |  |  | | Unbound | Unbound | Unbound |
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1larA02 |  |  |  |  |  |  |  | | Unbound | Unbound | Unbound |
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1larB02 |  |  |  |  |  |  |  | | Unbound | Unbound | Unbound |
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References for Catalytic Mechanism | References | Sections | No. of steps in catalysis |
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[6] | Scheme 2 | p.5640 | [8] | p.451-454 |
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references | [1] |
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Comments | MUTAGENESIS. |
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Medline ID | 90316093 |
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PubMed ID | 1695146 |
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Journal | EMBO J |
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Year | 1990 |
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Volume | 9 |
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Pages | 2399-407 |
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Authors | Streuli M, Krueger NX, Thai T, Tang M, Saito H |
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Title | Distinct functional roles of the two intracellular phosphatase like domains of the receptor-linked protein tyrosine phosphatases LCA and LAR. |
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Related UniProtKB | P10586 |
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[2] |
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PubMed ID | 1318316 |
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Journal | J Biol Chem |
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Year | 1992 |
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Volume | 267 |
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Pages | 12356-63 |
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Authors | Itoh M, Streuli M, Krueger NX, Saito H |
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Title | Purification and characterization of the catalytic domains of the human receptor-linked protein tyrosine phosphatases HPTP beta, leukocyte common antigen (LCA), and leukocyte common antigen-related molecule (LAR). |
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[3] |
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PubMed ID | 1303753 |
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Journal | Protein Sci |
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Year | 1992 |
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Volume | 1 |
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Pages | 1353-62 |
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Authors | Lee JP, Cho H, Bannwarth W, Kitas EA, Walsh CT |
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Title | NMR analysis of regioselectivity in dephosphorylation of a triphosphotyrosyl dodecapeptide autophosphorylation site of the insulin receptor by a catalytic fragment of LAR phosphotyrosine phosphatase. |
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[4] |
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PubMed ID | 8068021 |
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Journal | Biochem J |
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Year | 1994 |
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Volume | 302 |
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Pages | 39-47 |
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Authors | Zhang WR, Hashimoto N, Ahmad F, Ding W, Goldstein BJ |
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Title | Molecular cloning and expression of a unique receptor-like protein-tyrosine-phosphatase in the leucocyte-common-antigen-related phosphate family. |
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[5] |
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PubMed ID | 7665159 |
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Journal | Genomics |
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Year | 1995 |
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Volume | 27 |
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Pages | 124-30 |
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Authors | Schaapveld RQ, van den Maagdenberg AM, Schepens JT, Weghuis DO, Geurts van Kessel A, Wieringa B, Hendriks WJ |
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Title | The mouse gene Ptprf encoding the leukocyte common antigen-related molecule LAR: cloning, characterization, and chromosomal localization. |
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[6] |
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PubMed ID | 9548949 |
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Journal | Biochemistry |
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Year | 1998 |
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Volume | 37 |
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Pages | 5633-42 |
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Authors | Denu JM, Tanner KG |
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Title | Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: evidence for a sulfenic acid intermediate and implications for redox regulation. |
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[7] |
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PubMed ID | 9882618 |
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Journal | Biochem J |
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Year | 1999 |
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Volume | 337 |
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Pages | 219-23 |
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Authors | Desmarais S, Friesen RW, Zamboni R, Ramachandran C |
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Title | Difluro(phosphono)methyl]phenylalanine-containing peptide inhibitors of protein tyrosine phosphatases. |
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[8] |
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Comments | X-ray crystallography |
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PubMed ID | 10338209 |
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Journal | Cell |
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Year | 1999 |
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Volume | 97 |
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Pages | 449-57 |
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Authors | Nam HJ, Poy F, Krueger NX, Saito H, Frederick CA |
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Title | Crystal structure of the tandem phosphatase domains of RPTP LAR. |
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Related PDB | 1lar |
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[9] |
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PubMed ID | 10735562 |
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Journal | Biochem Cell Biol |
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Year | 2000 |
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Volume | 78 |
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Pages | 39-50 |
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Authors | Glover NR, Tracey AS |
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Title | The phosphatase domains of LAR, CD45, and PTP1B: structural correlations with peptide-based inhibitors. |
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[10] |
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PubMed ID | 10777529 |
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Journal | J Biol Chem |
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Year | 2000 |
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Volume | 275 |
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Pages | 12446-52 |
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Authors | Blanchetot C, den Hertog J |
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Title | Multiple interactions between receptor protein-tyrosine phosphatase (RPTP) alpha and membrane-distal protein-tyrosine phosphatase domains of various RPTPs. |
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[11] |
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PubMed ID | 11241288 |
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Journal | Eur J Immunol |
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Year | 2001 |
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Volume | 31 |
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Pages | 832-40 |
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Authors | Terszowski G, Jankowski A, Hendriks WJ, Rolink AG, Kisielow P |
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Title | Within the hemopoietic system, LAR phosphatase is a T cell lineage-specific adhesion receptor-like protein whose phosphatase activity appears dispensable for T cell development, repertoire selection and function. |
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[12] |
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PubMed ID | 11158333 |
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Journal | Mol Endocrinol |
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Year | 2001 |
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Volume | 15 |
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Pages | 271-80 |
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Authors | Tsujikawa K, Kawakami N, Uchino Y, Ichijo T, Furukawa T, Saito H, Yamamoto H |
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Title | Distinct functions of the two protein tyrosine phosphatase domains of LAR (leukocyte common antigen-related) on tyrosine dephosphorylation of insulin receptor. |
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[13] |
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PubMed ID | 12376545 |
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Journal | J Biol Chem |
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Year | 2002 |
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Volume | 277 |
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Pages | 47263-9 |
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Authors | Blanchetot C, Tertoolen LG, Overvoorde J, den Hertog J |
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Title | Intra- and intermolecular interactions between intracellular domains of receptor protein-tyrosine phosphatases. |
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[14] |
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PubMed ID | 11806712 |
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Journal | J Med Chem |
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Year | 2002 |
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Volume | 45 |
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Pages | 598-622 |
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Authors | Larsen SD, Barf T, Liljebris C, May PD, Ogg D, O'Sullivan TJ, Palazuk BJ, Schostarez HJ, Stevens FC, Bleasdale JE |
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Title | Synthesis and biological activity of a novel class of small molecular weight peptidomimetic competitive inhibitors of protein tyrosine phosphatase 1B. |
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[15] |
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PubMed ID | 12176037 |
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Journal | Biochem Biophys Res Commun |
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Year | 2002 |
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Volume | 296 |
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Pages | 692-7 |
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Authors | Caselli A, Mazzinghi B, Camici G, Manao G, Ramponi G |
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Title | Some protein tyrosine phosphatases target in part to lipid rafts and interact with caveolin-1. |
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[16] |
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PubMed ID | 9566880 |
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Journal | Mol Cell Biol |
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Year | 1998 |
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Volume | 18 |
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Pages | 2608-16 |
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Authors | Wallace MJ, Fladd C, Batt J, Rotin D |
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Title | The second catalytic domain of protein tyrosine phosphatase delta (PTP delta) binds to and inhibits the first catalytic domain of PTP sigma. |
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[17] |
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PubMed ID | 1730581 |
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Journal | J Biol Chem |
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Year | 1992 |
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Volume | 267 |
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Pages | 140-3 |
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Authors | Pot DA, Dixon JE |
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Title | Active site labeling of a receptor-like protein tyrosine phosphatase. |
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comments | This enzyme is composed of the N-terminal extracellular region, the transmembrane region, and the C-terminal cytoplasmic region. The C-terminal region contains two protein tyrosine phosphatase domains. Whilst the structures of the catalytic domains have been determined, the remainder has not been determined yet. However, according to the literature [4], homology search suggested that the N-terminal extracellular region seems to be composed of three immunoglobulin-like domains and eight fibronectin type III domains. According to the literature [8], the second phosphatase domain has no catalytic activity, whereas the first domain retains the activily. Considering the active site residues and mutational analysis, the loss of catalytic activity is due to two residues, Leu1644 and Glu1779. When these residues are mutated into Tyr and Asp, respectively, the activity was restored (see [8]). The corresponding tyrosine may interact with phosphorylated tyrosine (see [8]). According to the literature [8], in the first phosphatase domain, Cys1522 acts as a nucleophile, which will make an attack on an incoming phosphopeptide, whilst Asp1490 acts as a general acid. Moreover, the catalytic domain is homologous to other phosphatase enzyme domains (S00458, D00154 in EzCatDB). These domains has Ser or Thr next to the catalytic Arg, and it acts as a modulator interacting with catalytic Cys. As this enzyme also has got the residue at the position, it may play the same role as the counterparts.
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created | updated |
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2004-08-18 | 2009-02-26 |
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