A protein-tyrosine phosphatase with sequence similarity to the SH2 domain of the protein-tyrosine kinases.
about
Human 70-kDa SHP-1L differs from 68-kDa SHP-1 in its C-terminal structure and catalytic activityRegulation of acidification and apoptosis by SHP-1 and Bcl-2Negative regulation of Ros receptor tyrosine kinase signaling. An epithelial function of the SH2 domain protein tyrosine phosphatase SHP-1G6b, a novel immunoglobulin superfamily member encoded in the human major histocompatibility complex, interacts with SHP-1 and SHP-2Src kinase associates with a member of a distinct subfamily of protein-tyrosine phosphatases containing an ezrin-like domainIdentification of HS1 protein as a major substrate of protein-tyrosine kinase(s) upon B-cell antigen receptor-mediated signalingTyrosine phosphorylation of a human killer inhibitory receptor recruits protein tyrosine phosphatase 1CThe 64-kDa protein that associates with the platelet-derived growth factor receptor beta subunit via Tyr-1009 is the SH2-containing phosphotyrosine phosphatase SypCD22 associates with protein tyrosine phosphatase 1C, Syk, and phospholipase C-gamma(1) upon B cell activationInsulin receptor substrate proteins create a link between the tyrosine phosphorylation cascade and the Ca2+-ATPases in muscle and heartIn vivo binding properties of SH2 domains from GTPase-activating protein and phosphatidylinositol 3-kinaseCloning and expression of a cytosolic megakaryocyte protein-tyrosine-phosphatase with sequence homology to retinaldehyde-binding protein and yeast SEC14pRecruitment of tyrosine phosphatase HCP by the killer cell inhibitor receptorDifferential functions of the two Src homology 2 domains in protein tyrosine phosphatase SH-PTP1Interaction between Sam68 and Src family tyrosine kinases, Fyn and Lck, in T cell receptor signalingTyrosine phosphorylation of an SH2-containing protein tyrosine phosphatase is coupled to platelet thrombin receptor via a pertussis toxin-sensitive heterotrimeric G-proteinLck-dependent tyrosyl phosphorylation of the phosphotyrosine phosphatase SH-PTP1 in murine T cellsExpression of the receptor-linked protein tyrosine phosphatase LAR: proteolytic cleavage and shedding of the CAM-like extracellular regionIdentification of a human src homology 2-containing protein-tyrosine-phosphatase: a putative homolog of Drosophila corkscrewCloning and characterization of a mouse cDNA encoding a cytoplasmic protein-tyrosine-phosphataseCloning of ASH, a ubiquitous protein composed of one Src homology region (SH) 2 and two SH3 domains, from human and rat cDNA librariesHigh-efficiency expression/cloning of epidermal growth factor-receptor-binding proteins with Src homology 2 domainsIdentification of c-erbB-3 binding sites for phosphatidylinositol 3'-kinase and SHC using an EGF receptor/c-erbB-3 chimeraThe SH2 and SH3 domain-containing Nck protein is oncogenic and a common target for phosphorylation by different surface receptorsAssociation of hematopoietic cell phosphatase with c-Kit after stimulation with c-Kit ligandMultiple SH2-mediated interactions in v-src-transformed cells.Direct association with and dephosphorylation of Jak2 kinase by the SH2-domain-containing protein tyrosine phosphatase SHP-1A novel membrane glycoprotein, SHPS-1, that binds the SH2-domain-containing protein tyrosine phosphatase SHP-2 in response to mitogens and cell adhesionHematopoietic cell phosphatase, SHP-1, is constitutively associated with the SH2 domain-containing leukocyte protein, SLP-76, in B cellsOverexpression of PIAS3 suppresses cell growth and restores the drug sensitivity of human lung cancer cells in association with PI3-K/Akt inactivationIdentification of the tyrosine phosphatase PTP1C as a B cell antigen receptor-associated protein involved in the regulation of B cell signaling2-(oxalylamino)-benzoic acid is a general, competitive inhibitor of protein-tyrosine phosphatasesStructure-based design of a low molecular weight, nonphosphorus, nonpeptide, and highly selective inhibitor of protein-tyrosine phosphatase 1BCrystal structure of the catalytic domain of protein-tyrosine phosphatase SHP-1Mutations in a protein tyrosine phosphatase gene (PTP2) and a protein serine/threonine phosphatase gene (PTC1) cause a synthetic growth defect in Saccharomyces cerevisiae.Assembly and function of a cytosolic form of NADH-specific isocitrate dehydrogenase in yeast.Inactivation of protein-tyrosine phosphatases as mechanism of UV-induced signal transductionCharacterization of hematopoietic intracellular protein tyrosine phosphatases: description of a phosphatase containing an SH2 domain and another enriched in proline-, glutamic acid-, serine-, and threonine-rich sequencesConservation analysis and structure prediction of the SH2 family of phosphotyrosine binding domainsSrc kinase activity is regulated by the SHP-1 protein-tyrosine phosphatase
P2860
Q22010565-FB2A95D0-D663-492D-A466-8F710C5C524EQ22010599-D0B9C763-E285-464C-8715-8457456893D2Q24290967-3ECE63A8-94F5-429D-A870-B02DE1CA4F96Q24291649-B906C528-B097-49AF-94F1-82CF6645E43AQ24305967-955ED00D-9BE8-409D-907D-DE75FE649B03Q24309099-254E53A6-B60F-4220-B426-6CC803ABBF64Q24309260-36D84195-C285-4EF0-8219-296A6BB6F9F1Q24310396-FF8313D4-FDB9-4CAF-9865-1FD953CA723DQ24310493-6614378E-5AFE-436A-8371-63CDF5048E54Q24311811-F95995DD-8EEC-41BF-AF8A-BE36496D0CBBQ24314627-8796DCC6-64CE-4638-B60D-9E51D85E0EC4Q24318402-14B566B4-6CF9-495D-8ED7-0868151AADDFQ24318464-192A4D7F-9E2A-44A6-80EF-1445B692FCA5Q24319091-2EA34EF9-187F-4813-8035-E24747DDAE0CQ24322019-83E581D0-6F80-445E-90BF-C98A26BA90F8Q24322042-08FF7F66-E01D-4131-97F5-041BA78689C1Q24324441-45F4BBC4-97F3-4F1C-B5BF-C899BDC61A89Q24555697-C3875C6B-16A1-4936-8FA5-598D48F80849Q24563125-834B1D2A-7A41-49FD-8AF8-2EC405F325C4Q24563410-2C47A5DD-163F-4E65-91E9-5CDE0FBC1CC2Q24563818-164D2901-144C-4EF9-8FBA-35E1B7848FEDQ24563877-E0341C1A-2E92-476E-8B16-0A8D43A1023AQ24595150-078ED0E9-D941-4634-A80A-5FFB1C362131Q24600645-F48606AF-EDBD-4C77-949F-9698248E6A65Q24604791-F729E38B-72B4-45F7-9810-9B184D1BA467Q24606832-2F14938A-939D-4023-92DE-C3D388BBBFCCQ24647567-A32AE813-B340-4E58-BBDE-D26CE5B98231Q24647689-F565F79E-A423-42F0-BFE2-AFE0F9721FA1Q24677276-9287EAD1-712B-4134-8EA5-9DBF1DE3B38FQ24678516-C5A61815-88E7-4DC3-AFAD-F14E109B1DF6Q24678964-1C2BA11F-B686-4B6B-80F0-E9CC2921A15BQ27621646-40F0C2FF-EFF6-4757-B46E-7DAF78B6F4D8Q27622003-055843F0-EFFB-4C26-B97F-F5147BA58F7CQ27765696-B8E6F045-6764-48D0-8747-57D4FB55147BQ27930095-52C7AACA-7A03-4016-8622-C5BD39555EEDQ27931181-410C3B29-EDD9-476B-8C4C-CB5D840CD9E3Q28143762-4C70F431-3ADF-4DDA-A0C9-646B18988773Q28186547-35F85038-85F3-47AD-8E22-421076D862C3Q28187467-BBFF7696-2CE3-4C7C-A730-E0038400F4D2Q28246466-15E233CE-9859-4C8A-96C6-B4E359577748
P2860
A protein-tyrosine phosphatase with sequence similarity to the SH2 domain of the protein-tyrosine kinases.
description
1991 nî lūn-bûn
@nan
1991年の論文
@ja
1991年学术文章
@wuu
1991年学术文章
@zh
1991年学术文章
@zh-cn
1991年学术文章
@zh-hans
1991年学术文章
@zh-my
1991年学术文章
@zh-sg
1991年學術文章
@yue
1991年學術文章
@zh-hant
name
A protein-tyrosine phosphatase ...... the protein-tyrosine kinases.
@en
A protein-tyrosine phosphatase ...... the protein-tyrosine kinases.
@nl
type
label
A protein-tyrosine phosphatase ...... the protein-tyrosine kinases.
@en
A protein-tyrosine phosphatase ...... the protein-tyrosine kinases.
@nl
prefLabel
A protein-tyrosine phosphatase ...... the protein-tyrosine kinases.
@en
A protein-tyrosine phosphatase ...... the protein-tyrosine kinases.
@nl
P2093
P356
P1433
P1476
A protein-tyrosine phosphatase ...... the protein-tyrosine kinases.
@en
P2093
P2888
P304
P356
10.1038/352736A0
P407
P577
1991-08-01T00:00:00Z
P5875
P6179
1024837667