loading...| Preferred Name | SHP-1 and SHP-2 bind pBTLA | |
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Authored: Garapati, P V, 2008-12-16 11:12:19 Reviewed: Bluestone, JA, Esensten, J, 2009-06-01 18:47:33 Edited: Garapati, P V, 2008-12-16 11:12:19 The cytoplasmic tail of BTLA contains three tyrosine residues that are conserved in most organisms. The tyrosine residues Y257 and Y282 are both present in ITIM motif sequences. These tyrosine residues are phosphorylated after BTLA cross-linking, and both ITIM motifs recruit the tyrosine phosphatases SHP1 and SHP2. The targets of SHP1 and SHP2 recruited to BTLA are not known, although it is possible that they also have a role in dephosphorylating signaling intermediates downstream of antigen receptors in lymphocytes or in specifically targeting the PI3K-AKT pathway. |
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http://purl.obolibrary.org/obo/HINO_0017758 |
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Authored: Garapati, P V, 2008-12-16 11:12:19 Reviewed: Bluestone, JA, Esensten, J, 2009-06-01 18:47:33 Edited: Garapati, P V, 2008-12-16 11:12:19 The cytoplasmic tail of BTLA contains three tyrosine residues that are conserved in most organisms. The tyrosine residues Y257 and Y282 are both present in ITIM motif sequences. These tyrosine residues are phosphorylated after BTLA cross-linking, and both ITIM motifs recruit the tyrosine phosphatases SHP1 and SHP2. The targets of SHP1 and SHP2 recruited to BTLA are not known, although it is possible that they also have a role in dephosphorylating signaling intermediates downstream of antigen receptors in lymphocytes or in specifically targeting the PI3K-AKT pathway. |
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| definition source |
Pubmed12796776 Reactome, http://www.reactome.org Pubmed16932752 |
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SHP-1 and SHP-2 bind pBTLA |
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HINO:0017758 |
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SHP-1 and SHP-2 bind pBTLA |
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Reactome Database ID Release 43389941 ReactomeREACT_19365 |
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