| http://purl.uniprot.org/citations/15737992 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15737992 | http://www.w3.org/2000/01/rdf-schema#comment | "The Cbl adapter proteins typically function to down-regulate activated protein tyrosine kinases and other signaling proteins by coupling them to the ubiquitination machinery for degradation by the proteasome. Cbl proteins bind to specific tyrosine-phosphorylated sequences in target proteins via the tyrosine kinase-binding (TKB) domain, which comprises a four-helix bundle, an EF-hand calcium-binding domain, and a non-conventional Src homology-2 domain. The previously derived consensus sequence for phosphotyrosine recognition by the Cbl TKB domain is NXpY(S/T)XXP (X denotes lesser residue preference), wherein specificity is conferred primarily by residues C-terminal to the phosphotyrosine. Cbl is recruited to and phosphorylated by the insulin receptor in adipose cells through the adapter protein APS. APS is phosphorylated by the insulin receptor on a C-terminal tyrosine residue, which then serves as a binding site for the Cbl TKB domain. Using x-ray crystallography, site-directed mutagenesis, and calorimetric studies, we have characterized the interaction between the Cbl TKB domain and the Cbl recruitment site in APS, which contains a sequence motif, RA(V/I)XNQpY(S/T), that is conserved in the related adapter proteins SH2-B and Lnk. These studies reveal a novel mode of phosphopeptide interaction with the Cbl TKB domain, in which N-terminal residues distal to the phosphotyrosine directly contact residues of the four-helix bundle of the TKB domain."xsd:string |
| http://purl.uniprot.org/citations/15737992 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m414157200"xsd:string |
| http://purl.uniprot.org/citations/15737992 | http://purl.uniprot.org/core/author | "Hu J."xsd:string |
| http://purl.uniprot.org/citations/15737992 | http://purl.uniprot.org/core/author | "Hubbard S.R."xsd:string |
| http://purl.uniprot.org/citations/15737992 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/15737992 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/15737992 | http://purl.uniprot.org/core/pages | "18943-18949"xsd:string |
| http://purl.uniprot.org/citations/15737992 | http://purl.uniprot.org/core/title | "Structural characterization of a novel Cbl phosphotyrosine recognition motif in the APS family of adapter proteins."xsd:string |
| http://purl.uniprot.org/citations/15737992 | http://purl.uniprot.org/core/volume | "280"xsd:string |
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| http://purl.uniprot.org/uniprot/O14492 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/15737992 |