| http://purl.uniprot.org/citations/8194526 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/8194526 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/8194526 | http://www.w3.org/2000/01/rdf-schema#comment | "c-Crk is a proto-oncogene product composed largely of Src homology (SH) 2 and 3 domains. We have identified a kinase activity, which binds to the first Crk SH3 domain and phosphorylates c-Crk on tyrosine 221 (Y221), as c-Abl. c-Abl has a strong preference for c-Crk, when compared with common tyrosine kinase substrates. The phosphorylation of c-Crk Y221 creates a binding site for the Crk SH2 domain. Bacterially expressed c-Crk protein lacks phosphorylation on Y221 and can bind specifically to several proteins, while mammalian c-Crk, which is phosphorylated on tyrosine, remains uncomplexed. The protein binding activity of c-Crk is therefore likely regulated by a mechanism similar to that of the Src family kinases. v-Crk is truncated before c-Crk Y221 and forms constitutive complexes with c-Abl and other proteins. Our results suggest that c-Abl regulates c-Crk function and that it could be involved in v-Crk transformation."xsd:string |
| http://purl.uniprot.org/citations/8194526 | http://purl.org/dc/terms/identifier | "doi:10.1002/j.1460-2075.1994.tb06518.x"xsd:string |
| http://purl.uniprot.org/citations/8194526 | http://purl.org/dc/terms/identifier | "doi:10.1002/j.1460-2075.1994.tb06518.x"xsd:string |
| http://purl.uniprot.org/citations/8194526 | http://purl.uniprot.org/core/author | "Hanafusa H."xsd:string |
| http://purl.uniprot.org/citations/8194526 | http://purl.uniprot.org/core/author | "Hanafusa H."xsd:string |
| http://purl.uniprot.org/citations/8194526 | http://purl.uniprot.org/core/author | "Feller S.M."xsd:string |
| http://purl.uniprot.org/citations/8194526 | http://purl.uniprot.org/core/author | "Feller S.M."xsd:string |
| http://purl.uniprot.org/citations/8194526 | http://purl.uniprot.org/core/author | "Knudsen B."xsd:string |
| http://purl.uniprot.org/citations/8194526 | http://purl.uniprot.org/core/author | "Knudsen B."xsd:string |
| http://purl.uniprot.org/citations/8194526 | http://purl.uniprot.org/core/date | "1994"xsd:gYear |
| http://purl.uniprot.org/citations/8194526 | http://purl.uniprot.org/core/date | "1994"xsd:gYear |
| http://purl.uniprot.org/citations/8194526 | http://purl.uniprot.org/core/name | "EMBO J."xsd:string |
| http://purl.uniprot.org/citations/8194526 | http://purl.uniprot.org/core/name | "EMBO J."xsd:string |
| http://purl.uniprot.org/citations/8194526 | http://purl.uniprot.org/core/pages | "2341-2351"xsd:string |
| http://purl.uniprot.org/citations/8194526 | http://purl.uniprot.org/core/pages | "2341-2351"xsd:string |
| http://purl.uniprot.org/citations/8194526 | http://purl.uniprot.org/core/title | "c-Abl kinase regulates the protein binding activity of c-Crk."xsd:string |
| http://purl.uniprot.org/citations/8194526 | http://purl.uniprot.org/core/title | "c-Abl kinase regulates the protein binding activity of c-Crk."xsd:string |
| http://purl.uniprot.org/citations/8194526 | http://purl.uniprot.org/core/volume | "13"xsd:string |
| http://purl.uniprot.org/citations/8194526 | http://purl.uniprot.org/core/volume | "13"xsd:string |
| http://purl.uniprot.org/citations/8194526 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/8194526 |
| http://purl.uniprot.org/citations/8194526 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/8194526 |
| http://purl.uniprot.org/citations/8194526 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/8194526 |
| http://purl.uniprot.org/citations/8194526 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/8194526 |