| http://purl.uniprot.org/citations/10799524 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10799524 | http://www.w3.org/2000/01/rdf-schema#comment | "We recently identified BNIP-2, a previously cloned Bcl-2- and E1B-associated protein, as a putative substrate of the FGF receptor tyrosine kinase and showed that it possesses GTPase-activating activity toward Cdc42 despite the lack of homology to previously described catalytic domains of GTPase-activating proteins (GAPs). BNIP-2 contains many arginine residues at the carboxyl terminus, which includes the region of homology to the noncatalytic domain of Cdc42GAP, termed BNIP-2 and Cdc42GAP homology (BCH) domain. Using BNIP-2 glutathione S-transferase recombinants, it was found that its BCH bound Cdc42, and contributed the GAP activity. This domain was predicted to fold into alpha-helical bundles similar to the topology of the catalytic GAP domain of Cdc42GAP. Alignment of exposed arginine residues in this domain helped to identify Arg-235 and Arg-238 as good candidates for catalysis. Arg-238 matched well to the arginine "finger" required for enhanced GTP hydrolysis in homodimerized Cdc42. Site-directed mutagenesis confirmed that an R235K or R238K mutation severely impaired the BNIP-2 GAP activity without affecting its binding to Cdc42. From deletion studies, a region adjacent to the arginine patch ((288)EYV(290) on BNIP-2) and the Switch I and Rho family-specific "Insert" region on Cdc42 are involved in the binding. The results indicate that the BCH domain of BNIP-2 represents a novel GAP domain that employs an arginine patch motif similar to that of the Cdc42-homodimer."xsd:string |
| http://purl.uniprot.org/citations/10799524 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.275.19.14415"xsd:string |
| http://purl.uniprot.org/citations/10799524 | http://purl.uniprot.org/core/author | "Guy G.R."xsd:string |
| http://purl.uniprot.org/citations/10799524 | http://purl.uniprot.org/core/author | "Low B.C."xsd:string |
| http://purl.uniprot.org/citations/10799524 | http://purl.uniprot.org/core/author | "Seow K.T."xsd:string |
| http://purl.uniprot.org/citations/10799524 | http://purl.uniprot.org/core/date | "2000"xsd:gYear |
| http://purl.uniprot.org/citations/10799524 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/10799524 | http://purl.uniprot.org/core/pages | "14415-14422"xsd:string |
| http://purl.uniprot.org/citations/10799524 | http://purl.uniprot.org/core/title | "Evidence for a novel Cdc42GAP domain at the carboxyl terminus of BNIP-2."xsd:string |
| http://purl.uniprot.org/citations/10799524 | http://purl.uniprot.org/core/volume | "275"xsd:string |
| http://purl.uniprot.org/citations/10799524 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10799524 |
| http://purl.uniprot.org/citations/10799524 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/10799524 |
| http://purl.uniprot.org/uniprot/Q12982#attribution-4B361ECCE3AC9E79AAB6A0F140697A50 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/10799524 |