| http://purl.uniprot.org/citations/7891724 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/7891724 | http://www.w3.org/2000/01/rdf-schema#comment | "The cytoplasmic serine-threonine protein kinase coded for by the c-akt proto-oncogene features a protein kinase C-like catalytic domain and a unique NH2-terminal domain (AH domain). The AH domain is a member of a domain superfamily whose prototype was observed in pleckstrin (pleckstrin homology, or PH, domain). In this communication, we present evidence that the AH/PH domain is a domain of protein-protein interaction which mediates the formation of Akt protein complexes. The interaction between c-akt AH/PH domains is highly specific, as determined by the failure of this domain to bind AKT2. The AH/PH domain-mediated interactions depend on the integrity of the entire domain. Akt molecules with deletions of the NH2-terminal portion (amino acids 11 to 60) and AH/PH constructs with deletions of the C-terminal portion of this domain (amino acids 107 to 147) fail to interact with c-akt. To determine the significance of these findings, we carried out in vitro kinase assays using Akt immunoprecipitates from serum-starved and serum-starved, platelet-derived growth factor-stimulated NIH 3T3 cells. Addition of maltose-binding protein-AH/PH fusion recombinant protein, which is expected to bind Akt, to the immunoprecipitates from serum-starved cells induced the activation of the Akt kinase."xsd:string |
| http://purl.uniprot.org/citations/7891724 | http://purl.org/dc/terms/identifier | "doi:10.1128/mcb.15.4.2304"xsd:string |
| http://purl.uniprot.org/citations/7891724 | http://purl.uniprot.org/core/author | "Tsichlis P.N."xsd:string |
| http://purl.uniprot.org/citations/7891724 | http://purl.uniprot.org/core/author | "Kaplan D.R."xsd:string |
| http://purl.uniprot.org/citations/7891724 | http://purl.uniprot.org/core/author | "Golemis E.A."xsd:string |
| http://purl.uniprot.org/citations/7891724 | http://purl.uniprot.org/core/author | "Morrison D.K."xsd:string |
| http://purl.uniprot.org/citations/7891724 | http://purl.uniprot.org/core/author | "Datta K."xsd:string |
| http://purl.uniprot.org/citations/7891724 | http://purl.uniprot.org/core/author | "Franke T.F."xsd:string |
| http://purl.uniprot.org/citations/7891724 | http://purl.uniprot.org/core/author | "Makris A."xsd:string |
| http://purl.uniprot.org/citations/7891724 | http://purl.uniprot.org/core/author | "Chan T.O."xsd:string |
| http://purl.uniprot.org/citations/7891724 | http://purl.uniprot.org/core/author | "Yang S.I."xsd:string |
| http://purl.uniprot.org/citations/7891724 | http://purl.uniprot.org/core/date | "1995"xsd:gYear |
| http://purl.uniprot.org/citations/7891724 | http://purl.uniprot.org/core/name | "Mol Cell Biol"xsd:string |
| http://purl.uniprot.org/citations/7891724 | http://purl.uniprot.org/core/pages | "2304-2310"xsd:string |
| http://purl.uniprot.org/citations/7891724 | http://purl.uniprot.org/core/title | "AH/PH domain-mediated interaction between Akt molecules and its potential role in Akt regulation."xsd:string |
| http://purl.uniprot.org/citations/7891724 | http://purl.uniprot.org/core/volume | "15"xsd:string |
| http://purl.uniprot.org/citations/7891724 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/7891724 |
| http://purl.uniprot.org/citations/7891724 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/7891724 |
| http://purl.uniprot.org/uniprot/P31749#attribution-E75F6C6B9BD47F7FB66E113BBBB19369 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/7891724 |
| http://purl.uniprot.org/uniprot/#_P31749-mappedCitation-7891724 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/7891724 |
| http://purl.uniprot.org/uniprot/P31749 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/7891724 |