| http://purl.uniprot.org/citations/14732715 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/14732715 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/14732715 | http://www.w3.org/2000/01/rdf-schema#comment | "Huntingtin-interacting protein 1-related (HIP1r) is the only known mammalian relative of huntingtin-interacting protein 1 (HIP1), a protein that transforms fibroblasts via undefined mechanisms. Here we demonstrate that both HIP1r and HIP1 bind inositol lipids via their epsin N-terminal homology (ENTH) domains. In contrast to other ENTH domain-containing proteins, lipid binding is preferential to the 3-phosphate-containing inositol lipids, phosphatidylinositol 3,4-bisphosphate and phosphatidylinositol 3,5-bisphosphate. Furthermore, the HIP1r ENTH domain, like that of HIP1, is necessary for lipid binding, and expression of an ENTH domain-deletion mutant, HIP1r/deltaE, induces apoptosis. Consistent with the ability of HIP1r and HIP1 to affect cell survival, full-length HIP1 and HIP1r stabilize pools of growth factor receptors by prolonging their half-life following ligand-induced endocytosis. Although HIP1r and HIP1 display only a partially overlapping pattern of protein interactions, these data suggest that both proteins share a functional homology by binding 3-phosphorylated inositol lipids and stabilizing receptor tyrosine kinases in a fashion that may contribute to their ability to alter cell growth and survival."xsd:string |
| http://purl.uniprot.org/citations/14732715 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m312645200"xsd:string |
| http://purl.uniprot.org/citations/14732715 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m312645200"xsd:string |
| http://purl.uniprot.org/citations/14732715 | http://purl.uniprot.org/core/author | "Ross T.S."xsd:string |
| http://purl.uniprot.org/citations/14732715 | http://purl.uniprot.org/core/author | "Ross T.S."xsd:string |
| http://purl.uniprot.org/citations/14732715 | http://purl.uniprot.org/core/author | "Saint-Dic D."xsd:string |
| http://purl.uniprot.org/citations/14732715 | http://purl.uniprot.org/core/author | "Saint-Dic D."xsd:string |
| http://purl.uniprot.org/citations/14732715 | http://purl.uniprot.org/core/author | "Bradley S.V."xsd:string |
| http://purl.uniprot.org/citations/14732715 | http://purl.uniprot.org/core/author | "Bradley S.V."xsd:string |
| http://purl.uniprot.org/citations/14732715 | http://purl.uniprot.org/core/author | "Hyun T.S."xsd:string |
| http://purl.uniprot.org/citations/14732715 | http://purl.uniprot.org/core/author | "Hyun T.S."xsd:string |
| http://purl.uniprot.org/citations/14732715 | http://purl.uniprot.org/core/author | "Kumar P.D."xsd:string |
| http://purl.uniprot.org/citations/14732715 | http://purl.uniprot.org/core/author | "Kumar P.D."xsd:string |
| http://purl.uniprot.org/citations/14732715 | http://purl.uniprot.org/core/author | "Michael L.E."xsd:string |
| http://purl.uniprot.org/citations/14732715 | http://purl.uniprot.org/core/author | "Michael L.E."xsd:string |
| http://purl.uniprot.org/citations/14732715 | http://purl.uniprot.org/core/author | "Mizukami I.F."xsd:string |
| http://purl.uniprot.org/citations/14732715 | http://purl.uniprot.org/core/author | "Mizukami I.F."xsd:string |
| http://purl.uniprot.org/citations/14732715 | http://purl.uniprot.org/core/author | "Oravecz-Wilson K.I."xsd:string |
| http://purl.uniprot.org/citations/14732715 | http://purl.uniprot.org/core/author | "Oravecz-Wilson K.I."xsd:string |
| http://purl.uniprot.org/citations/14732715 | http://purl.uniprot.org/core/author | "Rao D.S."xsd:string |
| http://purl.uniprot.org/citations/14732715 | http://purl.uniprot.org/core/author | "Rao D.S."xsd:string |
| http://purl.uniprot.org/citations/14732715 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/14732715 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |