| http://purl.uniprot.org/citations/16000296 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16000296 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16000296 | http://www.w3.org/2000/01/rdf-schema#comment | "Covalent lipid modifications mediate the membrane attachment and biological activity of Ras proteins. All Ras isoforms are farnesylated and carboxyl-methylated at the terminal cysteine; H-Ras and N-Ras are further modified by palmitoylation. Yeast Ras is palmitoylated by the DHHC cysteine-rich domain-containing protein Erf2 in a complex with Erf4. Here we report that H- and N-Ras are palmitoylated by a human protein palmitoyltransferase encoded by the ZDHHC9 and GCP16 genes. DHHC9 is an integral membrane protein that contains a DHHC cysteine-rich domain. GCP16 encodes a Golgi-localized membrane protein that has limited sequence similarity to yeast Erf4. DHHC9 and GCP16 co-distribute in the Golgi apparatus, a location consistent with the site of mammalian Ras palmitoylation in vivo. Like yeast Erf2.Erf4, DHHC9 and GCP16 form a protein complex, and DHHC9 requires GCP16 for protein fatty acyltransferase activity and protein stability. Purified DHHC9.GCP16 exhibits substrate specificity, palmitoylating H- and N-Ras but not myristoylated G (alphai1) or GAP-43, proteins with N-terminal palmitoylation motifs. Hence, DHHC9.GCP16 displays the properties of a functional human ortholog of the yeast Ras palmitoyltransferase."xsd:string |
| http://purl.uniprot.org/citations/16000296 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m504113200"xsd:string |
| http://purl.uniprot.org/citations/16000296 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m504113200"xsd:string |
| http://purl.uniprot.org/citations/16000296 | http://purl.uniprot.org/core/author | "Lobo S."xsd:string |
| http://purl.uniprot.org/citations/16000296 | http://purl.uniprot.org/core/author | "Lobo S."xsd:string |
| http://purl.uniprot.org/citations/16000296 | http://purl.uniprot.org/core/author | "Deschenes R.J."xsd:string |
| http://purl.uniprot.org/citations/16000296 | http://purl.uniprot.org/core/author | "Deschenes R.J."xsd:string |
| http://purl.uniprot.org/citations/16000296 | http://purl.uniprot.org/core/author | "Farh L."xsd:string |
| http://purl.uniprot.org/citations/16000296 | http://purl.uniprot.org/core/author | "Farh L."xsd:string |
| http://purl.uniprot.org/citations/16000296 | http://purl.uniprot.org/core/author | "Greentree W.K."xsd:string |
| http://purl.uniprot.org/citations/16000296 | http://purl.uniprot.org/core/author | "Greentree W.K."xsd:string |
| http://purl.uniprot.org/citations/16000296 | http://purl.uniprot.org/core/author | "Linder M.E."xsd:string |
| http://purl.uniprot.org/citations/16000296 | http://purl.uniprot.org/core/author | "Linder M.E."xsd:string |
| http://purl.uniprot.org/citations/16000296 | http://purl.uniprot.org/core/author | "Croke M.R."xsd:string |
| http://purl.uniprot.org/citations/16000296 | http://purl.uniprot.org/core/author | "Croke M.R."xsd:string |
| http://purl.uniprot.org/citations/16000296 | http://purl.uniprot.org/core/author | "Swarthout J.T."xsd:string |
| http://purl.uniprot.org/citations/16000296 | http://purl.uniprot.org/core/author | "Swarthout J.T."xsd:string |
| http://purl.uniprot.org/citations/16000296 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/16000296 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/16000296 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/16000296 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/16000296 | http://purl.uniprot.org/core/pages | "31141-31148"xsd:string |
| http://purl.uniprot.org/citations/16000296 | http://purl.uniprot.org/core/pages | "31141-31148"xsd:string |