OSBP

Oxysterol binding protein
Identifiers
Symbols	OSBP; OSBP1
External IDs	OMIM: 167040 MGI: 97447 HomoloGene: 97668 GeneCards: OSBP Gene
Gene Ontology Molecular function • oxysterol binding • lipid binding Cellular component • Golgi membrane • cytoplasm • Golgi apparatus • membrane Biological process • transport • lipid transport Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	5007	76303
Ensembl	ENSG00000110048	ENSMUSG00000024687
UniProt	P22059	n/a
RefSeq (mRNA)	NM_002556	NM_001033174.1
RefSeq (protein)	NP_002547	NP_001028346.1
Location (UCSC)	Chr 11: 59.34 – 59.38 Mb	Chr 19: 12.04 – 12.07 Mb
PubMed search	[1]	[2]

Oxysterol-binding protein 1 is a protein that in humans is encoded by the OSBP gene.^[1]

Oxysterol binding protein is an intracellular protein that is believed to transport sterols from lysosomes to the nucleus where the sterol down-regulates the genes for the LDL receptor, HMG-CoA reductase, and HMG synthetase^[1]

Interactions

OSBP has been shown to interact with VAPA.^[2]

References

1. ^ ^{a b} "Entrez Gene: OSBP oxysterol binding protein". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5007. 
2. ^ Wyles, Jessica P; McMaster Christopher R, Ridgway Neale D (Aug. 2002). "Vesicle-associated membrane protein-associated protein-A (VAP-A) interacts with the oxysterol-binding protein to modify export from the endoplasmic reticulum". J. Biol. Chem. (United States) 277 (33): 29908–18. doi:10.1074/jbc.M201191200. ISSN 0021-9258. PMID 12023275. 

Further reading

• Ridgway ND, Dawson PA, Ho YK et al. (1992). "Translocation of oxysterol binding protein to Golgi apparatus triggered by ligand binding". J. Cell Biol. 116 (2): 307–19. doi:10.1083/jcb.116.2.307. PMC 2289278. PMID 1730758. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2289278. 
• Levanon D, Hsieh CL, Francke U et al. (1990). "cDNA cloning of human oxysterol-binding protein and localization of the gene to human chromosome 11 and mouse chromosome 19". Genomics 7 (1): 65–74. doi:10.1016/0888-7543(90)90519-Z. PMID 1970801. 
• Laitinen S, Olkkonen VM, Ehnholm C, Ikonen E (2000). "Family of human oxysterol binding protein (OSBP) homologues. A novel member implicated in brain sterol metabolism". J. Lipid Res. 40 (12): 2204–11. PMID 10588946. 
• Moreira EF, Jaworski C, Li A, Rodriguez IR (2001). "Molecular and biochemical characterization of a novel oxysterol-binding protein (OSBP2) highly expressed in retina". J. Biol. Chem. 276 (21): 18570–8. doi:10.1074/jbc.M011259200. PMID 11278871. 
• Jaworski CJ, Moreira E, Li A et al. (2002). "A family of 12 human genes containing oxysterol-binding domains". Genomics 78 (3): 185–96. doi:10.1006/geno.2001.6663. PMID 11735225. 
• Wyles JP, McMaster CR, Ridgway ND (2002). "Vesicle-associated membrane protein-associated protein-A (VAP-A) interacts with the oxysterol-binding protein to modify export from the endoplasmic reticulum". J. Biol. Chem. 277 (33): 29908–18. doi:10.1074/jbc.M201191200. PMID 12023275. 
• Strausberg RL, Feingold EA, Grouse LH et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Beausoleil SA, Jedrychowski M, Schwartz D et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=514446. 
• Gerhard DS, Wagner L, Feingold EA et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928. 
• Wang PY, Weng J, Anderson RG (2005). "OSBP is a cholesterol-regulated scaffolding protein in control of ERK 1/2 activation". Science 307 (5714): 1472–6. doi:10.1126/science.1107710. PMID 15746430. 
• Perry RJ, Ridgway ND (2006). "Oxysterol-binding protein and vesicle-associated membrane protein-associated protein are required for sterol-dependent activation of the ceramide transport protein". Mol. Biol. Cell 17 (6): 2604–16. doi:10.1091/mbc.E06-01-0060. PMC 1474796. PMID 16571669. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1474796. 
• Olsen JV, Blagoev B, Gnad F et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.