OSBP

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Oxysterol binding protein
Identifiers
Symbol(s) OSBP; OSBP1
External IDs OMIM: 167040 MGI: 97447 HomoloGene: 1919
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 5007 76303
Ensembl ENSG00000110048 ENSMUSG00000024687
Uniprot P22059 n/a
Refseq NM_002556 (mRNA)
NP_002547 (protein)		 XM_148904 (mRNA)
XP_148904 (protein)
Location Chr 11: 59.1 - 59.14 Mb Chr 19: 12.03 - 12.06 Mb
Pubmed search [1] [2]

Oxysterol binding protein, also known as OSBP, is a human 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]

[edit] References

  1. ^ a b Entrez Gene: OSBP oxysterol binding protein.

[edit] 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. PMID 1730758. 
  • 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. 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. PMID 12477932. 
  • 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. PMID 15302935. 
  • 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. PMID 15489334. 
  • 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. PMID 16571669. 
  • 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. 
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