OSBP

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Oxysterol binding protein
Identifiers
Symbols OSBP ; OSBP1
External IDs Template:OMIM5 Template:MGI HomoloGene1919
RNA expression pattern
File:PBB GE OSBP 201800 s at tn.png
File:PBB GE OSBP 201799 s at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

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]

References

  1. 1.0 1.1 "Entrez Gene: OSBP oxysterol binding protein".

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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