OSBPL1A: Difference between revisions
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'''Oxysterol-binding protein-related protein 1''' is a [[protein]] that in [[Human|humans]] is encoded by the ''OSBPL1A'' [[gene]].<ref name="pmid11279184">{{cite journal | vauthors = Xu Y, Liu Y, Ridgway ND, McMaster CR | title = Novel members of the human oxysterol-binding protein family bind phospholipids and regulate vesicle transport | journal = J Biol Chem | volume = 276 | issue = 21 | pages = 18407–14 |date=May 2001 | pmid = 11279184 | pmc = | doi = 10.1074/jbc.M101204200 }}</ref><ref name="pmid10588946">{{cite journal | vauthors = Laitinen S, Olkkonen VM, Ehnholm C, Ikonen E | title = Family of human oxysterol binding protein (OSBP) homologues. A novel member implicated in brain sterol metabolism | journal = J Lipid Res | volume = 40 | issue = 12 | pages = 2204–11 |date=Feb 2000 | pmid = 10588946 | pmc = | doi = }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: OSBPL1A oxysterol binding protein-like 1A| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=114876| accessdate = }}</ref> | '''Oxysterol-binding protein-related protein 1''' is a [[protein]] that in [[Human|humans]] is encoded by the ''OSBPL1A'' [[gene]].<ref name="pmid11279184">{{cite journal | vauthors = Xu Y, Liu Y, Ridgway ND, McMaster CR | title = Novel members of the human oxysterol-binding protein family bind phospholipids and regulate vesicle transport | journal = J Biol Chem | volume = 276 | issue = 21 | pages = 18407–14 |date=May 2001 | pmid = 11279184 | pmc = | doi = 10.1074/jbc.M101204200 }}</ref><ref name="pmid10588946">{{cite journal | vauthors = Laitinen S, Olkkonen VM, Ehnholm C, Ikonen E | title = Family of human oxysterol binding protein (OSBP) homologues. A novel member implicated in brain sterol metabolism | journal = J Lipid Res | volume = 40 | issue = 12 | pages = 2204–11 |date=Feb 2000 | pmid = 10588946 | pmc = | doi = }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: OSBPL1A oxysterol binding protein-like 1A| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=114876| accessdate = }}</ref> | ||
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{{PBB_Summary | {{PBB_Summary | ||
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| summary_text = This gene encodes a member of the [[oxysterol-binding protein]] (OSBP) family, a group of intracellular lipid receptors. Most members contain an N-terminal pleckstrin homology domain and a highly conserved C-terminal OSBP-like sterol-binding domain, although some members contain only the sterol-binding domain. Transcript variants derived from alternative promoter usage and/or alternative splicing exist; they encode different isoforms.<ref name="entrez">{{cite web | title = Entrez Gene: OSBPL1A oxysterol binding protein-like 1A| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=114876| accessdate = }}</ref> | | summary_text = This gene encodes a member of the [[oxysterol-binding protein]] (OSBP) family, a group of intracellular [[lipid]] receptors. Most members contain an N-terminal [[pleckstrin homology domain]] and a highly conserved C-terminal OSBP-like sterol-binding domain, although some members contain only the sterol-binding domain. [[Transcript variants]] derived from alternative promoter usage and/or alternative splicing exist; they encode different [[isoforms]].<ref name="entrez">{{cite web | title = Entrez Gene: OSBPL1A oxysterol binding protein-like 1A| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=114876| accessdate = }}</ref> | ||
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Latest revision as of 09:04, 9 January 2019
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Oxysterol-binding protein-related protein 1 is a protein that in humans is encoded by the OSBPL1A gene.[1][2][3]
This gene encodes a member of the oxysterol-binding protein (OSBP) family, a group of intracellular lipid receptors. Most members contain an N-terminal pleckstrin homology domain and a highly conserved C-terminal OSBP-like sterol-binding domain, although some members contain only the sterol-binding domain. Transcript variants derived from alternative promoter usage and/or alternative splicing exist; they encode different isoforms.[3]
References
- ↑ Xu Y, Liu Y, Ridgway ND, McMaster CR (May 2001). "Novel members of the human oxysterol-binding protein family bind phospholipids and regulate vesicle transport". J Biol Chem. 276 (21): 18407–14. doi:10.1074/jbc.M101204200. PMID 11279184.
- ↑ Laitinen S, Olkkonen VM, Ehnholm C, Ikonen E (Feb 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.
- ↑ 3.0 3.1 "Entrez Gene: OSBPL1A oxysterol binding protein-like 1A".
Further reading
- Lehto M, Laitinen S, Chinetti G, et al. (2001). "The OSBP-related protein family in humans". J. Lipid Res. 42 (8): 1203–13. PMID 11483621.
- 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.
- 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.
- Johansson M, Bocher V, Lehto M, et al. (2004). "The two variants of oxysterol binding protein-related protein-1 display different tissue expression patterns, have different intracellular localization, and are functionally distinct". Mol. Biol. Cell. 14 (3): 903–15. doi:10.1091/mbc.E02-08-0459. PMC 151568. PMID 12631712.
- Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
- Johansson M, Lehto M, Tanhuanpää K, et al. (2006). "The oxysterol-binding protein homologue ORP1L interacts with Rab7 and alters functional properties of late endocytic compartments". Mol. Biol. Cell. 16 (12): 5480–92. doi:10.1091/mbc.E05-03-0189. PMC 1289395. PMID 16176980.
- 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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