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GeneQ18034852· pop 5· linked from 2 articles

Also known as ORP-2, ORP2, DFNA67, DNFA67, oxysterol binding protein like 2

Oxysterol-binding protein-related protein 2 is a protein that in humans is encoded by the OSBPL2 gene.

Gene data

OSBPL2
Name
oxysterol binding protein like 2
Type
protein-coding
Position
62,231,922–62,296,213 (+)
Aliases
DFNA67, DIDA, DNFA67, ORP-2, ORP2
RefSeq RNA
NM_001001691.1, NM_001278649.3, NM_001363878.2, NM_014835.5, NM_144498.4
RefSeq protein
NP_001265578.1, NP_001350807.1, NP_055650.1, NP_653081.1

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 the encoded protein contains only the sterol-binding domain. In vitro studies have shown that the encoded protein can bind strongly to phosphatic acid and weakly to phosphatidylinositol 3-phosphate, but cannot bind to 25-hydroxycholesterol. The protein associates with the Golgi apparatus. Transcript variants encoding different isoforms have been described. [provided by RefSeq, Sep 2014].

via MyGene.info

Wikidata facts

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HomoloGene ID
77324
genomic start
60813580
genomic end
60871268
cytogenetic location
20q13.33
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Oxysterol-binding protein-related protein 2 is a protein that in humans is encoded by the OSBPL2 gene.

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. This encoded protein contains only the sterol-binding domain. In vitro studies have shown that the encoded protein can bind strongly to phosphatic acid and weakly to phosphatidylinositol 3-phosphate, but cannot bind to 25-hydroxycholesterol. The protein associates with the Golgi apparatus. Transcript variants encoding different isoforms have been described.

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