OSBPL2
entrez
9885
canonical
uniprot
Q9H1P3
canonical
ensembl
ENSG00000130703
resolver
ensp
ENSP00000316649
resolver
ensp
ENSP00000350755
resolver
ensp
ENSP00000397602
resolver
ensp
ENSP00000494921
resolver
ensp
ENSP00000495166
resolver
enst
ENST00000439951
resolver
enst
ENST00000645442
resolver
enst
ENST00000645520
resolver
genesymbol
OSBPL2
resolver
genesymbol_syn
KIAA0772
resolver
genesymbol_syn
ORP2
resolver
hgnc
HGNC:15761
resolver
uniprot
A0A2R8YDU7
resolver
uniprot
A8K736
resolver
uniprot
B4DKJ8
resolver
uniprot
E7ET92
resolver
uniprot
Q6IBT0
resolver
uniprot
Q9BZB1
resolver
uniprot
Q9Y4B8
resolver
uniprot_entry
A0A2R8YDU7_HUMAN
resolver
uniprot_entry
B4DKJ8_HUMAN
resolver
uniprot_entry
E7ET92_HUMAN
resolver
uniprot_entry
OSBL2_HUMAN
resolver
uniprot_sec
A8K736
resolver
uniprot_sec
Q6IBT0
resolver
uniprot_sec
Q9BZB1
resolver
uniprot_sec
Q9Y4B8
resolver
amino_acid_sequence
MNGEEEFFDAVTGFDSDNSSGEFSEANQKVTGMIDLDTSKNNRIGKTGERPSQENGIQKHRTSLPAPMFSRSDFSVWTILKKCVGLELSKITMPIAFNEPLSFLQRITEYMEHVYLIHRASCQPQPLERMQSVAAFAVSAVASQWERTGKPFNPLLGETYELIREDLGFRFISEQVSHHPPISAFHSEGLNHDFLFHGSIYPKLKFWGKSVEAEPRGTITLELLKHNEAYTWTNPTCCVHNVIIGKLWIEQYGTVEILNHRTGHKCVLHFKPCGLFGKELHKVEGHIQDKNKKKLFMIYGKWTECLWGIDPVSYESFKKQERRGDHLRKAKLDEDSGKADSDVADDVPVAQETVQVIPGSKLLWRINTRPPNSAQMYNFTSFTVSLNELETGMEKTLPPTDCRLRPDIRGMENGNMDLASQEKERLEEKQREARRERAKEEAEWQTRWFYPGNNPYTGTPDWLYAGDYFERNFSDCPDIY
uniprot
proteins
disease_involvement
DISEASE: Deafness, autosomal dominant, 67 (DFNA67) [MIM:616340]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. {ECO:0000269|PubMed:25077649, ECO:0000269|PubMed:25759012, ECO:0000269|PubMed:30894143}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Dyschromatosis, ichthyosis, deafness, and atopic disease (DIDA) [MIM:621400]: An autosomal recessive disease characterized by generalized hyperpigmentation with hypopigmentation spots, ichthyosis, sensorineural hearing loss, atopic dermatitis, asthma, and allergic rhinitis. {ECO:0000269|PubMed:38701954}. Note=The disease may be caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Intracellular transport protein that binds sterols and phospholipids and mediates lipid transport between intracellular compartments (PubMed:30581148, PubMed:32914503). Increases plasma membrane cholesterol levels and decreases phosphatidylinositol-4,5-bisphosphate levels in the cell membrane (PubMed:30581148, PubMed:32914503, PubMed:34124795). Exhibits strong binding to phosphatidic acid and weak binding to phosphatidylinositol 3-phosphate (PubMed:11279184). Binds cholesterol, dehydroergosterol, 22(R)-hydroxycholesterol and 25-hydroxycholesterol (in vitro) (PubMed:17428193, PubMed:19224871, PubMed:30581148). In conjunction with PLCB3, it may contribute to the control of keratinocyte proliferation and differentiation, probably through the regulation of the ERK pathway and the cell cycle (PubMed:38701954). Involved in angiogenic signaling pathways such as VEGFR2 in endothelial cells (PubMed:32914503). Controls LDL-cholesterol plasma membrane delivery, focal adhesion kinase (FAK) activation and PI(4,5)P2 generation, enhancing cell adhesion (PubMed:34124795). {ECO:0000269|PubMed:17428193, ECO:0000269|PubMed:19224871, ECO:0000269|PubMed:30581148, ECO:0000269|PubMed:32914503, ECO:0000269|PubMed:34124795, ECO:0000269|PubMed:38701954}.
uniprot
proteins
mass_dalton
55201
uniprot
proteins
mutagenesis
MUTAGEN 79; /note="I->A: No effect on phosphatidylinositide binding, but impaired tetramerization and decreased cholesterol binding, plus decreased cholesterol and phosphatidylinositide transport."; /evidence="ECO:0000269|PubMed:30581148"; MUTAGEN 83; /note="C->A: No effect on phosphatidylinositide binding, but impaired tetramerization and decreased cholesterol binding, plus decreased cholesterol and phosphatidylinositide transport."; /evidence="ECO:0000269|PubMed:30581148"; MUTAGEN 87..90; /note="Missing: Loss of the ability to promote cholesterol accumulation at the cell membrane. No effect on phosphatidylinositide levels at the cell membrane."; /evidence="ECO:0000269|PubMed:30581148"; MUTAGEN 93; /note="M->K: Mildly decreased 25-hydroxycholesterol binding."; /evidence="ECO:0000269|PubMed:17428193"; MUTAGEN 103; /note="F->W: Mildly decreased 25-hydroxycholesterol binding."; /evidence="ECO:0000269|PubMed:17428193"; MUTAGEN 110; /note="Y->A: No effect on phosphatidylinositide binding, but decreased cholesterol binding, plus decreased cholesterol and phosphatidylinositide transport."; /evidence="ECO:0000269|PubMed:30581148"; MUTAGEN 150; /note="K->A: Reduces 25-hydroxycholesterol binding."; /evidence="ECO:0000269|PubMed:17428193"; MUTAGEN 152; /note="F->D: Does not significantly impair 25-hydroxycholesterol binding."; /evidence="ECO:0000269|PubMed:17428193"; MUTAGEN 178..179; /note="HH->DD: Loss of increased cholesterol and decreased phosphatidylinositide accumulation at the cell membrane."; /evidence="ECO:0000269|PubMed:30581148"; MUTAGEN 215; /note="P->A: No effect on phosphatidylinositide binding, but decreased cholesterol binding, plus decreased cholesterol and phosphatidylinositide transport."; /evidence="ECO:0000269|PubMed:30581148"; MUTAGEN 249; /note="I->W: Reduces 25-hydroxycholesterol binding. Loss of 22(R)-hydroxycholesterol binding."; /evidence="ECO:0000269|PubMed:17428193, ECO:0000269|PubMed:19224871"; MUTAGEN 423; /note="K->A: Loss of increased cholesterol and decreased phosphatidylinositide accumulation at the cell membrane."; /evidence="ECO:0000269|PubMed:30581148
uniprot
proteins
protein_family
OSBP family
uniprot
proteins
pubmed
11279184
uniprot
proteins
pubmed
11483621
uniprot
proteins
pubmed
11735225
uniprot
proteins
pubmed
11780052
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17428193
uniprot
proteins
pubmed
19224871
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23325789
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25077649
uniprot
proteins
pubmed
25759012
uniprot
proteins
pubmed
30581148
uniprot
proteins
pubmed
30894143
uniprot
proteins
pubmed
32914503
uniprot
proteins
pubmed
34124795
uniprot
proteins
pubmed
38701954
uniprot
proteins
pubmed
9872452
uniprot
proteins
sequence_length
480
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:19224871, ECO:0000269|PubMed:30581148}. Lipid droplet {ECO:0000269|PubMed:19224871}. Cell membrane {ECO:0000269|PubMed:30581148}; Peripheral membrane protein {ECO:0000269|PubMed:30581148}; Cytoplasmic side {ECO:0000269|PubMed:30581148}. Cell projection, stereocilium {ECO:0000250|UniProtKB:Q8BX94}. Note=Detected on the surface of cytosolic lipid droplets (PubMed:19224871). Recruited to the cell membrane by phosphatidylinositol-phosphate binding (PubMed:30581148). {ECO:0000269|PubMed:19224871, ECO:0000269|PubMed:30581148}.
uniprot
proteins