Q9BXB5 · OSB10_HUMAN
- ProteinOxysterol-binding protein-related protein 10
- GeneOSBPL10
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids764 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Plays a role in negative regulation of lipid biosynthesis (PubMed:19554302).
Negatively regulates APOB secretion from hepatocytes (PubMed:19554302, PubMed:22906437).
Binds cholesterol and acidic phospholipids (PubMed:22906437).
Also binds 25-hydroxycholesterol (PubMed:17428193).
Binds phosphatidylserine (PubMed:23934110).
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 413-418 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) (UniProtKB | ChEBI) | ||||
Sequence: LTKVVL | ||||||
Binding site | 413-418 | a 1,2-diacyl-sn-glycero-3-phospho-L-serine (UniProtKB | ChEBI) | ||||
Sequence: LTKVVL | ||||||
Binding site | 477-480 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) (UniProtKB | ChEBI) | ||||
Sequence: KPYN | ||||||
Binding site | 480 | a 1,2-diacyl-sn-glycero-3-phospho-L-serine (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 535-536 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) (UniProtKB | ChEBI) | ||||
Sequence: HH | ||||||
Binding site | 561 | a 1,2-diacyl-sn-glycero-3-phospho-L-serine (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 721 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 725 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 729 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoskeleton | |
Cellular Component | cytosol | |
Cellular Component | membrane | |
Molecular Function | cholesterol binding | |
Molecular Function | phosphatidylserine binding | |
Molecular Function | phospholipid transporter activity | |
Biological Process | phosphatidylserine acyl-chain remodeling |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Chemistry
Names & Taxonomy
Protein names
- Recommended nameOxysterol-binding protein-related protein 10
- Short namesORP-10; OSBP-related protein 10
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9BXB5
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_022100 | 254 | in dbSNP:rs2290532 | |||
Sequence: N → D |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 867 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000100380 | 1-764 | UniProt | Oxysterol-binding protein-related protein 10 | |||
Sequence: MERAVQGTDGGGGSNSSSRSSSRATSAGSSPSCSLAGRGVSSRSAAAGLGGGGSRSSPGSVAASPSGGGGRRREPALEGVLSKYTNLLQGWQNRYFVLDFEAGILQYFVNEQSKHQKPRGVLSLSGAIVSLSDEAPHMLVVYSANGEMFKLRAADAKEKQFWVTQLRACAKYHMEMNSKSAPSSRSRSLTLLPHGTPNSASPCSQRHLSVGAPGVVTITHHKSPAAARRAKSQYSGQLHEVREMMNQVEGQQKNLVHAIESLPGSGPLTALDQDLLLLKATSAATLSCLGECLNLLQQSVHQAGQPSQKPGASENILGWHGSKSHSTEQLKNGTLGSLPSASANITWAILPNSAEDEQTSQPEPEPNSGSELVLSEDEKSDNEDKEETELGVMEDQRSIILHLISQLKLGMDLTKVVLPTFILEKRSLLEMYADFMAHPDLLLAITAGATPEERVICFVEYYLTAFHEGRKGALAKKPYNPIIGETFHCSWEVPKDRVKPKRTASRSPASCHEHPMADDPSKSYKLRFVAEQVSHHPPISCFYCECEEKRLCVNTHVWTKSKFMGMSVGVSMIGEGVLRLLEHGEEYVFTLPSAYARSILTIPWVELGGKVSINCAKTGYSATVIFHTKPFYGGKVHRVTAEVKHNPTNTIVCKAHGEWNGTLEFTYNNGETKVIDTTTLPVYPKKIRPLEKQGPMESRNLWREVTRYLRLGDIDAATEQKRHLEEKQRVEERKRENLRTPWKPKYFIQEGDGWVYFNPLWKAH | |||||||
Modified residue (large scale data) | 26 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 29 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 29 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 30 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 30 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 38 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue (large scale data) | 54 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 57 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 57 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 60 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 60 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 64 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 64 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 186 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 188 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 190 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 196 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 196 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 199 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 201 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 201 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 209 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 209 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 219 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 223 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 223 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 232 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 235 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 265 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 322 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 326 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 380 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 507 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 510 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9BXB5 | OSBPL9 Q96SU4 | 3 | EBI-2511286, EBI-2511368 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-74 | Disordered | ||||
Sequence: MERAVQGTDGGGGSNSSSRSSSRATSAGSSPSCSLAGRGVSSRSAAAGLGGGGSRSSPGSVAASPSGGGGRRRE | ||||||
Compositional bias | 9-39 | Polar residues | ||||
Sequence: DGGGGSNSSSRSSSRATSAGSSPSCSLAGRG | ||||||
Domain | 74-171 | PH | ||||
Sequence: EPALEGVLSKYTNLLQGWQNRYFVLDFEAGILQYFVNEQSKHQKPRGVLSLSGAIVSLSDEAPHMLVVYSANGEMFKLRAADAKEKQFWVTQLRACAK | ||||||
Region | 304-335 | Disordered | ||||
Sequence: GQPSQKPGASENILGWHGSKSHSTEQLKNGTL | ||||||
Compositional bias | 319-335 | Polar residues | ||||
Sequence: WHGSKSHSTEQLKNGTL | ||||||
Compositional bias | 354-368 | Polar residues | ||||
Sequence: AEDEQTSQPEPEPNS | ||||||
Region | 354-391 | Disordered | ||||
Sequence: AEDEQTSQPEPEPNSGSELVLSEDEKSDNEDKEETELG | ||||||
Region | 501-520 | Disordered | ||||
Sequence: KRTASRSPASCHEHPMADDP | ||||||
Coiled coil | 713-740 | |||||
Sequence: DIDAATEQKRHLEEKQRVEERKRENLRT |
Domain
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q9BXB5-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length764
- Mass (Da)83,970
- Last updated2002-02-11 v2
- Checksum62B1DF599C7C15FC
Q9BXB5-2
- Name2
- Differences from canonical
- 180-243: Missing
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A5F9ZH75 | A0A5F9ZH75_HUMAN | OSBPL10 | 371 | ||
H7C487 | H7C487_HUMAN | OSBPL10 | 538 | ||
H7C199 | H7C199_HUMAN | OSBPL10 | 173 | ||
A0A8V8TM06 | A0A8V8TM06_HUMAN | OSBPL10 | 392 |
Features
Showing features for compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 9-39 | Polar residues | ||||
Sequence: DGGGGSNSSSRSSSRATSAGSSPSCSLAGRG | ||||||
Alternative sequence | VSP_042930 | 180-243 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 319-335 | Polar residues | ||||
Sequence: WHGSKSHSTEQLKNGTL | ||||||
Compositional bias | 354-368 | Polar residues | ||||
Sequence: AEDEQTSQPEPEPNS |
Polymorphism
Association with peripheral arterial disease has also been observed (PubMed:20610895).
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF392451 EMBL· GenBank· DDBJ | AAL40664.1 EMBL· GenBank· DDBJ | mRNA | ||
AK304067 EMBL· GenBank· DDBJ | BAG64974.1 EMBL· GenBank· DDBJ | mRNA | ||
AC092024 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC094019 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC107620 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC108485 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC003168 EMBL· GenBank· DDBJ | AAH03168.2 EMBL· GenBank· DDBJ | mRNA | ||
AF346291 EMBL· GenBank· DDBJ | AAK31140.1 EMBL· GenBank· DDBJ | mRNA |