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P22059

- OSBP1_HUMAN

UniProt

P22059 - OSBP1_HUMAN

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Protein
Oxysterol-binding protein 1
Gene
OSBP, OSBP1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Binds cholesterol and a range of oxysterols. Cholesterol binding promotes the formation of a complex with PP2A and a tyrosine phosphatase which dephosphorylate ERK1/2, whereas 25-hydroxycholesterol causes its disassembly. Regulates cholesterol efflux by decreasing ABCA1 stability.2 Publications

GO - Molecular functioni

  1. oxysterol binding Source: ProtInc

GO - Biological processi

  1. lipid transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Lipid transport, Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiREACT_115810. Sphingolipid de novo biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Oxysterol-binding protein 1
Gene namesi
Name:OSBP
Synonyms:OSBP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:8503. OSBP.

Subcellular locationi

Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein
Note: When bound to oxysterols, translocates to the periphery of Golgi membranes.

GO - Cellular componenti

  1. Golgi apparatus Source: HPA
  2. Golgi membrane Source: UniProtKB-SubCell
  3. cell junction Source: HPA
  4. cytoplasm Source: HPA
  5. nucleolus Source: HPA
  6. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA32822.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 807807Oxysterol-binding protein 1
PRO_0000100364Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei190 – 1901Phosphoserine6 Publications
Modified residuei193 – 1931Phosphoserine7 Publications
Modified residuei198 – 1981Phosphoserine1 Publication
Modified residuei240 – 2401Phosphoserine By similarity
Modified residuei351 – 3511Phosphoserine7 Publications
Modified residuei382 – 3821Phosphoserine4 Publications
Modified residuei389 – 3891Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP22059.
PaxDbiP22059.
PeptideAtlasiP22059.
PRIDEiP22059.

PTM databases

PhosphoSiteiP22059.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

ArrayExpressiP22059.
BgeeiP22059.
CleanExiHS_OSBP.
GenevestigatoriP22059.

Organism-specific databases

HPAiHPA039227.
HPA043625.

Interactioni

Subunit structurei

Homodimer or homotrimer. Interacts with VAPA.1 Publication

Protein-protein interaction databases

BioGridi111048. 28 interactions.
IntActiP22059. 2 interactions.
MINTiMINT-5005941.
STRINGi9606.ENSP00000263847.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi377 – 3793

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RR3NMR-B346-379[»]
ProteinModelPortaliP22059.
SMRiP22059. Positions 91-180, 346-380, 405-801.

Miscellaneous databases

EvolutionaryTraceiP22059.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini88 – 18194PH
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni406 – 45752Sterol binding By similarity
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili291 – 32636 Reviewed prediction
Add
BLAST
Coiled coili730 – 76031 Reviewed prediction
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1 – 9393Ala/Gly-rich
Add
BLAST

Domaini

The PH and Ala/Gly-rich domains control cholesterol binding without affecting 25-hydroxycholesterol binding By similarity.
The second coiled-coil domain is required for interaction with the tyrosine phosphatase By similarity.

Sequence similaritiesi

Belongs to the OSBP family.
Contains 1 PH domain.

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG281324.
HOGENOMiHOG000231233.
HOVERGENiHBG053374.
InParanoidiP22059.
OMAiEYWECKE.
OrthoDBiEOG7MPRD7.
PhylomeDBiP22059.
TreeFamiTF320922.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR000648. Oxysterol-bd.
IPR018494. Oxysterol-bd_CS.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
[Graphical view]
PANTHERiPTHR10972. PTHR10972. 1 hit.
PfamiPF01237. Oxysterol_BP. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
[Graphical view]
PROSITEiPS01013. OSBP. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P22059-1 [UniParc]FASTAAdd to Basket

« Hide

MAATELRGVV GPGPAAIAAL GGGGAGPPVV GGGGGRGDAG PGSGAASGTV    50
VAAAAGGPGP GAGGVAAAGP APAPPTGGSG GSGAGGSGSA REGWLFKWTN 100
YIKGYQRRWF VLSNGLLSYY RSKAEMRHTC RGTINLATAN ITVEDSCNFI 150
ISNGGAQTYH LKASSEVERQ RWVTALELAK AKAVKMLAES DESGDEESVS 200
QTDKTELQNT LRTLSSKVED LSTCNDLIAK HGTALQRSLS ELESLKLPAE 250
SNEKIKQVNE RATLFRITSN AMINACRDFL MLAQTHSKKW QKSLQYERDQ 300
RIRLEETLEQ LAKQHNHLER AFRGATVLPA NTPGNVGSGK DQCCSGKGDM 350
SDEDDENEFF DAPEIITMPE NLGHKRTGSN ISGASSDISL DEQYKHQLEE 400
TKKEKRTRIP YKPNYSLNLW SIMKNCIGKE LSKIPMPVNF NEPLSMLQRL 450
TEDLEYHELL DRAAKCENSL EQLCYVAAFT VSSYSTTVFR TSKPFNPLLG 500
ETFELDRLEE NGYRSLCEQV SHHPPAAAHH AESKNGWTLR QEIKITSKFR 550
GKYLSIMPLG TIHCIFHATG HHYTWKKVTT TVHNIIVGKL WIDQSGEIDI 600
VNHKTGDKCN LKFVPYSYFS RDVARKVTGE VTDPSGKVHF ALLGTWDEKM 650
ECFKVQPVIG ENGGDARQRG HEAEESRVML WKRNPLPKNA ENMYYFSELA 700
LTLNAWESGT APTDSRLRPD QRLMENGRWD EANAEKQRLE EKQRLSRKKR 750
EAEAMKATED GTPYDPYKAL WFERKKDPVT KELTHIYRGE YWECKEKQDW 800
SSCPDIF 807
Length:807
Mass (Da):89,421
Last modified:August 1, 1991 - v1
Checksum:i2590A47BCB54FDFB
GO

Sequence cautioni

The sequence AAH63121.1 differs from that shown. Reason: Aberrant splicing.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti278 – 2781D → A in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036099

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M86917 mRNA. Translation: AAA59973.1.
AF185696 mRNA. Translation: AAG17011.1.
AF185705
, AF185697, AF185698, AF185699, AF185700, AF185701, AF185702, AF185703, AF185704 Genomic DNA. Translation: AAG28373.1.
BC011581 mRNA. Translation: AAH11581.1.
BC063121 mRNA. Translation: AAH63121.1. Sequence problems.
CCDSiCCDS7974.1.
PIRiA34581.
RefSeqiNP_002547.1. NM_002556.2.
UniGeneiHs.597091.

Genome annotation databases

EnsembliENST00000263847; ENSP00000263847; ENSG00000110048.
GeneIDi5007.
KEGGihsa:5007.
UCSCiuc001noc.1. human.

Polymorphism databases

DMDMi129308.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M86917 mRNA. Translation: AAA59973.1 .
AF185696 mRNA. Translation: AAG17011.1 .
AF185705
, AF185697 , AF185698 , AF185699 , AF185700 , AF185701 , AF185702 , AF185703 , AF185704 Genomic DNA. Translation: AAG28373.1 .
BC011581 mRNA. Translation: AAH11581.1 .
BC063121 mRNA. Translation: AAH63121.1 . Sequence problems.
CCDSi CCDS7974.1.
PIRi A34581.
RefSeqi NP_002547.1. NM_002556.2.
UniGenei Hs.597091.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2RR3 NMR - B 346-379 [» ]
ProteinModelPortali P22059.
SMRi P22059. Positions 91-180, 346-380, 405-801.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111048. 28 interactions.
IntActi P22059. 2 interactions.
MINTi MINT-5005941.
STRINGi 9606.ENSP00000263847.

PTM databases

PhosphoSitei P22059.

Polymorphism databases

DMDMi 129308.

Proteomic databases

MaxQBi P22059.
PaxDbi P22059.
PeptideAtlasi P22059.
PRIDEi P22059.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000263847 ; ENSP00000263847 ; ENSG00000110048 .
GeneIDi 5007.
KEGGi hsa:5007.
UCSCi uc001noc.1. human.

Organism-specific databases

CTDi 5007.
GeneCardsi GC11M059341.
HGNCi HGNC:8503. OSBP.
HPAi HPA039227.
HPA043625.
MIMi 167040. gene.
neXtProti NX_P22059.
PharmGKBi PA32822.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG281324.
HOGENOMi HOG000231233.
HOVERGENi HBG053374.
InParanoidi P22059.
OMAi EYWECKE.
OrthoDBi EOG7MPRD7.
PhylomeDBi P22059.
TreeFami TF320922.

Enzyme and pathway databases

Reactomei REACT_115810. Sphingolipid de novo biosynthesis.

Miscellaneous databases

ChiTaRSi OSBP. human.
EvolutionaryTracei P22059.
GeneWikii OSBP.
GenomeRNAii 5007.
NextBioi 19280.
PROi P22059.
SOURCEi Search...

Gene expression databases

ArrayExpressi P22059.
Bgeei P22059.
CleanExi HS_OSBP.
Genevestigatori P22059.

Family and domain databases

Gene3Di 2.30.29.30. 1 hit.
InterProi IPR000648. Oxysterol-bd.
IPR018494. Oxysterol-bd_CS.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
[Graphical view ]
PANTHERi PTHR10972. PTHR10972. 1 hit.
Pfami PF01237. Oxysterol_BP. 1 hit.
PF00169. PH. 1 hit.
[Graphical view ]
SMARTi SM00233. PH. 1 hit.
[Graphical view ]
PROSITEi PS01013. OSBP. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning of human oxysterol-binding protein and localization of the gene to human chromosome 11 and mouse chromosome 19."
    Levanon D., Hsieh C.L., Francke U., Dawson P.A., Ridgway N.D., Brown M.S., Goldstein J.L.
    Genomics 7:65-74(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Molecular and biochemical characterization of a novel oxysterol-binding protein (OSBP2) highly expressed in retina."
    Moreira E.F., Jaworski C., Li A., Rodriguez I.R.
    J. Biol. Chem. 276:18570-18578(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney and Placenta.
  4. "OSBP is a cholesterol-regulated scaffolding protein in control of ERK 1/2 activation."
    Wang P.-Y., Weng J., Anderson R.G.W.
    Science 307:1472-1476(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-193; SER-351 AND SER-382, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "OSBP negatively regulates ABCA1 protein stability."
    Bowden K., Ridgway N.D.
    J. Biol. Chem. 283:18210-18217(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-193; SER-351; SER-382 AND SER-389, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-193; SER-198; SER-351 AND SER-382, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-193 AND SER-351, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-193; SER-351 AND SER-382, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-193 AND SER-351, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193 AND SER-351, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Electrostatic interaction between oxysterol-binding protein and VAMP-associated protein A revealed by NMR and mutagenesis studies."
    Furuita K., Jee J., Fukada H., Mishima M., Kojima C.
    J. Biol. Chem. 285:12961-12970(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 346-379, INTERACTION WITH VAPA.
  16. Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-278.

Entry informationi

Entry nameiOSBP1_HUMAN
AccessioniPrimary (citable) accession number: P22059
Secondary accession number(s): Q6P524
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: September 3, 2014
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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