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P22059 (OSBP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Oxysterol-binding protein 1
Gene names
Name:OSBP
Synonyms:OSBP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length807 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4 Ref.6

Subunit structure

Homodimer or homotrimer. Interacts with VAPA. Ref.15

Subcellular location

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

Tissue specificity

Widely expressed. Ref.2

Domain

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 similarities

Belongs to the OSBP family.

Contains 1 PH domain.

Sequence caution

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

Ontologies

Keywords
   Biological processLipid transport
Transport
   Cellular componentCytoplasm
Golgi apparatus
Membrane
   Coding sequence diversityPolymorphism
   DomainCoiled coil
   LigandLipid-binding
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processlipid transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentGolgi apparatus

Inferred from direct assay. Source: HPA

Golgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell junction

Inferred from direct assay. Source: HPA

cytoplasm

Inferred from direct assay. Source: HPA

nucleolus

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionoxysterol binding

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 807807Oxysterol-binding protein 1
PRO_0000100364

Regions

Domain88 – 18194PH
Region406 – 45752Sterol binding By similarity
Coiled coil291 – 32636 Potential
Coiled coil730 – 76031 Potential
Compositional bias1 – 9393Ala/Gly-rich

Amino acid modifications

Modified residue1901Phosphoserine Ref.5 Ref.7 Ref.8 Ref.9 Ref.11 Ref.12
Modified residue1931Phosphoserine Ref.5 Ref.7 Ref.8 Ref.9 Ref.11 Ref.12 Ref.14
Modified residue1981Phosphoserine Ref.8
Modified residue2401Phosphoserine By similarity
Modified residue3511Phosphoserine Ref.5 Ref.7 Ref.8 Ref.9 Ref.11 Ref.12 Ref.14
Modified residue3821Phosphoserine Ref.5 Ref.7 Ref.8 Ref.11
Modified residue3891Phosphoserine Ref.7

Natural variations

Natural variant2781D → A in a colorectal cancer sample; somatic mutation. Ref.16
VAR_036099

Secondary structure

... 807
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P22059 [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: 2590A47BCB54FDFB

FASTA80789,421
        10         20         30         40         50         60 
MAATELRGVV GPGPAAIAAL GGGGAGPPVV GGGGGRGDAG PGSGAASGTV VAAAAGGPGP 

        70         80         90        100        110        120 
GAGGVAAAGP APAPPTGGSG GSGAGGSGSA REGWLFKWTN YIKGYQRRWF VLSNGLLSYY 

       130        140        150        160        170        180 
RSKAEMRHTC RGTINLATAN ITVEDSCNFI ISNGGAQTYH LKASSEVERQ RWVTALELAK 

       190        200        210        220        230        240 
AKAVKMLAES DESGDEESVS QTDKTELQNT LRTLSSKVED LSTCNDLIAK HGTALQRSLS 

       250        260        270        280        290        300 
ELESLKLPAE SNEKIKQVNE RATLFRITSN AMINACRDFL MLAQTHSKKW QKSLQYERDQ 

       310        320        330        340        350        360 
RIRLEETLEQ LAKQHNHLER AFRGATVLPA NTPGNVGSGK DQCCSGKGDM SDEDDENEFF 

       370        380        390        400        410        420 
DAPEIITMPE NLGHKRTGSN ISGASSDISL DEQYKHQLEE TKKEKRTRIP YKPNYSLNLW 

       430        440        450        460        470        480 
SIMKNCIGKE LSKIPMPVNF NEPLSMLQRL TEDLEYHELL DRAAKCENSL EQLCYVAAFT 

       490        500        510        520        530        540 
VSSYSTTVFR TSKPFNPLLG ETFELDRLEE NGYRSLCEQV SHHPPAAAHH AESKNGWTLR 

       550        560        570        580        590        600 
QEIKITSKFR GKYLSIMPLG TIHCIFHATG HHYTWKKVTT TVHNIIVGKL WIDQSGEIDI 

       610        620        630        640        650        660 
VNHKTGDKCN LKFVPYSYFS RDVARKVTGE VTDPSGKVHF ALLGTWDEKM ECFKVQPVIG 

       670        680        690        700        710        720 
ENGGDARQRG HEAEESRVML WKRNPLPKNA ENMYYFSELA LTLNAWESGT APTDSRLRPD 

       730        740        750        760        770        780 
QRLMENGRWD EANAEKQRLE EKQRLSRKKR EAEAMKATED GTPYDPYKAL WFERKKDPVT 

       790        800 
KELTHIYRGE YWECKEKQDW SSCPDIF 

« Hide

References

« Hide 'large scale' references
[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]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-278.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M86917 mRNA. Translation: AAA59973.1.
AF185696 mRNA. Translation: AAG17011.1.
AF185705 expand/collapse EMBL AC list , 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.
CCDSCCDS7974.1.
PIRA34581.
RefSeqNP_002547.1. NM_002556.2.
UniGeneHs.597091.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2RR3NMR-B346-379[»]
ProteinModelPortalP22059.
SMRP22059. Positions 91-180, 346-380, 405-801.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111048. 27 interactions.
IntActP22059. 2 interactions.
MINTMINT-5005941.
STRING9606.ENSP00000263847.

PTM databases

PhosphoSiteP22059.

Polymorphism databases

DMDM129308.

Proteomic databases

MaxQBP22059.
PaxDbP22059.
PeptideAtlasP22059.
PRIDEP22059.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263847; ENSP00000263847; ENSG00000110048.
GeneID5007.
KEGGhsa:5007.
UCSCuc001noc.1. human.

Organism-specific databases

CTD5007.
GeneCardsGC11M059341.
HGNCHGNC:8503. OSBP.
HPAHPA039227.
HPA043625.
MIM167040. gene.
neXtProtNX_P22059.
PharmGKBPA32822.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG281324.
HOGENOMHOG000231233.
HOVERGENHBG053374.
InParanoidP22059.
OMAEYWECKE.
OrthoDBEOG7MPRD7.
PhylomeDBP22059.
TreeFamTF320922.

Gene expression databases

ArrayExpressP22059.
BgeeP22059.
CleanExHS_OSBP.
GenevestigatorP22059.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
InterProIPR000648. Oxysterol-bd.
IPR018494. Oxysterol-bd_CS.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
[Graphical view]
PANTHERPTHR10972. PTHR10972. 1 hit.
PfamPF01237. Oxysterol_BP. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]
SMARTSM00233. PH. 1 hit.
[Graphical view]
PROSITEPS01013. OSBP. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSOSBP. human.
EvolutionaryTraceP22059.
GeneWikiOSBP.
GenomeRNAi5007.
NextBio19280.
PROP22059.
SOURCESearch...

Entry information

Entry nameOSBP1_HUMAN
AccessionPrimary (citable) accession number: P22059
Secondary accession number(s): Q6P524
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: July 9, 2014
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM