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P22059

- OSBP1_HUMAN

UniProt

P22059 - OSBP1_HUMAN

Protein

Oxysterol-binding protein 1

Gene

OSBP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 1 (01 Aug 1991)
      Previous versions | rss
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    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

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

    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 1PRO_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 – 2401PhosphoserineBy 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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FKBP6O753442EBI-2681902,EBI-744771

    Protein-protein interaction databases

    BioGridi111048. 28 interactions.
    IntActiP22059. 3 interactions.
    MINTiMINT-5005941.
    STRINGi9606.ENSP00000263847.

    Structurei

    Secondary structure

    1
    807
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP22059.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini88 – 18194PHPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni406 – 45752Sterol bindingBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili291 – 32636Sequence AnalysisAdd
    BLAST
    Coiled coili730 – 76031Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1 – 9393Ala/Gly-richAdd
    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.Curated
    Contains 1 PH domain.PROSITE-ProRule annotation

    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. 3 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

    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: October 1, 2014
    This is version 139 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