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Q12451

- OSH2_YEAST

UniProt

Q12451 - OSH2_YEAST

Protein

Oxysterol-binding protein homolog 2

Gene

OSH2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Lipid-binding protein involved in maintenance of intracellular sterol distribution and homeostasis. Binds to phosphoinositides.1 Publication

    GO - Molecular functioni

    1. 1-phosphatidylinositol binding Source: SGD
    2. lipid binding Source: SGD
    3. oxysterol binding Source: SGD
    4. protein binding Source: IntAct
    5. sterol transporter activity Source: SGD

    GO - Biological processi

    1. endocytosis Source: SGD
    2. ER to Golgi ceramide transport Source: SGD
    3. exocytosis Source: SGD
    4. maintenance of cell polarity Source: SGD
    5. sterol transport Source: SGD

    Keywords - Biological processi

    Lipid transport, Transport

    Keywords - Ligandi

    Lipid-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29448-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Oxysterol-binding protein homolog 2
    Gene namesi
    Name:OSH2
    Ordered Locus Names:YDL019C
    ORF Names:D2845
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    CYGDiYDL019c.
    SGDiS000002177. OSH2.

    Subcellular locationi

    Cell membrane 2 Publications; Peripheral membrane protein 2 Publications
    Note: Cell periphery, enriched in small buds of G1 phase cells and near the bud-neck region of S phase cells.

    GO - Cellular componenti

    1. cellular bud neck Source: SGD
    2. cortical endoplasmic reticulum Source: SGD
    3. endoplasmic reticulum Source: SGD
    4. plasma membrane Source: SGD

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12831283Oxysterol-binding protein homolog 2PRO_0000100388Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei422 – 4221Phosphoserine2 Publications
    Modified residuei445 – 4451Phosphoserine1 Publication
    Modified residuei451 – 4511Phosphoserine1 Publication
    Modified residuei455 – 4551Phosphoserine1 Publication
    Modified residuei458 – 4581Phosphoserine1 Publication
    Modified residuei459 – 4591Phosphoserine1 Publication
    Modified residuei486 – 4861Phosphoserine1 Publication
    Modified residuei488 – 4881Phosphothreonine1 Publication
    Modified residuei512 – 5121Phosphoserine1 Publication
    Modified residuei515 – 5151Phosphoserine1 Publication
    Modified residuei717 – 7171Phosphoserine1 Publication
    Modified residuei783 – 7831Phosphothreonine1 Publication
    Modified residuei787 – 7871Phosphoserine2 Publications
    Modified residuei825 – 8251Phosphoserine1 Publication
    Modified residuei1151 – 11511Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ12451.
    PaxDbiQ12451.
    PRIDEiQ12451.

    Expressioni

    Gene expression databases

    GenevestigatoriQ12451.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MYO3P360063EBI-12621,EBI-11670
    MYO5Q044396EBI-12621,EBI-11687

    Protein-protein interaction databases

    BioGridi32036. 46 interactions.
    DIPiDIP-6712N.
    IntActiQ12451. 5 interactions.
    MINTiMINT-599978.

    Structurei

    3D structure databases

    ProteinModelPortaliQ12451.
    SMRiQ12451. Positions 23-247, 293-384, 897-1283.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati106 – 13429ANK 1Add
    BLAST
    Repeati206 – 23530ANK 2Add
    BLAST
    Domaini289 – 38698PHPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi745 – 7517FFAT

    Domaini

    The FFAT motif is required for interaction with SCS2 and proper localization of the protein.1 Publication

    Sequence similaritiesi

    Belongs to the OSBP family.Curated
    Contains 2 ANK repeats.PROSITE-ProRule annotation
    Contains 1 PH domain.PROSITE-ProRule annotation

    Keywords - Domaini

    ANK repeat, Repeat

    Phylogenomic databases

    eggNOGiCOG0666.
    GeneTreeiENSGT00710000106456.
    HOGENOMiHOG000186039.
    KOiK06867.
    OMAiITLNAPQ.
    OrthoDBiEOG7N903T.

    Family and domain databases

    Gene3Di1.25.40.20. 2 hits.
    2.30.29.30. 1 hit.
    InterProiIPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR000648. Oxysterol-bd.
    IPR018494. Oxysterol-bd_CS.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    [Graphical view]
    PANTHERiPTHR10972. PTHR10972. 1 hit.
    PfamiPF00023. Ank. 1 hit.
    PF01237. Oxysterol_BP. 1 hit.
    PF00169. PH. 1 hit.
    [Graphical view]
    SMARTiSM00248. ANK. 2 hits.
    SM00233. PH. 1 hit.
    [Graphical view]
    SUPFAMiSSF48403. SSF48403. 1 hit.
    PROSITEiPS50297. ANK_REP_REGION. 2 hits.
    PS50088. ANK_REPEAT. 1 hit.
    PS01013. OSBP. 1 hit.
    PS50003. PH_DOMAIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q12451-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSREDLSIAE DLNQVSKPLL KVKLLEVLGQ GDFKHLKALV DNEFQPKDDP     50
    SVQQVLNLIL HYAVQVAPIL LIKEIVAHWV DQVGDEKSSS KSDDGIHLDL 100
    NYQDENGNTP LHLAAAQSRS DVISFLLSQK SINDCVKNKA HQQPLDMCKD 150
    LNVAQMIQLK RDDYFLETVH SLRAAMNKRD FSKLDSIWKN PRNLNLLDIN 200
    GIDPETGTTL LYEYSQKKDI EMCQWLLKHG AEATVKDGKG RSPLDLVKNI 250
    KLPAKPSNNV TPEIKLKNLL EKNLREQAIV HEDVASSKPP TYKGFLKKWT 300
    NFAHGYKLRW FILSGDGNLS YYKDQSHVDR PRGTLKVSTC RLHIDSSEKL 350
    NFELLGGITG TTRWRLKGNH PIETTRWVNA IQSAIRFAKD KEILNKKKAV 400
    PPSLALKNKS PALISHSKTQ GSLPEASQYY QHTLHKEVIQ PSSVSLYRRP 450
    SNNLSVVSSE IQLNDNLTES GKRFVSKMIE NRLDGSKTPV GVHTGSALQR 500
    VRSSNTLKSN RSMQSGSGVA SPIDKVPNGA NLSQSNTTTG STASLSDNNY 550
    IDNFEGDEAN SDDEEEDLGI NFDRDEEYIK AQYGPYKEKL DMYEQAISIE 600
    LSSLIELIEQ EEPSPEVWLT IKKSLINTST IFGKLKDLTY KRDKRLVDMV 650
    SKQGDVNNVW VQSVKELEME LSNKTERLAS IDKERRGLKK ILHKKLLESH 700
    ATAGNKESLE NDKEQESDTT ASTLGQIAKF ISATKEEDEA SDADEFYDAA 750
    ELVDEVTELT EAHPEISTAA APKHAPPPVP NETDNDSQYV QDEKSKIESN 800
    VEKTSQKFEK QNNLVTEDEP KTDQSLKNFK AEDKESQVKE KTKEIASSVI 850
    GEKTIVAVTT VQKRKEEYLL KEGSYLGYED GIRKRLSMDK DDRPKISLWA 900
    VLKSMVGKDM TRMTLPVTFN EPTSLLQRVA EDLEYSELLD QAATFEDSTL 950
    RTLYVAAFTA SSYASTTKRV AKPFNPLLGE TFEYSRPDKQ YRFFTEQVSH 1000
    HPPISATWTE SPRWDFWGES FVDTKFNGRS FNVKHLGLWH IKLRPNDNEK 1050
    EELYTWKKPN NTVIGILIGN PQVDNHGEVN VVNHTTGDHC KLYFKARGWR 1100
    SSGAYEITGE VYNKKKQKVW ILGGHWNEAI FAKKVVKDGD LSLEKTRTAA 1150
    SAGNGPTDDG TKFLIWKAND RPEEPFNLTP FAITLNAPQP HLLPWLPPTD 1200
    TRLRPDQRAM EDGRYDEAGD EKFRVEEKQR AARRKREENN LEYHPQWFVR 1250
    DTHPITKAKY WRYTGKYWVK RRDHDLKDCG DIF 1283
    Length:1,283
    Mass (Da):145,796
    Last modified:November 1, 1996 - v1
    Checksum:iD521957460E7F7C3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z74066 Genomic DNA. Translation: CAA98577.1.
    Z74067 Genomic DNA. Translation: CAA98578.1.
    Z48432 Genomic DNA. Translation: CAA88340.1.
    BK006938 Genomic DNA. Translation: DAA11831.1.
    PIRiS52500.
    RefSeqiNP_010265.1. NM_001180078.1.

    Genome annotation databases

    EnsemblFungiiYDL019C; YDL019C; YDL019C.
    GeneIDi851543.
    KEGGisce:YDL019C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z74066 Genomic DNA. Translation: CAA98577.1 .
    Z74067 Genomic DNA. Translation: CAA98578.1 .
    Z48432 Genomic DNA. Translation: CAA88340.1 .
    BK006938 Genomic DNA. Translation: DAA11831.1 .
    PIRi S52500.
    RefSeqi NP_010265.1. NM_001180078.1.

    3D structure databases

    ProteinModelPortali Q12451.
    SMRi Q12451. Positions 23-247, 293-384, 897-1283.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32036. 46 interactions.
    DIPi DIP-6712N.
    IntActi Q12451. 5 interactions.
    MINTi MINT-599978.

    Proteomic databases

    MaxQBi Q12451.
    PaxDbi Q12451.
    PRIDEi Q12451.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDL019C ; YDL019C ; YDL019C .
    GeneIDi 851543.
    KEGGi sce:YDL019C.

    Organism-specific databases

    CYGDi YDL019c.
    SGDi S000002177. OSH2.

    Phylogenomic databases

    eggNOGi COG0666.
    GeneTreei ENSGT00710000106456.
    HOGENOMi HOG000186039.
    KOi K06867.
    OMAi ITLNAPQ.
    OrthoDBi EOG7N903T.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29448-MONOMER.

    Miscellaneous databases

    NextBioi 968952.

    Gene expression databases

    Genevestigatori Q12451.

    Family and domain databases

    Gene3Di 1.25.40.20. 2 hits.
    2.30.29.30. 1 hit.
    InterProi IPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR000648. Oxysterol-bd.
    IPR018494. Oxysterol-bd_CS.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    [Graphical view ]
    PANTHERi PTHR10972. PTHR10972. 1 hit.
    Pfami PF00023. Ank. 1 hit.
    PF01237. Oxysterol_BP. 1 hit.
    PF00169. PH. 1 hit.
    [Graphical view ]
    SMARTi SM00248. ANK. 2 hits.
    SM00233. PH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48403. SSF48403. 1 hit.
    PROSITEi PS50297. ANK_REP_REGION. 2 hits.
    PS50088. ANK_REPEAT. 1 hit.
    PS01013. OSBP. 1 hit.
    PS50003. PH_DOMAIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
      Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
      , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
      Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. "Dual targeting of Osh1p, a yeast homologue of oxysterol-binding protein, to both the Golgi and the nucleus-vacuole junction."
      Levine T.P., Munro S.
      Mol. Biol. Cell 12:1633-1644(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    4. "Overlapping functions of the yeast oxysterol-binding protein homologues."
      Beh C.T., Cool L., Phillips J., Rine J.
      Genetics 157:1117-1140(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENETIC ANALYSIS.
    5. "A conserved ER targeting motif in three families of lipid binding proteins and in Opi1p binds VAP."
      Loewen C.J.R., Roy A., Levine T.P.
      EMBO J. 22:2025-2035(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN FFAT MOTIF, SUBCELLULAR LOCATION.
    6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    7. "A role for yeast oxysterol-binding protein homologs in endocytosis and in the maintenance of intracellular sterol-lipid distribution."
      Beh C.T., Rine J.
      J. Cell Sci. 117:2983-2996(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Genome-wide analysis of membrane targeting by S.cerevisiae pleckstrin homology domains."
      Yu J.W., Mendrola J.M., Audhya A., Singh S., Keleti D., DeWald D.B., Murray D., Emr S.D., Lemmon M.A.
      Mol. Cell 13:677-688(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHOINOSITIDE-BINDING.
    9. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    10. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
      Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
      Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-422, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-422; THR-488; SER-787 AND SER-1151, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445; SER-451; SER-455; SER-458; SER-459; SER-486; SER-512; SER-515; SER-717; THR-783; SER-787 AND SER-825, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiOSH2_YEAST
    AccessioniPrimary (citable) accession number: Q12451
    Secondary accession number(s): D6VRX1, P89891
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 5, 2002
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 132 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 1069 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome IV
      Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

    External Data

    Dasty 3