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P35845

- OSH1_YEAST

UniProt

P35845 - OSH1_YEAST

Protein

Oxysterol-binding protein homolog 1

Gene

SWH1

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 146 (01 Oct 2014)
      Sequence version 4 (06 Dec 2005)
      Previous versions | rss
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    Functioni

    Lipid-binding protein involved in maintenance of intracellular sterol distribution and homeostasis. Binds to phosphoinositides. May be involved in formation of PMN vesicles by altering the membrane lipid composition.1 Publication

    GO - Molecular functioni

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

    GO - Biological processi

    1. endocytosis Source: SGD
    2. exocytosis Source: SGD
    3. maintenance of cell polarity Source: SGD
    4. sterol transport Source: SGD

    Keywords - Biological processi

    Lipid transport, Transport

    Keywords - Ligandi

    Lipid-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-28883-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Oxysterol-binding protein homolog 1
    Gene namesi
    Name:SWH1
    Synonyms:OSH1
    Ordered Locus Names:YAR042W
    ORF Names:YAR044W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome I

    Organism-specific databases

    CYGDiYAR042w.
    SGDiS000000081. SWH1.

    Subcellular locationi

    Cytoplasm. Golgi apparatus membrane. Nucleus outer membrane
    Note: Soluble protein that accumulates on the surface of late Golgi membranes and at nucleus-vacuole (NV) junctions, interorganelle interfaces between the nuclear envelope and the vacuole membrane formed during piecemeal microautophagy of the nucleus (PMN). Targeted exclusively to NV junctions in stationary phase.

    GO - Cellular componenti

    1. early endosome Source: SGD
    2. endoplasmic reticulum Source: SGD
    3. Golgi membrane Source: UniProtKB-SubCell
    4. Golgi trans cisterna Source: SGD
    5. nuclear envelope Source: SGD
    6. nuclear outer membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Golgi apparatus, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi719 – 7191D → A: Abolishes function. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11881188Oxysterol-binding protein homolog 1PRO_0000100387Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei394 – 3941Phosphoserine1 Publication
    Modified residuei490 – 4901Phosphoserine3 Publications
    Modified residuei500 – 5001Phosphoserine1 Publication
    Modified residuei678 – 6781Phosphoserine3 Publications
    Modified residuei683 – 6831Phosphoserine1 Publication
    Modified residuei691 – 6911Phosphoserine1 Publication
    Modified residuei692 – 6921Phosphothreonine1 Publication
    Modified residuei694 – 6941Phosphothreonine2 Publications
    Modified residuei708 – 7081Phosphoserine3 Publications
    Modified residuei712 – 7121Phosphoserine3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP35845.
    PaxDbiP35845.
    PeptideAtlasiP35845.

    Expressioni

    Gene expression databases

    GenevestigatoriP35845.

    Interactioni

    Subunit structurei

    Interacts with NVJ1.1 Publication

    Protein-protein interaction databases

    BioGridi31812. 61 interactions.
    DIPiDIP-6269N.
    DIP-6839N.
    IntActiP35845. 26 interactions.
    MINTiMINT-571501.

    Structurei

    3D structure databases

    ProteinModelPortaliP35845.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati51 – 8030ANK 1Add
    BLAST
    Repeati96 – 12530ANK 2Add
    BLAST
    Repeati196 – 22530ANK 3Add
    BLAST
    Domaini330 – 37950PHPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi716 – 7227FFAT

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi434 – 47239Asn/Asp-richAdd
    BLAST

    Domaini

    The ankyrin repeats are required for targeting the protein to the NV junction.1 Publication
    The PH domain is required for targeting the protein to the late Golgi.1 Publication
    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 3 ANK repeats.PROSITE-ProRule annotation
    Contains 1 PH domain.PROSITE-ProRule annotation

    Keywords - Domaini

    ANK repeat, Repeat

    Phylogenomic databases

    eggNOGiCOG0666.
    GeneTreeiENSGT00710000106456.
    HOGENOMiHOG000186039.
    KOiK06867.
    OMAiGRYEHAN.
    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. 2 hits.
    PF01237. Oxysterol_BP. 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. 2 hits.
    PS01013. OSBP. 1 hit.
    PS50003. PH_DOMAIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P35845-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEQPDLSSVA ISKPLLKLKL LDALRQGSFP NLQDLLKKQF QPLDDPNVQQ     50
    VLHLMLHYAV QVAPMAVIKE IVHHWVSTTN TTFLNIHLDL NERDSNGNTP 100
    LHIAAYQSRG DIVAFLLDQP TINDCVLNNS HLQAIEMCKN LNIAQMMQVK 150
    RSTYVAETAQ EFRTAFNNRD FGHLESILSS PRNAELLDIN GMDPETGDTV 200
    LHEFVKKRDV IMCRWLLEHG ADPFKRDRKG KLPIELVRKV NENDTATNTK 250
    IAIDIELKKL LERATREQSV IDVTNNNLHE APTYKGYLKK WTNFAQGYKL 300
    RWFILSSDGK LSYYIDQADT KNACRGSLNM SSCSLHLDSS EKLKFEIIGG 350
    NNGVIRWHLK GNHPIETNRW VWAIQGAIRY AKDREILLHN GPYSPSLALS 400
    HGLSSKVSNK ENLHATSKRL TKSPHLSKST LTQNDHDNDD DSTNNNNNKS 450
    NNDYDDNNNN NNNDDDDYDD DDESRPLIEP LPLISSRSQS LSEITPGPHS 500
    RKSTVSSTRA ADIPSDDEGY SEDDSDDDGN SSYTMENGGE NDGDEDLNAI 550
    YGPYIQKLHM LQRSISIELA SLNELLQDKQ QHDEYWNTVN TSIETVSEFF 600
    DKLNRLTSQR EKRMIAQMTK QRDVNNVWIQ SVKDLEMELV DKDEKLVALD 650
    KERKNLKKML QKKLNNQPQV ETEANEESDD ANSMIKGSQE STNTLEEIVK 700
    FIEATKESDE DSDADEFFDA EEAASDKKAN DSEDLTTNKE TPANAKPQEE 750
    APEDESLIVI SSPQVEKKNQ LLKEGSFVGY EDPVRTKLAL DEDNRPKIGL 800
    WSVLKSMVGQ DLTKLTLPVS FNEPTSLLQR VSEDIEYSHI LDQAATFEDS 850
    SLRMLYVAAF TASMYASTTN RVSKPFNPLL GETFEYARTD GQYRFFTEQV 900
    SHHPPISATW TESPKWDFYG ECNVDSSFNG RTFAVQHLGL WYITIRPDHN 950
    ISVPEETYSW KKPNNTVIGI LMGKPQVDNS GDVKVTNHTT GDYCMLHYKA 1000
    HGWTSAGAYE VRGEVFNKDD KKLWVLGGHW NDSIYGKKVT ARGGELTLDR 1050
    IKTANSATGG PKLDGSKFLI WKANERPSVP FNLTSFALTL NALPPHLIPY 1100
    LAPTDSRLRP DQRAMENGEY DKAAAEKHRV EVKQRAAKKE REQKGEEYRP 1150
    KWFVQEEHPV TKSLYWKFNG EYWNKRKNHD FKDCADIF 1188
    Length:1,188
    Mass (Da):135,098
    Last modified:December 6, 2005 - v4
    Checksum:iB9DA826745CEB30B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti244 – 2441D → Y in CAA52646. (PubMed:8086466)Curated
    Sequence conflicti248 – 2481N → S1 PublicationCurated
    Sequence conflicti248 – 2481N → S(PubMed:7731988)Curated
    Sequence conflicti424 – 4241P → A in CAA52646. (PubMed:8086466)Curated
    Sequence conflicti464 – 4641D → NNN(PubMed:8086466)Curated
    Sequence conflicti468 – 4692YD → DY(PubMed:8086466)Curated
    Sequence conflicti495 – 4962TP → AS in CAA52646. (PubMed:8086466)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X74552 Genomic DNA. Translation: CAA52646.1.
    AY241177 Genomic DNA. Translation: AAP31019.1.
    L28920 Genomic DNA. Translation: AAC09496.2.
    AY260892 Genomic DNA. Translation: AAP21760.1.
    BK006935 Genomic DNA. Translation: DAA07006.1.
    PIRiS47536.
    RefSeqiNP_009421.3. NM_001178227.1.

    Genome annotation databases

    EnsemblFungiiYAR042W; YAR042W; YAR042W.
    GeneIDi851286.
    KEGGisce:YAR042W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X74552 Genomic DNA. Translation: CAA52646.1 .
    AY241177 Genomic DNA. Translation: AAP31019.1 .
    L28920 Genomic DNA. Translation: AAC09496.2 .
    AY260892 Genomic DNA. Translation: AAP21760.1 .
    BK006935 Genomic DNA. Translation: DAA07006.1 .
    PIRi S47536.
    RefSeqi NP_009421.3. NM_001178227.1.

    3D structure databases

    ProteinModelPortali P35845.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31812. 61 interactions.
    DIPi DIP-6269N.
    DIP-6839N.
    IntActi P35845. 26 interactions.
    MINTi MINT-571501.

    Proteomic databases

    MaxQBi P35845.
    PaxDbi P35845.
    PeptideAtlasi P35845.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YAR042W ; YAR042W ; YAR042W .
    GeneIDi 851286.
    KEGGi sce:YAR042W.

    Organism-specific databases

    CYGDi YAR042w.
    SGDi S000000081. SWH1.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci YEAST:G3O-28883-MONOMER.

    Miscellaneous databases

    NextBioi 968288.
    PROi P35845.

    Gene expression databases

    Genevestigatori P35845.

    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. 2 hits.
    PF01237. Oxysterol_BP. 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. 2 hits.
    PS01013. OSBP. 1 hit.
    PS50003. PH_DOMAIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "SWH1 from yeast encodes a candidate nuclear factor containing ankyrin repeats and showing homology to mammalian oxysterol-binding protein."
      Schmalix W.A., Bandlow W.
      Biochim. Biophys. Acta 1219:205-210(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: DL-1.
    2. "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: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DOMAIN FFAT MOTIF, MUTAGENESIS OF ASP-719, SUBCELLULAR LOCATION.
      Strain: ATCC 96099 / S288c / SEY6210.
    3. "Sequencing of chromosome I of Saccharomyces cerevisiae: analysis of the 52 Kbp CDC15-FLO1-PHO11-YAR074 region."
      Bussey H., Keng T., Storms R.K., Vo D., Zhong W., Fortin N., Barton A.B., Kaback D.B., Clark M.W.
      Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204511 / S288c / AB972.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. Sethuraman A., Cherry J.M.
      Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO C-TERMINUS.
    6. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    7. "Reinvestigation of the Saccharomyces cerevisiae genome annotation by comparison to the genome of a related fungus: Ashbya gossypii."
      Brachat S., Dietrich F.S., Voegeli S., Zhang Z., Stuart L., Lerch A., Gates K., Gaffney T.D., Philippsen P.
      Genome Biol. 4:R45.1-R45.13(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 199-264.
      Strain: ATCC 204511 / S288c / AB972.
    8. "A new family of yeast genes implicated in ergosterol synthesis is related to the human oxysterol binding protein."
      Jiang B., Brown J.L., Sheraton J., Fortin N., Bussey H.
      Yeast 10:341-353(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    9. "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.
    10. "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.
    11. "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.
    12. "Nvj1p is the outer-nuclear-membrane receptor for oxysterol-binding protein homolog Osh1p in Saccharomyces cerevisiae."
      Kvam E., Goldfarb D.S.
      J. Cell Sci. 117:4959-4968(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NVJ1, SUBCELLULAR LOCATION.
    13. "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.
    14. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-490; SER-678; SER-708 AND SER-712, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    15. "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-490; SER-500; SER-678; THR-694; SER-708 AND SER-712, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "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-490; SER-678; SER-683; SER-691; THR-692; THR-694; SER-708 AND SER-712, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiOSH1_YEAST
    AccessioniPrimary (citable) accession number: P35845
    Secondary accession number(s): D6VPN6
    , P39555, P80234, Q86ZC4, Q86ZS1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: December 6, 2005
    Last modified: October 1, 2014
    This is version 146 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    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 I
      Yeast (Saccharomyces cerevisiae) chromosome I: entries and gene names

    External Data

    Dasty 3