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P35845

- OSH1_YEAST

UniProt

P35845 - OSH1_YEAST

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Protein
Oxysterol-binding protein homolog 1
Gene
SWH1, OSH1, YAR042W, YAR044W
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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.3 Publications

GO - Cellular componenti

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

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 1
PRO_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.

Family & Domainsi

Domains and Repeats

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

Motif

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

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi434 – 47239Asn/Asp-rich
Add
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.
Contains 3 ANK repeats.
Contains 1 PH domain.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti244 – 2441D → Y in CAA52646. 1 Publication
Sequence conflicti248 – 2481N → S1 Publication
Sequence conflicti248 – 2481N → S1 Publication
Sequence conflicti424 – 4241P → A in CAA52646. 1 Publication
Sequence conflicti464 – 4641D → NNN1 Publication
Sequence conflicti468 – 4692YD → DY1 Publication
Sequence conflicti495 – 4962TP → AS in CAA52646. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 145 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

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