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P35845 (OSH1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 homolog 1
Gene names
Name:SWH1
Synonyms:OSH1
Ordered Locus Names:YAR042W
ORF Names:YAR044W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1188 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.11

Subunit structure

Interacts with NVJ1. Ref.12

Subcellular location

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. Ref.2 Ref.9 Ref.12

Domain

The ankyrin repeats are required for targeting the protein to the NV junction. Ref.2

The PH domain is required for targeting the protein to the late Golgi. Ref.2

The FFAT motif is required for interaction with SCS2 and proper localization of the protein. Ref.2

Sequence similarities

Belongs to the OSBP family.

Contains 3 ANK repeats.

Contains 1 PH domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11881188Oxysterol-binding protein homolog 1
PRO_0000100387

Regions

Repeat51 – 8030ANK 1
Repeat96 – 12530ANK 2
Repeat196 – 22530ANK 3
Domain330 – 37950PH
Motif716 – 7227FFAT
Compositional bias434 – 47239Asn/Asp-rich

Amino acid modifications

Modified residue3941Phosphoserine Ref.14
Modified residue4901Phosphoserine Ref.14 Ref.15 Ref.16
Modified residue5001Phosphoserine Ref.15
Modified residue6781Phosphoserine Ref.14 Ref.15 Ref.16
Modified residue6831Phosphoserine Ref.16
Modified residue6911Phosphoserine Ref.16
Modified residue6921Phosphothreonine Ref.16
Modified residue6941Phosphothreonine Ref.15 Ref.16
Modified residue7081Phosphoserine Ref.14 Ref.15 Ref.16
Modified residue7121Phosphoserine Ref.14 Ref.15 Ref.16

Experimental info

Mutagenesis7191D → A: Abolishes function. Ref.2
Sequence conflict2441D → Y in CAA52646. Ref.1
Sequence conflict2481N → S Ref.3
Sequence conflict2481N → S Ref.4
Sequence conflict4241P → A in CAA52646. Ref.1
Sequence conflict4641D → NNN Ref.1
Sequence conflict468 – 4692YD → DY Ref.1
Sequence conflict495 – 4962TP → AS in CAA52646. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P35845 [UniParc].

Last modified December 6, 2005. Version 4.
Checksum: B9DA826745CEB30B

FASTA1,188135,098
        10         20         30         40         50         60 
MEQPDLSSVA ISKPLLKLKL LDALRQGSFP NLQDLLKKQF QPLDDPNVQQ VLHLMLHYAV 

        70         80         90        100        110        120 
QVAPMAVIKE IVHHWVSTTN TTFLNIHLDL NERDSNGNTP LHIAAYQSRG DIVAFLLDQP 

       130        140        150        160        170        180 
TINDCVLNNS HLQAIEMCKN LNIAQMMQVK RSTYVAETAQ EFRTAFNNRD FGHLESILSS 

       190        200        210        220        230        240 
PRNAELLDIN GMDPETGDTV LHEFVKKRDV IMCRWLLEHG ADPFKRDRKG KLPIELVRKV 

       250        260        270        280        290        300 
NENDTATNTK IAIDIELKKL LERATREQSV IDVTNNNLHE APTYKGYLKK WTNFAQGYKL 

       310        320        330        340        350        360 
RWFILSSDGK LSYYIDQADT KNACRGSLNM SSCSLHLDSS EKLKFEIIGG NNGVIRWHLK 

       370        380        390        400        410        420 
GNHPIETNRW VWAIQGAIRY AKDREILLHN GPYSPSLALS HGLSSKVSNK ENLHATSKRL 

       430        440        450        460        470        480 
TKSPHLSKST LTQNDHDNDD DSTNNNNNKS NNDYDDNNNN NNNDDDDYDD DDESRPLIEP 

       490        500        510        520        530        540 
LPLISSRSQS LSEITPGPHS RKSTVSSTRA ADIPSDDEGY SEDDSDDDGN SSYTMENGGE 

       550        560        570        580        590        600 
NDGDEDLNAI YGPYIQKLHM LQRSISIELA SLNELLQDKQ QHDEYWNTVN TSIETVSEFF 

       610        620        630        640        650        660 
DKLNRLTSQR EKRMIAQMTK QRDVNNVWIQ SVKDLEMELV DKDEKLVALD KERKNLKKML 

       670        680        690        700        710        720 
QKKLNNQPQV ETEANEESDD ANSMIKGSQE STNTLEEIVK FIEATKESDE DSDADEFFDA 

       730        740        750        760        770        780 
EEAASDKKAN DSEDLTTNKE TPANAKPQEE APEDESLIVI SSPQVEKKNQ LLKEGSFVGY 

       790        800        810        820        830        840 
EDPVRTKLAL DEDNRPKIGL WSVLKSMVGQ DLTKLTLPVS FNEPTSLLQR VSEDIEYSHI 

       850        860        870        880        890        900 
LDQAATFEDS SLRMLYVAAF TASMYASTTN RVSKPFNPLL GETFEYARTD GQYRFFTEQV 

       910        920        930        940        950        960 
SHHPPISATW TESPKWDFYG ECNVDSSFNG RTFAVQHLGL WYITIRPDHN ISVPEETYSW 

       970        980        990       1000       1010       1020 
KKPNNTVIGI LMGKPQVDNS GDVKVTNHTT GDYCMLHYKA HGWTSAGAYE VRGEVFNKDD 

      1030       1040       1050       1060       1070       1080 
KKLWVLGGHW NDSIYGKKVT ARGGELTLDR IKTANSATGG PKLDGSKFLI WKANERPSVP 

      1090       1100       1110       1120       1130       1140 
FNLTSFALTL NALPPHLIPY LAPTDSRLRP DQRAMENGEY DKAAAEKHRV EVKQRAAKKE 

      1150       1160       1170       1180 
REQKGEEYRP KWFVQEEHPV TKSLYWKFNG EYWNKRKNHD FKDCADIF 

« Hide

References

« Hide 'large scale' references
[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]"The nucleotide sequence of chromosome I from Saccharomyces cerevisiae."
Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N., Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J., Storms R.K.
Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995) [PubMed] [Europe PMC] [Abstract]
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]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS47536.
RefSeqNP_009421.3. NM_001178227.1.

3D structure databases

ProteinModelPortalP35845.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31812. 61 interactions.
DIPDIP-6269N.
DIP-6839N.
IntActP35845. 26 interactions.
MINTMINT-571501.

Proteomic databases

MaxQBP35845.
PaxDbP35845.
PeptideAtlasP35845.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYAR042W; YAR042W; YAR042W.
GeneID851286.
KEGGsce:YAR042W.

Organism-specific databases

CYGDYAR042w.
SGDS000000081. SWH1.

Phylogenomic databases

eggNOGCOG0666.
GeneTreeENSGT00710000106456.
HOGENOMHOG000186039.
KOK06867.
OMAGRYEHAN.
OrthoDBEOG7N903T.

Enzyme and pathway databases

BioCycYEAST:G3O-28883-MONOMER.

Gene expression databases

GenevestigatorP35845.

Family and domain databases

Gene3D1.25.40.20. 2 hits.
2.30.29.30. 1 hit.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR000648. Oxysterol-bd.
IPR018494. Oxysterol-bd_CS.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
[Graphical view]
PANTHERPTHR10972. PTHR10972. 1 hit.
PfamPF00023. Ank. 2 hits.
PF01237. Oxysterol_BP. 1 hit.
[Graphical view]
SMARTSM00248. ANK. 2 hits.
SM00233. PH. 1 hit.
[Graphical view]
SUPFAMSSF48403. SSF48403. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 2 hits.
PS50088. ANK_REPEAT. 2 hits.
PS01013. OSBP. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio968288.
PROP35845.

Entry information

Entry nameOSH1_YEAST
AccessionPrimary (citable) accession number: P35845
Secondary accession number(s): D6VPN6 expand/collapse secondary AC list , P39555, P80234, Q86ZC4, Q86ZS1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: December 6, 2005
Last modified: May 14, 2014
This is version 144 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome I

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

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families