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Q12451 (OSH2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 130. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Oxysterol-binding protein homolog 2
Gene names
Name:OSH2
Ordered Locus Names:YDL019C
ORF Names:D2845
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1283 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. Ref.7

Subcellular location

Cell membrane; Peripheral membrane protein. Note: Cell periphery, enriched in small buds of G1 phase cells and near the bud-neck region of S phase cells. Ref.3 Ref.5

Domain

The FFAT motif is required for interaction with SCS2 and proper localization of the protein. Ref.5

Miscellaneous

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

Sequence similarities

Belongs to the OSBP family.

Contains 2 ANK repeats.

Contains 1 PH domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MYO3P360063EBI-12621,EBI-11670
MYO5Q044396EBI-12621,EBI-11687

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12831283Oxysterol-binding protein homolog 2
PRO_0000100388

Regions

Repeat106 – 13429ANK 1
Repeat206 – 23530ANK 2
Domain289 – 38698PH
Motif745 – 7517FFAT

Amino acid modifications

Modified residue4221Phosphoserine Ref.10 Ref.11
Modified residue4451Phosphoserine Ref.12
Modified residue4511Phosphoserine Ref.12
Modified residue4551Phosphoserine Ref.12
Modified residue4581Phosphoserine Ref.12
Modified residue4591Phosphoserine Ref.12
Modified residue4861Phosphoserine Ref.12
Modified residue4881Phosphothreonine Ref.11
Modified residue5121Phosphoserine Ref.12
Modified residue5151Phosphoserine Ref.12
Modified residue7171Phosphoserine Ref.12
Modified residue7831Phosphothreonine Ref.12
Modified residue7871Phosphoserine Ref.11 Ref.12
Modified residue8251Phosphoserine Ref.12
Modified residue11511Phosphoserine Ref.11

Sequences

Sequence LengthMass (Da)Tools
Q12451 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: D521957460E7F7C3

FASTA1,283145,796
        10         20         30         40         50         60 
MSREDLSIAE DLNQVSKPLL KVKLLEVLGQ GDFKHLKALV DNEFQPKDDP SVQQVLNLIL 

        70         80         90        100        110        120 
HYAVQVAPIL LIKEIVAHWV DQVGDEKSSS KSDDGIHLDL NYQDENGNTP LHLAAAQSRS 

       130        140        150        160        170        180 
DVISFLLSQK SINDCVKNKA HQQPLDMCKD LNVAQMIQLK RDDYFLETVH SLRAAMNKRD 

       190        200        210        220        230        240 
FSKLDSIWKN PRNLNLLDIN GIDPETGTTL LYEYSQKKDI EMCQWLLKHG AEATVKDGKG 

       250        260        270        280        290        300 
RSPLDLVKNI KLPAKPSNNV TPEIKLKNLL EKNLREQAIV HEDVASSKPP TYKGFLKKWT 

       310        320        330        340        350        360 
NFAHGYKLRW FILSGDGNLS YYKDQSHVDR PRGTLKVSTC RLHIDSSEKL NFELLGGITG 

       370        380        390        400        410        420 
TTRWRLKGNH PIETTRWVNA IQSAIRFAKD KEILNKKKAV PPSLALKNKS PALISHSKTQ 

       430        440        450        460        470        480 
GSLPEASQYY QHTLHKEVIQ PSSVSLYRRP SNNLSVVSSE IQLNDNLTES GKRFVSKMIE 

       490        500        510        520        530        540 
NRLDGSKTPV GVHTGSALQR VRSSNTLKSN RSMQSGSGVA SPIDKVPNGA NLSQSNTTTG 

       550        560        570        580        590        600 
STASLSDNNY IDNFEGDEAN SDDEEEDLGI NFDRDEEYIK AQYGPYKEKL DMYEQAISIE 

       610        620        630        640        650        660 
LSSLIELIEQ EEPSPEVWLT IKKSLINTST IFGKLKDLTY KRDKRLVDMV SKQGDVNNVW 

       670        680        690        700        710        720 
VQSVKELEME LSNKTERLAS IDKERRGLKK ILHKKLLESH ATAGNKESLE NDKEQESDTT 

       730        740        750        760        770        780 
ASTLGQIAKF ISATKEEDEA SDADEFYDAA ELVDEVTELT EAHPEISTAA APKHAPPPVP 

       790        800        810        820        830        840 
NETDNDSQYV QDEKSKIESN VEKTSQKFEK QNNLVTEDEP KTDQSLKNFK AEDKESQVKE 

       850        860        870        880        890        900 
KTKEIASSVI GEKTIVAVTT VQKRKEEYLL KEGSYLGYED GIRKRLSMDK DDRPKISLWA 

       910        920        930        940        950        960 
VLKSMVGKDM TRMTLPVTFN EPTSLLQRVA EDLEYSELLD QAATFEDSTL RTLYVAAFTA 

       970        980        990       1000       1010       1020 
SSYASTTKRV AKPFNPLLGE TFEYSRPDKQ YRFFTEQVSH HPPISATWTE SPRWDFWGES 

      1030       1040       1050       1060       1070       1080 
FVDTKFNGRS FNVKHLGLWH IKLRPNDNEK EELYTWKKPN NTVIGILIGN PQVDNHGEVN 

      1090       1100       1110       1120       1130       1140 
VVNHTTGDHC KLYFKARGWR SSGAYEITGE VYNKKKQKVW ILGGHWNEAI FAKKVVKDGD 

      1150       1160       1170       1180       1190       1200 
LSLEKTRTAA SAGNGPTDDG TKFLIWKAND RPEEPFNLTP FAITLNAPQP HLLPWLPPTD 

      1210       1220       1230       1240       1250       1260 
TRLRPDQRAM EDGRYDEAGD EKFRVEEKQR AARRKREENN LEYHPQWFVR DTHPITKAKY 

      1270       1280 
WRYTGKYWVK RRDHDLKDCG DIF 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"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.
[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]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z74066 Genomic DNA. Translation: CAA98577.1.
Z74067 Genomic DNA. Translation: CAA98578.1.
Z48432 Genomic DNA. Translation: CAA88340.1.
BK006938 Genomic DNA. Translation: DAA11831.1.
PIRS52500.
RefSeqNP_010265.1. NM_001180078.1.

3D structure databases

ProteinModelPortalQ12451.
SMRQ12451. Positions 23-247, 293-384, 897-1283.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32036. 46 interactions.
DIPDIP-6712N.
IntActQ12451. 5 interactions.
MINTMINT-599978.

Proteomic databases

MaxQBQ12451.
PaxDbQ12451.
PRIDEQ12451.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDL019C; YDL019C; YDL019C.
GeneID851543.
KEGGsce:YDL019C.

Organism-specific databases

CYGDYDL019c.
SGDS000002177. OSH2.

Phylogenomic databases

eggNOGCOG0666.
GeneTreeENSGT00710000106456.
HOGENOMHOG000186039.
KOK06867.
OMAITLNAPQ.
OrthoDBEOG7N903T.

Enzyme and pathway databases

BioCycYEAST:G3O-29448-MONOMER.

Gene expression databases

GenevestigatorQ12451.

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. 1 hit.
PF01237. Oxysterol_BP. 1 hit.
PF00169. PH. 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. 1 hit.
PS01013. OSBP. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio968952.

Entry information

Entry nameOSH2_YEAST
AccessionPrimary (citable) accession number: Q12451
Secondary accession number(s): D6VRX1, P89891
Entry history
Integrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: November 1, 1996
Last modified: June 11, 2014
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

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

Yeast

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

SIMILARITY comments

Index of protein domains and families