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Protein

Oxysterol-binding protein homolog 2

Gene

OSH2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: 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.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. ER to Golgi ceramide transport Source: SGD
  3. exocytosis Source: SGD
  4. maintenance of cell polarity Source: SGD
  5. sterol transport Source: SGD
Complete GO annotation...

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 Componenti: Chromosome IV

Organism-specific databases

CYGDiYDL019c.
EuPathDBiFungiDB:YDL019C.
SGDiS000002177. OSH2.

Subcellular locationi

  1. Cell membrane 2 Publications; Peripheral membrane protein 2 Publications

  2. 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. nuclear envelope Source: SGD
  5. plasma membrane Source: SGD
Complete GO annotation...

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 99-246, 289-384, 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.
GeneTreeiENSGT00760000119155.
HOGENOMiHOG000186039.
InParanoidiQ12451.
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

        10         20         30         40         50
MSREDLSIAE DLNQVSKPLL KVKLLEVLGQ GDFKHLKALV DNEFQPKDDP
60 70 80 90 100
SVQQVLNLIL HYAVQVAPIL LIKEIVAHWV DQVGDEKSSS KSDDGIHLDL
110 120 130 140 150
NYQDENGNTP LHLAAAQSRS DVISFLLSQK SINDCVKNKA HQQPLDMCKD
160 170 180 190 200
LNVAQMIQLK RDDYFLETVH SLRAAMNKRD FSKLDSIWKN PRNLNLLDIN
210 220 230 240 250
GIDPETGTTL LYEYSQKKDI EMCQWLLKHG AEATVKDGKG RSPLDLVKNI
260 270 280 290 300
KLPAKPSNNV TPEIKLKNLL EKNLREQAIV HEDVASSKPP TYKGFLKKWT
310 320 330 340 350
NFAHGYKLRW FILSGDGNLS YYKDQSHVDR PRGTLKVSTC RLHIDSSEKL
360 370 380 390 400
NFELLGGITG TTRWRLKGNH PIETTRWVNA IQSAIRFAKD KEILNKKKAV
410 420 430 440 450
PPSLALKNKS PALISHSKTQ GSLPEASQYY QHTLHKEVIQ PSSVSLYRRP
460 470 480 490 500
SNNLSVVSSE IQLNDNLTES GKRFVSKMIE NRLDGSKTPV GVHTGSALQR
510 520 530 540 550
VRSSNTLKSN RSMQSGSGVA SPIDKVPNGA NLSQSNTTTG STASLSDNNY
560 570 580 590 600
IDNFEGDEAN SDDEEEDLGI NFDRDEEYIK AQYGPYKEKL DMYEQAISIE
610 620 630 640 650
LSSLIELIEQ EEPSPEVWLT IKKSLINTST IFGKLKDLTY KRDKRLVDMV
660 670 680 690 700
SKQGDVNNVW VQSVKELEME LSNKTERLAS IDKERRGLKK ILHKKLLESH
710 720 730 740 750
ATAGNKESLE NDKEQESDTT ASTLGQIAKF ISATKEEDEA SDADEFYDAA
760 770 780 790 800
ELVDEVTELT EAHPEISTAA APKHAPPPVP NETDNDSQYV QDEKSKIESN
810 820 830 840 850
VEKTSQKFEK QNNLVTEDEP KTDQSLKNFK AEDKESQVKE KTKEIASSVI
860 870 880 890 900
GEKTIVAVTT VQKRKEEYLL KEGSYLGYED GIRKRLSMDK DDRPKISLWA
910 920 930 940 950
VLKSMVGKDM TRMTLPVTFN EPTSLLQRVA EDLEYSELLD QAATFEDSTL
960 970 980 990 1000
RTLYVAAFTA SSYASTTKRV AKPFNPLLGE TFEYSRPDKQ YRFFTEQVSH
1010 1020 1030 1040 1050
HPPISATWTE SPRWDFWGES FVDTKFNGRS FNVKHLGLWH IKLRPNDNEK
1060 1070 1080 1090 1100
EELYTWKKPN NTVIGILIGN PQVDNHGEVN VVNHTTGDHC KLYFKARGWR
1110 1120 1130 1140 1150
SSGAYEITGE VYNKKKQKVW ILGGHWNEAI FAKKVVKDGD LSLEKTRTAA
1160 1170 1180 1190 1200
SAGNGPTDDG TKFLIWKAND RPEEPFNLTP FAITLNAPQP HLLPWLPPTD
1210 1220 1230 1240 1250
TRLRPDQRAM EDGRYDEAGD EKFRVEEKQR AARRKREENN LEYHPQWFVR
1260 1270 1280
DTHPITKAKY WRYTGKYWVK RRDHDLKDCG DIF
Length:1,283
Mass (Da):145,796
Last modified:November 1, 1996 - v1
Checksum:iD521957460E7F7C3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ12451.
SMRiQ12451. Positions 99-246, 289-384, 897-1283.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

MaxQBiQ12451.
PaxDbiQ12451.
PRIDEiQ12451.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CYGDiYDL019c.
EuPathDBiFungiDB:YDL019C.
SGDiS000002177. OSH2.

Phylogenomic databases

eggNOGiCOG0666.
GeneTreeiENSGT00760000119155.
HOGENOMiHOG000186039.
InParanoidiQ12451.
KOiK06867.
OMAiITLNAPQ.
OrthoDBiEOG7N903T.

Enzyme and pathway databases

BioCyciYEAST:G3O-29448-MONOMER.

Miscellaneous databases

NextBioi968952.
PROiQ12451.

Gene expression databases

GenevestigatoriQ12451.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: April 29, 2015
This is version 138 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.