Q12451 (OSH2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Oxysterol-binding protein homolog 2

Gene names

Name:	OSH2
Ordered Locus Names:	YDL019C
ORF Names:	D2845

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	1283 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Lipid transport Transport
Cellular component	Cell membrane Membrane
Domain	ANK repeat Repeat
Ligand	Lipid-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	endocytosis Inferred from genetic interaction Ref.7. Source: SGD exocytosis Inferred from genetic interaction PubMed 17004323. Source: SGD maintenance of cell polarity Inferred from genetic interaction PubMed 17004323. Source: SGD
Cellular_component	cellular bud neck Inferred from direct assay Ref.3. Source: SGD cortical endoplasmic reticulum Inferred from direct assay PubMed 20008566. Source: SGD plasma membrane Inferred from direct assay Ref.3. Source: SGD
Molecular_function	1-phosphatidylinositol binding Inferred from sequence or structural similarity Ref.4. Source: SGD oxysterol binding Inferred from sequence or structural similarity Ref.4. Source: SGD sterol transporter activity Inferred from direct assay PubMed 20008566. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MYO5	Q04439	3	EBI-12621,EBI-11687

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1283	1283	Oxysterol-binding protein homolog 2		PRO_0000100388
Regions
	Repeat	106 – 134	29	ANK 1
	Repeat	206 – 235	30	ANK 2
	Domain	289 – 386	98	PH
	Motif	745 – 751	7	FFAT
Amino acid modifications
	Modified residue	7	1	Phosphoserine Ref.10
	Modified residue	422	1	Phosphoserine Ref.9 Ref.11
	Modified residue	445	1	Phosphoserine Ref.11
	Modified residue	488	1	Phosphothreonine Ref.11
	Modified residue	503	1	Phosphoserine Ref.9
	Modified residue	515	1	Phosphoserine Ref.11
	Modified residue	722	1	Phosphoserine Ref.11
	Modified residue	732	1	Phosphoserine Ref.11
	Modified residue	783	1	Phosphothreonine Ref.10
	Modified residue	787	1	Phosphoserine Ref.10 Ref.11
	Modified residue	825	1	Phosphoserine Ref.10 Ref.11
	Modified residue	1146	1	Phosphothreonine Ref.10 Ref.11
	Modified residue	1148	1	Phosphothreonine Ref.10 Ref.11
	Modified residue	1151	1	Phosphoserine Ref.10 Ref.11

Sequences

	Sequence		Length	Mass (Da)
	Q12451 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: D521957460E7F7C3	FASTA	1,283	145,796
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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]	"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 AND SER-503, MASS SPECTROMETRY.
[10]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; THR-783; SER-787; SER-825; THR-1146; THR-1148 AND SER-1151, MASS SPECTROMETRY.
[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; SER-445; THR-488; SER-515; SER-722; SER-732; SER-787; SER-825; THR-1146; THR-1148 AND SER-1151, MASS SPECTROMETRY.
+	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.
PIR	S52500.
RefSeq	NP_010265.1. NM_001180078.1.
3D structure databases
ProteinModelPortal	Q12451.
SMR	Q12451. Positions 24-247, 293-384, 888-1248.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6712N.
IntAct	Q12451. 3 interactions.
MINT	MINT-599978.
Proteomic databases
PaxDb	Q12451.
PRIDE	Q12451.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YDL019C; YDL019C; YDL019C.
GeneID	851543.
KEGG	sce:YDL019C.
Organism-specific databases
CYGD	YDL019c.
SGD	S000002177. OSH2.
Phylogenomic databases
eggNOG	COG0666.
GeneTree	ENSGT00700000104473.
HOGENOM	HOG000186039.
KO	K06867.
OMA	SPTIDHY.
OrthoDB	EOG4G7G6M.
Enzyme and pathway databases
BioCyc	YEAST:G3O-29448-MONOMER.
Gene expression databases
Genevestigator	Q12451.
GermOnline	YDL019C. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	1.25.40.20. 2 hits. 2.30.29.30. 1 hit.
InterPro	IPR002110. Ankyrin_rpt. IPR020683. Ankyrin_rpt-contain_dom. IPR000648. Oxysterol-bd. IPR018494. Oxysterol-bd_CS. IPR011993. PH_like_dom. IPR001849. Pleckstrin_homology. [Graphical view]
PANTHER	PTHR10972. PTHR10972. 1 hit.
Pfam	PF00023. Ank. 1 hit. PF01237. Oxysterol_BP. 1 hit. PF00169. PH. 1 hit. [Graphical view]
SMART	SM00248. ANK. 2 hits. SM00233. PH. 1 hit. [Graphical view]
SUPFAM	SSF48403. ANK. 1 hit.
PROSITE	PS50297. ANK_REP_REGION. 2 hits. PS50088. ANK_REPEAT. 1 hit. PS01013. OSBP. 1 hit. PS50003. PH_DOMAIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	968952.

Entry information

Entry name

OSH2_YEAST

Accession

Primary (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:	May 29, 2013
This is version 120 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program