CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006983
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Oxysterol-binding protein homolog 3 
Protein Synonyms/Alias
  
Gene Name
 OSH3 
Gene Synonyms/Alias
 YHR073W 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
548EETPLLGKSDQNEFTubiquitination[1, 2]
Reference
 [1] Sites of ubiquitin attachment in Saccharomyces cerevisiae.
 Starita LM, Lo RS, Eng JK, von Haller PD, Fields S.
 Proteomics. 2012 Jan;12(2):236-40. [PMID: 22106047]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301] 
Functional Description
  
Sequence Annotation
 DOMAIN 221 315 PH.
 MOTIF 514 520 FFAT.
 MOD_RES 190 190 Phosphoserine.
 MOD_RES 193 193 Phosphoserine.
 MOD_RES 210 210 Phosphothreonine.
 MOD_RES 323 323 Phosphothreonine.
 MOD_RES 324 324 Phosphoserine.
 MOD_RES 325 325 Phosphothreonine.
 MOD_RES 605 605 Phosphoserine.  
Keyword
 Complete proteome; Cytoplasm; Lipid transport; Lipid-binding; Phosphoprotein; Reference proteome; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 996 AA 
Protein Sequence
METIDIQNRS FVVRWVKCGR GDVINYQIKP LKKSIEVGIY KKLKSSVDDH ASAVHIAPDT 60
KTLLDYTTKS LLHKGSSSNI EEHHRRSSQH SHSSSNGSDN KRKERSYSSL SISGIQQQSQ 120
EIPLREKLSA SGFTLVKRVG NVSGNTMVQG DLEVKDTDYY YAFILDNSSS KNAKKKILFN 180
ASVINGDNQS MISTRSTPPA RPTALSRTST QQDMLFRVGQ GRYLQGYLLK KRRKRLQGFK 240
KRFFTLDFRY GTLSYYLNDH NQTCRGEIVI SLSSVSANKK DKIIIIDSGM EVWVLKATTK 300
ENWQSWVDAL QTCFDDQFED KDTSTLEENP DILDDDKEVI NKSSPQDHDH LTPTATTKSA 360
LSHRQHTQKD MDDIYVPLPS ESYATFSMNL RLIQQRLEQC KKDSLSYKPT TLHQRSEGLN 420
GTHSSSSVFT NNRVSSFNHS SSGMTSSDSL ASEEVPSNKT YIEHALYNQL ADLEVFVSRF 480
VTQGEVLFKD HQILCKKAKD TRVSLTSYLS ENDEFFDAEE EISRGVIILP DTEDDINNIV 540
EETPLLGKSD QNEFTKEVQL SGSEQIASSS VESYTTNDEN HSRKHLKNRH KNRRRGHPHH 600
QKTKSAQSST ETFTSKDLFA LSYPKSVTRR NDIPEAAASP PSLLSFLRKN VGKDLSSIAM 660
PVTSNEPISI LQLISETFEY APLLTKATQR PDPITFVSAF AISFLSIYRD KTRTLRKPFN 720
PLLAETFELI REDMGFRLIS EKVSHRPPVF AFFAEHLDWE CSYTVTPSQK FWGKSIELNN 780
EGILRLKFKT TGELFEWTQP TTILKNLIAG ERYMEPVNEF EVHSSKGDKS HILFDKAGMF 840
SGRSEGFKVS IIPPPSSNRK KETLAGKWTQ SLANETTHET IWEVGDLVSN PKKKYGFTKF 900
TANLNEITEI EKGNLPPTDS RLRPDIRAYE EGNVDKAEEW KLKLEQLQRE RRNKGQDVEP 960
KYFEKVSKNE WKYITGPKSY WERRKKHDWS DISQLW 996 
Gene Ontology
 GO:0032541; C:cortical endoplasmic reticulum; IDA:SGD.
 GO:0005545; F:1-phosphatidylinositol binding; ISS:SGD.
 GO:0008142; F:oxysterol binding; ISS:SGD.
 GO:0015248; F:sterol transporter activity; IDA:SGD.
 GO:0006897; P:endocytosis; IGI:SGD.
 GO:0006887; P:exocytosis; IGI:SGD.
 GO:0001403; P:invasive growth in response to glucose limitation; IGI:SGD.
 GO:0000742; P:karyogamy involved in conjugation with cellular fusion; IGI:SGD.
 GO:0030011; P:maintenance of cell polarity; IGI:SGD.
 GO:0010922; P:positive regulation of phosphatase activity; IDA:SGD.
 GO:0007124; P:pseudohyphal growth; IMP:SGD. 
Interpro
 IPR000648; Oxysterol-bd.
 IPR018494; Oxysterol-bd_CS.
 IPR011993; PH_like_dom.
 IPR001849; Pleckstrin_homology. 
Pfam
 PF01237; Oxysterol_BP 
SMART
 SM00233; PH 
PROSITE
 PS01013; OSBP
 PS50003; PH_DOMAIN 
PRINTS