CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011855
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Oxysterol-binding protein homolog 2 
Protein Synonyms/Alias
  
Gene Name
 OSH2 
Gene Synonyms/Alias
 YDL019C; D2845 
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
255KNIKLPAKPSNNVTPubiquitination[1]
587KAQYGPYKEKLDMYEubiquitination[1]
652RLVDMVSKQGDVNNVubiquitination[1]
821LVTEDEPKTDQSLKNubiquitination[1]
827PKTDQSLKNFKAEDKubiquitination[1]
834KNFKAEDKESQVKEKubiquitination[1]
Reference
 [1] 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, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301
Functional Description
 Lipid-binding protein involved in maintenance of intracellular sterol distribution and homeostasis. Binds to phosphoinositides. 
Sequence Annotation
 REPEAT 106 134 ANK 1.
 REPEAT 206 235 ANK 2.
 DOMAIN 289 386 PH.
 MOTIF 745 751 FFAT.
 MOD_RES 422 422 Phosphoserine.
 MOD_RES 445 445 Phosphoserine.
 MOD_RES 451 451 Phosphoserine.
 MOD_RES 455 455 Phosphoserine.
 MOD_RES 458 458 Phosphoserine.
 MOD_RES 459 459 Phosphoserine.
 MOD_RES 486 486 Phosphoserine.
 MOD_RES 488 488 Phosphothreonine.
 MOD_RES 512 512 Phosphoserine.
 MOD_RES 515 515 Phosphoserine.
 MOD_RES 717 717 Phosphoserine.
 MOD_RES 783 783 Phosphothreonine.
 MOD_RES 787 787 Phosphoserine.
 MOD_RES 825 825 Phosphoserine.
 MOD_RES 1151 1151 Phosphoserine.  
Keyword
 ANK repeat; Cell membrane; Complete proteome; Lipid transport; Lipid-binding; Membrane; Phosphoprotein; Reference proteome; Repeat; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1283 AA 
Protein Sequence
MSREDLSIAE DLNQVSKPLL KVKLLEVLGQ GDFKHLKALV DNEFQPKDDP SVQQVLNLIL 60
HYAVQVAPIL LIKEIVAHWV DQVGDEKSSS KSDDGIHLDL NYQDENGNTP LHLAAAQSRS 120
DVISFLLSQK SINDCVKNKA HQQPLDMCKD LNVAQMIQLK RDDYFLETVH SLRAAMNKRD 180
FSKLDSIWKN PRNLNLLDIN GIDPETGTTL LYEYSQKKDI EMCQWLLKHG AEATVKDGKG 240
RSPLDLVKNI KLPAKPSNNV TPEIKLKNLL EKNLREQAIV HEDVASSKPP TYKGFLKKWT 300
NFAHGYKLRW FILSGDGNLS YYKDQSHVDR PRGTLKVSTC RLHIDSSEKL NFELLGGITG 360
TTRWRLKGNH PIETTRWVNA IQSAIRFAKD KEILNKKKAV PPSLALKNKS PALISHSKTQ 420
GSLPEASQYY QHTLHKEVIQ PSSVSLYRRP SNNLSVVSSE IQLNDNLTES GKRFVSKMIE 480
NRLDGSKTPV GVHTGSALQR VRSSNTLKSN RSMQSGSGVA SPIDKVPNGA NLSQSNTTTG 540
STASLSDNNY IDNFEGDEAN SDDEEEDLGI NFDRDEEYIK AQYGPYKEKL DMYEQAISIE 600
LSSLIELIEQ EEPSPEVWLT IKKSLINTST IFGKLKDLTY KRDKRLVDMV SKQGDVNNVW 660
VQSVKELEME LSNKTERLAS IDKERRGLKK ILHKKLLESH ATAGNKESLE NDKEQESDTT 720
ASTLGQIAKF ISATKEEDEA SDADEFYDAA ELVDEVTELT EAHPEISTAA APKHAPPPVP 780
NETDNDSQYV QDEKSKIESN VEKTSQKFEK QNNLVTEDEP KTDQSLKNFK AEDKESQVKE 840
KTKEIASSVI GEKTIVAVTT VQKRKEEYLL KEGSYLGYED GIRKRLSMDK DDRPKISLWA 900
VLKSMVGKDM TRMTLPVTFN EPTSLLQRVA EDLEYSELLD QAATFEDSTL RTLYVAAFTA 960
SSYASTTKRV AKPFNPLLGE TFEYSRPDKQ YRFFTEQVSH HPPISATWTE SPRWDFWGES 1020
FVDTKFNGRS FNVKHLGLWH IKLRPNDNEK EELYTWKKPN NTVIGILIGN PQVDNHGEVN 1080
VVNHTTGDHC KLYFKARGWR SSGAYEITGE VYNKKKQKVW ILGGHWNEAI FAKKVVKDGD 1140
LSLEKTRTAA SAGNGPTDDG TKFLIWKAND RPEEPFNLTP FAITLNAPQP HLLPWLPPTD 1200
TRLRPDQRAM EDGRYDEAGD EKFRVEEKQR AARRKREENN LEYHPQWFVR DTHPITKAKY 1260
WRYTGKYWVK RRDHDLKDCG DIF 1283 
Gene Ontology
 GO:0005935; C:cellular bud neck; IDA:SGD.
 GO:0032541; C:cortical endoplasmic reticulum; IDA:SGD.
 GO:0005886; C:plasma membrane; 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:0030011; P:maintenance of cell polarity; IGI:SGD. 
Interpro
 IPR002110; Ankyrin_rpt.
 IPR020683; Ankyrin_rpt-contain_dom.
 IPR000648; Oxysterol-bd.
 IPR018494; Oxysterol-bd_CS.
 IPR011993; PH_like_dom.
 IPR001849; Pleckstrin_homology. 
Pfam
 PF00023; Ank
 PF01237; Oxysterol_BP
 PF00169; PH 
SMART
 SM00248; ANK
 SM00233; PH 
PROSITE
 PS50297; ANK_REP_REGION
 PS50088; ANK_REPEAT
 PS01013; OSBP
 PS50003; PH_DOMAIN 
PRINTS