CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020312
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Oxysterol-binding protein-related protein 11 
Protein Synonyms/Alias
 ORP-11; OSBP-related protein 11 
Gene Name
 OSBPL11 
Gene Synonyms/Alias
 ORP11; OSBP12 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
395LPTFILEKRSLLEMYubiquitination[1, 2, 3, 4, 5, 6]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [5] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [6] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789
Functional Description
  
Sequence Annotation
 DOMAIN 58 155 PH.
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 13 13 Phosphoserine (By similarity).
 MOD_RES 15 15 Phosphoserine (By similarity).
 MOD_RES 27 27 Phosphothreonine.
 MOD_RES 62 62 Phosphotyrosine.
 MOD_RES 172 172 Phosphoserine.
 MOD_RES 174 174 Phosphoserine.
 MOD_RES 177 177 Phosphoserine (By similarity).
 MOD_RES 181 181 Phosphoserine.
 MOD_RES 184 184 Phosphoserine (By similarity).
 MOD_RES 189 189 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Lipid transport; Lipid-binding; Phosphoprotein; Polymorphism; Reference proteome; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 747 AA 
Protein Sequence
MQGGEPVSTM KVSESEGKLE GQATAVTPNK NSSCGGGISS SSSSRGGSAK GWQYSDHMEN 60
VYGYLMKYTN LVTGWQYRFF VLNNEAGLLE YFVNEQSRNQ KPRGTLQLAG AVISPSDEDS 120
HTFTVNAASG EQYKLRATDA KERQHWVSRL QICTQHHTEA IGKNNPPLKS RSFSLASSSN 180
SPISQRRPSQ NAISFFNVGH SKLQSLSKRT NLPPDHLVEV REMMSHAEGQ QRDLIRRIEC 240
LPTSGHLSSL DQDLLMLKAT SMATMNCLND CFHILQLQHA SHQKGSLPSG TTIEWLEPKI 300
SLSNHYKNGA DQPFATDQSK PVAVPEEQPV AESGLLAREP EEINADDEIE DTCDHKEDDL 360
GAVEEQRSVI LHLLSQLKLG MDLTRVVLPT FILEKRSLLE MYADFMSHPD LFIAITNGAT 420
AEDRMIRFVE YYLTSFHEGR KGAIAKKPYN PIIGETFHCS WKMPKSEVAS SVFSSSSTQG 480
VTNHAPLSGE SLTQVGSDCY TVRFVAEQVS HHPPVSGFYA ECTERKMCVN AHVWTKSKFL 540
GMSIGVTMVG EGILSLLEHG EEYTFSLPCA YARSILTVPW VELGGKVSVN CAKTGYSASI 600
TFHTKPFYGG KLHRVTAEVK HNITNTVVCR VQGEWNSVLE FTYSNGETKY VDLTKLAVTK 660
KRVRPLEKQD PFESRRLWKN VTDSLRESEI DKATEHKHTL EERQRTEERH RTETGTPWKT 720
KYFIKEGDGW VYHKPLWKII PTTQPAE 747 
Gene Ontology
 GO:0005543; F:phospholipid binding; IEA:InterPro.
 GO:0045444; P:fat cell differentiation; IMP:BHF-UCL.
 GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
 GO:0010890; P:positive regulation of sequestering of triglyceride; IMP:BHF-UCL. 
Interpro
 IPR000648; Oxysterol-bd.
 IPR018494; Oxysterol-bd_CS.
 IPR011993; PH_like_dom.
 IPR001849; Pleckstrin_homology. 
Pfam
 PF01237; Oxysterol_BP
 PF00169; PH 
SMART
 SM00233; PH 
PROSITE
 PS01013; OSBP
 PS50003; PH_DOMAIN 
PRINTS