CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021382
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Oxysterol-binding protein-related protein 3 
Protein Synonyms/Alias
 ORP-3; OSBP-related protein 3 
Gene Name
 OSBPL3 
Gene Synonyms/Alias
 KIAA0704; ORP3; OSBP3 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
55TQEPPVQKGFLLKKRubiquitination[1, 2, 3, 4]
129HIYHLKVKSEEVFDEubiquitination[2]
542NIGKDLSKVAMPVELubiquitination[2, 5]
829LEEAEIQKQRIEQLQubiquitination[2, 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] 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]
 [4] 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]
 [5] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [6] 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
Functional Description
  
Sequence Annotation
 DOMAIN 51 146 PH.
 MOD_RES 16 16 Phosphoserine.
 MOD_RES 34 34 Phosphoserine.
 MOD_RES 251 251 Phosphoserine.
 MOD_RES 304 304 Phosphoserine.
 MOD_RES 372 372 Phosphoserine.
 MOD_RES 410 410 Phosphoserine.
 MOD_RES 437 437 Phosphoserine.  
Keyword
 Alternative splicing; Complete proteome; Lipid transport; Lipid-binding; Phosphoprotein; Polymorphism; Reference proteome; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 887 AA 
Protein Sequence
MMSDEKNLGV SQKLVSPSRS TSSCSSKQGS RQDSWEVVEG LRGEMNYTQE PPVQKGFLLK 60
KRKWPLKGWH KRFFYLDKGI LKYAKSQTDI EREKLHGCID VGLSVMSVKK SSKCIDLDTE 120
EHIYHLKVKS EEVFDEWVSK LRHHRMYRQN EIAMFPHEVN HFFSGSTITD SSSGVFDSIS 180
SRKRSSISKQ NLFQTGSNVS FSCGGETRVP LWLQSSEDME KCSKDLAHCH AYLVEMSQLL 240
QSMDVLHRTY SAPAINAIQG GSFESPKKEK RSHRRWRSRA IGKDAKGTLQ VPKPFSGPVR 300
LHSSNPNLST LDFGEEKNYS DGSETSSEFS KMQEDLCHIA HKVYFTLRSA FNIMSAEREK 360
LKQLMEQDAS SSPSAQVIGL KNALSSALAQ NTDLKERLRR IHAESLLLDS PAVAKSGDNL 420
AEENSRDENR ALVHQLSNES RLSITDSLSE FFDAQEVLLS PSSSENEISD DDSYVSDISD 480
NLSLDNLSND LDNERQTLGP VLDSGREAKS RRRTCLPAPC PSSSNISLWN ILRNNIGKDL 540
SKVAMPVELN EPLNTLQRLC EELEYSELLD KAAQIPSPLE RMVYVAAFAI SAYASSYYRA 600
GSKPFNPVLG ETYECIREDK GFQFFSEQVS HHPPISACHA ESRNFVFWQD VRWKNKFWGK 660
SMEIVPIGTT HVTLPVFGDH FEWNKVTSCI HNILSGQRWI EHYGEIVIKN LHDDSCYCKV 720
NFIKAKYWST NAHEIEGTVF DRSGKAVHRL FGKWHESIYC GGGSSSACVW RANPMPKGYE 780
QYYSFTQFAL ELNEMDPSSK SLLPPTDTRF RPDQRFLEEG NLEEAEIQKQ RIEQLQRERR 840
RVLEENHVEH QPRFFRKSDD DSWVSNGTYL ELRKDLGFSK LDHPVLW 887 
Gene Ontology
 GO:0005829; C:cytosol; IDA:BHF-UCL.
 GO:0031965; C:nuclear membrane; IDA:BHF-UCL.
 GO:0097038; C:perinuclear endoplasmic reticulum; IDA:BHF-UCL.
 GO:0005886; C:plasma membrane; IDA:BHF-UCL.
 GO:0015485; F:cholesterol binding; IDA:BHF-UCL.
 GO:0005543; F:phospholipid binding; IEA:InterPro.
 GO:0006869; P:lipid transport; IEA:UniProtKB-KW. 
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