CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005037
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Oxysterol-binding protein 1 
Protein Synonyms/Alias
  
Gene Name
 OSBP 
Gene Synonyms/Alias
 OSBP1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
103FKWTNYIKGYQRRWFacetylation[1]
230TCNDLIAKHGTALQRubiquitination[2]
292THSKKWQKSLQYERDubiquitination[3]
429IMKNCIGKELSKIPMubiquitination[4]
433CIGKELSKIPMPVNFubiquitination[2, 5]
493TTVFRTSKPFNPLLGubiquitination[5]
544WTLRQEIKITSKFRGubiquitination[2]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] 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]
 [3] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [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] 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
Functional Description
 Binds cholesterol and a range of oxysterols. Cholesterol binding promotes the formation of a complex with PP2A and a tyrosine phosphatase which dephosphorylate ERK1/2, whereas 25- hydroxycholesterol causes its disassembly. Regulates cholesterol efflux by decreasing ABCA1 stability. 
Sequence Annotation
 DOMAIN 88 181 PH.
 REGION 406 457 Sterol binding (By similarity).
 MOD_RES 103 103 N6-acetyllysine.
 MOD_RES 190 190 Phosphoserine.
 MOD_RES 193 193 Phosphoserine.
 MOD_RES 198 198 Phosphoserine.
 MOD_RES 238 238 Phosphoserine (By similarity).
 MOD_RES 351 351 Phosphoserine.
 MOD_RES 377 377 Phosphothreonine (By similarity).
 MOD_RES 379 379 Phosphoserine (By similarity).
 MOD_RES 382 382 Phosphoserine.
 MOD_RES 389 389 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Coiled coil; Complete proteome; Cytoplasm; Golgi apparatus; Lipid transport; Lipid-binding; Membrane; Phosphoprotein; Polymorphism; Reference proteome; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 807 AA 
Protein Sequence
MAATELRGVV GPGPAAIAAL GGGGAGPPVV GGGGGRGDAG PGSGAASGTV VAAAAGGPGP 60
GAGGVAAAGP APAPPTGGSG GSGAGGSGSA REGWLFKWTN YIKGYQRRWF VLSNGLLSYY 120
RSKAEMRHTC RGTINLATAN ITVEDSCNFI ISNGGAQTYH LKASSEVERQ RWVTALELAK 180
AKAVKMLAES DESGDEESVS QTDKTELQNT LRTLSSKVED LSTCNDLIAK HGTALQRSLS 240
ELESLKLPAE SNEKIKQVNE RATLFRITSN AMINACRDFL MLAQTHSKKW QKSLQYERDQ 300
RIRLEETLEQ LAKQHNHLER AFRGATVLPA NTPGNVGSGK DQCCSGKGDM SDEDDENEFF 360
DAPEIITMPE NLGHKRTGSN ISGASSDISL DEQYKHQLEE TKKEKRTRIP YKPNYSLNLW 420
SIMKNCIGKE LSKIPMPVNF NEPLSMLQRL TEDLEYHELL DRAAKCENSL EQLCYVAAFT 480
VSSYSTTVFR TSKPFNPLLG ETFELDRLEE NGYRSLCEQV SHHPPAAAHH AESKNGWTLR 540
QEIKITSKFR GKYLSIMPLG TIHCIFHATG HHYTWKKVTT TVHNIIVGKL WIDQSGEIDI 600
VNHKTGDKCN LKFVPYSYFS RDVARKVTGE VTDPSGKVHF ALLGTWDEKM ECFKVQPVIG 660
ENGGDARQRG HEAEESRVML WKRNPLPKNA ENMYYFSELA LTLNAWESGT APTDSRLRPD 720
QRLMENGRWD EANAEKQRLE EKQRLSRKKR EAEAMKATED GTPYDPYKAL WFERKKDPVT 780
KELTHIYRGE YWECKEKQDW SSCPDIF 807 
Gene Ontology
 GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
 GO:0008142; F:oxysterol binding; TAS:ProtInc.
 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