CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021343
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Golgi resident protein GCP60 
Protein Synonyms/Alias
 Acyl-CoA-binding domain-containing protein 3; Golgi complex-associated protein 1; GOCAP1; Golgi phosphoprotein 1; GOLPH1; PBR- and PKA-associated protein 7; Peripheral benzodiazepine receptor-associated protein PAP7 
Gene Name
 ACBD3 
Gene Synonyms/Alias
 GCP60; GOCAP1; GOLPH1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
163DAMVEFVKLLNRCCHubiquitination[1, 2]
347THTDSSEKELEPEAAacetylation[3]
386QIKDFKEKIQQDADSubiquitination[4, 5, 6, 7, 8, 9]
507GRGVYLLKFDNSYSLubiquitination[1, 2, 4, 6, 7, 8, 9, 10, 11]
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] 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]
 [3] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [4] 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]
 [5] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [10] 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]
 [11] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724
Functional Description
 Involved in the maintenance of Golgi structure by interacting with giantin, affecting protein transport between the endoplasmic reticulum and Golgi. Involved in hormone-induced steroid biosynthesis in testicular Leydig cells (By similarity). 
Sequence Annotation
 DOMAIN 83 174 ACB.
 DOMAIN 384 526 GOLD.
 MOD_RES 13 13 Phosphoserine.
 MOD_RES 20 20 Phosphoserine.
 MOD_RES 43 43 Phosphoserine.  
Keyword
 Coiled coil; Complete proteome; Direct protein sequencing; Golgi apparatus; Lipid biosynthesis; Lipid metabolism; Membrane; Mitochondrion; Phosphoprotein; Polymorphism; Reference proteome; Steroid biosynthesis. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 528 AA 
Protein Sequence
MAAVLNAERL EVSVDGLTLS PDPEERPGAE GAPLLPPPLP PPSPPGSGRG PGASGEQPEP 60
GEAAAGGAAE EARRLEQRWG FGLEELYGLA LRFFKEKDGK AFHPTYEEKL KLVALHKQVL 120
MGPYNPDTCP EVGFFDVLGN DRRREWAALG NMSKEDAMVE FVKLLNRCCH LFSTYVASHK 180
IEKEEQEKKR KEEEERRRRE EEERERLQKE EEKRRREEEE RLRREEEERR RIEEERLRLE 240
QQKQQIMAAL NSQTAVQFQQ YAAQQYPGNY EQQQILIRQL QEQHYQQYMQ QLYQVQLAQQ 300
QAALQKQQEV VVAGSSLPTS SKVNATVPSN MMSVNGQAKT HTDSSEKELE PEAAEEALEN 360
GPKESLPVIA APSMWTRPQI KDFKEKIQQD ADSVITVGRG EVVTVRVPTH EEGSYLFWEF 420
ATDNYDIGFG VYFEWTDSPN TAVSVHVSES SDDDEEEEEN IGCEEKAKKN ANKPLLDEIV 480
PVYRRDCHEE VYAGSHQYPG RGVYLLKFDN SYSLWRSKSV YYRVYYTR 528 
Gene Ontology
 GO:0005794; C:Golgi apparatus; IDA:HPA.
 GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
 GO:0016021; C:integral to membrane; IEA:InterPro.
 GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
 GO:0000062; F:fatty-acyl-CoA binding; IEA:InterPro.
 GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW.
 GO:0006810; P:transport; IEA:InterPro. 
Interpro
 IPR022408; Acyl-CoA-binding_prot_CS.
 IPR000582; Acyl-CoA-binding_protein.
 IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
 IPR009038; GOLD. 
Pfam
 PF00887; ACBP
 PF13897; GOLD_2 
SMART
  
PROSITE
 PS00880; ACB_1
 PS51228; ACB_2
 PS50866; GOLD 
PRINTS