CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-025528
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 ATP-citrate synthase 
Protein Synonyms/Alias
  
Gene Name
 Acly 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
488SPRSLQGKSATLFSRacetylation[1]
488SPRSLQGKSATLFSRubiquitination[2]
538YPFTGDHKQKFYWGHacetylation[3]
538YPFTGDHKQKFYWGHubiquitination[2]
540FTGDHKQKFYWGHKEacetylation[4]
546QKFYWGHKEILIPVFacetylation[5]
546QKFYWGHKEILIPVFubiquitination[2]
554EILIPVFKNMADAMKacetylation[1, 3, 5, 6]
616LIKKADQKGVTIIGPubiquitination[2]
630PATVGGIKPGCFKIGacetylation[5]
630PATVGGIKPGCFKIGubiquitination[2]
650LDNILASKLYRPGSVubiquitination[2]
780VAKNQALKEAGVFVPubiquitination[2]
836RELGLIRKPASFMTSacetylation[5]
836RELGLIRKPASFMTSubiquitination[2]
918IICARAGKDLVSSLTubiquitination[2]
944GALDAAAKMFSKAFDubiquitination[2]
948AAAKMFSKAFDSGIIacetylation[3, 5]
948AAAKMFSKAFDSGIIubiquitination[2]
962IPMEFVNKMKKEGKLacetylation[5]
962IPMEFVNKMKKEGKLubiquitination[2]
968NKMKKEGKLIMGIGHacetylation[4, 6]
978MGIGHRVKSINNPDMacetylation[1, 5]
978MGIGHRVKSINNPDMubiquitination[2]
991DMRVQILKDFVKQHFacetylation[5]
991DMRVQILKDFVKQHFubiquitination[2]
1077IGHYLDQKRLKQGLYubiquitination[2]
1080YLDQKRLKQGLYRHPubiquitination[2]
Reference
 [1] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [2] 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]
 [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] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [5] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [6] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758] 
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1101 AA 
Protein Sequence
MSAKAISEQT GKELLYKYIC TTSAIQNRFK YARVTPDTDW AHLLQDHPWL LSQSLVVKPD 60
QLIKRRGKLG LVGVNLSLDG VKSWLKPRLG HEATVGKAKG FLKNFLIEPF VPHSQAEEFY 120
VCIYATREGD YVLFHHEGGV DVGDVDAKAQ KLLVGVDEKL NTEDIKRHLL VHAPEDKKEV 180
LASFISGLFN FYEDLYFTYL EINPLVVTKD GVYILDLAAK VDATADYICK VKWGDIEFPP 240
PFGREAYPEE AYIADLDAKS GASLKLTLLN PKGRIWTMVA GGGASVVYSD TICDLGGVNE 300
LANYGEYSGA PSEQQTYDYA KTILSLMTRE KHPEGKILII GGSIANFTNV AATFKGIVRA 360
IRDYQGPLKE HEVTIFVRRG GPNYQEGLRV MGEVGKTTGI PIHVFGTETH MTAIVGMALG 420
HRPIPNQPPT AAHTANFLLN ASGSTSTPAP SRTASFSESR ADEVAPAKKA KPAMPQDSVP 480
SPRSLQGKSA TLFSRHTKAI VWGMQTRAVQ GMLDFDYVCS RDEPSVAAMV YPFTGDHKQK 540
FYWGHKEILI PVFKNMADAM KKHPEVDVLI NFASLRSAYD STMETMNYAQ IRTIAIIAEG 600
IPEALTRKLI KKADQKGVTI IGPATVGGIK PGCFKIGNTG GMLDNILASK LYRPGSVAYV 660
SRSGGMSNEL NNIISRTTDG VYEGVAIGGD RYPGSTFMDH VLRYQDTPGV KMIVVLGEIG 720
GTEEYKICRG IKEGRLTKPV VCWCIGTCAT MFSSEVQFGH AGACANQASE TAVAKNQALK 780
EAGVFVPRSF DELGEIIQSV YEDLVAKGAI VPAQEVPPPT VPMDYSWARE LGLIRKPASF 840
MTSICDERGQ ELIYAGMPIT EVFKEEMGIG GVLGLLWFQR RLPKYSCQFI EMCLMVTADH 900
GPAVSGAHNT IICARAGKDL VSSLTSGLLT IGDRFGGALD AAAKMFSKAF DSGIIPMEFV 960
NKMKKEGKLI MGIGHRVKSI NNPDMRVQIL KDFVKQHFPA TPLLDYALEV EKITTSKKPN 1020
LILNVDGFIG VAFVDMLRNC GSFTREEADE YVDIGALNGI FVLGRSMGFI GHYLDQKRLK 1080
QGLYRHPWDD ISYVLPEHMS M 1101 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0005886; C:plasma membrane; IEA:Compara.
 GO:0005524; F:ATP binding; IEA:InterPro.
 GO:0003878; F:ATP citrate synthase activity; TAS:MGI.
 GO:0048037; F:cofactor binding; IEA:InterPro.
 GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IEA:InterPro.
 GO:0006085; P:acetyl-CoA biosynthetic process; TAS:MGI.
 GO:0044262; P:cellular carbohydrate metabolic process; IEA:InterPro. 
Interpro
 IPR014608; ATP-citrate_synthase.
 IPR013650; ATP-grasp_succ-CoA_synth-type.
 IPR013816; ATP_grasp_subdomain_2.
 IPR017440; Cit_synth/succinyl-CoA_lig_AS.
 IPR016143; Citrate_synth-like_sm_a-sub.
 IPR002020; Citrate_synthase-like.
 IPR016141; Citrate_synthase-like_core.
 IPR003781; CoA-bd.
 IPR005810; CoA_lig_alpha.
 IPR005811; CoA_ligase.
 IPR016040; NAD(P)-bd_dom.
 IPR017866; Succ-CoA_synthase_bsu_CS.
 IPR016102; Succinyl-CoA_synth-like. 
Pfam
 PF08442; ATP-grasp_2
 PF00285; Citrate_synt
 PF02629; CoA_binding
 PF00549; Ligase_CoA 
SMART
  
PROSITE
 PS01216; SUCCINYL_COA_LIG_1
 PS00399; SUCCINYL_COA_LIG_2
 PS01217; SUCCINYL_COA_LIG_3 
PRINTS