CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-031567
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 ATP-citrate synthase 
Protein Synonyms/Alias
 cDNA FLJ55447, highly similar to ATP-citrate synthase (EC 2.3.3.8) 
Gene Name
 ACLY 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
4****MSAKAISEQTGubiquitination[1, 2, 3]
12AISEQTGKELLYKFIubiquitination[2, 4, 5]
17TGKELLYKFICTTSAubiquitination[3]
58LSQNLVVKPDQLIKRubiquitination[2, 3, 4, 5, 6, 7]
64VKPDQLIKRRGKLGLubiquitination[2, 4, 5]
68QLIKRRGKLGLVGVNubiquitination[2, 3, 4, 5]
82NLTLDGVKSWLKPRLubiquitination[2, 3, 8]
86DGVKSWLKPRLGQEAubiquitination[2, 6]
108RDYQGPLKEHEVTIFacetylation[3]
108RDYQGPLKEHEVTIFubiquitination[2, 3, 6]
207ADEVAPAKKAKPAMPubiquitination[9]
210VAPAKKAKPAMPQGKubiquitination[4, 5]
217KPAMPQGKSTTLFSRubiquitination[4, 5]
227TLFSRHTKAIVWGMQubiquitination[2, 4, 5, 7]
267YPFTGDHKQKFYWGHubiquitination[6, 7]
269FTGDHKQKFYWGHKEubiquitination[2]
275QKFYWGHKEILIPVFubiquitination[1, 2, 3, 4, 5, 7]
283EILIPVFKNMADAMRacetylation[10, 11]
283EILIPVFKNMADAMRubiquitination[2]
291NMADAMRKHPEVDVLubiquitination[2]
345LIKKADQKGVTIIGPubiquitination[2]
359PATVGGIKPGCFKIGubiquitination[1, 2, 3, 4, 5]
364GIKPGCFKIGNTGGMubiquitination[2, 3]
379LDNILASKLYRPGSVubiquitination[1, 2, 3, 7, 8]
461YKICRGIKEGRLTKPubiquitination[9]
509VAKNQALKEAGVFVPubiquitination[1, 2, 3, 6, 7, 8, 9]
565RELGLIRKPASFMTSubiquitination[2, 3, 7]
647IICARAGKDLVSSLTubiquitination[2, 3, 4, 5, 6, 7]
673GALDAAAKMFSKAFDubiquitination[2, 4, 5, 6]
677AAAKMFSKAFDSGIIubiquitination[2, 3, 4, 5]
691IPMEFVNKMKKEGKLubiquitination[7]
693MEFVNKMKKEGKLIMubiquitination[2]
697NKMKKEGKLIMGIGHacetylation[3, 10, 11]
697NKMKKEGKLIMGIGHubiquitination[2]
707MGIGHRVKSINNPDMubiquitination[2, 3]
720DMRVQILKDYVRQHFubiquitination[1, 2, 4, 5, 7]
806IGHYLDQKRLKQGLYacetylation[3]
806IGHYLDQKRLKQGLYubiquitination[2, 3, 4, 5, 6, 8]
809YLDQKRLKQGLYRHPubiquitination[2, 3, 4, 5, 6]
Reference
 [1] 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]
 [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] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [11] 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] 
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 830 AA 
Protein Sequence
MSAKAISEQT GKELLYKFIC TTSAIQNRFK YARVTPDTDW ARLLQDHPWL LSQNLVVKPD 60
QLIKRRGKLG LVGVNLTLDG VKSWLKPRLG QEATGIVRAI RDYQGPLKEH EVTIFVRRGG 120
PNYQEGLRVM GEVGKTTGIP IHVFGTETHM TAIVGMALGH RPIPNQPPTA AHTANFLLNA 180
SGSTSTPAPS RTASFSESRA DEVAPAKKAK PAMPQGKSTT LFSRHTKAIV WGMQTRAVQG 240
MLDFDYVCSR DEPSVAAMVY PFTGDHKQKF YWGHKEILIP VFKNMADAMR KHPEVDVLIN 300
FASLRSAYDS TMETMNYAQI RTIAIIAEGI PEALTRKLIK KADQKGVTII GPATVGGIKP 360
GCFKIGNTGG MLDNILASKL YRPGSVAYVS RSGGMSNELN NIISRTTDGV YEGVAIGGDR 420
YPGSTFMDHV LRYQDTPGVK MIVVLGEIGG TEEYKICRGI KEGRLTKPIV CWCIGTCATM 480
FSSEVQFGHA GACANQASET AVAKNQALKE AGVFVPRSFD ELGEIIQSVY EDLVANGVIV 540
PAQEVPPPTV PMDYSWAREL GLIRKPASFM TSICDERGQE LIYAGMPITE VFKEEMGIGG 600
VLGLLWFQKR LPKYSCQFIE MCLMVTADHG PAVSGAHNTI ICARAGKDLV SSLTSGLLTI 660
GDRFGGALDA AAKMFSKAFD SGIIPMEFVN KMKKEGKLIM GIGHRVKSIN NPDMRVQILK 720
DYVRQHFPAT PLLDYALEVE KITTSKKPNL ILNVDGLIGV AFVDMLRNCG SFTREEADEY 780
IDIGALNGIF VLGRSMGFIG HYLDQKRLKQ GLYRHPWDDI SYVLPEHMSM 830 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0005886; C:plasma membrane; IDA:HPA.
 GO:0003878; F:ATP citrate synthase activity; IEA:InterPro.
 GO:0048037; F:cofactor binding; IEA:InterPro.
 GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IEA:InterPro.
 GO:0044262; P:cellular carbohydrate metabolic process; IEA:InterPro. 
Interpro
 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.
 IPR016102; Succinyl-CoA_synth-like. 
Pfam
 PF00285; Citrate_synt
 PF02629; CoA_binding
 PF00549; Ligase_CoA 
SMART
  
PROSITE
 PS01216; SUCCINYL_COA_LIG_1
 PS00399; SUCCINYL_COA_LIG_2 
PRINTS