CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004487
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 ATP-citrate synthase 
Protein Synonyms/Alias
 ATP-citrate (pro-S-)-lyase; Citrate cleavage enzyme 
Gene Name
 Acly 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
12AISEQTGKELLYKYIubiquitination[1]
68QLIKRRGKLGLVGVNubiquitination[1]
230ATADYICKVKWGDIEubiquitination[1]
259YIADLDAKSGASLKLubiquitination[1]
265AKSGASLKLTLLNPKubiquitination[1]
272KLTLLNPKGRIWTMVubiquitination[1]
537YPFTGDHKQKFYWGHubiquitination[1]
545QKFYWGHKEILIPVFubiquitination[1]
615LIKKADQKGVTIIGPubiquitination[1]
629PATVGGIKPGCFKIGubiquitination[1]
634GIKPGCFKIGNTGGMubiquitination[2]
649LDNILASKLYRPGSVubiquitination[1]
779VAKNQALKEAGVFVPubiquitination[1]
835RELGLIRKPASFMTSubiquitination[1]
917IICARAGKDLVSSLTubiquitination[1]
943GALDAAAKMFSKAFDubiquitination[1]
947AAAKMFSKAFDSGIIubiquitination[1]
961IPMEFVNKMKKEGKLubiquitination[1]
977MGIGHRVKSINNPDMubiquitination[1]
990DMRVQILKDFVKQHFubiquitination[1]
Reference
 [1] 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]
 [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
Functional Description
 ATP citrate-lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. Has a central role in de novo lipid synthesis. In nervous tissue it may be involved in the biosynthesis of acetylcholine. 
Sequence Annotation
 NP_BIND 700 720 ATP (By similarity).
 NP_BIND 751 777 ATP (By similarity).
 REGION 778 788 CoA-binding (Potential).
 ACT_SITE 759 759 Tele-phosphohistidine intermediate.
 METAL 717 717 Magnesium (By similarity).
 BINDING 346 346 Citrate; via amide nitrogen (By
 BINDING 348 348 Citrate (By similarity).
 BINDING 379 379 Citrate (By similarity).
 MOD_RES 131 131 Phosphotyrosine (By similarity).
 MOD_RES 446 446 Phosphothreonine.
 MOD_RES 450 450 Phosphoserine.
 MOD_RES 454 454 Phosphoserine; by PKA and PKB/AKT1 or
 MOD_RES 480 480 Phosphoserine (By similarity).
 MOD_RES 545 545 N6-acetyllysine (By similarity).
 MOD_RES 553 553 N6-acetyllysine (By similarity).
 MOD_RES 638 638 Phosphothreonine (By similarity).
 MOD_RES 662 662 Phosphoserine (By similarity).
 MOD_RES 681 681 Phosphotyrosine (By similarity).
 MOD_RES 838 838 Phosphoserine (By similarity).
 MOD_RES 947 947 N6-acetyllysine (By similarity).
 MOD_RES 967 967 N6-acetyllysine (By similarity).
 MOD_RES 1076 1076 N6-acetyllysine (By similarity).
 MOD_RES 1099 1099 Phosphoserine (By similarity).  
Keyword
 Acetylation; Alternative splicing; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Lipid biosynthesis; Lipid metabolism; Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1100 AA 
Protein Sequence
MSAKAISEQT GKELLYKYIC TTSAIQNRFK YARVTPDTDW AHLLQDHPWL LSQSLVVKPD 60
QLIKRRGKLG LVGVNLSLDG VKSWLKPRLG HEATVGKAKG FLKNFLIEPF VPHSQAEEFY 120
VCIYATREGD YVLFHHEGGV DVGDVDTKAQ KLLVGVDEKL NAEDIKRHLL VHAPEDKKEI 180
LASFISGLFN FYEDLYFTYL EINPLVVTKD GVYILDLAAK VDATADYICK VKWGDIEFPP 240
PFGREAYPEE AYIADLDAKS GASLKLTLLN PKGRIWTMVA GGGASVVYSD TICDLGGVNE 300
LANYGEYSGA PSEQQTYDYA KTILSLMTRE KHPDGKILII GGSIANFTNV AATFKGIVRA 360
IRDYQGSLKE HEVTIFVRRG GPNYQEGLRV MGEVGKTTGI PIHVFGTETH MTAIVGMAWA 420
PAIPNQPPTA AHTANFLLNA SGSTSTPAPS RTASFSESRA DEVAPAKKAK PAMPQDSVPS 480
PRSLQGKSAT LFSRHTKAIV WGMQTRAVQG MLDFDYVCSR DEPSVAAMVY PFTGDHKQKF 540
YWGHKEILIP VFKNMADAMK KHPEVDVLIN FASLRSAYDS TMETMNYAQI RTIAIIAEGI 600
PEALTRKLIK KADQKGVTII GPATVGGIKP GCFKIGNTGG MLDNILASKL YRPGSVAYVS 660
RSGGMSNELN NIISRTTDGV YEGVAIGGDR YPGSTFMDHV LRYQDTPGVK MIVVLGEIGG 720
TEEYKICRGI KEGRLTKPVV CWCIGTCATM FSSEVQFGHA GACANQASET AVAKNQALKE 780
AGVFVPRSFD ELGEIIQSVY EDLVAKGAIV PAQEVPPPTV PMDYSWAREL GLIRKPASFM 840
TSICDERGQE LIYAGMPITE VFKEEMGIGG VLGLLWFQRR LPKYSCQFIE MCLMVTADHG 900
PAVSGAHNTI ICARAGKDLV SSLTSGLLTI GDRFGGALDA AAKMFSKAFD SGIIPMEFVN 960
KMKKEGKLIM GIGHRVKSIN NPDMRVQILK DFVKQHFPAT PLLDYALEVE KITTSKKPNL 1020
ILNVDGFIGV AFVDMLRNCG SFTREEADEY VDIGALNGVF VLGRSMGFIG HYLDQKRLKQ 1080
GLYRHPWDDI SYVLPEHMSM 1100 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003878; F:ATP citrate synthase activity; IDA:RGD.
 GO:0048037; F:cofactor binding; IEA:InterPro.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IEA:InterPro.
 GO:0006085; P:acetyl-CoA biosynthetic process; NAS:RGD.
 GO:0044262; P:cellular carbohydrate metabolic process; IEA:InterPro.
 GO:0006101; P:citrate metabolic process; IDA:RGD.
 GO:0006633; P:fatty acid biosynthetic process; IDA:RGD. 
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