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UniProtKB/Swiss-Prot entry P53396


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ACLY_HUMAN
Primary accession number P53396
Secondary accession numbers Q13037 Q9BRL0
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on October 17, 2006 (Sequence version 3)
Annotations were last modified on    June 16, 2009 (Entry version 100)
Name and origin of the protein
Protein name ATP-citrate synthase
Synonyms EC 2.3.3.8
ATP-citrate (pro-S-)-lyase
Citrate cleavage enzyme
Gene name
Name: ACLY
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASP-175.
TISSUE=Liver;
DOI=10.1111/j.1432-1033.1992.tb16659.x; PubMed=1371749 [NCBI, ExPASy, EBI, Israel, Japan]
Elshourbagy N.A., Near J.C., Kmetz P.J., Wells T.N.C., Groot P.H.E., Saxty B.A., Hughes S.A., Franklin M., Gloger I.S.;
"Cloning and expression of a human ATP-citrate lyase cDNA.";
Eur. J. Biochem. 204:491-499(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASP-175.
TISSUE=Liver;
DOI=10.1006/prep.1996.0668; PubMed=9116495 [NCBI, ExPASy, EBI, Israel, Japan]
Lord K.A., Wang X.M., Simmons S.J., Bruckner R.C., Loscig J., O'Connor B., Bentley R., Smallwood A., Chadwick C.C., Stevis P.E., Ciccarelli R.B.;
"Variant cDNA sequences of human ATP:citrate lyase: cloning, expression, and purification from baculovirus-infected insect cells.";
Protein Expr. Purif. 9:133-141(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lymph;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-131 AND TYR-682, AND MASS SPECTROMETRY.
DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan]
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
Nat. Biotechnol. 23:94-101(2005).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455 AND SER-481, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455 AND SER-481, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1021/pr070152u; PubMed=17924679 [NCBI, ExPASy, EBI, Israel, Japan]
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, AND MASS SPECTROMETRY.
DOI=10.2116/analsci.24.161; PubMed=18187866 [NCBI, ExPASy, EBI, Israel, Japan]
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Anal. Sci. 24:161-166(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455, AND MASS SPECTROMETRY.
TISSUE=Platelet;
DOI=10.1021/pr0704130; PubMed=18088087 [NCBI, ExPASy, EBI, Israel, Japan]
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455 AND SER-481, AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan]
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455; SER-481 AND SER-1100, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X64330; CAA45614.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U18197; AAB60340.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC006195; AAH06195.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00021290; -.
PIR S21173; S21173.
RefSeq NP_001087.2; -.
NP_942127.1; -.
UniGene Hs.387567
3D structure databases
HSSP P07459; 1JKJ. [HSSP ENTRY / PDB]
ModBase P53396.
Protein-protein interaction databases
IntAct P53396; 11.
PTM databases
PhosphoSite P53396; -.
Enzyme and pathway databases
BRENDA 2.3.3.8; 247.
Reactome REACT_1505; Integration of energy metabolism.
REACT_602; Lipid and lipoprotein metabolism.
Organism-specific databases
GeneCards GC17M037276; -.
H-InvDB HIX0013825; -.
HGNC HGNC:115; ACLY.
GenAtlas ACLY.
HPA CAB007783; -.
MIM 108728; gene. [NCBI / EBI]
PharmGKB PA24441; -.
Gene expression databases
ArrayExpress P53396; -.
Bgee P53396; -.
CleanEx HS_ACLY; -.
GermOnline ENSG00000131473; Homo sapiens.
Ontologies
GO
GO:0009346; Cellular component: citrate lyase complex (traceable author statement from ProtInc).
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0003878; Molecular function: ATP citrate synthase activity (traceable author statement from ProtInc).
GO:0008815; Molecular function: citrate (pro-3S)-lyase activity (inferred from experiment from Reactome).
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0004775; Molecular function: succinate-CoA ligase (ADP-forming) activity (inferred from electronic annotation from InterPro).
GO:0006200; Biological process: ATP catabolic process (traceable author statement from ProtInc).
GO:0044262; Biological process: cellular carbohydrate metabolic process (inferred from electronic annotation from InterPro).
GO:0006101; Biological process: citrate metabolic process (traceable author statement from ProtInc).
GO:0015936; Biological process: coenzyme A metabolic process (traceable author statement from ProtInc).
GO:0008610; Biological process: lipid biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR014608; ATP-citrate_synthase.
IPR013816; ATP_grasp_subdomain_2.
IPR017440; Cit_synth/succinyl-CoA_lig_AS.
IPR016143; Citrate_synth-like_sm_a-sub.
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.
Graphical view of domain structure.
Gene3D G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 1.
G3DSA:1.10.230.10; Citrate_synthase_sm_a-sub; 1.
G3DSA:3.40.50.720; NAD(P)-bd; 1.
G3DSA:3.40.50.261; Succinyl-CoA_synth-like; 1.
Pfam PF02629; CoA_binding; 1.
PF00549; Ligase_CoA; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF036511; ATP_citrt_syn; 1.
PROSITE PS01216; SUCCINYL_COA_LIG_1; 1.
PS00399; SUCCINYL_COA_LIG_2; 1.
PS01217; SUCCINYL_COA_LIG_3; 1.
Proteomic databases
PeptideAtlas P53396; -.
PRIDE P53396; -.
Genome annotation databases
Ensembl ENSG00000131473; Homo sapiens. [Contig view]
GeneID 47; -.
KEGG hsa:47; -.
Phylogenomic databases
HOVERGEN P53396; -.
OMA P53396; IKKADQK.
Other
NextBio 181; -.
SOURCE ACLY; Homo sapiens.
ProtoNet P53396.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Cytoplasm; Lipid synthesis; Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein; Polymorphism; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   1101  1101     ATP-citrate synthase. PRO_0000102781
NP_BIND   701    721  21     ATP (By similarity). 
NP_BIND   752    778  27     ATP (By similarity). 
REGION   779    789  11     CoA-binding (Potential). 
ACT_SITE   760    760        Tele-phosphohistidine intermediate (By similarity). 
METAL   718    718        Magnesium (By similarity). 
MOD_RES   131    131        Phosphotyrosine. 
MOD_RES   455    455        Phosphoserine. 
MOD_RES   481    481        Phosphoserine. 
MOD_RES   682    682        Phosphotyrosine. 
MOD_RES   1100   1100        Phosphoserine. 
VARIANT   175    175  1     E -> D (in dbSNP:rs2304497 [NCBI]). VAR_028230 
CONFLICT   75     75        N -> D (in Ref. 1; CAA45614). 
CONFLICT   111    111        V -> A (in Ref. 1; CAA45614). 
CONFLICT   245    245        E -> V (in Ref. 1; CAA45614). 
CONFLICT   419    423        LGHRP -> WAPA (in Ref. 1; CAA45614). 
CONFLICT   442    444        SGS -> QRE (in Ref. 1; CAA45614). 
CONFLICT   457    459        SES -> YESMVDEV (in Ref. 1; CAA45614). 
CONFLICT   653    656        RPGS -> PQAA (in Ref. 1; CAA45614). 
CONFLICT   728    728        C -> S (in Ref. 1; CAA45614). 
CONFLICT   872    872        V -> A (in Ref. 1; CAA45614). 
CONFLICT   916    919        AGKD -> TAVE (in Ref. 1; CAA45614). 
Sequence information
Length: 1101 AA [This is the length of the unprocessed precursor] Molecular weight: 120839 Da [This is the MW of the unprocessed precursor] CRC64: 12BB4416A30DC30C [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSAKAISEQT GKELLYKFIC TTSAIQNRFK YARVTPDTDW ARLLQDHPWL LSQNLVVKPD 

        70         80         90        100        110        120 
QLIKRRGKLG LVGVNLTLDG VKSWLKPRLG QEATVGKATG FLKNFLIEPF VPHSQAEEFY 

       130        140        150        160        170        180 
VCIYATREGD YVLFHHEGGV DVGDVDAKAQ KLLVGVDEKL NPEDIKKHLL VHAPEDKKEI 

       190        200        210        220        230        240 
LASFISGLFN FYEDLYFTYL EINPLVVTKD GVYVLDLAAK VDATADYICK VKWGDIEFPP 

       250        260        270        280        290        300 
PFGREAYPEE AYIADLDAKS GASLKLTLLN PKGRIWTMVA GGGASVVYSD TICDLGGVNE 

       310        320        330        340        350        360 
LANYGEYSGA PSEQQTYDYA KTILSLMTRE KHPDGKILII GGSIANFTNV AATFKGIVRA 

       370        380        390        400        410        420 
IRDYQGPLKE HEVTIFVRRG GPNYQEGLRV MGEVGKTTGI PIHVFGTETH MTAIVGMALG 

       430        440        450        460        470        480 
HRPIPNQPPT AAHTANFLLN ASGSTSTPAP SRTASFSESR ADEVAPAKKA KPAMPQDSVP 

       490        500        510        520        530        540 
SPRSLQGKST TLFSRHTKAI VWGMQTRAVQ GMLDFDYVCS RDEPSVAAMV YPFTGDHKQK 

       550        560        570        580        590        600 
FYWGHKEILI PVFKNMADAM RKHPEVDVLI NFASLRSAYD STMETMNYAQ IRTIAIIAEG 

       610        620        630        640        650        660 
IPEALTRKLI KKADQKGVTI IGPATVGGIK PGCFKIGNTG GMLDNILASK LYRPGSVAYV 

       670        680        690        700        710        720 
SRSGGMSNEL NNIISRTTDG VYEGVAIGGD RYPGSTFMDH VLRYQDTPGV KMIVVLGEIG 

       730        740        750        760        770        780 
GTEEYKICRG IKEGRLTKPI VCWCIGTCAT MFSSEVQFGH AGACANQASE TAVAKNQALK 

       790        800        810        820        830        840 
EAGVFVPRSF DELGEIIQSV YEDLVANGVI VPAQEVPPPT VPMDYSWARE LGLIRKPASF 

       850        860        870        880        890        900 
MTSICDERGQ ELIYAGMPIT EVFKEEMGIG GVLGLLWFQK RLPKYSCQFI EMCLMVTADH 

       910        920        930        940        950        960 
GPAVSGAHNT IICARAGKDL VSSLTSGLLT IGDRFGGALD AAAKMFSKAF DSGIIPMEFV 

       970        980        990       1000       1010       1020 
NKMKKEGKLI MGIGHRVKSI NNPDMRVQIL KDYVRQHFPA TPLLDYALEV EKITTSKKPN 

      1030       1040       1050       1060       1070       1080 
LILNVDGLIG VAFVDMLRNC GSFTREEADE YIDIGALNGI FVLGRSMGFI GHYLDQKRLK 

      1090       1100 
QGLYRHPWDD ISYVLPEHMS M 

P53396 in FASTA format

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