Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P53396 (ACLY_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP-citrate synthase

EC=2.3.3.8
Alternative name(s):
ATP-citrate (pro-S-)-lyase
Short name=ACL
Citrate cleavage enzyme
Gene names
Name:ACLY
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1101 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.20

Catalytic activity

ADP + phosphate + acetyl-CoA + oxaloacetate = ATP + citrate + CoA.

Cofactor

Magnesium.

Subunit structure

Homotetramer.

Subcellular location

Cytoplasm.

Post-translational modification

ISGylated. Ref.6

Acetylated at Lys-540, Lys-546 and Lys-554 by KAT2B/PCAF. Acetylation is promoted by glucose and stabilizes the protein, probably by preventing ubiquitination at the same sites. Acetylation promotes de novo lipid synthesis. Deacetylated by SIRT2. Ref.20

Ubiquitinated at Lys-540, Lys-546 and Lys-554 by UBR4, leading to its degradation. Ubiquitination is probably inhibited by acetylation at same site Probable. Ref.20

Sequence similarities

In the N-terminal section; belongs to the succinate/malate CoA ligase beta subunit family.

In the C-terminal section; belongs to the succinate/malate CoA ligase alpha subunit family.

Contains 1 ATP-grasp domain.

Ontologies

Keywords
   Biological processLipid biosynthesis
Lipid metabolism
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionTransferase
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Traceable author statement Ref.1. Source: ProtInc

cellular carbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

cellular lipid metabolic process

Traceable author statement. Source: Reactome

citrate metabolic process

Traceable author statement Ref.1. Source: ProtInc

coenzyme A metabolic process

Traceable author statement Ref.1. Source: ProtInc

energy reserve metabolic process

Traceable author statement. Source: Reactome

lipid biosynthetic process

Inferred from direct assay Ref.20. Source: UniProtKB

long-chain fatty-acyl-CoA biosynthetic process

Traceable author statement. Source: Reactome

positive regulation of cellular metabolic process

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

triglyceride biosynthetic process

Traceable author statement. Source: Reactome

   Cellular_componentcitrate lyase complex

Traceable author statement Ref.1. Source: ProtInc

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337. Source: UniProt

mitochondrion

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay. Source: HPA

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP citrate synthase activity

Traceable author statement Ref.20. Source: UniProtKB

cofactor binding

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

succinate-CoA ligase (ADP-forming) activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P53396-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P53396-2)

The sequence of this isoform differs from the canonical sequence as follows:
     476-485: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11011101ATP-citrate synthase
PRO_0000102781

Regions

Domain4 – 265262ATP-grasp
Nucleotide binding66 – 672ATP
Nucleotide binding109 – 1113ATP
Nucleotide binding701 – 72121ATP By similarity
Nucleotide binding752 – 77827ATP By similarity
Region779 – 78911CoA-binding Potential

Sites

Active site7601Tele-phosphohistidine intermediate By similarity
Metal binding2011Magnesium By similarity
Metal binding2031Magnesium By similarity
Metal binding7181Magnesium By similarity
Binding site581ATP
Binding site1181ATP
Binding site3461Citrate; via amide nitrogen
Binding site3481Citrate
Binding site3791Citrate

Amino acid modifications

Modified residue1311Phosphotyrosine Ref.7
Modified residue4471Phosphothreonine By similarity
Modified residue4511Phosphoserine By similarity
Modified residue4551Phosphoserine; by PKA and PKB/AKT1 or PKB/AKT2 Ref.12 Ref.17 Ref.19
Modified residue4811Phosphoserine Ref.8 Ref.9 Ref.11 Ref.12 Ref.14 Ref.15 Ref.17 Ref.19
Modified residue5401N6-acetyllysine; alternate Ref.20
Modified residue5461N6-acetyllysine; alternate Ref.16 Ref.20
Modified residue5541N6-acetyllysine; alternate Ref.16 Ref.20
Modified residue6391Phosphothreonine Ref.14
Modified residue6631Phosphoserine Ref.14
Modified residue6821Phosphotyrosine Ref.7 Ref.14
Modified residue8391Phosphoserine Ref.14
Modified residue9481N6-acetyllysine Ref.16
Modified residue9681N6-acetyllysine Ref.16
Modified residue9781N6-acetyllysine By similarity
Modified residue10771N6-acetyllysine Ref.16
Modified residue11001Phosphoserine Ref.12 Ref.14
Cross-link540Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate Probable
Cross-link546Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate Probable
Cross-link554Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate Probable

Natural variations

Alternative sequence476 – 48510Missing in isoform 2.
VSP_042201
Natural variant1751E → D. Ref.1 Ref.2 Ref.3
Corresponds to variant rs2304497 [ dbSNP | Ensembl ].
VAR_028230

Experimental info

Mutagenesis5401K → R or Q: Decreased acetylation and increased de novo lipid synthesis; when associated with R,Q-546 and R,Q-554. Ref.20
Mutagenesis5461K → R or Q: Decreased acetylation and increased de novo lipid synthesis; when associated with R,Q-540 and R,Q-554. Ref.20
Mutagenesis5541K → R or Q: Decreased acetylation and increased de novo lipid synthesis; when associated with R,Q-540 and R,Q-546. Ref.20
Sequence conflict751N → D in CAA45614. Ref.1
Sequence conflict1111V → A in CAA45614. Ref.1
Sequence conflict2451E → V in CAA45614. Ref.1
Sequence conflict419 – 4235LGHRP → WAPA in CAA45614. Ref.1
Sequence conflict442 – 4443SGS → QRE in CAA45614. Ref.1
Sequence conflict457 – 4593SES → YESMVDEV in CAA45614. Ref.1
Sequence conflict653 – 6564RPGS → PQAA in CAA45614. Ref.1
Sequence conflict7281C → S in CAA45614. Ref.1
Sequence conflict8721V → A in CAA45614. Ref.1
Sequence conflict916 – 9194AGKD → TAVE in CAA45614. Ref.1

Secondary structure

...................................................................................................................................... 1101
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 17, 2006. Version 3.
Checksum: 12BB4416A30DC30C

FASTA1,101120,839
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 04EB8D05059409E5
Show »

FASTA1,091119,772

References

« Hide 'large scale' references
[1]"Cloning and expression of a human ATP-citrate lyase cDNA."
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.
Eur. J. Biochem. 204:491-499(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ASP-175.
Tissue: Liver.
[2]"Variant cDNA sequences of human ATP:citrate lyase: cloning, expression, and purification from baculovirus-infected insect cells."
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.
Protein Expr. Purif. 9:133-141(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ASP-175.
Tissue: Liver.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT ASP-175.
Tissue: Hippocampus.
[4]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Lymph.
[6]"Proteomic identification of proteins conjugated to ISG15 in mouse and human cells."
Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J., Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.
Biochem. Biophys. Res. Commun. 336:496-506(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ISGYLATION.
[7]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
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.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-131 AND TYR-682, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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."
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[11]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455; SER-481 AND SER-1100, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481; THR-639; SER-663; TYR-682; SER-839 AND SER-1100, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[16]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-546; LYS-554; LYS-948; LYS-968 AND LYS-1077, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455 AND SER-481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455 AND SER-481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Acetylation stabilizes ATP-citrate lyase to promote lipid biosynthesis and tumor growth."
Lin R., Tao R., Gao X., Li T., Zhou X., Guan K.L., Xiong Y., Lei Q.Y.
Mol. Cell 51:506-518(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ACETYLATION AT LYS-540; LYS-546 AND LYS-554, UBIQUITINATION AT LYS-540; LYS-546 AND LYS-554, MUTAGENESIS OF LYS-540; LYS-546 AND LYS-554.
[21]"Identification of the citrate-binding site of human ATP-citrate lyase using X-ray crystallography."
Sun T., Hayakawa K., Bateman K.S., Fraser M.E.
J. Biol. Chem. 285:27418-27428(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-425 AND 487-820 IN COMPLEX WITH CITRATE, CITRATE-BINDING SITES.
[22]"ADP-Mg2+ bound to the ATP-grasp domain of ATP-citrate lyase."
Sun T., Hayakawa K., Fraser M.E.
Acta Crystallogr. F 67:1168-1172(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-817 IN COMPLEX WITH ADP.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X64330 mRNA. Translation: CAA45614.1.
U18197 mRNA. Translation: AAB60340.1.
AK295675 mRNA. Translation: BAG58532.1.
AC091172 Genomic DNA. No translation available.
BC006195 mRNA. Translation: AAH06195.1.
PIRS21173.
RefSeqNP_001087.2. NM_001096.2.
NP_942127.1. NM_198830.1.
XP_005257452.1. XM_005257395.1.
UniGeneHs.387567.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3MWDX-ray2.10A1-425[»]
B487-820[»]
3MWEX-ray2.20A1-425[»]
B487-821[»]
3PFFX-ray2.30A1-817[»]
ProteinModelPortalP53396.
SMRP53396. Positions 2-820, 832-1086.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106563. 34 interactions.
IntActP53396. 6 interactions.
MINTMINT-3019895.
STRING9606.ENSP00000253792.

Chemistry

BindingDBP53396.
ChEMBLCHEMBL3720.

PTM databases

PhosphoSiteP53396.

Polymorphism databases

DMDM116241237.

Proteomic databases

PaxDbP53396.
PeptideAtlasP53396.
PRIDEP53396.

Protocols and materials databases

DNASU47.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000352035; ENSP00000253792; ENSG00000131473. [P53396-1]
ENST00000353196; ENSP00000345398; ENSG00000131473. [P53396-2]
ENST00000393896; ENSP00000377474; ENSG00000131473. [P53396-2]
ENST00000564506; ENSP00000455275; ENSG00000260245. [P53396-1]
ENST00000567793; ENSP00000456811; ENSG00000260245. [P53396-2]
ENST00000590151; ENSP00000466259; ENSG00000131473. [P53396-1]
GeneID47.
KEGGhsa:47.
UCSCuc002hyg.3. human. [P53396-1]
uc002hyh.3. human. [P53396-2]

Organism-specific databases

CTD47.
GeneCardsGC17M040023.
HGNCHGNC:115. ACLY.
HPACAB007783.
HPA022434.
HPA022953.
HPA022959.
HPA028758.
MIM108728. gene.
neXtProtNX_P53396.
PharmGKBPA24441.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0372.
HOGENOMHOG000151479.
HOVERGENHBG003318.
InParanoidP53396.
KOK01648.
OMARLPKYAC.
PhylomeDBP53396.
TreeFamTF300560.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
SABIO-RKP53396.

Gene expression databases

ArrayExpressP53396.
BgeeP53396.
CleanExHS_ACLY.
GenevestigatorP53396.

Family and domain databases

Gene3D1.10.230.10. 1 hit.
3.30.470.20. 1 hit.
3.40.50.261. 2 hits.
3.40.50.720. 1 hit.
InterProIPR014608. 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.
[Graphical view]
PfamPF08442. ATP-grasp_2. 1 hit.
PF00285. Citrate_synt. 1 hit.
PF02629. CoA_binding. 1 hit.
PF00549. Ligase_CoA. 1 hit.
[Graphical view]
PIRSFPIRSF036511. ATP_citrt_syn. 1 hit.
SUPFAMSSF48256. SSF48256. 2 hits.
SSF52210. SSF52210. 1 hit.
PROSITEPS01216. SUCCINYL_COA_LIG_1. 1 hit.
PS00399. SUCCINYL_COA_LIG_2. 1 hit.
PS01217. SUCCINYL_COA_LIG_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSACLY. human.
EvolutionaryTraceP53396.
GenomeRNAi47.
NextBio181.
PROP53396.
SOURCESearch...

Entry information

Entry nameACLY_HUMAN
AccessionPrimary (citable) accession number: P53396
Secondary accession number(s): B4DIM0, Q13037, Q9BRL0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 17, 2006
Last modified: April 16, 2014
This is version 151 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM