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Q91V92 (ACLY_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·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
Citrate cleavage enzyme
Gene names
Name:Acly
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1091 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 By similarity.

Catalytic activity

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

Cofactor

Magnesium By similarity.

Subunit structure

Homotetramer By similarity.

Subcellular location

Cytoplasm By similarity.

Post-translational modification

ISGylated. Ref.3

Acetylated at Lys-530, Lys-536 and Lys-544 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 By similarity.

Ubiquitinated at Lys-530, Lys-536 and Lys-544 by UBR4, leading to its degradation. Ubiquitination is probably inhibited by acetylation at same site By similarity.

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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Mef2cQ8CFN5-43EBI-644049,EBI-643822

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10911091ATP-citrate synthase
PRO_0000102782

Regions

Domain4 – 265262ATP-grasp
Nucleotide binding66 – 672ATP By similarity
Nucleotide binding109 – 1113ATP By similarity
Nucleotide binding691 – 71121ATP By similarity
Nucleotide binding742 – 76827ATP By similarity
Region769 – 77911CoA-binding Potential

Sites

Active site7501Tele-phosphohistidine intermediate By similarity
Metal binding2011Magnesium By similarity
Metal binding2031Magnesium By similarity
Metal binding7081Magnesium By similarity
Binding site581ATP By similarity
Binding site1181ATP By similarity
Binding site3461Citrate; via amide nitrogen By similarity
Binding site3481Citrate By similarity
Binding site3791Citrate By similarity

Amino acid modifications

Modified residue1311Phosphotyrosine By similarity
Modified residue4471Phosphothreonine By similarity
Modified residue4511Phosphoserine By similarity
Modified residue4551Phosphoserine; by PKA and PKB/AKT1 or PKB/AKT2 Ref.6
Modified residue5301N6-acetyllysine; alternate By similarity
Modified residue5361N6-acetyllysine; alternate By similarity
Modified residue5441N6-acetyllysine; alternate By similarity
Modified residue6291Phosphothreonine By similarity
Modified residue6531Phosphoserine By similarity
Modified residue6721Phosphotyrosine Ref.4 Ref.5
Modified residue8291Phosphoserine By similarity
Modified residue9381N6-acetyllysine By similarity
Modified residue9581N6-acetyllysine By similarity
Modified residue9681N6-acetyllysine Ref.7
Modified residue10671N6-acetyllysine By similarity
Modified residue10901Phosphoserine By similarity
Cross-link530Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity
Cross-link536Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity
Cross-link544Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q91V92 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 660293D027D797DD

FASTA1,091119,728
        10         20         30         40         50         60 
MSAKAISEQT GKELLYKYIC TTSAIQNRFK YARVTPDTDW AHLLQDHPWL LSQSLVVKPD 

        70         80         90        100        110        120 
QLIKRRGKLG LVGVNLSLDG VKSWLKPRLG HEATVGKAKG FLKNFLIEPF VPHSQAEEFY 

       130        140        150        160        170        180 
VCIYATREGD YVLFHHEGGV DVGDVDAKAQ KLLVGVDEKL NTEDIKRHLL VHAPEDKKEV 

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

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

       310        320        330        340        350        360 
LANYGEYSGA PSEQQTYDYA KTILSLMTRE KHPEGKILII 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 KPAMPQGKSA 

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

       550        560        570        580        590        600 
PVFKNMADAM KKHPEVDVLI NFASLRSAYD STMETMNYAQ IRTIAIIAEG IPEALTRKLI 

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

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

       730        740        750        760        770        780 
IKEGRLTKPV VCWCIGTCAT MFSSEVQFGH AGACANQASE TAVAKNQALK EAGVFVPRSF 

       790        800        810        820        830        840 
DELGEIIQSV YEDLVAKGAI VPAQEVPPPT VPMDYSWARE LGLIRKPASF MTSICDERGQ 

       850        860        870        880        890        900 
ELIYAGMPIT EVFKEEMGIG GVLGLLWFQR RLPKYSCQFI EMCLMVTADH GPAVSGAHNT 

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

       970        980        990       1000       1010       1020 
MGIGHRVKSI NNPDMRVQIL KDFVKQHFPA TPLLDYALEV EKITTSKKPN LILNVDGFIG 

      1030       1040       1050       1060       1070       1080 
VAFVDMLRNC GSFTREEADE YVDIGALNGI FVLGRSMGFI GHYLDQKRLK QGLYRHPWDD 

      1090 
ISYVLPEHMS M 

« Hide

References

« Hide 'large scale' references
[1]"High-throughput sequence identification of gene coding variants within alcohol-related QTLs."
Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J., Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.
Mamm. Genome 12:657-663(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: ILS and ISS.
[2]"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].
Strain: C57BL/6.
Tissue: Brain.
[3]"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.
[4]"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-672, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Mast cell.
[5]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-672, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[6]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[7]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-968, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF332052 mRNA. Translation: AAK56081.1.
AF332051 mRNA. Translation: AAK56080.1.
BC056378 mRNA. Translation: AAH56378.1.
RefSeqNP_598798.1. NM_134037.3.
UniGeneMm.282039.

3D structure databases

ProteinModelPortalQ91V92.
SMRQ91V92. Positions 2-810, 878-1075.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid222369. 1 interaction.
IntActQ91V92. 6 interactions.
MINTMINT-1700320.

Chemistry

ChEMBLCHEMBL3264.

PTM databases

PhosphoSiteQ91V92.

Proteomic databases

PaxDbQ91V92.
PRIDEQ91V92.

Protocols and materials databases

DNASU104112.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000007131; ENSMUSP00000007131; ENSMUSG00000020917.
ENSMUST00000165111; ENSMUSP00000127632; ENSMUSG00000020917.
GeneID104112.
KEGGmmu:104112.
UCSCuc007lll.2. mouse.

Organism-specific databases

CTD47.
MGIMGI:103251. Acly.

Phylogenomic databases

eggNOGCOG0372.
GeneTreeENSGT00530000063275.
HOGENOMHOG000151479.
HOVERGENHBG003318.
KOK01648.

Gene expression databases

ArrayExpressQ91V92.
BgeeQ91V92.
CleanExMM_ACLY.
GenevestigatorQ91V92.

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. mouse.
NextBio356548.
PROQ91V92.
SOURCESearch...

Entry information

Entry nameACLY_MOUSE
AccessionPrimary (citable) accession number: Q91V92
Entry history
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot