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Q91V92

- ACLY_MOUSE

UniProt

Q91V92 - ACLY_MOUSE

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Protein
ATP-citrate synthase
Gene
Acly
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

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

Cofactori

Magnesium By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei58 – 581ATP By similarity
Binding sitei118 – 1181ATP By similarity
Metal bindingi201 – 2011Magnesium By similarity
Metal bindingi203 – 2031Magnesium By similarity
Binding sitei346 – 3461Citrate; via amide nitrogen By similarity
Binding sitei348 – 3481Citrate By similarity
Binding sitei379 – 3791Citrate By similarity
Metal bindingi708 – 7081Magnesium By similarity
Active sitei750 – 7501Tele-phosphohistidine intermediate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi66 – 672ATP By similarity
Nucleotide bindingi109 – 1113ATP By similarity
Nucleotide bindingi691 – 71121ATP By similarity
Add
BLAST
Nucleotide bindingi742 – 76827ATP By similarity
Add
BLAST

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ATP citrate synthase activity Source: MGI
  3. cofactor binding Source: InterPro
  4. metal ion binding Source: UniProtKB-KW
  5. protein binding Source: IntAct
  6. succinate-CoA ligase (ADP-forming) activity Source: InterPro

GO - Biological processi

  1. acetyl-CoA biosynthetic process Source: MGI
  2. cellular carbohydrate metabolic process Source: InterPro
  3. lipid biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-citrate synthase (EC:2.3.3.8)
Alternative name(s):
ATP-citrate (pro-S-)-lyase
Citrate cleavage enzyme
Gene namesi
Name:Acly
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:103251. Acly.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. intracellular Source: MGI
  2. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10911091ATP-citrate synthase
PRO_0000102782Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei131 – 1311Phosphotyrosine By similarity
Modified residuei447 – 4471Phosphothreonine By similarity
Modified residuei451 – 4511Phosphoserine By similarity
Modified residuei455 – 4551Phosphoserine; by PKA and PKB/AKT1 or PKB/AKT21 Publication
Modified residuei530 – 5301N6-acetyllysine; alternate By similarity
Cross-linki530 – 530Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity
Modified residuei536 – 5361N6-acetyllysine; alternate By similarity
Cross-linki536 – 536Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity
Modified residuei544 – 5441N6-acetyllysine; alternate By similarity
Cross-linki544 – 544Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity
Modified residuei629 – 6291Phosphothreonine By similarity
Modified residuei653 – 6531Phosphoserine By similarity
Modified residuei672 – 6721Phosphotyrosine2 Publications
Modified residuei829 – 8291Phosphoserine By similarity
Modified residuei938 – 9381N6-acetyllysine By similarity
Modified residuei958 – 9581N6-acetyllysine By similarity
Modified residuei968 – 9681N6-acetyllysine1 Publication
Modified residuei1067 – 10671N6-acetyllysine By similarity
Modified residuei1090 – 10901Phosphoserine By similarity

Post-translational modificationi

ISGylated.1 Publication
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.

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ91V92.
PaxDbiQ91V92.
PRIDEiQ91V92.

PTM databases

PhosphoSiteiQ91V92.

Expressioni

Gene expression databases

ArrayExpressiQ91V92.
BgeeiQ91V92.
CleanExiMM_ACLY.
GenevestigatoriQ91V92.

Interactioni

Subunit structurei

Homotetramer By similarity.

Binary interactionsi

WithEntry#Exp.IntActNotes
Mef2cQ8CFN5-43EBI-644049,EBI-643822

Protein-protein interaction databases

BioGridi222369. 2 interactions.
IntActiQ91V92. 6 interactions.
MINTiMINT-1700320.

Structurei

3D structure databases

ProteinModelPortaliQ91V92.
SMRiQ91V92. Positions 2-810, 901-1065.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 265262ATP-grasp
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni769 – 77911CoA-binding Reviewed prediction
Add
BLAST

Sequence similaritiesi

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.

Phylogenomic databases

eggNOGiCOG0372.
GeneTreeiENSGT00530000063275.
HOGENOMiHOG000151479.
HOVERGENiHBG003318.
KOiK01648.

Family and domain databases

Gene3Di1.10.230.10. 1 hit.
3.30.470.20. 1 hit.
3.40.50.261. 2 hits.
3.40.50.720. 1 hit.
InterProiIPR014608. 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]
PfamiPF08442. ATP-grasp_2. 1 hit.
PF00285. Citrate_synt. 1 hit.
PF02629. CoA_binding. 1 hit.
PF00549. Ligase_CoA. 1 hit.
[Graphical view]
PIRSFiPIRSF036511. ATP_citrt_syn. 1 hit.
SUPFAMiSSF48256. SSF48256. 2 hits.
SSF52210. SSF52210. 1 hit.
PROSITEiPS01216. SUCCINYL_COA_LIG_1. 1 hit.
PS00399. SUCCINYL_COA_LIG_2. 1 hit.
PS01217. SUCCINYL_COA_LIG_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q91V92-1 [UniParc]FASTAAdd to Basket

« Hide

MSAKAISEQT GKELLYKYIC TTSAIQNRFK YARVTPDTDW AHLLQDHPWL     50
LSQSLVVKPD QLIKRRGKLG LVGVNLSLDG VKSWLKPRLG HEATVGKAKG 100
FLKNFLIEPF VPHSQAEEFY VCIYATREGD YVLFHHEGGV DVGDVDAKAQ 150
KLLVGVDEKL NTEDIKRHLL VHAPEDKKEV LASFISGLFN FYEDLYFTYL 200
EINPLVVTKD GVYILDLAAK VDATADYICK VKWGDIEFPP PFGREAYPEE 250
AYIADLDAKS GASLKLTLLN PKGRIWTMVA GGGASVVYSD TICDLGGVNE 300
LANYGEYSGA PSEQQTYDYA KTILSLMTRE KHPEGKILII GGSIANFTNV 350
AATFKGIVRA IRDYQGPLKE HEVTIFVRRG GPNYQEGLRV MGEVGKTTGI 400
PIHVFGTETH MTAIVGMALG HRPIPNQPPT AAHTANFLLN ASGSTSTPAP 450
SRTASFSESR ADEVAPAKKA KPAMPQGKSA TLFSRHTKAI VWGMQTRAVQ 500
GMLDFDYVCS RDEPSVAAMV YPFTGDHKQK FYWGHKEILI PVFKNMADAM 550
KKHPEVDVLI NFASLRSAYD STMETMNYAQ IRTIAIIAEG IPEALTRKLI 600
KKADQKGVTI IGPATVGGIK PGCFKIGNTG GMLDNILASK LYRPGSVAYV 650
SRSGGMSNEL NNIISRTTDG VYEGVAIGGD RYPGSTFMDH VLRYQDTPGV 700
KMIVVLGEIG GTEEYKICRG IKEGRLTKPV VCWCIGTCAT MFSSEVQFGH 750
AGACANQASE TAVAKNQALK EAGVFVPRSF DELGEIIQSV YEDLVAKGAI 800
VPAQEVPPPT VPMDYSWARE LGLIRKPASF MTSICDERGQ ELIYAGMPIT 850
EVFKEEMGIG GVLGLLWFQR RLPKYSCQFI EMCLMVTADH GPAVSGAHNT 900
IICARAGKDL VSSLTSGLLT IGDRFGGALD AAAKMFSKAF DSGIIPMEFV 950
NKMKKEGKLI MGIGHRVKSI NNPDMRVQIL KDFVKQHFPA TPLLDYALEV 1000
EKITTSKKPN LILNVDGFIG VAFVDMLRNC GSFTREEADE YVDIGALNGI 1050
FVLGRSMGFI GHYLDQKRLK QGLYRHPWDD ISYVLPEHMS M 1091
Length:1,091
Mass (Da):119,728
Last modified:December 1, 2001 - v1
Checksum:i660293D027D797DD
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF332052 mRNA. Translation: AAK56081.1.
AF332051 mRNA. Translation: AAK56080.1.
BC056378 mRNA. Translation: AAH56378.1.
CCDSiCCDS25425.1.
RefSeqiNP_598798.1. NM_134037.3.
UniGeneiMm.282039.

Genome annotation databases

EnsembliENSMUST00000007131; ENSMUSP00000007131; ENSMUSG00000020917.
ENSMUST00000165111; ENSMUSP00000127632; ENSMUSG00000020917.
GeneIDi104112.
KEGGimmu:104112.
UCSCiuc007lll.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF332052 mRNA. Translation: AAK56081.1 .
AF332051 mRNA. Translation: AAK56080.1 .
BC056378 mRNA. Translation: AAH56378.1 .
CCDSi CCDS25425.1.
RefSeqi NP_598798.1. NM_134037.3.
UniGenei Mm.282039.

3D structure databases

ProteinModelPortali Q91V92.
SMRi Q91V92. Positions 2-810, 901-1065.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 222369. 2 interactions.
IntActi Q91V92. 6 interactions.
MINTi MINT-1700320.

Chemistry

ChEMBLi CHEMBL3264.

PTM databases

PhosphoSitei Q91V92.

Proteomic databases

MaxQBi Q91V92.
PaxDbi Q91V92.
PRIDEi Q91V92.

Protocols and materials databases

DNASUi 104112.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000007131 ; ENSMUSP00000007131 ; ENSMUSG00000020917 .
ENSMUST00000165111 ; ENSMUSP00000127632 ; ENSMUSG00000020917 .
GeneIDi 104112.
KEGGi mmu:104112.
UCSCi uc007lll.2. mouse.

Organism-specific databases

CTDi 47.
MGIi MGI:103251. Acly.

Phylogenomic databases

eggNOGi COG0372.
GeneTreei ENSGT00530000063275.
HOGENOMi HOG000151479.
HOVERGENi HBG003318.
KOi K01648.

Miscellaneous databases

ChiTaRSi ACLY. mouse.
NextBioi 356548.
PROi Q91V92.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q91V92.
Bgeei Q91V92.
CleanExi MM_ACLY.
Genevestigatori Q91V92.

Family and domain databases

Gene3Di 1.10.230.10. 1 hit.
3.30.470.20. 1 hit.
3.40.50.261. 2 hits.
3.40.50.720. 1 hit.
InterProi 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.
[Graphical view ]
Pfami PF08442. ATP-grasp_2. 1 hit.
PF00285. Citrate_synt. 1 hit.
PF02629. CoA_binding. 1 hit.
PF00549. Ligase_CoA. 1 hit.
[Graphical view ]
PIRSFi PIRSF036511. ATP_citrt_syn. 1 hit.
SUPFAMi SSF48256. SSF48256. 2 hits.
SSF52210. SSF52210. 1 hit.
PROSITEi PS01216. SUCCINYL_COA_LIG_1. 1 hit.
PS00399. SUCCINYL_COA_LIG_2. 1 hit.
PS01217. SUCCINYL_COA_LIG_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiACLY_MOUSE
AccessioniPrimary (citable) accession number: Q91V92
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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