Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q91V92

- ACLY_MOUSE

UniProt

Q91V92 - ACLY_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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).By similarity

Catalytic activityi

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

Cofactori

Magnesium.By similarity

Enzyme regulationi

Phosphorylation results in a 6-fold increase in V(max) and the conversion of citrate dependence from sigmoidal to hyperbolic. Fructose 6-phosphate (F6P) is also a potent activator.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei58 – 581ATPBy similarity
Binding sitei118 – 1181ATPBy similarity
Metal bindingi201 – 2011MagnesiumBy similarity
Metal bindingi203 – 2031MagnesiumBy similarity
Binding sitei346 – 3461Citrate; via amide nitrogenBy similarity
Binding sitei348 – 3481CitrateBy similarity
Binding sitei379 – 3791CitrateBy similarity
Metal bindingi708 – 7081MagnesiumBy similarity
Active sitei750 – 7501Tele-phosphohistidine intermediateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi66 – 672ATPBy similarity
Nucleotide bindingi109 – 1113ATPBy similarity
Nucleotide bindingi691 – 71121ATPBy similarityAdd
BLAST
Nucleotide bindingi742 – 76827ATPBy similarityAdd
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. 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 synthasePRO_0000102782Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ91V92.
PaxDbiQ91V92.
PRIDEiQ91V92.

PTM databases

PhosphoSiteiQ91V92.

Expressioni

Gene expression databases

BgeeiQ91V92.
CleanExiMM_ACLY.
ExpressionAtlasiQ91V92. baseline and differential.
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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni769 – 77911CoA-bindingSequence AnalysisAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the succinate/malate CoA ligase beta subunit family.Curated
In the C-terminal section; belongs to the succinate/malate CoA ligase alpha subunit family.Curated
Contains 1 ATP-grasp domain.Curated

Phylogenomic databases

eggNOGiCOG0372.
GeneTreeiENSGT00530000063275.
HOGENOMiHOG000151479.
HOVERGENiHBG003318.
InParanoidiQ91V92.
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

        10         20         30         40         50
MSAKAISEQT GKELLYKYIC TTSAIQNRFK YARVTPDTDW AHLLQDHPWL
60 70 80 90 100
LSQSLVVKPD QLIKRRGKLG LVGVNLSLDG VKSWLKPRLG HEATVGKAKG
110 120 130 140 150
FLKNFLIEPF VPHSQAEEFY VCIYATREGD YVLFHHEGGV DVGDVDAKAQ
160 170 180 190 200
KLLVGVDEKL NTEDIKRHLL VHAPEDKKEV LASFISGLFN FYEDLYFTYL
210 220 230 240 250
EINPLVVTKD GVYILDLAAK VDATADYICK VKWGDIEFPP PFGREAYPEE
260 270 280 290 300
AYIADLDAKS GASLKLTLLN PKGRIWTMVA GGGASVVYSD TICDLGGVNE
310 320 330 340 350
LANYGEYSGA PSEQQTYDYA KTILSLMTRE KHPEGKILII GGSIANFTNV
360 370 380 390 400
AATFKGIVRA IRDYQGPLKE HEVTIFVRRG GPNYQEGLRV MGEVGKTTGI
410 420 430 440 450
PIHVFGTETH MTAIVGMALG HRPIPNQPPT AAHTANFLLN ASGSTSTPAP
460 470 480 490 500
SRTASFSESR ADEVAPAKKA KPAMPQGKSA TLFSRHTKAI VWGMQTRAVQ
510 520 530 540 550
GMLDFDYVCS RDEPSVAAMV YPFTGDHKQK FYWGHKEILI PVFKNMADAM
560 570 580 590 600
KKHPEVDVLI NFASLRSAYD STMETMNYAQ IRTIAIIAEG IPEALTRKLI
610 620 630 640 650
KKADQKGVTI IGPATVGGIK PGCFKIGNTG GMLDNILASK LYRPGSVAYV
660 670 680 690 700
SRSGGMSNEL NNIISRTTDG VYEGVAIGGD RYPGSTFMDH VLRYQDTPGV
710 720 730 740 750
KMIVVLGEIG GTEEYKICRG IKEGRLTKPV VCWCIGTCAT MFSSEVQFGH
760 770 780 790 800
AGACANQASE TAVAKNQALK EAGVFVPRSF DELGEIIQSV YEDLVAKGAI
810 820 830 840 850
VPAQEVPPPT VPMDYSWARE LGLIRKPASF MTSICDERGQ ELIYAGMPIT
860 870 880 890 900
EVFKEEMGIG GVLGLLWFQR RLPKYSCQFI EMCLMVTADH GPAVSGAHNT
910 920 930 940 950
IICARAGKDL VSSLTSGLLT IGDRFGGALD AAAKMFSKAF DSGIIPMEFV
960 970 980 990 1000
NKMKKEGKLI MGIGHRVKSI NNPDMRVQIL KDFVKQHFPA TPLLDYALEV
1010 1020 1030 1040 1050
EKITTSKKPN LILNVDGFIG VAFVDMLRNC GSFTREEADE YVDIGALNGI
1060 1070 1080 1090
FVLGRSMGFI GHYLDQKRLK QGLYRHPWDD ISYVLPEHMS M
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.
InParanoidi Q91V92.
KOi K01648.

Miscellaneous databases

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

Gene expression databases

Bgeei Q91V92.
CleanExi MM_ACLY.
ExpressionAtlasi Q91V92. baseline and differential.
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: October 29, 2014
This is version 122 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