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Protein

ATP-citrate synthase

Gene

ACLY

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

ATP-citrate synthase 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.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei58ATP1
Binding sitei118ATP1
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi201MagnesiumBy similarity1
Metal bindingi203MagnesiumBy similarity1
Binding sitei346Citrate; via amide nitrogen1 Publication1
Binding sitei348Citrate1 Publication1
Binding sitei379Citrate1 Publication1
Metal bindingi718MagnesiumBy similarity1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei760Tele-phosphohistidine intermediateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi66 – 67ATP2
Nucleotide bindingi109 – 111ATP3
Nucleotide bindingi701 – 721ATPBy similarityAdd BLAST21
Nucleotide bindingi752 – 778ATPBy similarityAdd BLAST27

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • ATP binding Source: BHF-UCL
  • ATP citrate synthase activity Source: BHF-UCL
  • cofactor binding Source: InterPro
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionTransferase
Biological processLipid biosynthesis, Lipid metabolism
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:HS05535-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.3.3.8 2681

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-163765 ChREBP activates metabolic gene expression
R-HSA-6798695 Neutrophil degranulation
R-HSA-75105 Fatty acyl-CoA biosynthesis

SABIO-RK: Biochemical Reaction Kinetics Database

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SABIO-RKi
P53396

SIGNOR Signaling Network Open Resource

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SIGNORi
P53396

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000000779

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
ATP-citrate synthase (EC:2.3.3.8)
Alternative name(s):
ATP-citrate (pro-S-)-lyase
Short name:
ACL
Citrate cleavage enzyme
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ACLY
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 17

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000131473.16

Human Gene Nomenclature Database

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HGNCi
HGNC:115 ACLY

Online Mendelian Inheritance in Man (OMIM)

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MIMi
108728 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P53396

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi540K → R or Q: Decreased acetylation and increased de novo lipid synthesis; when associated with R,Q-546 and R,Q-554. 1 Publication1
Mutagenesisi546K → R or Q: Decreased acetylation and increased de novo lipid synthesis; when associated with R,Q-540 and R,Q-554. 1 Publication1
Mutagenesisi554K → R or Q: Decreased acetylation and increased de novo lipid synthesis; when associated with R,Q-540 and R,Q-546. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
47

Open Targets

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OpenTargetsi
ENSG00000131473

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA24441

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL3720

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
ACLY

Domain mapping of disease mutations (DMDM)

More...
DMDMi
116241237

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001027811 – 1101ATP-citrate synthaseAdd BLAST1101

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei131PhosphotyrosineCombined sources1
Modified residuei263PhosphoserineBy similarity1
Modified residuei447PhosphothreonineBy similarity1
Modified residuei451PhosphoserineBy similarity1
Modified residuei455Phosphoserine; by PKA and PKB/AKT1 or PKB/AKT2Combined sources1
Modified residuei459PhosphoserineCombined sources1
Modified residuei481PhosphoserineCombined sources1
Modified residuei540N6-acetyllysine; alternate1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki540Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Modified residuei546N6-acetyllysine; alternateCombined sources1 Publication1
Cross-linki546Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Modified residuei554N6-acetyllysine; alternateCombined sources1 Publication1
Cross-linki554Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Modified residuei639PhosphothreonineCombined sources1
Modified residuei663PhosphoserineCombined sources1
Modified residuei682PhosphotyrosineCombined sources1
Modified residuei839PhosphoserineCombined sources1
Modified residuei948N6-acetyllysineCombined sources1
Modified residuei968N6-acetyllysineCombined sources1
Modified residuei978N6-acetyllysineBy similarity1
Modified residuei1077N6-acetyllysineCombined sources1
Modified residuei1100PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

ISGylated.1 Publication
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 SIRT2.1 Publication
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).1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P53396

MaxQB - The MaxQuant DataBase

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MaxQBi
P53396

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P53396

PeptideAtlas

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PeptideAtlasi
P53396

PRoteomics IDEntifications database

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PRIDEi
P53396

ProteomicsDB human proteome resource

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ProteomicsDBi
56581
56582 [P53396-2]

PTM databases

CarbonylDB database of protein carbonylation sites

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CarbonylDBi
P53396

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P53396

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P53396

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P53396

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000131473 Expressed in 236 organ(s), highest expression level in liver

CleanEx database of gene expression profiles

More...
CleanExi
HS_ACLY

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P53396 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P53396 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB007783
HPA022434
HPA022953
HPA022959
HPA028758

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotetramer.2 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
106563, 86 interactors

Protein interaction database and analysis system

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IntActi
P53396, 20 interactors

Molecular INTeraction database

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MINTi
P53396

STRING: functional protein association networks

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STRINGi
9606.ENSP00000253792

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P53396

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11101
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P53396

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P53396

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P53396

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini4 – 265ATP-graspAdd BLAST262

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni779 – 789CoA-bindingSequence analysisAdd BLAST11

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG1254 Eukaryota
COG0045 LUCA
COG0074 LUCA
COG0372 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000154881

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000151479

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG003318

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P53396

KEGG Orthology (KO)

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KOi
K01648

Identification of Orthologs from Complete Genome Data

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OMAi
MMDNILH

Database of Orthologous Groups

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OrthoDBi
EOG091G0OYH

Database for complete collections of gene phylogenies

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PhylomeDBi
P53396

TreeFam database of animal gene trees

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TreeFami
TF300560

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.230.10, 1 hit
3.40.50.261, 2 hits

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR014608 ATP-citrate_synthase
IPR017440 Cit_synth/succinyl-CoA_lig_AS
IPR032263 Citrate-bd
IPR016143 Citrate_synth-like_sm_a-sub
IPR002020 Citrate_synthase
IPR036969 Citrate_synthase_sf
IPR033847 Citrt_syn/SCS-alpha_CS
IPR003781 CoA-bd
IPR005811 CoA_ligase
IPR036291 NAD(P)-bd_dom_sf
IPR017866 Succ-CoA_synthase_bsu_CS
IPR016102 Succinyl-CoA_synth-like

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF16114 Citrate_bind, 1 hit
PF00285 Citrate_synt, 1 hit
PF02629 CoA_binding, 1 hit
PF00549 Ligase_CoA, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF036511 ATP_citrt_syn, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00881 CoA_binding, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF48256 SSF48256, 1 hit
SSF51735 SSF51735, 1 hit
SSF52210 SSF52210, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS01216 SUCCINYL_COA_LIG_1, 1 hit
PS00399 SUCCINYL_COA_LIG_2, 1 hit
PS01217 SUCCINYL_COA_LIG_3, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P53396-1) [UniParc]FASTAAdd to basket

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.

« Hide
        10         20         30         40         50
MSAKAISEQT GKELLYKFIC TTSAIQNRFK YARVTPDTDW ARLLQDHPWL
60 70 80 90 100
LSQNLVVKPD QLIKRRGKLG LVGVNLTLDG VKSWLKPRLG QEATVGKATG
110 120 130 140 150
FLKNFLIEPF VPHSQAEEFY VCIYATREGD YVLFHHEGGV DVGDVDAKAQ
160 170 180 190 200
KLLVGVDEKL NPEDIKKHLL VHAPEDKKEI LASFISGLFN FYEDLYFTYL
210 220 230 240 250
EINPLVVTKD GVYVLDLAAK VDATADYICK VKWGDIEFPP PFGREAYPEE
260 270 280 290 300
AYIADLDAKS GASLKLTLLN PKGRIWTMVA GGGASVVYSD TICDLGGVNE
310 320 330 340 350
LANYGEYSGA PSEQQTYDYA KTILSLMTRE KHPDGKILII 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 KPAMPQDSVP SPRSLQGKST TLFSRHTKAI
510 520 530 540 550
VWGMQTRAVQ GMLDFDYVCS RDEPSVAAMV YPFTGDHKQK FYWGHKEILI
560 570 580 590 600
PVFKNMADAM RKHPEVDVLI NFASLRSAYD STMETMNYAQ IRTIAIIAEG
610 620 630 640 650
IPEALTRKLI KKADQKGVTI IGPATVGGIK PGCFKIGNTG GMLDNILASK
660 670 680 690 700
LYRPGSVAYV SRSGGMSNEL NNIISRTTDG VYEGVAIGGD RYPGSTFMDH
710 720 730 740 750
VLRYQDTPGV KMIVVLGEIG GTEEYKICRG IKEGRLTKPI VCWCIGTCAT
760 770 780 790 800
MFSSEVQFGH AGACANQASE TAVAKNQALK EAGVFVPRSF DELGEIIQSV
810 820 830 840 850
YEDLVANGVI VPAQEVPPPT VPMDYSWARE LGLIRKPASF MTSICDERGQ
860 870 880 890 900
ELIYAGMPIT EVFKEEMGIG GVLGLLWFQK RLPKYSCQFI EMCLMVTADH
910 920 930 940 950
GPAVSGAHNT IICARAGKDL VSSLTSGLLT IGDRFGGALD AAAKMFSKAF
960 970 980 990 1000
DSGIIPMEFV NKMKKEGKLI MGIGHRVKSI NNPDMRVQIL KDYVRQHFPA
1010 1020 1030 1040 1050
TPLLDYALEV EKITTSKKPN LILNVDGLIG VAFVDMLRNC GSFTREEADE
1060 1070 1080 1090 1100
YIDIGALNGI FVLGRSMGFI GHYLDQKRLK QGLYRHPWDD ISYVLPEHMS

M
Length:1,101
Mass (Da):120,839
Last modified:October 17, 2006 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i12BB4416A30DC30C
GO
Isoform 2 (identifier: P53396-2) [UniParc]FASTAAdd to basket

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

Show »
Length:1,091
Mass (Da):119,772
Checksum:i04EB8D05059409E5
GO
Isoform 3 (identifier: P53396-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     95-355: Missing.
     476-485: Missing.

Note: No experimental confirmation available.
Show »
Length:830
Mass (Da):91,099
Checksum:i1F3758EEAACA3730
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
K7EIE7K7EIE7_HUMAN
ATP-citrate synthase
ACLY
133Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
K7ESG8K7ESG8_HUMAN
ATP-citrate synthase
ACLY
109Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti75N → D in CAA45614 (PubMed:1371749).Curated1
Sequence conflicti111V → A in CAA45614 (PubMed:1371749).Curated1
Sequence conflicti245E → V in CAA45614 (PubMed:1371749).Curated1
Sequence conflicti419 – 423LGHRP → WAPA in CAA45614 (PubMed:1371749).Curated5
Sequence conflicti442 – 444SGS → QRE in CAA45614 (PubMed:1371749).Curated3
Sequence conflicti457 – 459SES → YESMVDEV in CAA45614 (PubMed:1371749).Curated3
Sequence conflicti653 – 656RPGS → PQAA in CAA45614 (PubMed:1371749).Curated4
Sequence conflicti728C → S in CAA45614 (PubMed:1371749).Curated1
Sequence conflicti872V → A in CAA45614 (PubMed:1371749).Curated1
Sequence conflicti916 – 919AGKD → TAVE in CAA45614 (PubMed:1371749).Curated4

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_028230175E → D3 PublicationsCorresponds to variant dbSNP:rs2304497Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_05723095 – 355Missing in isoform 3. 1 PublicationAdd BLAST261
Alternative sequenceiVSP_042201476 – 485Missing in isoform 2 and isoform 3. 1 Publication10

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X64330 mRNA Translation: CAA45614.1
U18197 mRNA Translation: AAB60340.1
AK295675 mRNA Translation: BAG58532.1
AK304802 mRNA Translation: BAG65552.1
AC091172 Genomic DNA No translation available.
AC125257 Genomic DNA No translation available.
BC006195 mRNA Translation: AAH06195.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS11412.1 [P53396-1]
CCDS11413.1 [P53396-2]

Protein sequence database of the Protein Information Resource

More...
PIRi
S21173

NCBI Reference Sequences

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RefSeqi
NP_001087.2, NM_001096.2 [P53396-1]
NP_001290203.1, NM_001303274.1
NP_001290204.1, NM_001303275.1
NP_942127.1, NM_198830.1 [P53396-2]
XP_005257452.1, XM_005257395.1 [P53396-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.387567

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000352035; ENSP00000253792; ENSG00000131473 [P53396-1]
ENST00000353196; ENSP00000345398; ENSG00000131473 [P53396-2]
ENST00000393896; ENSP00000377474; ENSG00000131473 [P53396-2]
ENST00000537919; ENSP00000445349; ENSG00000131473 [P53396-3]
ENST00000590151; ENSP00000466259; ENSG00000131473 [P53396-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
47

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:47

UCSC genome browser

More...
UCSCi
uc002hyg.4 human [P53396-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64330 mRNA Translation: CAA45614.1
U18197 mRNA Translation: AAB60340.1
AK295675 mRNA Translation: BAG58532.1
AK304802 mRNA Translation: BAG65552.1
AC091172 Genomic DNA No translation available.
AC125257 Genomic DNA No translation available.
BC006195 mRNA Translation: AAH06195.1
CCDSiCCDS11412.1 [P53396-1]
CCDS11413.1 [P53396-2]
PIRiS21173
RefSeqiNP_001087.2, NM_001096.2 [P53396-1]
NP_001290203.1, NM_001303274.1
NP_001290204.1, NM_001303275.1
NP_942127.1, NM_198830.1 [P53396-2]
XP_005257452.1, XM_005257395.1 [P53396-1]
UniGeneiHs.387567

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3MWDX-ray2.10A1-425[»]
B487-820[»]
3MWEX-ray2.20A1-425[»]
B487-821[»]
3PFFX-ray2.30A1-817[»]
5TDEX-ray1.70A1-425[»]
B487-810[»]
5TDFX-ray1.80A1-425[»]
B487-810[»]
5TDMX-ray2.10A1-425[»]
B487-810[»]
5TDZX-ray2.00A1-425[»]
B487-810[»]
5TE1X-ray2.25A/B1-817[»]
5TEQX-ray2.30A/B1-817[»]
5TESX-ray2.40A1-425[»]
B487-810[»]
5TETX-ray2.20A1-425[»]
B487-810[»]
ProteinModelPortaliP53396
SMRiP53396
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106563, 86 interactors
IntActiP53396, 20 interactors
MINTiP53396
STRINGi9606.ENSP00000253792

Chemistry databases

BindingDBiP53396
ChEMBLiCHEMBL3720
SwissLipidsiSLP:000000779

PTM databases

CarbonylDBiP53396
iPTMnetiP53396
PhosphoSitePlusiP53396
SwissPalmiP53396

Polymorphism and mutation databases

BioMutaiACLY
DMDMi116241237

Proteomic databases

EPDiP53396
MaxQBiP53396
PaxDbiP53396
PeptideAtlasiP53396
PRIDEiP53396
ProteomicsDBi56581
56582 [P53396-2]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
47
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000352035; ENSP00000253792; ENSG00000131473 [P53396-1]
ENST00000353196; ENSP00000345398; ENSG00000131473 [P53396-2]
ENST00000393896; ENSP00000377474; ENSG00000131473 [P53396-2]
ENST00000537919; ENSP00000445349; ENSG00000131473 [P53396-3]
ENST00000590151; ENSP00000466259; ENSG00000131473 [P53396-1]
GeneIDi47
KEGGihsa:47
UCSCiuc002hyg.4 human [P53396-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
47
DisGeNETi47
EuPathDBiHostDB:ENSG00000131473.16

GeneCards: human genes, protein and diseases

More...
GeneCardsi
ACLY
HGNCiHGNC:115 ACLY
HPAiCAB007783
HPA022434
HPA022953
HPA022959
HPA028758
MIMi108728 gene
neXtProtiNX_P53396
OpenTargetsiENSG00000131473
PharmGKBiPA24441

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1254 Eukaryota
COG0045 LUCA
COG0074 LUCA
COG0372 LUCA
GeneTreeiENSGT00940000154881
HOGENOMiHOG000151479
HOVERGENiHBG003318
InParanoidiP53396
KOiK01648
OMAiMMDNILH
OrthoDBiEOG091G0OYH
PhylomeDBiP53396
TreeFamiTF300560

Enzyme and pathway databases

BioCyciMetaCyc:HS05535-MONOMER
BRENDAi2.3.3.8 2681
ReactomeiR-HSA-163765 ChREBP activates metabolic gene expression
R-HSA-6798695 Neutrophil degranulation
R-HSA-75105 Fatty acyl-CoA biosynthesis
SABIO-RKiP53396
SIGNORiP53396

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
ACLY human
EvolutionaryTraceiP53396

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
47

Protein Ontology

More...
PROi
PR:P53396

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000131473 Expressed in 236 organ(s), highest expression level in liver
CleanExiHS_ACLY
ExpressionAtlasiP53396 baseline and differential
GenevisibleiP53396 HS

Family and domain databases

Gene3Di1.10.230.10, 1 hit
3.40.50.261, 2 hits
InterProiView protein in InterPro
IPR014608 ATP-citrate_synthase
IPR017440 Cit_synth/succinyl-CoA_lig_AS
IPR032263 Citrate-bd
IPR016143 Citrate_synth-like_sm_a-sub
IPR002020 Citrate_synthase
IPR036969 Citrate_synthase_sf
IPR033847 Citrt_syn/SCS-alpha_CS
IPR003781 CoA-bd
IPR005811 CoA_ligase
IPR036291 NAD(P)-bd_dom_sf
IPR017866 Succ-CoA_synthase_bsu_CS
IPR016102 Succinyl-CoA_synth-like
PfamiView protein in Pfam
PF16114 Citrate_bind, 1 hit
PF00285 Citrate_synt, 1 hit
PF02629 CoA_binding, 1 hit
PF00549 Ligase_CoA, 1 hit
PIRSFiPIRSF036511 ATP_citrt_syn, 1 hit
SMARTiView protein in SMART
SM00881 CoA_binding, 1 hit
SUPFAMiSSF48256 SSF48256, 1 hit
SSF51735 SSF51735, 1 hit
SSF52210 SSF52210, 1 hit
PROSITEiView protein in PROSITE
PS01216 SUCCINYL_COA_LIG_1, 1 hit
PS00399 SUCCINYL_COA_LIG_2, 1 hit
PS01217 SUCCINYL_COA_LIG_3, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiACLY_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P53396
Secondary accession number(s): B4DIM0
, B4E3P0, Q13037, Q9BRL0
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 17, 2006
Last modified: December 5, 2018
This is version 201 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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