Gene
Entrez ID Entrez Gene ID - the GENE ID in NCBI Gene database.
47
Gene name Gene Name - the full gene name approved by the HGNC.
ATP citrate lyase
Gene symbol Gene Symbol - the official gene symbol approved by the HGNC.
ACLY
Synonyms (NCBI Gene) Gene synonyms aliases
ACL, ATPCL, CLATP
Chromosome Chromosome number
17
Chromosome location Chromosomal Location - indicates the cytogenetic location of the gene or region on the chromosome.
17q21.2
Summary Summary of gene provided in NCBI Entrez Gene.
ATP citrate lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. The enzyme is a tetramer (relative molecular weight approximately 440,000) of apparently identical subunits. It catalyzes the formation of acety
miRNA miRNA information provided by mirtarbase database.
miRTarBase ID miRNA Experiments Reference
MIRT049373 hsa-miR-92a-3p CLASH 23622248
MIRT049373 hsa-miR-92a-3p CLASH 23622248
MIRT047450 hsa-miR-10b-5p CLASH 23622248
MIRT045906 hsa-miR-125b-5p CLASH 23622248
MIRT045416 hsa-miR-149-5p CLASH 23622248
Transcription factors
Transcription factor Regulation Reference
SREBF1 Activation 10777536
Gene ontology (GO) Gene ontology information of associated ontologies with gene provided by GO database.
GO ID Ontology Definition Evidence Reference
GO:0000166 Function Nucleotide binding IEA
GO:0003824 Function Catalytic activity IEA
GO:0003878 Function ATP citrate synthase activity IBA
GO:0003878 Function ATP citrate synthase activity IDA 1371749, 9116495, 10653665, 19286649
GO:0003878 Function ATP citrate synthase activity IEA
Other IDs Other ids provides unique ids of gene in databases such as OMIM, HGNC, ENSEMBLE.
MIM HGNC e!Ensembl
108728 115 ENSG00000131473
Protein
UniProt ID P53396
Protein name ATP-citrate synthase (EC 2.3.3.8) (ATP-citrate (pro-S-)-lyase) (ACL) (Citrate cleavage enzyme)
Protein function Catalyzes the cleavage of citrate into oxaloacetate and acetyl-CoA, the latter serving as common substrate in multiple biochemical reactions in protein, carbohydrate and lipid metabolism. {ECO:0000269|PubMed:10653665, ECO:0000269|PubMed:1371749,
PDB 3MWD , 3MWE , 3PFF , 5TDE , 5TDF , 5TDM , 5TDZ , 5TE1 , 5TEQ , 5TES , 5TET , 6HXH , 6HXK , 6HXL , 6HXM , 6O0H , 6POE , 6POF , 6QFB , 6UI9 , 6UIA , 6UUW , 6UUZ , 6UV5 , 6Z2H , 7LIW , 7LJ9 , 7LLA , 7RIG , 7RKZ , 7RMP , 8G1E , 8G1F , 8G5C , 8G5D
Family and domains

Pfam

Accession ID Position in sequence Description Type
PF16114 Citrate_bind 244 421 ATP citrate lyase citrate-binding Domain
PF02629 CoA_binding 494 600 CoA binding domain Domain
PF00549 Ligase_CoA 660 785 CoA-ligase Domain
PF00285 Citrate_synt 883 1086 Citrate synthase, C-terminal domain Domain
Sequence
MSAKAISEQTGKELLYKFICTTSAIQNRFKYARVTPDTDWARLLQDHPWLLSQNLVVKPD
QLIKRRGKLGLVGVNLTLDGVKSWLKPRLGQEATVGKATGFLKNFLIEPFVPHSQAEEFY
VCIYATREGDYVLFHHEGGVDVGDVDAKAQKLLVGVDEKLNPEDIKKHLLVHAPEDKKEI
LASFISGLFNFYEDLYFTYLEINPLVVTKDGVYVLDLAAKVDATADYICKVKWGDIEFPP
PFGREAYPEEAYIADLDAKSGASLKLTLLNPKGRIWTMVAGGGASVVYSDTICDLGGVNE
LANYGEYSGAPSEQQTYDYAKTILSLMTREKHPDGKILIIGGSIANFTNVAATFKGIVRA
IRDYQGPLKEHEVTIFVRRGGPNYQEGLRVMGEVGKTTGIPIHVFGTETHMTAIVGMALG
H
RPIPNQPPTAAHTANFLLNASGSTSTPAPSRTASFSESRADEVAPAKKAKPAMPQDSVP
SPRSLQGKSTTLFSRHTKAIVWGMQTRAVQGMLDFDYVCSRDEPSVAAMVYPFTGDHKQK
FYWGHKEILIPVFKNMADAMRKHPEVDVLINFASLRSAYDSTMETMNYAQIRTIAIIAEG

IPEALTRKLIKKADQKGVTIIGPATVGGIKPGCFKIGNTGGMLDNILASKLYRPGSVAYV
SRSGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVLRYQDTPGVKMIVVLGEIG
GTEEYKICRGIKEGRLTKPIVCWCIGTCATMFSSEVQFGHAGACANQASETAVAKNQALK
EAGVF
VPRSFDELGEIIQSVYEDLVANGVIVPAQEVPPPTVPMDYSWARELGLIRKPASF
MTSICDERGQELIYAGMPITEVFKEEMGIGGVLGLLWFQKRLPKYSCQFIEMCLMVTADH
GPAVSGAHNTIICARAGKDLVSSLTSGLLTIGDRFGGALDAAAKMFSKAFDSGIIPMEFV
NKMKKEGKLIMGIGHRVKSINNPDMRVQILKDYVRQHFPATPLLDYALEVEKITTSKKPN
LILNVDGLIGVAFVDMLRNCGSFTREEADEYIDIGALNGIFVLGRSMGFIGHYLDQKRLK
QGLYRH
PWDDISYVLPEHMSM
Sequence length 1101
Interactions View interactions
Pathways Pathway information has different metabolic/signaling pathways associated with genes.
  KEGG   Reactome
  Citrate cycle (TCA cycle)
Metabolic pathways
  ChREBP activates metabolic gene expression
Neutrophil degranulation
Fatty acyl-CoA biosynthesis
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