ACLY
entrez
47
canonical
uniprot
P53396
canonical
ensembl
ENSG00000131473
resolver
ensp
ENSP00000253792
resolver
ensp
ENSP00000345398
resolver
ensp
ENSP00000554561
resolver
genesymbol
ACLY
resolver
hgnc
HGNC:115
resolver
uniprot
B4DIM0
resolver
uniprot
B4E3P0
resolver
uniprot
Q13037
resolver
uniprot
Q9BRL0
resolver
uniprot_entry
ACLY_HUMAN
resolver
uniprot_sec
B4DIM0
resolver
uniprot_sec
B4E3P0
resolver
uniprot_sec
Q13037
resolver
uniprot_sec
Q9BRL0
resolver
activity_regulation
ACTIVITY REGULATION: Phosphorylation results in activation of its activity (PubMed:10653665). Glucose 6-phosphate, fructose 6-phosphate, fructose 2,6-bisphosphate, ribulose 5-phosphate, and fructose 1,6-bisphosphate also act as activators (PubMed:10653665). {ECO:0000269|PubMed:10653665}.
uniprot
proteins
amino_acid_sequence
MSAKAISEQTGKELLYKFICTTSAIQNRFKYARVTPDTDWARLLQDHPWLLSQNLVVKPDQLIKRRGKLGLVGVNLTLDGVKSWLKPRLGQEATVGKATGFLKNFLIEPFVPHSQAEEFYVCIYATREGDYVLFHHEGGVDVGDVDAKAQKLLVGVDEKLNPEDIKKHLLVHAPEDKKEILASFISGLFNFYEDLYFTYLEINPLVVTKDGVYVLDLAAKVDATADYICKVKWGDIEFPPPFGREAYPEEAYIADLDAKSGASLKLTLLNPKGRIWTMVAGGGASVVYSDTICDLGGVNELANYGEYSGAPSEQQTYDYAKTILSLMTREKHPDGKILIIGGSIANFTNVAATFKGIVRAIRDYQGPLKEHEVTIFVRRGGPNYQEGLRVMGEVGKTTGIPIHVFGTETHMTAIVGMALGHRPIPNQPPTAAHTANFLLNASGSTSTPAPSRTASFSESRADEVAPAKKAKPAMPQDSVPSPRSLQGKSTTLFSRHTKAIVWGMQTRAVQGMLDFDYVCSRDEPSVAAMVYPFTGDHKQKFYWGHKEILIPVFKNMADAMRKHPEVDVLINFASLRSAYDSTMETMNYAQIRTIAIIAEGIPEALTRKLIKKADQKGVTIIGPATVGGIKPGCFKIGNTGGMLDNILASKLYRPGSVAYVSRSGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVLRYQDTPGVKMIVVLGEIGGTEEYKICRGIKEGRLTKPIVCWCIGTCATMFSSEVQFGHAGACANQASETAVAKNQALKEAGVFVPRSFDELGEIIQSVYEDLVANGVIVPAQEVPPPTVPMDYSWARELGLIRKPASFMTSICDERGQELIYAGMPITEVFKEEMGIGGVLGLLWFQKRLPKYSCQFIEMCLMVTADHGPAVSGAHNTIICARAGKDLVSSLTSGLLTIGDRFGGALDAAAKMFSKAFDSGIIPMEFVNKMKKEGKLIMGIGHRVKSINNPDMRVQILKDYVRQHFPATPLLDYALEVEKITTSKKPNLILNVDGLIGVAFVDMLRNCGSFTREEADEYIDIGALNGIFVLGRSMGFIGHYLDQKRLKQGLYRHPWDDISYVLPEHMSM
uniprot
proteins
ec_number
2.3.3.8
uniprot
proteins
function
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, ECO:0000269|PubMed:19286649, ECO:0000269|PubMed:23932781, ECO:0000269|PubMed:39881208, ECO:0000269|PubMed:9116495}.
uniprot
proteins
mass_dalton
120839
uniprot
proteins
mutagenesis
MUTAGEN 540; /note="K->R,Q: Decreased acetylation and increased de novo lipid synthesis; when associated with R,Q-546 and R,Q-554. Abolished ubiquitination by the BCR(KLHL25)complex; when associated with R-546 and R-554."; /evidence="ECO:0000269|PubMed:23932781, ECO:0000269|PubMed:27664236"; MUTAGEN 546; /note="K->R,Q: Decreased acetylation and increased de novo lipid synthesis; when associated with R,Q-540 and R,Q-554. Abolished ubiquitination by the BCR(KLHL25) complex; when associated with R-540 and R-554."; /evidence="ECO:0000269|PubMed:23932781, ECO:0000269|PubMed:27664236"; MUTAGEN 554; /note="K->R,Q: Decreased acetylation and increased de novo lipid synthesis; when associated with R,Q-540 and R,Q-546. Abolished ubiquitination by the BCR(KLHL25) complex; when associated with R-540 and R-546."; /evidence="ECO:0000269|PubMed:23932781, ECO:0000269|PubMed:27664236"; MUTAGEN 760; /note="H->A: Reduced enzyme activity."; /evidence="ECO:0000269|PubMed:1371749"; MUTAGEN 978; /note="K->A: Abolished debenzoylation by SIRT3."; /evidence="ECO:0000269|PubMed:39524354
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by PKA and GSK3 in a sequential manner; phosphorylation results in activation of its activity (PubMed:10653665). Phosphorylation on Thr-447 and Ser-451 depends on the phosphorylation state of Ser-455 (By similarity). Phosphorylation on Ser-455 is decreased by prior phosphorylation on the other 2 residues (By similarity). Phosphorylated at Ser-455 by BCKDK and dephosphorylated by protein phosphatase PPM1K. {ECO:0000250|UniProtKB:P16638, ECO:0000269|PubMed:10653665, ECO:0000269|PubMed:29779826}.; PTM: ISGylated. {ECO:0000269|PubMed:16139798}.; PTM: Acetylated at Lys-540, Lys-546 and Lys-554 by KAT2B/PCAF (PubMed:23932781). Acetylation is promoted by glucose and stabilizes the protein, probably by preventing ubiquitination at the same sites (PubMed:23932781). Acetylation promotes de novo lipid synthesis (PubMed:23932781). Deacetylated by SIRT2. {ECO:0000269|PubMed:23932781}.; PTM: Benzoylated at Lys-978 (PubMed:39524354). Debenzoylated by SIRT3; inhibiting the ATP-citrate synthase activity (PubMed:39524354). {ECO:0000269|PubMed:39524354}.; PTM: Ubiquitinated at Lys-540, Lys-546 and Lys-554 by the BCR(KLHL25) E3 ubiquitin ligase complex and UBR4, leading to its degradation (PubMed:23932781, PubMed:27664236, PubMed:34491895). Ubiquitination is probably inhibited by acetylation at same site (PubMed:23932781). BCR(KLHL25)-mediated degradation of ACLY promotes fatty acid oxidation and is required for differentiation of inducible regulatory T (iTreg) cells (PubMed:34491895). {ECO:0000269|PubMed:23932781, ECO:0000269|PubMed:27664236, ECO:0000269|PubMed:34491895}.
uniprot
proteins
protein_family
Succinate/malate CoA ligase beta subunit family; Succinate/malate CoA ligase alpha subunit family
uniprot
proteins
pubmed
10653665
uniprot
proteins
pubmed
1371749
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15592455
uniprot
proteins
pubmed
16139798
uniprot
proteins
pubmed
16625196
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17924679
uniprot
proteins
pubmed
18088087
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19286649
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20558738
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22102020
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23932781
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
27664236
uniprot
proteins
pubmed
29779826
uniprot
proteins
pubmed
34491895
uniprot
proteins
pubmed
39524354
uniprot
proteins
pubmed
39881208
uniprot
proteins
pubmed
9116495
uniprot
proteins
sequence_length
1101
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:9116495}.
uniprot
proteins