Acly
entrez
24159
canonical
uniprot
P16638
canonical
ensembl
ENSRNOG00000016924
resolver
ensp
ENSRNOP00000023447
resolver
ensp
ENSRNOP00000046597
resolver
enst
ENSRNOT00000023447
resolver
enst
ENSRNOT00000043172
resolver
genesymbol
Acly
resolver
uniprot
G3V888
resolver
uniprot
G3V9G4
resolver
uniprot
Q497C7
resolver
uniprot
Q8VIQ1
resolver
uniprot_entry
ACLY_RAT
resolver
uniprot_entry
G3V888_RAT
resolver
uniprot_entry
G3V9G4_RAT
resolver
uniprot_sec
Q497C7
resolver
uniprot_sec
Q8VIQ1
resolver
activity_regulation
ACTIVITY REGULATION: Phosphorylation results in activation of its activity (By similarity). Glucose 6-phosphate, fructose 6-phosphate, fructose 2,6-bisphosphate, ribulose 5-phosphate, and fructose 1,6-bisphosphate also act as activators (By similarity). {ECO:0000250|UniProtKB:P53396}.
uniprot
proteins
amino_acid_sequence
MSAKAISEQTGKELLYKYICTTSAIQNRFKYARVTPDTDWAHLLQDHPWLLSQSLVVKPDQLIKRRGKLGLVGVNLSLDGVKSWLKPRLGHEATVGKAKGFLKNFLIEPFVPHSQAEEFYVCIYATREGDYVLFHHEGGVDVGDVDTKAQKLLVGVDEKLNAEDIKRHLLVHAPEDKKEILASFISGLFNFYEDLYFTYLEINPLVVTKDGVYILDLAAKVDATADYICKVKWGDIEFPPPFGREAYPEEAYIADLDAKSGASLKLTLLNPKGRIWTMVAGGGASVVYSDTICDLGGVNELANYGEYSGAPSEQQTYDYAKTILSLMTREKHPDGKILIIGGSIANFTNVAATFKGIVRAIRDYQGSLKEHEVTIFVRRGGPNYQEGLRVMGEVGKTTGIPIHVFGTETHMTAIVGMAWAPAIPNQPPTAAHTANFLLNASGSTSTPAPSRTASFSESRADEVAPAKKAKPAMPQDSVPSPRSLQGKSATLFSRHTKAIVWGMQTRAVQGMLDFDYVCSRDEPSVAAMVYPFTGDHKQKFYWGHKEILIPVFKNMADAMKKHPEVDVLINFASLRSAYDSTMETMNYAQIRTIAIIAEGIPEALTRKLIKKADQKGVTIIGPATVGGIKPGCFKIGNTGGMLDNILASKLYRPGSVAYVSRSGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVLRYQDTPGVKMIVVLGEIGGTEEYKICRGIKEGRLTKPVVCWCIGTCATMFSSEVQFGHAGACANQASETAVAKNQALKEAGVFVPRSFDELGEIIQSVYEDLVAKGAIVPAQEVPPPTVPMDYSWARELGLIRKPASFMTSICDERGQELIYAGMPITEVFKEEMGIGGVLGLLWFQRRLPKYSCQFIEMCLMVTADHGPAVSGAHNTIICARAGKDLVSSLTSGLLTIGDRFGGALDAAAKMFSKAFDSGIIPMEFVNKMKKEGKLIMGIGHRVKSINNPDMRVQILKDFVKQHFPATPLLDYALEVEKITTSKKPNLILNVDGFIGVAFVDMLRNCGSFTREEADEYVDIGALNGVFVLGRSMGFIGHYLDQKRLKQGLYRHPWDDISYVLPEHMSM
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:9116495}.
uniprot
proteins
mass_dalton
120636
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by PKA and GSK3 in a sequential manner; phosphorylation results in activation of its activity (By similarity). Phosphorylation on Thr-446 and Ser-450 depends on the phosphorylation state of Ser-454 (PubMed:12107176, PubMed:2176822). Phosphorylation on Ser-454 is decreased by prior phosphorylation on the other 2 residues (PubMed:12107176, PubMed:2176822). Phosphorylated at Ser-454 by BCKDK and dephosphorylated by protein phosphatase PPM1K. {ECO:0000250|UniProtKB:P53396, ECO:0000269|PubMed:12107176, ECO:0000269|PubMed:2176822, ECO:0000269|PubMed:29779826}.; PTM: The N-terminus is blocked. {ECO:0000269|PubMed:2295639}.; PTM: ISGylated. {ECO:0000250|UniProtKB:P53396}.; PTM: Acetylated at Lys-539, Lys-545 and Lys-553 by KAT2B/PCAF (By similarity). Acetylation is promoted by glucose and stabilizes the protein, probably by preventing ubiquitination at the same sites (By similarity). Acetylation promotes de novo lipid synthesis (By similarity). Deacetylated by SIRT2 (By similarity). {ECO:0000250|UniProtKB:P53396}.; PTM: Ubiquitinated at Lys-539, Lys-545 and Lys-553 by the BCR(KLHL25) E3 ubiquitin ligase complex and UBR4, leading to its degradation (By similarity). Ubiquitination is probably inhibited by acetylation at same site (By similarity). BCR(KLHL25)-mediated degradation of ACLY promotes fatty acid oxidation and is required for differentiation of inducible regulatory T (iTreg) cells (By similarity). {ECO:0000250|UniProtKB:P53396, ECO:0000250|UniProtKB:Q91V92}.; PTM: Benzoylated at Lys-977. Debenzoylated by SIRT3; inhibiting the ATP-citrate synthase activity. {ECO:0000250|UniProtKB:P53396}.
uniprot
proteins
protein_family
Succinate/malate CoA ligase beta subunit family; Succinate/malate CoA ligase alpha subunit family
uniprot
proteins
pubmed
12107176
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16396499
uniprot
proteins
pubmed
2176822
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
2295639
uniprot
proteins
pubmed
29779826
uniprot
proteins
pubmed
8688462
uniprot
proteins
pubmed
9116495
uniprot
proteins
sequence_length
1100
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P53396}.
uniprot
proteins