ACACA
entrez
31
canonical
uniprot
Q13085
canonical
ensembl
ENSG00000275176
resolver
ensembl
ENSG00000278540
resolver
ensp
ENSP00000478547
resolver
ensp
ENSP00000482269
resolver
ensp
ENSP00000482368
resolver
ensp
ENSP00000483300
resolver
genesymbol
ACACA
resolver
genesymbol_syn
ACAC
resolver
genesymbol_syn
ACC1
resolver
genesymbol_syn
ACCA
resolver
hgnc
HGNC:84
resolver
uniprot
B2RP68
resolver
uniprot
B2ZZ90
resolver
uniprot
Q6KEV6
resolver
uniprot
Q6XDA8
resolver
uniprot
Q7Z2G8
resolver
uniprot
Q7Z561
resolver
uniprot
Q7Z563
resolver
uniprot
Q7Z564
resolver
uniprot
Q7Z5W8
resolver
uniprot
Q86WB2
resolver
uniprot
Q86WB3
resolver
uniprot_entry
ACACA_HUMAN
resolver
uniprot_entry
Q7Z5W8_HUMAN
resolver
uniprot_sec
B2RP68
resolver
uniprot_sec
B2ZZ90
resolver
uniprot_sec
Q6KEV6
resolver
uniprot_sec
Q6XDA8
resolver
uniprot_sec
Q7Z2G8
resolver
uniprot_sec
Q7Z561
resolver
uniprot_sec
Q7Z563
resolver
uniprot_sec
Q7Z564
resolver
uniprot_sec
Q86WB2
resolver
uniprot_sec
Q86WB3
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by phosphorylation (PubMed:16326698, PubMed:29899443). Citrate promotes oligomerization of the protein into filaments that correspond to the most active form of the carboxylase (PubMed:29899443). Inhibited by palmitoyl-CoA (PubMed:29899443). {ECO:0000269|PubMed:16326698, ECO:0000269|PubMed:29899443}.
uniprot
proteins
amino_acid_sequence
MDEPSPLAQPLELNQHSRFIIGSVSEDNSEDEISNLVKLDLLEEKEGSLSPASVGSDTLSDLGISSLQDGLALHIRSSMSGLHLVKQGRDRKKIDSQRDFTVASPAEFVTRFGGNKVIEKVLIANNGIAAVKCMRSIRRWSYEMFRNERAIRFVVMVTPEDLKANAEYIKMADHYVPVPGGPNNNNYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSGSGLRVDWQENDFSKRILNVPQELYEKGYVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVPGSPIFVMRLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLYRIKDIRMMYGVSPWGDSPIDFEDSAHVPCPRGHVIAARITSENPDEGFKPSSGTVQELNFRSNKNVWGYFSVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGDFRTTVEYLIKLLETESFQMNRIDTGWLDRLIAEKVQAERPDTMLGVVCGALHVADVSLRNSVSNFLHSLERGQVLPAHTLLNTVDVELIYEGVKYVLKVTRQSPNSYVVIMNGSCVEVDVHRLSDGGLLLSYDGSSYTTYMKEEVDRYRITIGNKTCVFEKENDPSVMRSPSAGKLIQYIVEDGGHVFAGQCYAEIEVMKMVMTLTAVESGCIHYVKRPGAALDPGCVLAKMQLDNPSKVQQAELHTGSLPRIQSTALRGEKLHRVFHYVLDNLVNVMNGYCLPDPFFSSKVKDWVERLMKTLRDPSLPLLELQDIMTSVSGRIPPNVEKSIKKEMAQYASNITSVLCQFPSQQIANILDSHAATLNRKSEREVFFMNTQSIVQLVQRYRSGIRGHMKAVVMDLLRQYLRVETQFQNGHYDKCVFALREENKSDMNTVLNYIFSHAQVTKKNLLVTMLIDQLCGRDPTLTDELLNILTELTQLSKTTNAKVALRARQVLIASHLPSYELRHNQVESIFLSAIDMYGHQFCIENLQKLILSETSIFDVLPNFFYHSNQVVRMAALEVYVRRAYIAYELNSVQHRQLKDNTCVVEFQFMLPTSHPNRGNIPTLNRMSFSSNLNHYGMTHVASVSDVLLDNSFTPPCQRMGGMVSFRTFEDFVRIFDEVMGCFSDSPPQSPTFPEAGHTSLYDEDKVPRDEPIHILNVAIKTDCDIEDDRLAAMFREFTQQNKATLVDHGIRRLTFLVAQKDFRKQVNYEVDRRFHREFPKFFTFRARDKFEEDRIYRHLEPALAFQLELNRMRNFDLTAIPCANHKMHLYLGAAKVEVGTEVTDYRFFVRAIIRHSDLVTKEASFEYLQNEGERLLLEAMDELEVAFNNTNVRTDCNHIFLNFVPTVIMDPSKIEESVRSMVMRYGSRLWKLRVLQAELKINIRLTPTGKAIPIRLFLTNESGYYLDISLYKEVTDSRTAQIMFQAYGDKQGPLHGMLINTPYVTKDLLQSKRFQAQSLGTTYIYDIPEMFRQSLIKLWESMSTQAFLPSPPLPSDMLTYTELVLDDQGQLVHMNRLPGGNEIGMVAWKMTFKSPEYPEGRDIIVIGNDITYRIGSFGPQEDLLFLRASELARAEGIPRIYVSANSGARIGLAEEIRHMFHVAWVDPEDPYKGYRYLYLTPQDYKRVSALNSVHCEHVEDEGESRYKITDIIGKEEGIGPENLRGSGMIAGESSLAYNEIITISLVTCRAIGIGAYLVRLGQRTIQVENSHLILTGAGALNKVLGREVYTSNNQLGGIQIMHNNGVTHCTVCDDFEGVFTVLHWLSYMPKSVHSSVPLLNSKDPIDRIIEFVPTKTPYDPRWMLAGRPHPTQKGQWLSGFFDYGSFSEIMQPWAQTVVVGRARLGGIPVGVVAVETRTVELSIPADPANLDSEAKIIQQAGQVWFPDSAFKTYQAIKDFNREGLPLMVFANWRGFSGGMKDMYDQVLKFGAYIVDGLRECCQPVLVYIPPQAELRGGSWVVIDSSINPRHMEMYADRESRGSVLEPEGTVEIKFRRKDLVKTMRRVDPVYIHLAERLGTPELSTAERKELENKLKEREEFLIPIYHQVAVQFADLHDTPGRMQEKGVISDILDWKTSRTFFYWRLRRLLLEDLVKKKIHNANPELTDGQIQAMLRRWFVEVEGTVKAYVWDNNKDLAEWLEKQLTEEDGVHSVIEENIKCISRDYVLKQIRSLVQANPEVAMDSIIHMTQHISPTQRAEVIRILSTMDSPST
uniprot
proteins
disease_involvement
DISEASE: Acetyl-CoA carboxylase-alpha deficiency (ACACAD) [MIM:613933]: An autosomal recessive inborn error of de novo fatty acid synthesis associated with severe brain damage, persistent myopathy and poor growth. {ECO:0000269|PubMed:6114432}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
6.4.1.2
uniprot
proteins
function
FUNCTION: Cytosolic enzyme that catalyzes the carboxylation of acetyl-CoA to malonyl-CoA, the first and rate-limiting step of de novo fatty acid biosynthesis (PubMed:20457939, PubMed:20952656, PubMed:29899443). This is a 2 steps reaction starting with the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carrier (BCC) domain followed by the transfer of the carboxyl group from carboxylated biotin to acetyl-CoA (PubMed:20457939, PubMed:20952656, PubMed:29899443). {ECO:0000269|PubMed:20457939, ECO:0000269|PubMed:20952656, ECO:0000269|PubMed:29899443}.
uniprot
proteins
mass_dalton
265554
uniprot
proteins
mutagenesis
MUTAGEN 78; /note="S->A: No effect on interaction with BRCA1."; /evidence="ECO:0000269|PubMed:16698035"; MUTAGEN 344; /note="S->A: No effect on interaction with BRCA1."; /evidence="ECO:0000269|PubMed:16698035"; MUTAGEN 432; /note="S->A: No effect on interaction with BRCA1."; /evidence="ECO:0000269|PubMed:16698035"; MUTAGEN 1201; /note="S->A: No effect on interaction with BRCA1."; /evidence="ECO:0000269|PubMed:16698035"; MUTAGEN 1263; /note="S->A: Abolishes interaction with BRCA1."; /evidence="ECO:0000269|PubMed:16698035"; MUTAGEN 1585; /note="S->A: No effect on interaction with BRCA1."; /evidence="ECO:0000269|PubMed:16698035"; MUTAGEN 1952; /note="S->A: No effect on interaction with BRCA1."; /evidence="ECO:0000269|PubMed:16698035"; MUTAGEN 2211; /note="S->A: No effect on interaction with BRCA1."; /evidence="ECO:0000269|PubMed:16698035
uniprot
proteins
pathway_participation
PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. {ECO:0000305|PubMed:20457939, ECO:0000305|PubMed:20952656}.
uniprot
proteins
post_translational_modification
PTM: Phosphorylation on Ser-1263 is required for interaction with BRCA1. {ECO:0000269|PubMed:16698035, ECO:0000269|Ref.9}.; PTM: Phosphorylation at Ser-80 by AMPK inactivates enzyme activity. {ECO:0000250|UniProtKB:P11497}.; PTM: The biotin cofactor is covalently attached to the central biotinyl-binding domain and is required for the catalytic activity. {ECO:0000269|PubMed:29899443}.
uniprot
proteins
pubmed
12360400
uniprot
proteins
pubmed
12810950
uniprot
proteins
pubmed
14643797
uniprot
proteins
pubmed
15333468
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15607423
uniprot
proteins
pubmed
16326698
uniprot
proteins
pubmed
16698035
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18452305
uniprot
proteins
pubmed
18487259
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20457939
uniprot
proteins
pubmed
20952656
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
29899443
uniprot
proteins
pubmed
6114432
uniprot
proteins
pubmed
7732023
uniprot
proteins
sequence_length
2346
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q5SWU9}.
uniprot
proteins