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Protein

Acetyl-CoA carboxylase 1

Gene

ACACA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the rate-limiting reaction in the biogenesis of long-chain fatty acids. Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase.1 Publication

Catalytic activityi

ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.1 Publication
ATP + [biotin carboxyl-carrier protein]-biotin-N6-L-lysine + hydrogencarbonate- = ADP + phosphate + [biotin carboxyl-carrier protein]-carboxybiotin-N6-L-lysine.1 Publication

Cofactori

Protein has several cofactor binding sites:
  • biotin
  • Mn2+Note: Binds 2 manganese ions per subunit.

Activity regulationi

By phosphorylation (By similarity). Activity is increased by oligomerization. Citrate and MID1IP1 promote oligomerization.By similarity1 Publication

Pathwayi: malonyl-CoA biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes malonyl-CoA from acetyl-CoA.
Proteins known to be involved in this subpathway in this organism are:
  1. Acetyl-CoA carboxylase 2 (ACACB), Acetyl-CoA carboxylase 1 (ACACA)
This subpathway is part of the pathway malonyl-CoA biosynthesis, which is itself part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes malonyl-CoA from acetyl-CoA, the pathway malonyl-CoA biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi424Manganese 1By similarity1
Metal bindingi437Manganese 1By similarity1
Metal bindingi437Manganese 2By similarity1
Metal bindingi439Manganese 2By similarity1
Active sitei441By similarity1
Binding sitei1823Coenzyme ABy similarity1
Binding sitei2127Coenzyme ABy similarity1
Binding sitei2129Coenzyme ABy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi315 – 320ATPPROSITE-ProRule annotation6

GO - Molecular functioni

  • acetyl-CoA carboxylase activity Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • biotin carboxylase activity Source: UniProtKB-EC
  • identical protein binding Source: IntAct
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

Keywordsi

Molecular functionAllosteric enzyme, Ligase, Multifunctional enzyme
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
LigandATP-binding, Biotin, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS05598-MONOMER
BRENDAi6.4.1.2 2681
ReactomeiR-HSA-163765 ChREBP activates metabolic gene expression
R-HSA-196780 Biotin transport and metabolism
R-HSA-200425 Import of palmitoyl-CoA into the mitochondrial matrix
R-HSA-2426168 Activation of gene expression by SREBF (SREBP)
R-HSA-3371599 Defective HLCS causes multiple carboxylase deficiency
R-HSA-75105 Fatty acyl-CoA biosynthesis
SABIO-RKiQ13085
SIGNORiQ13085
UniPathwayi
UPA00655;UER00711

Chemistry databases

SwissLipidsiSLP:000000729

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-CoA carboxylase 1 (EC:6.4.1.21 Publication)
Short name:
ACC1
Alternative name(s):
ACC-alpha
Including the following 1 domains:
Biotin carboxylase (EC:6.3.4.141 Publication)
Gene namesi
Name:ACACA
Synonyms:ACAC, ACC1, ACCA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

EuPathDBiHostDB:ENSG00000278540.4
HGNCiHGNC:84 ACACA
MIMi200350 gene
neXtProtiNX_Q13085

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

Pathology & Biotechi

Involvement in diseasei

Acetyl-CoA carboxylase 1 deficiency (ACACAD)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn inborn error of de novo fatty acid synthesis associated with severe brain damage, persistent myopathy and poor growth.
See also OMIM:613933

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi78S → A: No effect on interaction with BRCA1. 1 Publication1
Mutagenesisi344S → A: No effect on interaction with BRCA1. 1 Publication1
Mutagenesisi432S → A: No effect on interaction with BRCA1. 1 Publication1
Mutagenesisi1201S → A: No effect on interaction with BRCA1. 1 Publication1
Mutagenesisi1263S → A: Abolishes interaction with BRCA1. 1 Publication1
Mutagenesisi1585S → A: No effect on interaction with BRCA1. 1 Publication1
Mutagenesisi1952S → A: No effect on interaction with BRCA1. 1 Publication1
Mutagenesisi2211S → A: No effect on interaction with BRCA1. 1 Publication1

Organism-specific databases

DisGeNETi31
MalaCardsiACACA
MIMi613933 phenotype
OpenTargetsiENSG00000278540
PharmGKBiPA24421

Chemistry databases

ChEMBLiCHEMBL3351
DrugBankiDB00121 Biotin
GuidetoPHARMACOLOGYi1263

Polymorphism and mutation databases

BioMutaiACACA
DMDMi118601083

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001467641 – 2346Acetyl-CoA carboxylase 1Add BLAST2346

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1 Publication1
Modified residuei5PhosphoserineCombined sources1
Modified residuei23PhosphoserineCombined sources1
Modified residuei25PhosphoserineCombined sources1
Modified residuei29PhosphoserineCombined sources1
Modified residuei34PhosphoserineBy similarity1
Modified residuei48PhosphoserineCombined sources1
Modified residuei50PhosphoserineBy similarity1
Modified residuei53PhosphoserineCombined sources1
Modified residuei58PhosphothreonineBy similarity1
Modified residuei78PhosphoserineBy similarity1
Modified residuei80PhosphoserineCombined sources1 Publication1
Modified residuei488PhosphoserineCombined sources1
Modified residuei610PhosphothreonineCombined sources1
Modified residuei786N6-biotinyllysinePROSITE-ProRule annotationBy similarity1
Modified residuei835PhosphoserineCombined sources1
Modified residuei1201PhosphoserineBy similarity1
Modified residuei1216PhosphoserineBy similarity1
Modified residuei1218PhosphoserineBy similarity1
Modified residuei1227PhosphothreonineBy similarity1
Modified residuei1259PhosphoserineBy similarity1
Modified residuei1263Phosphoserine1 Publication1
Modified residuei1273PhosphoserineCombined sources1
Modified residuei1334N6-acetyllysineCombined sources1
Modified residuei2153PhosphothreonineCombined sources1

Post-translational modificationi

Phosphorylation on Ser-1263 is required for interaction with BRCA1.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ13085
MaxQBiQ13085
PaxDbiQ13085
PeptideAtlasiQ13085
PRIDEiQ13085
ProteomicsDBi59139
59140 [Q13085-2]
59141 [Q13085-3]
59142 [Q13085-4]

PTM databases

iPTMnetiQ13085
PhosphoSitePlusiQ13085
SwissPalmiQ13085

Expressioni

Tissue specificityi

Expressed in brain, placental, skeletal muscle, renal, pancreatic and adipose tissues; expressed at low level in pulmonary tissue; not detected in the liver.

Gene expression databases

BgeeiENSG00000278540 Expressed in 219 organ(s), highest expression level in adrenal tissue
ExpressionAtlasiQ13085 baseline and differential
GenevisibleiQ13085 HS

Organism-specific databases

HPAiCAB013715
HPA036650
HPA063018

Interactioni

Subunit structurei

Monomer, homodimer, and homotetramer. Can form filamentous polymers. Interacts in its inactive phosphorylated form with the BRCT domains of BRCA1 which prevents ACACA dephosphorylation and inhibits lipid synthesis. Interacts with MID1IP1; interaction with MID1IP1 promotes oligomerization and increases its activity.3 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi106549, 82 interactors
DIPiDIP-36122N
ELMiQ13085
IntActiQ13085, 37 interactors
MINTiQ13085
STRINGi9606.ENSP00000344789

Chemistry databases

BindingDBiQ13085

Structurei

Secondary structure

12346
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ13085
SMRiQ13085
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13085

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini117 – 618Biotin carboxylationAdd BLAST502
Domaini275 – 466ATP-graspPROSITE-ProRule annotationAdd BLAST192
Domaini745 – 819Biotinyl-bindingPROSITE-ProRule annotationAdd BLAST75
Domaini1576 – 1914CoA carboxyltransferase N-terminalPROSITE-ProRule annotationAdd BLAST339
Domaini1918 – 2234CoA carboxyltransferase C-terminalPROSITE-ProRule annotationAdd BLAST317

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1576 – 2234CarboxyltransferasePROSITE-ProRule annotationAdd BLAST659

Phylogenomic databases

eggNOGiKOG0368 Eukaryota
COG0439 LUCA
COG0511 LUCA
COG4799 LUCA
GeneTreeiENSGT00550000074703
HOVERGENiHBG005371
InParanoidiQ13085
KOiK11262
OMAiIPTLNRM
OrthoDBiEOG091G02ND
PhylomeDBiQ13085
TreeFamiTF300061

Family and domain databases

Gene3Di3.30.1490.20, 1 hit
InterProiView protein in InterPro
IPR034733 AcCoA_carboxyl
IPR013537 AcCoA_COase_cen
IPR011761 ATP-grasp
IPR013815 ATP_grasp_subdomain_1
IPR005481 BC-like_N
IPR001882 Biotin_BS
IPR011764 Biotin_carboxylation_dom
IPR005482 Biotin_COase_C
IPR000089 Biotin_lipoyl
IPR005479 CbamoylP_synth_lsu-like_ATP-bd
IPR029045 ClpP/crotonase-like_dom_sf
IPR011763 COA_CT_C
IPR011762 COA_CT_N
IPR016185 PreATP-grasp_dom_sf
IPR011054 Rudment_hybrid_motif
IPR011053 Single_hybrid_motif
PfamiView protein in Pfam
PF08326 ACC_central, 1 hit
PF02785 Biotin_carb_C, 1 hit
PF00289 Biotin_carb_N, 1 hit
PF00364 Biotin_lipoyl, 1 hit
PF01039 Carboxyl_trans, 1 hit
PF02786 CPSase_L_D2, 1 hit
SMARTiView protein in SMART
SM00878 Biotin_carb_C, 1 hit
SUPFAMiSSF51230 SSF51230, 1 hit
SSF51246 SSF51246, 1 hit
SSF52096 SSF52096, 2 hits
SSF52440 SSF52440, 1 hit
PROSITEiView protein in PROSITE
PS50975 ATP_GRASP, 1 hit
PS50979 BC, 1 hit
PS00188 BIOTIN, 1 hit
PS50968 BIOTINYL_LIPOYL, 1 hit
PS50989 COA_CT_CTER, 1 hit
PS50980 COA_CT_NTER, 1 hit
PS00866 CPSASE_1, 1 hit
PS00867 CPSASE_2, 1 hit

Sequences (4+)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative promoter usage. AlignAdd to basket

This entry has 4 described isoforms and 9 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q13085-1) [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
MDEPSPLAQP LELNQHSRFI IGSVSEDNSE DEISNLVKLD LLEEKEGSLS
60 70 80 90 100
PASVGSDTLS DLGISSLQDG LALHIRSSMS GLHLVKQGRD RKKIDSQRDF
110 120 130 140 150
TVASPAEFVT RFGGNKVIEK VLIANNGIAA VKCMRSIRRW SYEMFRNERA
160 170 180 190 200
IRFVVMVTPE DLKANAEYIK MADHYVPVPG GPNNNNYANV ELILDIAKRI
210 220 230 240 250
PVQAVWAGWG HASENPKLPE LLLKNGIAFM GPPSQAMWAL GDKIASSIVA
260 270 280 290 300
QTAGIPTLPW SGSGLRVDWQ ENDFSKRILN VPQELYEKGY VKDVDDGLQA
310 320 330 340 350
AEEVGYPVMI KASEGGGGKG IRKVNNADDF PNLFRQVQAE VPGSPIFVMR
360 370 380 390 400
LAKQSRHLEV QILADQYGNA ISLFGRDCSV QRRHQKIIEE APATIATPAV
410 420 430 440 450
FEHMEQCAVK LAKMVGYVSA GTVEYLYSQD GSFYFLELNP RLQVEHPCTE
460 470 480 490 500
MVADVNLPAA QLQIAMGIPL YRIKDIRMMY GVSPWGDSPI DFEDSAHVPC
510 520 530 540 550
PRGHVIAARI TSENPDEGFK PSSGTVQELN FRSNKNVWGY FSVAAAGGLH
560 570 580 590 600
EFADSQFGHC FSWGENREEA ISNMVVALKE LSIRGDFRTT VEYLIKLLET
610 620 630 640 650
ESFQMNRIDT GWLDRLIAEK VQAERPDTML GVVCGALHVA DVSLRNSVSN
660 670 680 690 700
FLHSLERGQV LPAHTLLNTV DVELIYEGVK YVLKVTRQSP NSYVVIMNGS
710 720 730 740 750
CVEVDVHRLS DGGLLLSYDG SSYTTYMKEE VDRYRITIGN KTCVFEKEND
760 770 780 790 800
PSVMRSPSAG KLIQYIVEDG GHVFAGQCYA EIEVMKMVMT LTAVESGCIH
810 820 830 840 850
YVKRPGAALD PGCVLAKMQL DNPSKVQQAE LHTGSLPRIQ STALRGEKLH
860 870 880 890 900
RVFHYVLDNL VNVMNGYCLP DPFFSSKVKD WVERLMKTLR DPSLPLLELQ
910 920 930 940 950
DIMTSVSGRI PPNVEKSIKK EMAQYASNIT SVLCQFPSQQ IANILDSHAA
960 970 980 990 1000
TLNRKSEREV FFMNTQSIVQ LVQRYRSGIR GHMKAVVMDL LRQYLRVETQ
1010 1020 1030 1040 1050
FQNGHYDKCV FALREENKSD MNTVLNYIFS HAQVTKKNLL VTMLIDQLCG
1060 1070 1080 1090 1100
RDPTLTDELL NILTELTQLS KTTNAKVALR ARQVLIASHL PSYELRHNQV
1110 1120 1130 1140 1150
ESIFLSAIDM YGHQFCIENL QKLILSETSI FDVLPNFFYH SNQVVRMAAL
1160 1170 1180 1190 1200
EVYVRRAYIA YELNSVQHRQ LKDNTCVVEF QFMLPTSHPN RGNIPTLNRM
1210 1220 1230 1240 1250
SFSSNLNHYG MTHVASVSDV LLDNSFTPPC QRMGGMVSFR TFEDFVRIFD
1260 1270 1280 1290 1300
EVMGCFSDSP PQSPTFPEAG HTSLYDEDKV PRDEPIHILN VAIKTDCDIE
1310 1320 1330 1340 1350
DDRLAAMFRE FTQQNKATLV DHGIRRLTFL VAQKDFRKQV NYEVDRRFHR
1360 1370 1380 1390 1400
EFPKFFTFRA RDKFEEDRIY RHLEPALAFQ LELNRMRNFD LTAIPCANHK
1410 1420 1430 1440 1450
MHLYLGAAKV EVGTEVTDYR FFVRAIIRHS DLVTKEASFE YLQNEGERLL
1460 1470 1480 1490 1500
LEAMDELEVA FNNTNVRTDC NHIFLNFVPT VIMDPSKIEE SVRSMVMRYG
1510 1520 1530 1540 1550
SRLWKLRVLQ AELKINIRLT PTGKAIPIRL FLTNESGYYL DISLYKEVTD
1560 1570 1580 1590 1600
SRTAQIMFQA YGDKQGPLHG MLINTPYVTK DLLQSKRFQA QSLGTTYIYD
1610 1620 1630 1640 1650
IPEMFRQSLI KLWESMSTQA FLPSPPLPSD MLTYTELVLD DQGQLVHMNR
1660 1670 1680 1690 1700
LPGGNEIGMV AWKMTFKSPE YPEGRDIIVI GNDITYRIGS FGPQEDLLFL
1710 1720 1730 1740 1750
RASELARAEG IPRIYVSANS GARIGLAEEI RHMFHVAWVD PEDPYKGYRY
1760 1770 1780 1790 1800
LYLTPQDYKR VSALNSVHCE HVEDEGESRY KITDIIGKEE GIGPENLRGS
1810 1820 1830 1840 1850
GMIAGESSLA YNEIITISLV TCRAIGIGAY LVRLGQRTIQ VENSHLILTG
1860 1870 1880 1890 1900
AGALNKVLGR EVYTSNNQLG GIQIMHNNGV THCTVCDDFE GVFTVLHWLS
1910 1920 1930 1940 1950
YMPKSVHSSV PLLNSKDPID RIIEFVPTKT PYDPRWMLAG RPHPTQKGQW
1960 1970 1980 1990 2000
LSGFFDYGSF SEIMQPWAQT VVVGRARLGG IPVGVVAVET RTVELSIPAD
2010 2020 2030 2040 2050
PANLDSEAKI IQQAGQVWFP DSAFKTYQAI KDFNREGLPL MVFANWRGFS
2060 2070 2080 2090 2100
GGMKDMYDQV LKFGAYIVDG LRECCQPVLV YIPPQAELRG GSWVVIDSSI
2110 2120 2130 2140 2150
NPRHMEMYAD RESRGSVLEP EGTVEIKFRR KDLVKTMRRV DPVYIHLAER
2160 2170 2180 2190 2200
LGTPELSTAE RKELENKLKE REEFLIPIYH QVAVQFADLH DTPGRMQEKG
2210 2220 2230 2240 2250
VISDILDWKT SRTFFYWRLR RLLLEDLVKK KIHNANPELT DGQIQAMLRR
2260 2270 2280 2290 2300
WFVEVEGTVK AYVWDNNKDL AEWLEKQLTE EDGVHSVIEE NIKCISRDYV
2310 2320 2330 2340
LKQIRSLVQA NPEVAMDSII HMTQHISPTQ RAEVIRILST MDSPST
Length:2,346
Mass (Da):265,554
Last modified:October 31, 2006 - v2
Checksum:iF1F0A518F8824FFC
GO
Isoform 2 (identifier: Q13085-2) [UniParc]FASTAAdd to basket
Also known as: E5A

The sequence of this isoform differs from the canonical sequence as follows:
     1-75: MDEPSPLAQP...SLQDGLALHI → MEGSPEENKEMRYYMLQ

Show »
Length:2,288
Mass (Da):259,686
Checksum:i4E2C75958216CC8B
GO
Isoform 3 (identifier: Q13085-3) [UniParc]FASTAAdd to basket
Also known as: E5B

The sequence of this isoform differs from the canonical sequence as follows:
     1-78: Missing.

Show »
Length:2,268
Mass (Da):257,239
Checksum:iC78033F62C492D3E
GO
Isoform 4 (identifier: Q13085-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MWWSTLMSILRARSFWKWISTQTVRIIRAVRAHFGGIM

Show »
Length:2,383
Mass (Da):269,999
Checksum:i1F2B8F96208B9983
GO

Computationally mapped potential isoform sequencesi

There are 9 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A087X126A0A087X126_HUMAN
Acetyl-CoA carboxylase 1
ACACA
112Annotation score:
A0A0C4DGT1A0A0C4DGT1_HUMAN
Acetyl-CoA carboxylase 1
ACACA
120Annotation score:
Q59FY4Q59FY4_HUMAN
Acetyl-CoA carboxylase 1
ACACA
998Annotation score:
A0A087X0W4A0A087X0W4_HUMAN
Acetyl-CoA carboxylase 1
ACACA
94Annotation score:
A0A087WWN5A0A087WWN5_HUMAN
Acetyl-CoA carboxylase 1
ACACA
52Annotation score:
A0A087WVR6A0A087WVR6_HUMAN
Acetyl-CoA carboxylase 1
ACACA
42Annotation score:
A0A087WYK6A0A087WYK6_HUMAN
Acetyl-CoA carboxylase 1
ACACA
114Annotation score:
A0A087WYS8A0A087WYS8_HUMAN
Acetyl-CoA carboxylase 1
ACACA
96Annotation score:
A0A087X2F8A0A087X2F8_HUMAN
Acetyl-CoA carboxylase 1
ACACA
84Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti66S → A in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti79M → W in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti89R → G in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti182P → A in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti234S → N in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti299Q → K in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti303E → K in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti364A → V in AAP94122 (PubMed:12810950).Curated1
Sequence conflicti446H → Q in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti494D → N in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti554D → G in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti622Q → R in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti640A → G in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti814V → I in AAP94122 (PubMed:12810950).Curated1
Sequence conflicti1061N → S in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti1094 – 1095EL → DV in AAC50139 (PubMed:7732023).Curated2
Sequence conflicti1225S → A in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti1257S → C in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti1297C → G in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti1320V → A in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti1444N → S in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti1474F → L in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti1665 – 1666TF → SL in AAC50139 (PubMed:7732023).Curated2
Sequence conflicti1677I → V in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti1741P → S in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti1762S → G in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti1822C → S in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti1875M → T in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti1888D → G in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti1997I → V in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti2013Q → H in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti2058D → H in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti2075C → S in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti2098 – 2099SS → PT in AAC50139 (PubMed:7732023).Curated2
Sequence conflicti2158 – 2159TA → PT in AAC50139 (PubMed:7732023).Curated2
Sequence conflicti2166N → S in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti2234N → S in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti2321H → R in AAP94122 (PubMed:12810950).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_042941838R → W. Corresponds to variant dbSNP:rs2287351Ensembl.1
Natural variantiVAR_0365141687R → Q in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_0289292271A → V Rare polymorphism; frequency <0.004; may play a role in breast cancer susceptibility. 1 PublicationCorresponds to variant dbSNP:rs146351326Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0260981 – 78Missing in isoform 3. 2 PublicationsAdd BLAST78
Alternative sequenceiVSP_0260991 – 75MDEPS…LALHI → MEGSPEENKEMRYYMLQ in isoform 2. 2 PublicationsAdd BLAST75
Alternative sequenceiVSP_0261001M → MWWSTLMSILRARSFWKWIS TQTVRIIRAVRAHFGGIM in isoform 4. 2 Publications1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19822 mRNA Translation: AAC50139.1
AY315619 mRNA Translation: AAP94114.1
AY315620 mRNA Translation: AAP94115.1
AY315621 mRNA Translation: AAP94116.1
AY315623 mRNA Translation: AAP94118.1
AY315627 mRNA Translation: AAP94122.1
AY237919 mRNA Translation: AAP69841.1
BC137287 mRNA Translation: AAI37288.1
AJ534888 mRNA Translation: CAD59556.1
AJ534889 mRNA Translation: CAD59557.1
AJ564444 mRNA Translation: CAD92089.1
CCDSiCCDS11317.1 [Q13085-1]
CCDS11318.1 [Q13085-2]
CCDS42302.1 [Q13085-4]
CCDS42303.1 [Q13085-3]
PIRiI38928
RefSeqiNP_942131.1, NM_198834.2 [Q13085-4]
NP_942133.1, NM_198836.2 [Q13085-1]
NP_942134.1, NM_198837.1 [Q13085-2]
NP_942135.1, NM_198838.1 [Q13085-3]
NP_942136.1, NM_198839.2 [Q13085-1]
XP_011523005.1, XM_011524703.1 [Q13085-1]
XP_016880044.1, XM_017024555.1 [Q13085-1]
UniGeneiHs.160556

Genome annotation databases

EnsembliENST00000611803; ENSP00000479901; ENSG00000275176 [Q13085-2]
ENST00000612895; ENSP00000482269; ENSG00000278540 [Q13085-2]
ENST00000613687; ENSP00000483674; ENSG00000275176 [Q13085-1]
ENST00000614428; ENSP00000478547; ENSG00000278540 [Q13085-1]
ENST00000616317; ENSP00000483300; ENSG00000278540 [Q13085-4]
ENST00000617649; ENSP00000482368; ENSG00000278540 [Q13085-3]
ENST00000619487; ENSP00000478577; ENSG00000275176 [Q13085-4]
ENST00000621312; ENSP00000480031; ENSG00000275176 [Q13085-3]
GeneIDi31
KEGGihsa:31
UCSCiuc002hnk.4 human [Q13085-1]

Keywords - Coding sequence diversityi

Alternative promoter usage, Polymorphism

Similar proteinsi

Cross-referencesi

Web resourcesi

Wikipedia

Acetyl-CoA carboxylase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19822 mRNA Translation: AAC50139.1
AY315619 mRNA Translation: AAP94114.1
AY315620 mRNA Translation: AAP94115.1
AY315621 mRNA Translation: AAP94116.1
AY315623 mRNA Translation: AAP94118.1
AY315627 mRNA Translation: AAP94122.1
AY237919 mRNA Translation: AAP69841.1
BC137287 mRNA Translation: AAI37288.1
AJ534888 mRNA Translation: CAD59556.1
AJ534889 mRNA Translation: CAD59557.1
AJ564444 mRNA Translation: CAD92089.1
CCDSiCCDS11317.1 [Q13085-1]
CCDS11318.1 [Q13085-2]
CCDS42302.1 [Q13085-4]
CCDS42303.1 [Q13085-3]
PIRiI38928
RefSeqiNP_942131.1, NM_198834.2 [Q13085-4]
NP_942133.1, NM_198836.2 [Q13085-1]
NP_942134.1, NM_198837.1 [Q13085-2]
NP_942135.1, NM_198838.1 [Q13085-3]
NP_942136.1, NM_198839.2 [Q13085-1]
XP_011523005.1, XM_011524703.1 [Q13085-1]
XP_016880044.1, XM_017024555.1 [Q13085-1]
UniGeneiHs.160556

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2YL2X-ray2.30A/B78-617[»]
3COJX-ray3.21H/I/J/K/L/M/N/O1258-1270[»]
4ASIX-ray2.80A/B/C/D/E/F1571-2338[»]
6G2Delectron microscopy5.40B/C/D/F1-2346[»]
6G2Helectron microscopy4.60A/B/C/D/E/F1-2346[»]
6G2Ielectron microscopy5.90A/B/C/D/E/F/G/J/Q/R1-2346[»]
ProteinModelPortaliQ13085
SMRiQ13085
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106549, 82 interactors
DIPiDIP-36122N
ELMiQ13085
IntActiQ13085, 37 interactors
MINTiQ13085
STRINGi9606.ENSP00000344789

Chemistry databases

BindingDBiQ13085
ChEMBLiCHEMBL3351
DrugBankiDB00121 Biotin
GuidetoPHARMACOLOGYi1263
SwissLipidsiSLP:000000729

PTM databases

iPTMnetiQ13085
PhosphoSitePlusiQ13085
SwissPalmiQ13085

Polymorphism and mutation databases

BioMutaiACACA
DMDMi118601083

Proteomic databases

EPDiQ13085
MaxQBiQ13085
PaxDbiQ13085
PeptideAtlasiQ13085
PRIDEiQ13085
ProteomicsDBi59139
59140 [Q13085-2]
59141 [Q13085-3]
59142 [Q13085-4]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000611803; ENSP00000479901; ENSG00000275176 [Q13085-2]
ENST00000612895; ENSP00000482269; ENSG00000278540 [Q13085-2]
ENST00000613687; ENSP00000483674; ENSG00000275176 [Q13085-1]
ENST00000614428; ENSP00000478547; ENSG00000278540 [Q13085-1]
ENST00000616317; ENSP00000483300; ENSG00000278540 [Q13085-4]
ENST00000617649; ENSP00000482368; ENSG00000278540 [Q13085-3]
ENST00000619487; ENSP00000478577; ENSG00000275176 [Q13085-4]
ENST00000621312; ENSP00000480031; ENSG00000275176 [Q13085-3]
GeneIDi31
KEGGihsa:31
UCSCiuc002hnk.4 human [Q13085-1]

Organism-specific databases

CTDi31
DisGeNETi31
EuPathDBiHostDB:ENSG00000278540.4
GeneCardsiACACA
HGNCiHGNC:84 ACACA
HPAiCAB013715
HPA036650
HPA063018
MalaCardsiACACA
MIMi200350 gene
613933 phenotype
neXtProtiNX_Q13085
OpenTargetsiENSG00000278540
PharmGKBiPA24421
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0368 Eukaryota
COG0439 LUCA
COG0511 LUCA
COG4799 LUCA
GeneTreeiENSGT00550000074703
HOVERGENiHBG005371
InParanoidiQ13085
KOiK11262
OMAiIPTLNRM
OrthoDBiEOG091G02ND
PhylomeDBiQ13085
TreeFamiTF300061

Enzyme and pathway databases

UniPathwayi
UPA00655;UER00711

BioCyciMetaCyc:HS05598-MONOMER
BRENDAi6.4.1.2 2681
ReactomeiR-HSA-163765 ChREBP activates metabolic gene expression
R-HSA-196780 Biotin transport and metabolism
R-HSA-200425 Import of palmitoyl-CoA into the mitochondrial matrix
R-HSA-2426168 Activation of gene expression by SREBF (SREBP)
R-HSA-3371599 Defective HLCS causes multiple carboxylase deficiency
R-HSA-75105 Fatty acyl-CoA biosynthesis
SABIO-RKiQ13085
SIGNORiQ13085

Miscellaneous databases

ChiTaRSiACACA human
EvolutionaryTraceiQ13085
GeneWikiiACACA
GenomeRNAii31
PROiPR:Q13085
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000278540 Expressed in 219 organ(s), highest expression level in adrenal tissue
ExpressionAtlasiQ13085 baseline and differential
GenevisibleiQ13085 HS

Family and domain databases

Gene3Di3.30.1490.20, 1 hit
InterProiView protein in InterPro
IPR034733 AcCoA_carboxyl
IPR013537 AcCoA_COase_cen
IPR011761 ATP-grasp
IPR013815 ATP_grasp_subdomain_1
IPR005481 BC-like_N
IPR001882 Biotin_BS
IPR011764 Biotin_carboxylation_dom
IPR005482 Biotin_COase_C
IPR000089 Biotin_lipoyl
IPR005479 CbamoylP_synth_lsu-like_ATP-bd
IPR029045 ClpP/crotonase-like_dom_sf
IPR011763 COA_CT_C
IPR011762 COA_CT_N
IPR016185 PreATP-grasp_dom_sf
IPR011054 Rudment_hybrid_motif
IPR011053 Single_hybrid_motif
PfamiView protein in Pfam
PF08326 ACC_central, 1 hit
PF02785 Biotin_carb_C, 1 hit
PF00289 Biotin_carb_N, 1 hit
PF00364 Biotin_lipoyl, 1 hit
PF01039 Carboxyl_trans, 1 hit
PF02786 CPSase_L_D2, 1 hit
SMARTiView protein in SMART
SM00878 Biotin_carb_C, 1 hit
SUPFAMiSSF51230 SSF51230, 1 hit
SSF51246 SSF51246, 1 hit
SSF52096 SSF52096, 2 hits
SSF52440 SSF52440, 1 hit
PROSITEiView protein in PROSITE
PS50975 ATP_GRASP, 1 hit
PS50979 BC, 1 hit
PS00188 BIOTIN, 1 hit
PS50968 BIOTINYL_LIPOYL, 1 hit
PS50989 COA_CT_CTER, 1 hit
PS50980 COA_CT_NTER, 1 hit
PS00866 CPSASE_1, 1 hit
PS00867 CPSASE_2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiACACA_HUMAN
AccessioniPrimary (citable) accession number: Q13085
Secondary accession number(s): B2RP68
, Q6KEV6, Q6XDA8, Q7Z2G8, Q7Z561, Q7Z563, Q7Z564, Q86WB2, Q86WB3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 31, 2006
Last modified: October 10, 2018
This is version 191 of the entry and version 2 of the sequence. See complete history.
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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