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Acetyl-CoA carboxylase 1 (ACC1) (EC 6.4.1.2) (ACC-alpha) [Includes: Biotin carboxylase (EC 6.3.4.14)]

 ACACA_HUMAN             Reviewed;        2346 AA.
Q13085; B2RP68; Q6KEV6; Q6XDA8; Q7Z2G8; Q7Z561; Q7Z563; Q7Z564;
Q86WB2; Q86WB3;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
31-OCT-2006, sequence version 2.
22-NOV-2017, entry version 183.
RecName: Full=Acetyl-CoA carboxylase 1;
Short=ACC1;
EC=6.4.1.2 {ECO:0000269|PubMed:20952656};
AltName: Full=ACC-alpha;
Includes:
RecName: Full=Biotin carboxylase;
EC=6.3.4.14 {ECO:0000269|PubMed:20952656};
Name=ACACA; Synonyms=ACAC, ACC1, ACCA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=7732023; DOI=10.1073/pnas.92.9.4011;
Abu-Elheiga L., Jayakumar A., Baldini A., Chirala S.S., Wakil S.J.;
"Human acetyl-CoA carboxylase: characterization, molecular cloning,
and evidence for two isoforms.";
Proc. Natl. Acad. Sci. U.S.A. 92:4011-4015(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF
1-366 (ISOFORMS 2 AND 3), AND NUCLEOTIDE SEQUENCE [MRNA] OF 1-120
(ISOFORM 4).
TISSUE=Adipocyte;
PubMed=12810950; DOI=10.1073/pnas.1332670100;
Mao J., Chirala S.S., Wakil S.J.;
"Human acetyl-CoA carboxylase 1 gene: presence of three promoters and
heterogeneity at the 5'-untranslated mRNA region.";
Proc. Natl. Acad. Sci. U.S.A. 100:7515-7520(2003).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT VAL-2271.
PubMed=15333468; DOI=10.1093/carcin/bgh273;
Sinilnikova O.M., Ginolhac S.M., Magnard C., Leone M., Anczukow O.,
Hughes D., Moreau K., Thompson D., Coutanson C., Hall J.,
Romestaing P., Gerard J.-P., Bonadona V., Lasset C., Goldgar D.E.,
Joulin V., Venezia N.D., Lenoir G.M.;
"Acetyl-CoA carboxylase alpha gene and breast cancer susceptibility.";
Carcinogenesis 25:2417-2424(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-113 (ISOFORM 2), AND NUCLEOTIDE
SEQUENCE [MRNA] OF 1-93 (ISOFORM 3).
TISSUE=Mammary gland, and Testis;
PubMed=14643797; DOI=10.1016/j.bbalip.2003.09.005;
Travers M.T., Vallance A.J., Clegg R.A., Thomson R., Price N.T.,
Barber M.C.;
"Characterisation of an N-terminal variant of acetyl-CoA carboxylase-
alpha: expression in human tissues and evolutionary aspects.";
Biochim. Biophys. Acta 1634:97-106(2003).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-47 (ISOFORM 1).
TISSUE=Testis;
PubMed=15607423; DOI=10.1016/j.ygeno.2004.10.001;
Travers M.T., Cambot M., Kennedy H.T., Lenoir G.M., Barber M.C.,
Joulin V.;
"Asymmetric expression of transcripts derived from the shared promoter
between the divergently oriented ACACA and TADA2L genes.";
Genomics 85:71-84(2005).
[7]
PROTEIN SEQUENCE OF 1-18; 39-45; 77-86; 99-111; 121-132; 153-170;
218-224; 267-276; 278-288; 323-335; 568-579; 589-615; 646-657;
748-755; 818-838; 985-992; 997-1008; 1083-1096; 1147-1169; 1192-1199;
1233-1247; 1283-1294; 1317-1325; 1327-1334; 1372-1385; 1401-1420;
1508-1514; 1553-1564; 1668-1687; 1714-1731; 1750-1759; 1782-1798;
1824-1833; 1838-1856; 1905-1916; 1922-1929; 1978-2009; 2063-2072;
2104-2111; 2115-2127; 2139-2161; 2200-2209; 2213-2218; 2221-2229 AND
2261-2293, ACETYLATION AT MET-1, PHOSPHORYLATION AT SER-80, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Hepatoma;
Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.;
Submitted (JUL-2007) to UniProtKB.
[8]
INTERACTION WITH BRCA1.
PubMed=12360400; DOI=10.1038/sj.onc.1205915;
Magnard C., Bachelier R., Vincent A., Jaquinod M., Kieffer S.,
Lenoir G.M., Venezia N.D.;
"BRCA1 interacts with acetyl-CoA carboxylase through its tandem of
BRCT domains.";
Oncogene 21:6729-6739(2002).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29 AND SER-53, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[10]
INTERACTION WITH BRCA1.
PubMed=16326698; DOI=10.1074/jbc.M504652200;
Moreau K., Dizin E., Ray H., Luquain C., Lefai E., Foufelle F.,
Billaud M., Lenoir G.M., Venezia N.D.;
"BRCA1 affects lipid synthesis through its interaction with acetyl-CoA
carboxylase.";
J. Biol. Chem. 281:3172-3181(2006).
[11]
PHOSPHORYLATION AT SER-1263, AND MUTAGENESIS OF SER-78; SER-344;
SER-432; SER-1201; SER-1263; SER-1585; SER-1952 AND SER-2211.
PubMed=16698035; DOI=10.1016/j.jmb.2006.04.010;
Ray H., Moreau K., Dizin E., Callebaut I., Venezia N.D.;
"ACCA phosphopeptide recognition by the BRCT repeats of BRCA1.";
J. Mol. Biol. 359:973-982(2006).
[12]
INVOLVEMENT IN ACACAD.
PubMed=6114432;
Blom W., de Muinck Keizer S.M.P.F., Scholte H.R.;
"Acetyl-CoA carboxylase deficiency: an inborn error of de novo fatty
acid synthesis.";
N. Engl. J. Med. 305:465-466(1981).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-25; SER-29 AND
SER-80, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-5 AND SER-29, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-25 AND SER-29,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[19]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1334, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[20]
FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, ENZYME REGULATION, AND
INTERACTION WITH MID1IP1.
PubMed=20952656; DOI=10.1073/pnas.1012736107;
Colbert C.L., Kim C.W., Moon Y.A., Henry L., Palnitkar M.,
McKean W.B., Fitzgerald K., Deisenhofer J., Horton J.D., Kwon H.J.;
"Crystal structure of Spot 14, a modulator of fatty acid synthesis.";
Proc. Natl. Acad. Sci. U.S.A. 107:18820-18825(2010).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-5; SER-23; SER-29; SER-48 AND SER-80, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29 AND SER-80, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-25; SER-29;
SER-80; THR-610; SER-835 AND THR-2153, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-29 AND SER-1273,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[26]
VARIANT [LARGE SCALE ANALYSIS] GLN-1687.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: 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. {ECO:0000269|PubMed:20952656}.
-!- CATALYTIC ACTIVITY: ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate
+ malonyl-CoA. {ECO:0000269|PubMed:20952656}.
-!- CATALYTIC ACTIVITY: ATP + biotin-[carboxyl-carrier-protein] +
HCO(3)(-) = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-
protein]. {ECO:0000269|PubMed:20952656}.
-!- COFACTOR:
Name=biotin; Xref=ChEBI:CHEBI:57586;
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Note=Binds 2 manganese ions per subunit.;
-!- ENZYME REGULATION: By phosphorylation (By similarity). Activity is
increased by oligomerization. Citrate and MID1IP1 promote
oligomerization. {ECO:0000250, ECO:0000269|PubMed:20952656}.
-!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA
from acetyl-CoA: step 1/1.
-!- SUBUNIT: 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. {ECO:0000269|PubMed:12360400,
ECO:0000269|PubMed:16326698, ECO:0000269|PubMed:20952656}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-717681, EBI-717681;
O60218:AKR1B10; NbExp=4; IntAct=EBI-717681, EBI-1572139;
P38398:BRCA1; NbExp=2; IntAct=EBI-717681, EBI-349905;
Q9CQ20:Mid1ip1 (xeno); NbExp=4; IntAct=EBI-717681, EBI-473024;
Q96EB6:SIRT1; NbExp=3; IntAct=EBI-717681, EBI-1802965;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage; Named isoforms=4;
Name=1;
IsoId=Q13085-1; Sequence=Displayed;
Name=2; Synonyms=E5A;
IsoId=Q13085-2; Sequence=VSP_026099;
Name=3; Synonyms=E5B;
IsoId=Q13085-3; Sequence=VSP_026098;
Name=4;
IsoId=Q13085-4; Sequence=VSP_026100;
-!- TISSUE SPECIFICITY: Expressed in brain, placental, skeletal
muscle, renal, pancreatic and adipose tissues; expressed at low
level in pulmonary tissue; not detected in the liver.
-!- PTM: Phosphorylation on Ser-1263 is required for interaction with
BRCA1. {ECO:0000269|PubMed:16698035, ECO:0000269|Ref.7}.
-!- DISEASE: Acetyl-CoA carboxylase 1 deficiency (ACACAD)
[MIM:613933]: An 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 mutations affecting the gene represented in this entry.
-!- WEB RESOURCE: Name=Wikipedia; Note=Acetyl-CoA carboxylase entry;
URL="https://en.wikipedia.org/wiki/Acetyl-CoA_carboxylase";
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EMBL; U19822; AAC50139.1; -; mRNA.
EMBL; AY315619; AAP94114.1; -; mRNA.
EMBL; AY315620; AAP94115.1; -; mRNA.
EMBL; AY315621; AAP94116.1; -; mRNA.
EMBL; AY315623; AAP94118.1; -; mRNA.
EMBL; AY315627; AAP94122.1; -; mRNA.
EMBL; AY237919; AAP69841.1; -; mRNA.
EMBL; BC137287; AAI37288.1; -; mRNA.
EMBL; AJ534888; CAD59556.1; -; mRNA.
EMBL; AJ534889; CAD59557.1; -; mRNA.
EMBL; AJ564444; CAD92089.1; -; mRNA.
CCDS; CCDS11317.1; -. [Q13085-1]
CCDS; CCDS11318.1; -. [Q13085-2]
CCDS; CCDS42302.1; -. [Q13085-4]
CCDS; CCDS42303.1; -. [Q13085-3]
PIR; I38928; I38928.
RefSeq; NP_942131.1; NM_198834.2. [Q13085-4]
RefSeq; NP_942133.1; NM_198836.2. [Q13085-1]
RefSeq; NP_942134.1; NM_198837.1. [Q13085-2]
RefSeq; NP_942135.1; NM_198838.1. [Q13085-3]
RefSeq; NP_942136.1; NM_198839.2. [Q13085-1]
RefSeq; XP_011523005.1; XM_011524703.1. [Q13085-1]
RefSeq; XP_016880044.1; XM_017024555.1. [Q13085-1]
UniGene; Hs.160556; -.
PDB; 2YL2; X-ray; 2.30 A; A/B=78-617.
PDB; 3COJ; X-ray; 3.21 A; H/I/J/K/L/M/N/O=1258-1270.
PDB; 4ASI; X-ray; 2.80 A; A/B/C/D/E/F=1571-2338.
PDBsum; 2YL2; -.
PDBsum; 3COJ; -.
PDBsum; 4ASI; -.
ProteinModelPortal; Q13085; -.
SMR; Q13085; -.
BioGrid; 106549; 80.
DIP; DIP-36122N; -.
ELM; Q13085; -.
IntAct; Q13085; 33.
MINT; MINT-1415014; -.
STRING; 9606.ENSP00000344789; -.
BindingDB; Q13085; -.
ChEMBL; CHEMBL3351; -.
DrugBank; DB00121; Biotin.
GuidetoPHARMACOLOGY; 1263; -.
SwissLipids; SLP:000000729; -.
iPTMnet; Q13085; -.
PhosphoSitePlus; Q13085; -.
SwissPalm; Q13085; -.
BioMuta; ACACA; -.
DMDM; 118601083; -.
EPD; Q13085; -.
MaxQB; Q13085; -.
PaxDb; Q13085; -.
PeptideAtlas; Q13085; -.
PRIDE; Q13085; -.
Ensembl; ENST00000611803; ENSP00000479901; ENSG00000275176. [Q13085-2]
Ensembl; ENST00000612895; ENSP00000482269; ENSG00000278540. [Q13085-2]
Ensembl; ENST00000613687; ENSP00000483674; ENSG00000275176. [Q13085-1]
Ensembl; ENST00000614428; ENSP00000478547; ENSG00000278540. [Q13085-1]
Ensembl; ENST00000616317; ENSP00000483300; ENSG00000278540. [Q13085-4]
Ensembl; ENST00000617649; ENSP00000482368; ENSG00000278540. [Q13085-3]
Ensembl; ENST00000619487; ENSP00000478577; ENSG00000275176. [Q13085-4]
Ensembl; ENST00000621312; ENSP00000480031; ENSG00000275176. [Q13085-3]
GeneID; 31; -.
KEGG; hsa:31; -.
UCSC; uc002hnk.4; human. [Q13085-1]
CTD; 31; -.
DisGeNET; 31; -.
EuPathDB; HostDB:ENSG00000278540.4; -.
GeneCards; ACACA; -.
HGNC; HGNC:84; ACACA.
HPA; CAB013715; -.
HPA; HPA036650; -.
HPA; HPA063018; -.
MalaCards; ACACA; -.
MIM; 200350; gene.
MIM; 613933; phenotype.
neXtProt; NX_Q13085; -.
OpenTargets; ENSG00000278540; -.
PharmGKB; PA24421; -.
eggNOG; KOG0368; Eukaryota.
eggNOG; COG0439; LUCA.
eggNOG; COG0511; LUCA.
eggNOG; COG4799; LUCA.
GeneTree; ENSGT00550000074703; -.
HOVERGEN; HBG005371; -.
InParanoid; Q13085; -.
KO; K11262; -.
OMA; FTPPCQR; -.
OrthoDB; EOG091G02ND; -.
PhylomeDB; Q13085; -.
TreeFam; TF300061; -.
BRENDA; 6.4.1.2; 2681.
Reactome; R-HSA-163765; ChREBP activates metabolic gene expression.
Reactome; R-HSA-196780; Biotin transport and metabolism.
Reactome; R-HSA-200425; Import of palmitoyl-CoA into the mitochondrial matrix.
Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP).
Reactome; R-HSA-3371599; Defective HLCS causes multiple carboxylase deficiency.
Reactome; R-HSA-75105; Fatty acyl-CoA biosynthesis.
SABIO-RK; Q13085; -.
SIGNOR; Q13085; -.
UniPathway; UPA00655; UER00711.
ChiTaRS; ACACA; human.
EvolutionaryTrace; Q13085; -.
GeneWiki; ACACA; -.
GenomeRNAi; 31; -.
PRO; PR:Q13085; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000278540; -.
ExpressionAtlas; Q13085; baseline and differential.
Genevisible; Q13085; HS.
GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0001650; C:fibrillar center; IDA:HPA.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0003989; F:acetyl-CoA carboxylase activity; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006084; P:acetyl-CoA metabolic process; ISS:UniProtKB.
GO; GO:0006768; P:biotin metabolic process; TAS:Reactome.
GO; GO:0006853; P:carnitine shuttle; TAS:Reactome.
GO; GO:0071380; P:cellular response to prostaglandin E stimulus; IEA:Ensembl.
GO; GO:0006633; P:fatty acid biosynthetic process; ISS:UniProtKB.
GO; GO:0046949; P:fatty-acyl-CoA biosynthetic process; TAS:Reactome.
GO; GO:0055088; P:lipid homeostasis; IEA:Ensembl.
GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0044268; P:multicellular organismal protein metabolic process; IEA:Ensembl.
GO; GO:0031325; P:positive regulation of cellular metabolic process; TAS:Reactome.
GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
GO; GO:0045540; P:regulation of cholesterol biosynthetic process; TAS:Reactome.
GO; GO:0001894; P:tissue homeostasis; IEA:Ensembl.
Gene3D; 3.30.1490.20; -; 1.
InterPro; IPR034733; AcCoA_carboxyl.
InterPro; IPR013537; AcCoA_COase_cen.
InterPro; IPR011761; ATP-grasp.
InterPro; IPR013815; ATP_grasp_subdomain_1.
InterPro; IPR005481; BC-like_N.
InterPro; IPR001882; Biotin_BS.
InterPro; IPR011764; Biotin_carboxylation_dom.
InterPro; IPR005482; Biotin_COase_C.
InterPro; IPR000089; Biotin_lipoyl.
InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
InterPro; IPR011763; COA_CT_C.
InterPro; IPR011762; COA_CT_N.
InterPro; IPR016185; PreATP-grasp_dom_sf.
InterPro; IPR011054; Rudment_hybrid_motif.
InterPro; IPR011053; Single_hybrid_motif.
Pfam; PF08326; ACC_central; 1.
Pfam; PF02785; Biotin_carb_C; 1.
Pfam; PF00289; Biotin_carb_N; 1.
Pfam; PF00364; Biotin_lipoyl; 1.
Pfam; PF01039; Carboxyl_trans; 1.
Pfam; PF02786; CPSase_L_D2; 1.
SMART; SM00878; Biotin_carb_C; 1.
SUPFAM; SSF51230; SSF51230; 1.
SUPFAM; SSF51246; SSF51246; 1.
SUPFAM; SSF52096; SSF52096; 2.
SUPFAM; SSF52440; SSF52440; 1.
PROSITE; PS50975; ATP_GRASP; 1.
PROSITE; PS50979; BC; 1.
PROSITE; PS00188; BIOTIN; 1.
PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
PROSITE; PS50989; COA_CT_CTER; 1.
PROSITE; PS50980; COA_CT_NTER; 1.
PROSITE; PS00866; CPSASE_1; 1.
PROSITE; PS00867; CPSASE_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Allosteric enzyme;
Alternative promoter usage; ATP-binding; Biotin; Complete proteome;
Cytoplasm; Direct protein sequencing; Fatty acid biosynthesis;
Fatty acid metabolism; Ligase; Lipid biosynthesis; Lipid metabolism;
Manganese; Metal-binding; Multifunctional enzyme; Nucleotide-binding;
Phosphoprotein; Polymorphism; Reference proteome.
CHAIN 1 2346 Acetyl-CoA carboxylase 1.
/FTId=PRO_0000146764.
DOMAIN 117 618 Biotin carboxylation.
DOMAIN 275 466 ATP-grasp. {ECO:0000255|PROSITE-
ProRule:PRU00409}.
DOMAIN 745 819 Biotinyl-binding. {ECO:0000255|PROSITE-
ProRule:PRU01066}.
DOMAIN 1576 1914 CoA carboxyltransferase N-terminal.
{ECO:0000255|PROSITE-ProRule:PRU01136}.
DOMAIN 1918 2234 CoA carboxyltransferase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU01137}.
NP_BIND 315 320 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00409}.
REGION 1576 2234 Carboxyltransferase.
{ECO:0000255|PROSITE-ProRule:PRU01138}.
ACT_SITE 441 441 {ECO:0000250}.
METAL 424 424 Manganese 1. {ECO:0000250}.
METAL 437 437 Manganese 1. {ECO:0000250}.
METAL 437 437 Manganese 2. {ECO:0000250}.
METAL 439 439 Manganese 2. {ECO:0000250}.
BINDING 1823 1823 Coenzyme A. {ECO:0000250}.
BINDING 2127 2127 Coenzyme A. {ECO:0000250}.
BINDING 2129 2129 Coenzyme A. {ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:20068231,
ECO:0000269|Ref.7}.
MOD_RES 5 5 Phosphoserine.
{ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 23 23 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231}.
MOD_RES 25 25 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 29 29 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 34 34 Phosphoserine.
{ECO:0000250|UniProtKB:P11497}.
MOD_RES 48 48 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 50 50 Phosphoserine.
{ECO:0000250|UniProtKB:P11497}.
MOD_RES 53 53 Phosphoserine.
{ECO:0000244|PubMed:17081983}.
MOD_RES 58 58 Phosphothreonine.
{ECO:0000250|UniProtKB:Q5SWU9}.
MOD_RES 78 78 Phosphoserine.
{ECO:0000250|UniProtKB:P11497}.
MOD_RES 80 80 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|Ref.7}.
MOD_RES 488 488 Phosphoserine.
{ECO:0000244|PubMed:18220336}.
MOD_RES 610 610 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 786 786 N6-biotinyllysine. {ECO:0000250,
ECO:0000255|PROSITE-ProRule:PRU01066}.
MOD_RES 835 835 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1201 1201 Phosphoserine.
{ECO:0000250|UniProtKB:P11497}.
MOD_RES 1216 1216 Phosphoserine.
{ECO:0000250|UniProtKB:P11497}.
MOD_RES 1218 1218 Phosphoserine.
{ECO:0000250|UniProtKB:Q5SWU9}.
MOD_RES 1227 1227 Phosphothreonine.
{ECO:0000250|UniProtKB:Q5SWU9}.
MOD_RES 1259 1259 Phosphoserine.
{ECO:0000250|UniProtKB:Q5SWU9}.
MOD_RES 1263 1263 Phosphoserine.
{ECO:0000269|PubMed:16698035}.
MOD_RES 1273 1273 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1334 1334 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 2153 2153 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 78 Missing (in isoform 3).
{ECO:0000303|PubMed:12810950,
ECO:0000303|PubMed:14643797}.
/FTId=VSP_026098.
VAR_SEQ 1 75 MDEPSPLAQPLELNQHSRFIIGSVSEDNSEDEISNLVKLDL
LEEKEGSLSPASVGSDTLSDLGISSLQDGLALHI -> MEG
SPEENKEMRYYMLQ (in isoform 2).
{ECO:0000303|PubMed:12810950,
ECO:0000303|PubMed:14643797}.
/FTId=VSP_026099.
VAR_SEQ 1 1 M -> MWWSTLMSILRARSFWKWISTQTVRIIRAVRAHFGG
IM (in isoform 4).
{ECO:0000303|PubMed:12810950,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_026100.
VARIANT 838 838 R -> W (in dbSNP:rs2287351).
/FTId=VAR_042941.
VARIANT 1687 1687 R -> Q (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036514.
VARIANT 2271 2271 A -> V (rare polymorphism; frequency
<0.004; may play a role in breast cancer
susceptibility; dbSNP:rs146351326).
{ECO:0000269|PubMed:15333468}.
/FTId=VAR_028929.
MUTAGEN 78 78 S->A: No effect on interaction with
BRCA1. {ECO:0000269|PubMed:16698035}.
MUTAGEN 344 344 S->A: No effect on interaction with
BRCA1. {ECO:0000269|PubMed:16698035}.
MUTAGEN 432 432 S->A: No effect on interaction with
BRCA1. {ECO:0000269|PubMed:16698035}.
MUTAGEN 1201 1201 S->A: No effect on interaction with
BRCA1. {ECO:0000269|PubMed:16698035}.
MUTAGEN 1263 1263 S->A: Abolishes interaction with BRCA1.
{ECO:0000269|PubMed:16698035}.
MUTAGEN 1585 1585 S->A: No effect on interaction with
BRCA1. {ECO:0000269|PubMed:16698035}.
MUTAGEN 1952 1952 S->A: No effect on interaction with
BRCA1. {ECO:0000269|PubMed:16698035}.
MUTAGEN 2211 2211 S->A: No effect on interaction with
BRCA1. {ECO:0000269|PubMed:16698035}.
CONFLICT 66 66 S -> A (in Ref. 1; AAC50139).
{ECO:0000305}.
CONFLICT 79 79 M -> W (in Ref. 1; AAC50139).
{ECO:0000305}.
CONFLICT 89 89 R -> G (in Ref. 1; AAC50139).
{ECO:0000305}.
CONFLICT 182 182 P -> A (in Ref. 1; AAC50139).
{ECO:0000305}.
CONFLICT 234 234 S -> N (in Ref. 1; AAC50139).
{ECO:0000305}.
CONFLICT 299 299 Q -> K (in Ref. 1; AAC50139).
{ECO:0000305}.
CONFLICT 303 303 E -> K (in Ref. 1; AAC50139).
{ECO:0000305}.
CONFLICT 364 364 A -> V (in Ref. 2; AAP94122).
{ECO:0000305}.
CONFLICT 446 446 H -> Q (in Ref. 1; AAC50139).
{ECO:0000305}.
CONFLICT 494 494 D -> N (in Ref. 1; AAC50139).
{ECO:0000305}.
CONFLICT 554 554 D -> G (in Ref. 1; AAC50139).
{ECO:0000305}.
CONFLICT 622 622 Q -> R (in Ref. 1; AAC50139).
{ECO:0000305}.
CONFLICT 640 640 A -> G (in Ref. 1; AAC50139).
{ECO:0000305}.
CONFLICT 814 814 V -> I (in Ref. 2; AAP94122).
{ECO:0000305}.
CONFLICT 1061 1061 N -> S (in Ref. 1; AAC50139).
{ECO:0000305}.
CONFLICT 1094 1095 EL -> DV (in Ref. 1; AAC50139).
{ECO:0000305}.
CONFLICT 1225 1225 S -> A (in Ref. 1; AAC50139).
{ECO:0000305}.
CONFLICT 1257 1257 S -> C (in Ref. 1; AAC50139).
{ECO:0000305}.
CONFLICT 1297 1297 C -> G (in Ref. 1; AAC50139).
{ECO:0000305}.
CONFLICT 1320 1320 V -> A (in Ref. 1; AAC50139).
{ECO:0000305}.
CONFLICT 1444 1444 N -> S (in Ref. 1; AAC50139).
{ECO:0000305}.
CONFLICT 1474 1474 F -> L (in Ref. 1; AAC50139).
{ECO:0000305}.
CONFLICT 1665 1666 TF -> SL (in Ref. 1; AAC50139).
{ECO:0000305}.
CONFLICT 1677 1677 I -> V (in Ref. 1; AAC50139).
{ECO:0000305}.
CONFLICT 1741 1741 P -> S (in Ref. 1; AAC50139).
{ECO:0000305}.
CONFLICT 1762 1762 S -> G (in Ref. 1; AAC50139).
{ECO:0000305}.
CONFLICT 1822 1822 C -> S (in Ref. 1; AAC50139).
{ECO:0000305}.
CONFLICT 1875 1875 M -> T (in Ref. 1; AAC50139).
{ECO:0000305}.
CONFLICT 1888 1888 D -> G (in Ref. 1; AAC50139).
{ECO:0000305}.
CONFLICT 1997 1997 I -> V (in Ref. 1; AAC50139).
{ECO:0000305}.
CONFLICT 2013 2013 Q -> H (in Ref. 1; AAC50139).
{ECO:0000305}.
CONFLICT 2058 2058 D -> H (in Ref. 1; AAC50139).
{ECO:0000305}.
CONFLICT 2075 2075 C -> S (in Ref. 1; AAC50139).
{ECO:0000305}.
CONFLICT 2098 2099 SS -> PT (in Ref. 1; AAC50139).
{ECO:0000305}.
CONFLICT 2158 2159 TA -> PT (in Ref. 1; AAC50139).
{ECO:0000305}.
CONFLICT 2166 2166 N -> S (in Ref. 1; AAC50139).
{ECO:0000305}.
CONFLICT 2234 2234 N -> S (in Ref. 1; AAC50139).
{ECO:0000305}.
CONFLICT 2321 2321 H -> R (in Ref. 2; AAP94122).
{ECO:0000305}.
HELIX 105 111 {ECO:0000244|PDB:2YL2}.
STRAND 120 123 {ECO:0000244|PDB:2YL2}.
HELIX 127 145 {ECO:0000244|PDB:2YL2}.
STRAND 150 157 {ECO:0000244|PDB:2YL2}.
HELIX 159 163 {ECO:0000244|PDB:2YL2}.
HELIX 168 171 {ECO:0000244|PDB:2YL2}.
STRAND 172 177 {ECO:0000244|PDB:2YL2}.
HELIX 183 185 {ECO:0000244|PDB:2YL2}.
TURN 186 188 {ECO:0000244|PDB:2YL2}.
HELIX 190 199 {ECO:0000244|PDB:2YL2}.
STRAND 203 206 {ECO:0000244|PDB:2YL2}.
TURN 211 214 {ECO:0000244|PDB:2YL2}.
HELIX 217 224 {ECO:0000244|PDB:2YL2}.
STRAND 228 231 {ECO:0000244|PDB:2YL2}.
HELIX 234 241 {ECO:0000244|PDB:2YL2}.
HELIX 243 252 {ECO:0000244|PDB:2YL2}.
TURN 261 264 {ECO:0000244|PDB:2YL2}.
HELIX 283 289 {ECO:0000244|PDB:2YL2}.
HELIX 294 304 {ECO:0000244|PDB:2YL2}.
STRAND 306 312 {ECO:0000244|PDB:2YL2}.
STRAND 320 324 {ECO:0000244|PDB:2YL2}.
TURN 327 329 {ECO:0000244|PDB:2YL2}.
HELIX 330 340 {ECO:0000244|PDB:2YL2}.
STRAND 346 350 {ECO:0000244|PDB:2YL2}.
STRAND 356 364 {ECO:0000244|PDB:2YL2}.
STRAND 370 382 {ECO:0000244|PDB:2YL2}.
STRAND 385 392 {ECO:0000244|PDB:2YL2}.
HELIX 398 415 {ECO:0000244|PDB:2YL2}.
STRAND 419 427 {ECO:0000244|PDB:2YL2}.
STRAND 433 439 {ECO:0000244|PDB:2YL2}.
TURN 444 446 {ECO:0000244|PDB:2YL2}.
HELIX 447 453 {ECO:0000244|PDB:2YL2}.
HELIX 457 465 {ECO:0000244|PDB:2YL2}.
HELIX 470 472 {ECO:0000244|PDB:2YL2}.
HELIX 474 479 {ECO:0000244|PDB:2YL2}.
TURN 492 495 {ECO:0000244|PDB:2YL2}.
STRAND 496 498 {ECO:0000244|PDB:2YL2}.
STRAND 503 510 {ECO:0000244|PDB:2YL2}.
STRAND 526 530 {ECO:0000244|PDB:2YL2}.
STRAND 537 542 {ECO:0000244|PDB:2YL2}.
STRAND 557 566 {ECO:0000244|PDB:2YL2}.
HELIX 567 582 {ECO:0000244|PDB:2YL2}.
HELIX 589 599 {ECO:0000244|PDB:2YL2}.
HELIX 601 604 {ECO:0000244|PDB:2YL2}.
HELIX 612 616 {ECO:0000244|PDB:2YL2}.
HELIX 1582 1592 {ECO:0000244|PDB:4ASI}.
HELIX 1598 1600 {ECO:0000244|PDB:4ASI}.
HELIX 1601 1619 {ECO:0000244|PDB:4ASI}.
HELIX 1628 1631 {ECO:0000244|PDB:4ASI}.
STRAND 1632 1639 {ECO:0000244|PDB:4ASI}.
STRAND 1645 1648 {ECO:0000244|PDB:4ASI}.
STRAND 1656 1666 {ECO:0000244|PDB:4ASI}.
STRAND 1675 1682 {ECO:0000244|PDB:4ASI}.
HELIX 1687 1689 {ECO:0000244|PDB:4ASI}.
HELIX 1693 1709 {ECO:0000244|PDB:4ASI}.
STRAND 1713 1717 {ECO:0000244|PDB:4ASI}.
HELIX 1728 1731 {ECO:0000244|PDB:4ASI}.
STRAND 1735 1739 {ECO:0000244|PDB:4ASI}.
HELIX 1744 1746 {ECO:0000244|PDB:4ASI}.
STRAND 1748 1753 {ECO:0000244|PDB:4ASI}.
HELIX 1755 1761 {ECO:0000244|PDB:4ASI}.
HELIX 1762 1764 {ECO:0000244|PDB:4ASI}.
STRAND 1767 1774 {ECO:0000244|PDB:4ASI}.
STRAND 1777 1785 {ECO:0000244|PDB:4ASI}.
HELIX 1795 1813 {ECO:0000244|PDB:4ASI}.
STRAND 1816 1820 {ECO:0000244|PDB:4ASI}.
STRAND 1822 1825 {ECO:0000244|PDB:4ASI}.
HELIX 1827 1834 {ECO:0000244|PDB:4ASI}.
STRAND 1837 1841 {ECO:0000244|PDB:4ASI}.
STRAND 1845 1849 {ECO:0000244|PDB:4ASI}.
HELIX 1851 1858 {ECO:0000244|PDB:4ASI}.
HELIX 1866 1870 {ECO:0000244|PDB:4ASI}.
HELIX 1872 1875 {ECO:0000244|PDB:4ASI}.
TURN 1876 1879 {ECO:0000244|PDB:4ASI}.
STRAND 1882 1887 {ECO:0000244|PDB:4ASI}.
HELIX 1888 1899 {ECO:0000244|PDB:4ASI}.
STRAND 1914 1917 {ECO:0000244|PDB:4ASI}.
HELIX 1934 1939 {ECO:0000244|PDB:4ASI}.
STRAND 1944 1946 {ECO:0000244|PDB:4ASI}.
STRAND 1961 1964 {ECO:0000244|PDB:4ASI}.
STRAND 1971 1978 {ECO:0000244|PDB:4ASI}.
STRAND 1981 1988 {ECO:0000244|PDB:4ASI}.
STRAND 1993 1996 {ECO:0000244|PDB:4ASI}.
STRAND 2010 2013 {ECO:0000244|PDB:4ASI}.
HELIX 2020 2036 {ECO:0000244|PDB:4ASI}.
STRAND 2040 2043 {ECO:0000244|PDB:4ASI}.
HELIX 2053 2057 {ECO:0000244|PDB:4ASI}.
HELIX 2060 2072 {ECO:0000244|PDB:4ASI}.
STRAND 2078 2082 {ECO:0000244|PDB:4ASI}.
STRAND 2087 2089 {ECO:0000244|PDB:4ASI}.
HELIX 2090 2094 {ECO:0000244|PDB:4ASI}.
HELIX 2098 2100 {ECO:0000244|PDB:4ASI}.
TURN 2102 2104 {ECO:0000244|PDB:4ASI}.
STRAND 2105 2110 {ECO:0000244|PDB:4ASI}.
STRAND 2114 2118 {ECO:0000244|PDB:4ASI}.
HELIX 2120 2127 {ECO:0000244|PDB:4ASI}.
HELIX 2130 2140 {ECO:0000244|PDB:4ASI}.
HELIX 2142 2150 {ECO:0000244|PDB:4ASI}.
HELIX 2158 2188 {ECO:0000244|PDB:4ASI}.
HELIX 2193 2198 {ECO:0000244|PDB:4ASI}.
STRAND 2201 2206 {ECO:0000244|PDB:4ASI}.
HELIX 2208 2210 {ECO:0000244|PDB:4ASI}.
HELIX 2211 2235 {ECO:0000244|PDB:4ASI}.
HELIX 2241 2256 {ECO:0000244|PDB:4ASI}.
HELIX 2258 2265 {ECO:0000244|PDB:4ASI}.
HELIX 2267 2278 {ECO:0000244|PDB:4ASI}.
HELIX 2289 2310 {ECO:0000244|PDB:4ASI}.
HELIX 2312 2314 {ECO:0000244|PDB:4ASI}.
HELIX 2315 2322 {ECO:0000244|PDB:4ASI}.
HELIX 2323 2325 {ECO:0000244|PDB:4ASI}.
HELIX 2328 2337 {ECO:0000244|PDB:4ASI}.
SEQUENCE 2346 AA; 265554 MW; F1F0A518F8824FFC CRC64;
MDEPSPLAQP LELNQHSRFI IGSVSEDNSE DEISNLVKLD LLEEKEGSLS PASVGSDTLS
DLGISSLQDG LALHIRSSMS GLHLVKQGRD RKKIDSQRDF TVASPAEFVT RFGGNKVIEK
VLIANNGIAA VKCMRSIRRW SYEMFRNERA IRFVVMVTPE DLKANAEYIK MADHYVPVPG
GPNNNNYANV ELILDIAKRI PVQAVWAGWG HASENPKLPE LLLKNGIAFM GPPSQAMWAL
GDKIASSIVA QTAGIPTLPW SGSGLRVDWQ ENDFSKRILN VPQELYEKGY VKDVDDGLQA
AEEVGYPVMI KASEGGGGKG IRKVNNADDF PNLFRQVQAE VPGSPIFVMR LAKQSRHLEV
QILADQYGNA ISLFGRDCSV QRRHQKIIEE APATIATPAV FEHMEQCAVK LAKMVGYVSA
GTVEYLYSQD GSFYFLELNP RLQVEHPCTE MVADVNLPAA QLQIAMGIPL YRIKDIRMMY
GVSPWGDSPI DFEDSAHVPC PRGHVIAARI TSENPDEGFK PSSGTVQELN FRSNKNVWGY
FSVAAAGGLH EFADSQFGHC FSWGENREEA ISNMVVALKE LSIRGDFRTT VEYLIKLLET
ESFQMNRIDT GWLDRLIAEK VQAERPDTML GVVCGALHVA DVSLRNSVSN FLHSLERGQV
LPAHTLLNTV DVELIYEGVK YVLKVTRQSP NSYVVIMNGS CVEVDVHRLS DGGLLLSYDG
SSYTTYMKEE VDRYRITIGN KTCVFEKEND PSVMRSPSAG KLIQYIVEDG GHVFAGQCYA
EIEVMKMVMT LTAVESGCIH YVKRPGAALD PGCVLAKMQL DNPSKVQQAE LHTGSLPRIQ
STALRGEKLH RVFHYVLDNL VNVMNGYCLP DPFFSSKVKD WVERLMKTLR DPSLPLLELQ
DIMTSVSGRI PPNVEKSIKK EMAQYASNIT SVLCQFPSQQ IANILDSHAA TLNRKSEREV
FFMNTQSIVQ LVQRYRSGIR GHMKAVVMDL LRQYLRVETQ FQNGHYDKCV FALREENKSD
MNTVLNYIFS HAQVTKKNLL VTMLIDQLCG RDPTLTDELL NILTELTQLS KTTNAKVALR
ARQVLIASHL PSYELRHNQV ESIFLSAIDM YGHQFCIENL QKLILSETSI FDVLPNFFYH
SNQVVRMAAL EVYVRRAYIA YELNSVQHRQ LKDNTCVVEF QFMLPTSHPN RGNIPTLNRM
SFSSNLNHYG MTHVASVSDV LLDNSFTPPC QRMGGMVSFR TFEDFVRIFD EVMGCFSDSP
PQSPTFPEAG HTSLYDEDKV PRDEPIHILN VAIKTDCDIE DDRLAAMFRE FTQQNKATLV
DHGIRRLTFL VAQKDFRKQV NYEVDRRFHR EFPKFFTFRA RDKFEEDRIY RHLEPALAFQ
LELNRMRNFD LTAIPCANHK MHLYLGAAKV EVGTEVTDYR FFVRAIIRHS DLVTKEASFE
YLQNEGERLL LEAMDELEVA FNNTNVRTDC NHIFLNFVPT VIMDPSKIEE SVRSMVMRYG
SRLWKLRVLQ AELKINIRLT PTGKAIPIRL FLTNESGYYL DISLYKEVTD SRTAQIMFQA
YGDKQGPLHG MLINTPYVTK DLLQSKRFQA QSLGTTYIYD IPEMFRQSLI KLWESMSTQA
FLPSPPLPSD MLTYTELVLD DQGQLVHMNR LPGGNEIGMV AWKMTFKSPE YPEGRDIIVI
GNDITYRIGS FGPQEDLLFL RASELARAEG IPRIYVSANS GARIGLAEEI RHMFHVAWVD
PEDPYKGYRY LYLTPQDYKR VSALNSVHCE HVEDEGESRY KITDIIGKEE GIGPENLRGS
GMIAGESSLA YNEIITISLV TCRAIGIGAY LVRLGQRTIQ VENSHLILTG AGALNKVLGR
EVYTSNNQLG GIQIMHNNGV THCTVCDDFE GVFTVLHWLS YMPKSVHSSV PLLNSKDPID
RIIEFVPTKT PYDPRWMLAG RPHPTQKGQW LSGFFDYGSF SEIMQPWAQT VVVGRARLGG
IPVGVVAVET RTVELSIPAD PANLDSEAKI IQQAGQVWFP DSAFKTYQAI KDFNREGLPL
MVFANWRGFS GGMKDMYDQV LKFGAYIVDG LRECCQPVLV YIPPQAELRG GSWVVIDSSI
NPRHMEMYAD RESRGSVLEP EGTVEIKFRR KDLVKTMRRV DPVYIHLAER LGTPELSTAE
RKELENKLKE REEFLIPIYH QVAVQFADLH DTPGRMQEKG VISDILDWKT SRTFFYWRLR
RLLLEDLVKK KIHNANPELT DGQIQAMLRR WFVEVEGTVK AYVWDNNKDL AEWLEKQLTE
EDGVHSVIEE NIKCISRDYV LKQIRSLVQA NPEVAMDSII HMTQHISPTQ RAEVIRILST
MDSPST


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