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Acetyl-CoA carboxylase 2 (EC 6.4.1.2) (ACC-beta) [Includes: Biotin carboxylase (EC 6.3.4.14)]

 ACACB_HUMAN             Reviewed;        2458 AA.
O00763; A6NK36; Q16852; Q1HEC1; Q6KE87; Q6KE89; Q6TY48;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
05-OCT-2010, sequence version 3.
13-FEB-2019, entry version 189.
RecName: Full=Acetyl-CoA carboxylase 2;
EC=6.4.1.2 {ECO:0000269|PubMed:16854592, ECO:0000269|PubMed:20952656};
AltName: Full=ACC-beta;
Includes:
RecName: Full=Biotin carboxylase;
EC=6.3.4.14;
Flags: Precursor;
Name=ACACB; Synonyms=ACC2, ACCB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
TISSUE=Liver;
PubMed=9099716; DOI=10.1074/jbc.272.16.10669;
Abu-Elheiga L., Almarza-Ortega D.B., Baldini A., Wakil S.J.;
"Human acetyl-CoA carboxylase 2. Molecular cloning, characterization,
chromosomal mapping, and evidence for two isoforms.";
J. Biol. Chem. 272:10669-10677(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), COFACTOR, BIOPHYSICOCHEMICAL
PROPERTIES, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND VARIANT
ILE-2141.
PubMed=16854592; DOI=10.1016/j.pep.2006.06.005;
Cheng D., Chu C.-H., Chen L., Feder J.N., Mintier G.A., Wu Y.,
Cook J.W., Harpel M.R., Locke G.A., An Y., Tamura J.K.;
"Expression, purification, and characterization of human and rat
acetyl coenzyme A carboxylase (ACC) isozymes.";
Protein Expr. Purif. 51:11-21(2007).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ILE-2141.
TISSUE=Heart;
Peng X.R., Lindgren K., Corneliussen B.;
"Corrected sequence for human acetyl-CoA carboxylase 2 obtained by
alignment to human genomic DNA and PCR cloning from human skeletal
muscle and heart cDNA.";
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Heart;
Mao J., Wakil S.J.;
"Alternative splicing in the human acetyl-CoA carboxylase 2 (ACC2)
gene.";
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1324-2109.
TISSUE=Adipose tissue;
PubMed=8670171; DOI=10.1042/bj3160915;
Widmer J., Fassihi K.S., Schlichter S.C., Wheeler K.S., Crute B.E.,
King N., Nutile-Mcmenemy N., Noll W.W., Daniel S., Ha J., Kim K.-H.,
Witters L.A.;
"Identification of a second human acetyl-CoA carboxylase gene.";
Biochem. J. 316:915-922(1996).
[7]
SUBCELLULAR LOCATION.
PubMed=10677481; DOI=10.1073/pnas.97.4.1444;
Abu-Elheiga L., Brinkley W.R., Zhong L., Chirala S.S.,
Woldegiorgis G., Wakil S.J.;
"The subcellular localization of acetyl-CoA carboxylase 2.";
Proc. Natl. Acad. Sci. U.S.A. 97:1444-1449(2000).
[8]
PHOSPHORYLATION AT SER-222 BY AMPK.
PubMed=12488245; DOI=10.1152/ajpendo.00436.2002;
Wojtaszewski J.F., MacDonald C., Nielsen J.N., Hellsten Y.,
Hardie D.G., Kemp B.E., Kiens B., Richter E.A.;
"Regulation of 5'AMP-activated protein kinase activity and substrate
utilization in exercising human skeletal muscle.";
Am. J. Physiol. 284:E813-E822(2003).
[9]
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).
[10]
BIOPHYSICOCHEMICAL PROPERTIES, ALTERNATIVE SPLICING (ISOFORM 3), AND
TISSUE SPECIFICITY.
PubMed=19190759; DOI=10.1371/journal.pone.0004369;
Castle J.C., Hara Y., Raymond C.K., Garrett-Engele P., Ohwaki K.,
Kan Z., Kusunoki J., Johnson J.M.;
"ACC2 is expressed at high levels in human white adipose and has an
isoform with a novel N-terminus.";
PLoS ONE 4:E4369-E4369(2009).
[11]
CATALYTIC ACTIVITY, SUBUNIT, ACTIVITY 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).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35; THR-70; SER-91;
SER-95; SER-200; SER-469 AND THR-1342, 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).
[13]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 217-775.
PubMed=17876819; DOI=10.1002/prot.21611;
Cho Y.S., Lee J.I., Shin D., Kim H.T., Cheon Y.H., Seo C.I., Kim Y.E.,
Hyun Y.L., Lee Y.S., Sugiyama K., Park S.Y., Ro S., Cho J.M.,
Lee T.G., Heo Y.S.;
"Crystal structure of the biotin carboxylase domain of human acetyl-
CoA carboxylase 2.";
Proteins 70:268-272(2008).
[14]
STRUCTURE BY NMR OF 885-971.
RIKEN structural genomics initiative (RSGI);
"Solution structure of RSGI RUH-053, an apo-biotin carboxy carrier
protein from human transcarboxylase.";
Submitted (OCT-2006) to the PDB data bank.
[15]
VARIANT [LARGE SCALE ANALYSIS] LEU-193.
PubMed=18772397; DOI=10.1126/science.1164368;
Jones S., Zhang X., Parsons D.W., Lin J.C., Leary R.J., Angenendt P.,
Mankoo P., Carter H., Kamiyama H., Jimeno A., Hong S.M., Fu B.,
Lin M.T., Calhoun E.S., Kamiyama M., Walter K., Nikolskaya T.,
Nikolsky Y., Hartigan J., Smith D.R., Hidalgo M., Leach S.D.,
Klein A.P., Jaffee E.M., Goggins M., Maitra A., Iacobuzio-Donahue C.,
Eshleman J.R., Kern S.E., Hruban R.H., Karchin R., Papadopoulos N.,
Parmigiani G., Vogelstein B., Velculescu V.E., Kinzler K.W.;
"Core signaling pathways in human pancreatic cancers revealed by
global genomic analyses.";
Science 321:1801-1806(2008).
-!- FUNCTION: Catalyzes the ATP-dependent carboxylation of acetyl-CoA
to malonyl-CoA. Carries out three functions: biotin carboxyl
carrier protein, biotin carboxylase and carboxyltransferase.
Involved in inhibition of fatty acid and glucose oxidation and
enhancement of fat storage (By similarity). May play a role in
regulation of mitochondrial fatty acid oxidation through malonyl-
CoA-dependent inhibition of carnitine palmitoyltransferase 1 (By
similarity). {ECO:0000250|UniProtKB:E9Q4Z2,
ECO:0000269|PubMed:20952656}.
-!- CATALYTIC ACTIVITY:
Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) +
malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308,
ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384,
ChEBI:CHEBI:456216; EC=6.4.1.2;
Evidence={ECO:0000269|PubMed:16854592,
ECO:0000269|PubMed:20952656};
-!- CATALYTIC ACTIVITY:
Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein]
= ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] +
phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505,
Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544,
ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144,
ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14;
Evidence={ECO:0000250|UniProtKB:Q13085};
-!- COFACTOR:
Name=biotin; Xref=ChEBI:CHEBI:57586;
Evidence={ECO:0000269|PubMed:16854592};
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
Note=Binds 2 manganese ions per subunit. {ECO:0000250};
-!- ACTIVITY REGULATION: Activity is increased by oligomerization.
Activated by citrate. Citrate and MID1IP1 promote oligomerization.
Inhibited by malonyl-CoA. {ECO:0000269|PubMed:16854592,
ECO:0000269|PubMed:20952656}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=120 uM for ATP {ECO:0000269|PubMed:16854592};
KM=110 uM for ATP (isoform 2) {ECO:0000269|PubMed:19190759};
KM=58 uM for acetyl-CoA {ECO:0000269|PubMed:16854592};
KM=94 uM for acetyl-CoA (isoform 3)
{ECO:0000269|PubMed:19190759};
KM=6.5 mM for NaHCO3 (isoform 3) {ECO:0000269|PubMed:19190759};
KM=3.0 mM for NaHCO(3) {ECO:0000269|PubMed:16854592};
-!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA
from acetyl-CoA: step 1/1.
-!- SUBUNIT: Monomer, homodimer, and homotetramer. Can form
filamentous polymers. Interacts with MID1IP1; interaction with
MID1IP1 promotes oligomerization and increases its activity.
{ECO:0000269|PubMed:20952656}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-2211739, EBI-2211739;
P50747:HLCS; NbExp=4; IntAct=EBI-2211739, EBI-3915568;
Q9CQ20:Mid1ip1 (xeno); NbExp=4; IntAct=EBI-2211739, EBI-473024;
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10677481}.
Nucleus {ECO:0000269|PubMed:10677481}. Endomembrane system.
Note=May associate with membranes.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=Long;
IsoId=O00763-1; Sequence=Displayed;
Name=2; Synonyms=Short;
IsoId=O00763-2; Sequence=VSP_000547;
Name=3 {ECO:0000305}; Synonyms=ACC2.v2
{ECO:0000303|PubMed:19190759};
IsoId=O00763-3; Sequence=VSP_057081, VSP_057082;
-!- TISSUE SPECIFICITY: Widely expressed with highest levels in heart,
skeletal muscle, liver, adipose tissue, mammary gland, adrenal
gland and colon (PubMed:9099716). Isoform 3 is expressed in
skeletal muscle, adipose tissue and liver (at protein level)
(PubMed:19190759). Isoform 3 is detected at high levels in adipose
tissue with lower levels in heart, liver, skeletal muscle and
testis (PubMed:19190759). {ECO:0000269|PubMed:19190759,
ECO:0000269|PubMed:9099716}.
-!- PTM: Phosphorylated by AMPK, leading to inactivation of the
enzyme. Required for the maintenance of skeletal muscle lipid and
glucose homeostasis (By similarity).
{ECO:0000250|UniProtKB:E9Q4Z2, ECO:0000269|PubMed:12488245}.
-!- BIOTECHNOLOGY: Inhibition of ACACB may prevent lipid-induced
insulin resistance and type 2 diabetes, making the enzyme a
potential pharmaceutical target for treatment of obesity and type
2 diabetes. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB58382.1; Type=Miscellaneous discrepancy; Note=Many Frameshifts and conflicts.; Evidence={ECO:0000305};
Sequence=CAE01470.2; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
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EMBL; U89344; AAB58382.1; ALT_SEQ; mRNA.
EMBL; DQ493870; ABF48723.1; -; mRNA.
EMBL; AJ575431; CAE01470.2; ALT_SEQ; mRNA.
EMBL; AJ575592; CAE01471.3; -; mRNA.
EMBL; AY382667; AAR37018.1; -; mRNA.
EMBL; AC007637; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; U34591; AAC50571.1; -; mRNA.
CCDS; CCDS31898.1; -. [O00763-1]
PIR; S71091; S71091.
RefSeq; NP_001084.3; NM_001093.3. [O00763-1]
RefSeq; XP_005253933.1; XM_005253876.4. [O00763-1]
RefSeq; XP_006719430.1; XM_006719367.3. [O00763-3]
RefSeq; XP_011536561.1; XM_011538259.2. [O00763-1]
UniGene; Hs.234898; -.
UniGene; Hs.676621; -.
PDB; 2DN8; NMR; -; A=885-971.
PDB; 2HJW; X-ray; 2.50 A; A=217-775.
PDB; 2KCC; NMR; -; A=891-965.
PDB; 3FF6; X-ray; 3.19 A; A/B/C/D=1693-2450.
PDB; 3GID; X-ray; 2.30 A; A/B=238-760.
PDB; 3GLK; X-ray; 2.10 A; A=238-760.
PDB; 3JRW; X-ray; 2.60 A; A=217-775.
PDB; 3JRX; X-ray; 2.50 A; A=217-775.
PDB; 3TDC; X-ray; 2.41 A; A=1690-2445.
PDB; 4HQ6; X-ray; 2.70 A; A=217-776.
PDB; 5KKN; X-ray; 2.60 A; B/C=238-760.
PDBsum; 2DN8; -.
PDBsum; 2HJW; -.
PDBsum; 2KCC; -.
PDBsum; 3FF6; -.
PDBsum; 3GID; -.
PDBsum; 3GLK; -.
PDBsum; 3JRW; -.
PDBsum; 3JRX; -.
PDBsum; 3TDC; -.
PDBsum; 4HQ6; -.
PDBsum; 5KKN; -.
ProteinModelPortal; O00763; -.
SMR; O00763; -.
BioGrid; 106550; 16.
DIP; DIP-51617N; -.
IntAct; O00763; 10.
MINT; O00763; -.
STRING; 9606.ENSP00000341044; -.
BindingDB; O00763; -.
ChEMBL; CHEMBL4829; -.
DrugBank; DB07870; (2S)-2-(4-{[3-CHLORO-5-(TRIFLUOROMETHYL)PYRIDIN-2-YL]OXY}PHENOXY)PROPANOIC ACID.
DrugBank; DB00173; Adenine.
DrugBank; DB00121; Biotin.
DrugBank; DB02859; Soraphen A.
GuidetoPHARMACOLOGY; 1264; -.
SwissLipids; SLP:000000730; -.
iPTMnet; O00763; -.
PhosphoSitePlus; O00763; -.
BioMuta; ACACB; -.
EPD; O00763; -.
jPOST; O00763; -.
MaxQB; O00763; -.
PaxDb; O00763; -.
PeptideAtlas; O00763; -.
PRIDE; O00763; -.
ProteomicsDB; 48022; -.
ProteomicsDB; 48023; -. [O00763-2]
DNASU; 32; -.
Ensembl; ENST00000338432; ENSP00000341044; ENSG00000076555. [O00763-1]
Ensembl; ENST00000377848; ENSP00000367079; ENSG00000076555. [O00763-1]
GeneID; 32; -.
KEGG; hsa:32; -.
UCSC; uc001tob.4; human. [O00763-1]
CTD; 32; -.
DisGeNET; 32; -.
EuPathDB; HostDB:ENSG00000076555.15; -.
GeneCards; ACACB; -.
H-InvDB; HIX0036741; -.
HGNC; HGNC:85; ACACB.
HPA; HPA006554; -.
MIM; 601557; gene.
neXtProt; NX_O00763; -.
OpenTargets; ENSG00000076555; -.
PharmGKB; PA24422; -.
eggNOG; KOG0368; Eukaryota.
eggNOG; COG0439; LUCA.
eggNOG; COG0511; LUCA.
eggNOG; COG4799; LUCA.
GeneTree; ENSGT00940000155049; -.
HOVERGEN; HBG005371; -.
InParanoid; O00763; -.
KO; K01946; -.
OMA; YLQVEHH; -.
OrthoDB; 861989at2759; -.
PhylomeDB; O00763; -.
TreeFam; TF300061; -.
BioCyc; MetaCyc:HS01211-MONOMER; -.
BRENDA; 6.3.4.14; 2681.
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).
SABIO-RK; O00763; -.
SIGNOR; O00763; -.
UniPathway; UPA00655; UER00711.
ChiTaRS; ACACB; human.
EvolutionaryTrace; O00763; -.
GeneWiki; ACACB; -.
GenomeRNAi; 32; -.
PRO; PR:O00763; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000076555; Expressed in 225 organ(s), highest expression level in parietal pleura.
ExpressionAtlas; O00763; baseline and differential.
Genevisible; O00763; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003989; F:acetyl-CoA carboxylase activity; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0009374; F:biotin binding; IEA:Ensembl.
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; IDA:UniProtKB.
GO; GO:0006853; P:carnitine shuttle; TAS:Reactome.
GO; GO:0097009; P:energy homeostasis; IEA:Ensembl.
GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0043086; P:negative regulation of catalytic activity; IEA:Ensembl.
GO; GO:0031999; P:negative regulation of fatty acid beta-oxidation; IEA:Ensembl.
GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
GO; GO:0031325; P:positive regulation of cellular metabolic process; TAS:Reactome.
GO; GO:0060421; P:positive regulation of heart growth; IEA:Ensembl.
GO; GO:0010884; P:positive regulation of lipid storage; IEA:Ensembl.
GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
GO; GO:0045540; P:regulation of cholesterol biosynthetic process; TAS:Reactome.
GO; GO:0010906; P:regulation of glucose metabolic process; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
GO; GO:0014070; P:response to organic cyclic compound; 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; 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; 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; Allosteric enzyme; Alternative splicing; ATP-binding;
Biotin; Complete proteome; Fatty acid biosynthesis;
Fatty acid metabolism; Ligase; Lipid biosynthesis; Lipid metabolism;
Manganese; Membrane; Metal-binding; Mitochondrion;
Multifunctional enzyme; Nucleotide-binding; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Transit peptide.
TRANSIT 1 ? Mitochondrion.
{ECO:0000250|UniProtKB:E9Q4Z2}.
CHAIN ? 2458 Acetyl-CoA carboxylase 2. {ECO:0000305}.
/FTId=PRO_0000146767.
DOMAIN 259 761 Biotin carboxylation.
DOMAIN 414 609 ATP-grasp. {ECO:0000255|PROSITE-
ProRule:PRU00409}.
DOMAIN 888 962 Biotinyl-binding. {ECO:0000255|PROSITE-
ProRule:PRU01066}.
DOMAIN 1695 2025 CoA carboxyltransferase N-terminal.
{ECO:0000255|PROSITE-ProRule:PRU01136}.
DOMAIN 2029 2345 CoA carboxyltransferase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU01137}.
NP_BIND 458 463 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00409}.
REGION 1695 2345 Carboxyltransferase.
{ECO:0000255|PROSITE-ProRule:PRU01138}.
ACT_SITE 584 584 {ECO:0000250}.
METAL 567 567 Manganese 1. {ECO:0000250}.
METAL 580 580 Manganese 1. {ECO:0000250}.
METAL 580 580 Manganese 2. {ECO:0000250}.
METAL 582 582 Manganese 2. {ECO:0000250}.
BINDING 1934 1934 Coenzyme A. {ECO:0000250}.
BINDING 2238 2238 Coenzyme A. {ECO:0000250}.
BINDING 2240 2240 Coenzyme A. {ECO:0000250}.
MOD_RES 35 35 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 70 70 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 91 91 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 95 95 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 169 169 Phosphoserine.
{ECO:0000250|UniProtKB:Q13085}.
MOD_RES 175 175 Phosphoserine.
{ECO:0000250|UniProtKB:Q13085}.
MOD_RES 192 192 Phosphoserine.
{ECO:0000250|UniProtKB:Q13085}.
MOD_RES 195 195 Phosphoserine.
{ECO:0000250|UniProtKB:Q13085}.
MOD_RES 200 200 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 207 207 Phosphothreonine.
{ECO:0000250|UniProtKB:E9Q4Z2}.
MOD_RES 220 220 Phosphoserine.
{ECO:0000250|UniProtKB:P11497}.
MOD_RES 222 222 Phosphoserine; by AMPK.
{ECO:0000269|PubMed:12488245}.
MOD_RES 469 469 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 753 753 Phosphothreonine.
{ECO:0000250|UniProtKB:Q13085}.
MOD_RES 929 929 N6-biotinyllysine. {ECO:0000250,
ECO:0000255|PROSITE-ProRule:PRU01066}.
MOD_RES 1340 1340 Phosphoserine.
{ECO:0000250|UniProtKB:E9Q4Z2}.
MOD_RES 1342 1342 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1360 1360 Phosphoserine.
{ECO:0000250|UniProtKB:E9Q4Z2}.
MOD_RES 1405 1405 Phosphoserine.
{ECO:0000250|UniProtKB:Q13085}.
VAR_SEQ 1 202 Missing (in isoform 3).
{ECO:0000269|PubMed:19190759}.
/FTId=VSP_057081.
VAR_SEQ 203 218 AYLTTGEAETRVPTMR -> MSPAKCKICFPDREVK (in
isoform 3).
{ECO:0000269|PubMed:19190759}.
/FTId=VSP_057082.
VAR_SEQ 1118 1187 Missing (in isoform 2).
{ECO:0000303|PubMed:9099716}.
/FTId=VSP_000547.
VARIANT 193 193 R -> L (in a pancreatic ductal
adenocarcinoma sample; somatic mutation).
{ECO:0000269|PubMed:18772397}.
/FTId=VAR_062667.
VARIANT 552 552 I -> V (in dbSNP:rs16940029).
/FTId=VAR_031255.
VARIANT 651 651 A -> T (in dbSNP:rs2300455).
/FTId=VAR_031256.
VARIANT 2141 2141 V -> I (in dbSNP:rs2075260).
{ECO:0000269|PubMed:16854592,
ECO:0000269|Ref.3}.
/FTId=VAR_031257.
CONFLICT 9 9 C -> R (in Ref. 2; ABF48723).
{ECO:0000305}.
CONFLICT 120 120 T -> I (in Ref. 4; AAR37018).
{ECO:0000305}.
CONFLICT 422 422 I -> T (in Ref. 4; AAR37018).
{ECO:0000305}.
CONFLICT 1340 1340 S -> N (in Ref. 6; AAC50571).
{ECO:0000305}.
CONFLICT 1383 1383 D -> G (in Ref. 6; AAC50571).
{ECO:0000305}.
CONFLICT 1425 1425 V -> M (in Ref. 6; AAC50571).
{ECO:0000305}.
CONFLICT 1819 1821 AEG -> PEA (in Ref. 6; AAC50571).
{ECO:0000305}.
CONFLICT 1892 1893 MI -> IM (in Ref. 6; AAC50571).
{ECO:0000305}.
HELIX 247 253 {ECO:0000244|PDB:3GLK}.
STRAND 262 265 {ECO:0000244|PDB:3GLK}.
HELIX 269 287 {ECO:0000244|PDB:3GLK}.
STRAND 292 299 {ECO:0000244|PDB:3GLK}.
HELIX 301 305 {ECO:0000244|PDB:3GLK}.
HELIX 309 313 {ECO:0000244|PDB:3GLK}.
STRAND 314 319 {ECO:0000244|PDB:3GLK}.
HELIX 325 327 {ECO:0000244|PDB:3GLK}.
TURN 328 330 {ECO:0000244|PDB:3GLK}.
HELIX 332 341 {ECO:0000244|PDB:3GLK}.
STRAND 345 348 {ECO:0000244|PDB:3GLK}.
HELIX 353 356 {ECO:0000244|PDB:3GLK}.
HELIX 359 366 {ECO:0000244|PDB:3GLK}.
STRAND 370 373 {ECO:0000244|PDB:3GLK}.
HELIX 376 379 {ECO:0000244|PDB:3GLK}.
HELIX 385 394 {ECO:0000244|PDB:3GLK}.
TURN 403 406 {ECO:0000244|PDB:3GLK}.
HELIX 426 431 {ECO:0000244|PDB:3GLK}.
HELIX 437 447 {ECO:0000244|PDB:3GLK}.
STRAND 449 455 {ECO:0000244|PDB:3GLK}.
STRAND 464 467 {ECO:0000244|PDB:3GLK}.
TURN 470 472 {ECO:0000244|PDB:3GLK}.
HELIX 473 483 {ECO:0000244|PDB:3GLK}.
STRAND 489 493 {ECO:0000244|PDB:3GLK}.
STRAND 496 507 {ECO:0000244|PDB:3GLK}.
STRAND 509 511 {ECO:0000244|PDB:3JRX}.
STRAND 513 523 {ECO:0000244|PDB:3GLK}.
STRAND 524 527 {ECO:0000244|PDB:4HQ6}.
STRAND 530 535 {ECO:0000244|PDB:3GLK}.
HELIX 541 558 {ECO:0000244|PDB:3GLK}.
STRAND 562 571 {ECO:0000244|PDB:3GLK}.
STRAND 572 574 {ECO:0000244|PDB:2HJW}.
STRAND 576 582 {ECO:0000244|PDB:3GLK}.
HELIX 589 596 {ECO:0000244|PDB:3GLK}.
HELIX 600 608 {ECO:0000244|PDB:3GLK}.
HELIX 613 615 {ECO:0000244|PDB:3GLK}.
HELIX 617 622 {ECO:0000244|PDB:3GLK}.
STRAND 635 637 {ECO:0000244|PDB:2HJW}.
STRAND 646 653 {ECO:0000244|PDB:3GLK}.
STRAND 669 671 {ECO:0000244|PDB:3GLK}.
STRAND 679 685 {ECO:0000244|PDB:3GLK}.
STRAND 700 709 {ECO:0000244|PDB:3GLK}.
HELIX 710 724 {ECO:0000244|PDB:3GLK}.
HELIX 728 730 {ECO:0000244|PDB:2HJW}.
HELIX 732 742 {ECO:0000244|PDB:3GLK}.
HELIX 744 748 {ECO:0000244|PDB:3GLK}.
HELIX 754 756 {ECO:0000244|PDB:2HJW}.
STRAND 896 898 {ECO:0000244|PDB:2DN8}.
STRAND 900 902 {ECO:0000244|PDB:2KCC}.
STRAND 903 910 {ECO:0000244|PDB:2DN8}.
STRAND 914 916 {ECO:0000244|PDB:2DN8}.
STRAND 921 927 {ECO:0000244|PDB:2DN8}.
STRAND 930 935 {ECO:0000244|PDB:2DN8}.
STRAND 937 944 {ECO:0000244|PDB:2DN8}.
STRAND 957 961 {ECO:0000244|PDB:2DN8}.
TURN 1698 1700 {ECO:0000244|PDB:3FF6}.
HELIX 1703 1711 {ECO:0000244|PDB:3TDC}.
HELIX 1717 1719 {ECO:0000244|PDB:3TDC}.
HELIX 1720 1732 {ECO:0000244|PDB:3TDC}.
STRAND 1742 1750 {ECO:0000244|PDB:3TDC}.
STRAND 1756 1759 {ECO:0000244|PDB:3TDC}.
STRAND 1767 1777 {ECO:0000244|PDB:3TDC}.
STRAND 1786 1793 {ECO:0000244|PDB:3TDC}.
HELIX 1798 1800 {ECO:0000244|PDB:3TDC}.
HELIX 1804 1820 {ECO:0000244|PDB:3TDC}.
STRAND 1824 1828 {ECO:0000244|PDB:3TDC}.
HELIX 1839 1842 {ECO:0000244|PDB:3TDC}.
STRAND 1846 1850 {ECO:0000244|PDB:3TDC}.
HELIX 1855 1857 {ECO:0000244|PDB:3TDC}.
STRAND 1859 1864 {ECO:0000244|PDB:3TDC}.
HELIX 1866 1872 {ECO:0000244|PDB:3TDC}.
TURN 1873 1876 {ECO:0000244|PDB:3TDC}.
STRAND 1878 1885 {ECO:0000244|PDB:3TDC}.
STRAND 1888 1896 {ECO:0000244|PDB:3TDC}.
STRAND 1899 1901 {ECO:0000244|PDB:3TDC}.
HELIX 1905 1924 {ECO:0000244|PDB:3TDC}.
STRAND 1927 1931 {ECO:0000244|PDB:3TDC}.
STRAND 1933 1936 {ECO:0000244|PDB:3TDC}.
HELIX 1938 1946 {ECO:0000244|PDB:3TDC}.
STRAND 1948 1952 {ECO:0000244|PDB:3TDC}.
STRAND 1956 1960 {ECO:0000244|PDB:3TDC}.
HELIX 1962 1969 {ECO:0000244|PDB:3TDC}.
HELIX 1977 1981 {ECO:0000244|PDB:3TDC}.
HELIX 1983 1986 {ECO:0000244|PDB:3TDC}.
TURN 1987 1990 {ECO:0000244|PDB:3TDC}.
STRAND 1993 1998 {ECO:0000244|PDB:3TDC}.
HELIX 1999 2010 {ECO:0000244|PDB:3TDC}.
HELIX 2045 2050 {ECO:0000244|PDB:3TDC}.
STRAND 2055 2057 {ECO:0000244|PDB:3TDC}.
STRAND 2072 2075 {ECO:0000244|PDB:3TDC}.
STRAND 2082 2089 {ECO:0000244|PDB:3TDC}.
STRAND 2092 2099 {ECO:0000244|PDB:3TDC}.
STRAND 2104 2108 {ECO:0000244|PDB:3TDC}.
STRAND 2120 2124 {ECO:0000244|PDB:3TDC}.
HELIX 2131 2147 {ECO:0000244|PDB:3TDC}.
STRAND 2151 2154 {ECO:0000244|PDB:3TDC}.
HELIX 2164 2168 {ECO:0000244|PDB:3TDC}.
HELIX 2171 2183 {ECO:0000244|PDB:3TDC}.
STRAND 2189 2193 {ECO:0000244|PDB:3TDC}.
STRAND 2198 2200 {ECO:0000244|PDB:3TDC}.
HELIX 2201 2205 {ECO:0000244|PDB:3TDC}.
HELIX 2209 2211 {ECO:0000244|PDB:3TDC}.
TURN 2213 2215 {ECO:0000244|PDB:3TDC}.
STRAND 2216 2221 {ECO:0000244|PDB:3TDC}.
STRAND 2225 2229 {ECO:0000244|PDB:3TDC}.
HELIX 2231 2238 {ECO:0000244|PDB:3TDC}.
HELIX 2241 2251 {ECO:0000244|PDB:3TDC}.
HELIX 2253 2261 {ECO:0000244|PDB:3TDC}.
HELIX 2269 2299 {ECO:0000244|PDB:3TDC}.
HELIX 2300 2302 {ECO:0000244|PDB:3TDC}.
HELIX 2304 2309 {ECO:0000244|PDB:3TDC}.
STRAND 2312 2317 {ECO:0000244|PDB:3TDC}.
HELIX 2319 2321 {ECO:0000244|PDB:3TDC}.
HELIX 2322 2344 {ECO:0000244|PDB:3TDC}.
HELIX 2345 2348 {ECO:0000244|PDB:3FF6}.
HELIX 2352 2365 {ECO:0000244|PDB:3TDC}.
HELIX 2369 2376 {ECO:0000244|PDB:3TDC}.
HELIX 2378 2388 {ECO:0000244|PDB:3TDC}.
HELIX 2404 2420 {ECO:0000244|PDB:3TDC}.
TURN 2423 2425 {ECO:0000244|PDB:3FF6}.
HELIX 2426 2435 {ECO:0000244|PDB:3FF6}.
HELIX 2439 2448 {ECO:0000244|PDB:3FF6}.
SEQUENCE 2458 AA; 276541 MW; ED12674A1A8A0706 CRC64;
MVLLLCLSCL IFSCLTFSWL KIWGKMTDSK PITKSKSEAN LIPSQEPFPA SDNSGETPQR
NGEGHTLPKT PSQAEPASHK GPKDAGRRRN SLPPSHQKPP RNPLSSSDAA PSPELQANGT
GTQGLEATDT NGLSSSARPQ GQQAGSPSKE DKKQANIKRQ LMTNFILGSF DDYSSDEDSV
AGSSRESTRK GSRASLGALS LEAYLTTGEA ETRVPTMRPS MSGLHLVKRG REHKKLDLHR
DFTVASPAEF VTRFGGDRVI EKVLIANNGI AAVKCMRSIR RWAYEMFRNE RAIRFVVMVT
PEDLKANAEY IKMADHYVPV PGGPNNNNYA NVELIVDIAK RIPVQAVWAG WGHASENPKL
PELLCKNGVA FLGPPSEAMW ALGDKIASTV VAQTLQVPTL PWSGSGLTVE WTEDDLQQGK
RISVPEDVYD KGCVKDVDEG LEAAERIGFP LMIKASEGGG GKGIRKAESA EDFPILFRQV
QSEIPGSPIF LMKLAQHARH LEVQILADQY GNAVSLFGRD CSIQRRHQKI VEEAPATIAP
LAIFEFMEQC AIRLAKTVGY VSAGTVEYLY SQDGSFHFLE LNPRLQVEHP CTEMIADVNL
PAAQLQIAMG VPLHRLKDIR LLYGESPWGV TPISFETPSN PPLARGHVIA ARITSENPDE
GFKPSSGTVQ ELNFRSSKNV WGYFSVAATG GLHEFADSQF GHCFSWGENR EEAISNMVVA
LKELSIRGDF RTTVEYLINL LETESFQNND IDTGWLDYLI AEKVQAEKPD IMLGVVCGAL
NVADAMFRTC MTDFLHSLER GQVLPADSLL NLVDVELIYG GVKYILKVAR QSLTMFVLIM
NGCHIEIDAH RLNDGGLLLS YNGNSYTTYM KEEVDSYRIT IGNKTCVFEK ENDPTVLRSP
SAGKLTQYTV EDGGHVEAGS SYAEMEVMKM IMTLNVQERG RVKYIKRPGA VLEAGCVVAR
LELDDPSKVH PAEPFTGELP AQQTLPILGE KLHQVFHSVL ENLTNVMSGF CLPEPVFSIK
LKEWVQKLMM TLRHPSLPLL ELQEIMTSVA GRIPAPVEKS VRRVMAQYAS NITSVLCQFP
SQQIATILDC HAATLQRKAD REVFFINTQS IVQLVQRYRS GIRGYMKTVV LDLLRRYLRV
EHHFQQAHYD KCVINLREQF KPDMSQVLDC IFSHAQVAKK NQLVIMLIDE LCGPDPSLSD
ELISILNELT QLSKSEHCKV ALRARQILIA SHLPSYELRH NQVESIFLSA IDMYGHQFCP
ENLKKLILSE TTIFDVLPTF FYHANKVVCM ASLEVYVRRG YIAYELNSLQ HRQLPDGTCV
VEFQFMLPSS HPNRMTVPIS ITNPDLLRHS TELFMDSGFS PLCQRMGAMV AFRRFEDFTR
NFDEVISCFA NVPKDTPLFS EARTSLYSED DCKSLREEPI HILNVSIQCA DHLEDEALVP
ILRTFVQSKK NILVDYGLRR ITFLIAQEKE FPKFFTFRAR DEFAEDRIYR HLEPALAFQL
ELNRMRNFDL TAVPCANHKM HLYLGAAKVK EGVEVTDHRF FIRAIIRHSD LITKEASFEY
LQNEGERLLL EAMDELEVAF NNTSVRTDCN HIFLNFVPTV IMDPFKIEES VRYMVMRYGS
RLWKLRVLQA EVKINIRQTT TGSAVPIRLF ITNESGYYLD ISLYKEVTDS RSGNIMFHSF
GNKQGPQHGM LINTPYVTKD LLQAKRFQAQ TLGTTYIYDF PEMFRQALFK LWGSPDKYPK
DILTYTELVL DSQGQLVEMN RLPGGNEVGM VAFKMRFKTQ EYPEGRDVIV IGNDITFRIG
SFGPGEDLLY LRASEMARAE GIPKIYVAAN SGARIGMAEE IKHMFHVAWV DPEDPHKGFK
YLYLTPQDYT RISSLNSVHC KHIEEGGESR YMITDIIGKD DGLGVENLRG SGMIAGESSL
AYEEIVTISL VTCRAIGIGA YLVRLGQRVI QVENSHIILT GASALNKVLG REVYTSNNQL
GGVQIMHYNG VSHITVPDDF EGVYTILEWL SYMPKDNHSP VPIITPTDPI DREIEFLPSR
APYDPRWMLA GRPHPTLKGT WQSGFFDHGS FKEIMAPWAQ TVVTGRARLG GIPVGVIAVE
TRTVEVAVPA DPANLDSEAK IIQQAGQVWF PDSAYKTAQA VKDFNREKLP LMIFANWRGF
SGGMKDMYDQ VLKFGAYIVD GLRQYKQPIL IYIPPYAELR GGSWVVIDAT INPLCIEMYA
DKESRGGVLE PEGTVEIKFR KKDLIKSMRR IDPAYKKLME QLGEPDLSDK DRKDLEGRLK
AREDLLLPIY HQVAVQFADF HDTPGRMLEK GVISDILEWK TARTFLYWRL RRLLLEDQVK
QEILQASGEL SHVHIQSMLR RWFVETEGAV KAYLWDNNQV VVQWLEQHWQ AGDGPRSTIR
ENITYLKHDS VLKTIRGLVE ENPEVAVDCV IYLSQHISPA ERAQVVHLLS TMDSPAST


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Kits Elisa; taq POLYMERASE

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Gentaur; yes we can

Pathways :
WP1493: Carbon assimilation C4 pathway
WP296: TCA Cycle - biocyc
WP1045: TGF-beta Receptor Signaling Pathway
WP1048: TGF Beta Signaling Pathway
WP105: Fatty Acid Beta Oxidation 2
WP1058: Senescence and Autophagy
WP1061: Fatty Acid Beta Oxidation
WP1106: Keap1-Nrf2
WP1107: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP113: TGF Beta Signaling Pathway
WP1161: TGF-beta Receptor Signaling Pathway
WP1164: TGF Beta Signaling Pathway
WP1177: Fatty Acid Beta Oxidation
WP1207: Fatty Acid Beta Oxidation
WP1224: EBV LMP1 signaling
WP1225: estrogen signalling
WP1226: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP1237: Fatty Acid Beta Oxidation
WP126: Fatty Acid Beta Oxidation 1
WP1269: Fatty Acid Beta Oxidation
WP1307: Fatty Acid Beta Oxidation
WP1367: TGF-beta Receptor Signaling Pathway
WP1370: TGF Beta Signaling Pathway
WP143: Fatty Acid Beta Oxidation
WP1434: Osteopontin Signaling

Related Genes :
[Acacb Acc2 Accb] Acetyl-CoA carboxylase 2 (EC 6.4.1.2) (ACC-beta) [Includes: Biotin carboxylase (EC 6.3.4.14)]
[ACC1 ABP2 FAS3 MTR7 YNR016C N3175] Acetyl-CoA carboxylase (ACC) (EC 6.4.1.2) (Fatty acid synthetase 3) (mRNA transport-defective protein 7) [Includes: Biotin carboxylase (EC 6.3.4.14)]
[ACC1 EMB22 GK PAS3 At1g36160 F15C21.1] Acetyl-CoA carboxylase 1 (AtACC1) (EC 6.4.1.2) (Protein EMBRYO DEFECTIVE 22) (Protein GURKE) (Protein PASTICCINO 3) [Includes: Biotin carboxylase (EC 6.3.4.14)]
[Acaca Acac] Acetyl-CoA carboxylase 1 (ACC1) (EC 6.4.1.2) (ACC-alpha) [Includes: Biotin carboxylase (EC 6.3.4.14)]
[HFA1 YMR207C YM8261.01C YM8325.08C] Acetyl-CoA carboxylase, mitochondrial (ACC) (EC 6.4.1.2) [Includes: Biotin carboxylase (EC 6.3.4.14)]
[HLCS] Biotin--protein ligase (EC 6.3.4.-) (Biotin apo-protein ligase) [Includes: Biotin--[methylmalonyl-CoA-carboxytransferase] ligase (EC 6.3.4.9); Biotin--[propionyl-CoA-carboxylase [ATP-hydrolyzing]] ligase (EC 6.3.4.10) (Holocarboxylase synthetase) (HCS); Biotin--[methylcrotonoyl-CoA-carboxylase] ligase (EC 6.3.4.11); Biotin--[acetyl-CoA-carboxylase] ligase (EC 6.3.4.15)]
[CAC2 At5g35360 T26D22.8] Biotin carboxylase, chloroplastic (EC 6.3.4.14) (Acetyl-CoA carboxylase subunit A) (ACC) (EC 6.4.1.2)
[ACC2 At1g36180 F15C21.2] Acetyl-CoA carboxylase 2 (EC 6.4.1.2) [Includes: Biotin carboxylase (EC 6.3.4.14)]
[HFA1 EC1118_1M3_4049g] Acetyl-CoA carboxylase, mitochondrial (ACC) (EC 6.4.1.2) [Includes: Biotin carboxylase (EC 6.3.4.14)]
[MCCC2 MCCB] Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial (MCCase subunit beta) (EC 6.4.1.4) (3-methylcrotonyl-CoA carboxylase 2) (3-methylcrotonyl-CoA carboxylase non-biotin-containing subunit) (3-methylcrotonyl-CoA:carbon dioxide ligase subunit beta)
[MCCC1 MCCA] Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial (MCCase subunit alpha) (EC 6.4.1.4) (3-methylcrotonyl-CoA carboxylase 1) (3-methylcrotonyl-CoA carboxylase biotin-containing subunit) (3-methylcrotonyl-CoA:carbon dioxide ligase subunit alpha)
[ACC1 Os10g0363300 LOC_Os10g21910 OsJ_31236 OSJNBa0073L01.2] Acetyl-CoA carboxylase 1 (EC 6.4.1.2) [Includes: Biotin carboxylase (EC 6.3.4.14)]
[birA bioR dhbB b3973 JW3941] Bifunctional ligase/repressor BirA (Biotin operon repressor) (Biotin--[acetyl-CoA-carboxylase] ligase) (EC 6.3.4.15) (Biotin--protein ligase) (Biotin-[acetyl-CoA carboxylase] synthetase)
[ACC2 Os05g0295300 LOC_Os05g22940 OsJ_17935] Acetyl-CoA carboxylase 2 (EC 6.4.1.2) [Includes: Biotin carboxylase (EC 6.3.4.14)]
[accD dedB usg b2316 JW2313] Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta (ACCase subunit beta) (Acetyl-CoA carboxylase carboxyltransferase subunit beta) (EC 2.1.3.15)
[accD ycf11 zfpA] Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic (ACCase subunit beta) (Acetyl-CoA carboxylase carboxyltransferase subunit beta) (EC 2.1.3.15)
[accA b0185 JW0180] Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha (ACCase subunit alpha) (Acetyl-CoA carboxylase carboxyltransferase subunit alpha) (EC 2.1.3.15)
[accD A6592_11000 A8C65_11680 A8M42_11610 A9819_13610 A9R57_18405 AC067_01610 ACN002_2374 ACN77_22040 ACN81_17485 ACU57_26670 ACU90_07195 AJ318_08915 AKG99_12410 AM270_05725 AM446_09235 AM464_02920 AM465_12940 AMK83_13675 AML07_04515 AML35_07465 APT94_13525 APU18_03020 APZ14_22065 ARC77_07895 AU473_10370 AUQ13_04600 AUS26_02075 AW059_07255 AW106_12960 AWP75_23110 B1K96_04830 B7C53_22355 B9M99_08445 B9N33_02175 B9T59_22175 BB545_16860 BE963_27395 BEN53_14785 BER14_17395 BET08_21000 BH694_03705 BHF46_01565 BHS81_14340 BHS87_13215 BIU72_23275 BIZ41_10400 BJJ90_07685 BK248_00685 BK292_05455 BK334_03625 BK375_19740 BK383_00085 BK400_08035 BMT49_14870 BMT53_24450 BMT91_07940 BN17_16211 BTQ04_02065 BTQ06_04250 BUE81_00910 BVL39_15780 BW690_09570 BWP17_05895 BXT93_15275 BZL31_15320 BZL69_14870 C2M16_08740 C2U48_22830 C3K24_06280 C4J69_20755 C4K41_06095 C4M78_23045 C5715_07235 C5N07_04020 C5P01_06965 C5P43_07205 C5P44_06955 C6669_17490 C6986_15090 C6B13_00955 C7235_07955 C7B02_03615 C7B06_10160 C7B07_13395 C7B08_04395 C9E25_01020 CA593_15605 CCZ14_19125 CCZ17_09750 CDL37_03775 CG691_00540 CG692_16120 CG705_00540 CG706_06250 CIJ94_13080 COD30_04170 COD46_01380 CR539_16410 CRD98_01035 CRE06_18705 CRM83_28840 CSB64_11255 CT143_04840 CT146_08800 CVH05_16405 CWM24_16870 CWS33_01390 CXB56_11320 D0X26_14060 D1900_18750 D2183_09190 D2F89_06325 D3I61_13360 DD762_01525 DIV22_21250 DIV25_14090 DL545_08390 DL800_17595 DNQ41_16775 DNQ45_20785 DNR41_06090 DQE83_15930 DS966_01915 DTL43_00535 DTL84_02310 DTL90_12935 DTM25_04385 DTM27_10375 DTM45_16530 EC1094V2_1362 EC3234A_175c00960 EC95NR1_01423 ECONIH1_13475 ECs3200 EL75_1315 EL79_1324 EL80_1347 ERS085365_00035 ERS085366_01185 ERS085374_00256 ERS085379_00221 ERS085383_01916 ERS085386_00175 ERS085404_01886 ERS085406_01061 ERS085416_03311 ERS139211_00974 ERS150873_00376 ERS150876_02626 FORC28_1699 GJ11_15515 HW43_15815 JD73_19120 MS6198_26500 MS8345_02432 NCTC10082_03977 NCTC10090_04587 NCTC10418_02465 NCTC10764_00825 NCTC10766_00246 NCTC10767_02793 NCTC10865_01993 NCTC11022_02313 NCTC11126_04245 NCTC11181_03783 NCTC11341_00667 NCTC13127_01978 NCTC13462_05265 NCTC13846_01642 NCTC7922_01198 NCTC7927_01783 NCTC7928_01092 NCTC8179_00790 NCTC8450_03975 NCTC8621_01654 NCTC8622_03850 NCTC8959_02253 NCTC8960_04339 NCTC8985_06455 NCTC9007_03430 NCTC9010_01654 NCTC9036_01608 NCTC9037_01680 NCTC9045_01838 NCTC9050_04842 NCTC9055_03491 NCTC9058_05280 NCTC9062_01575 NCTC9073_04231 NCTC9075_02235 NCTC9111_05405 NCTC9117_02148 NCTC9119_01725 NCTC9434_01580 NCTC9701_01685 NCTC9703_00830 NCTC9706_04820 NCTC9775_05421 NCTC9777_05034 NCTC9969_01750 PU06_12770 RG28_10250 RK56_005330 RX35_01224 SAMEA3472033_00453 SAMEA3472044_01675 SAMEA3472047_02573 SAMEA3472056_00609 SAMEA3472067_00028 SAMEA3472070_00270 SAMEA3472080_03253 SAMEA3472108_00768 SAMEA3472110_03636 SAMEA3472112_03651 SAMEA3472147_01507 SAMEA3484427_04420 SAMEA3484429_04511 SAMEA3484433_00770 SAMEA3484434_02461 SAMEA3485101_03103 SAMEA3485113_00630 SAMEA3752372_03694 SAMEA3752557_00659 SAMEA3752559_01767 SAMEA3753097_01640 SAMEA3753106_00362 SAMEA3753300_00057 SAMEA3753391_01056 SAMEA3753397_03889 SK85_02566 SY51_13225 UC41_09130 UN86_09770 UN91_13420 WQ89_02245 WR15_08745 YDC107_849] Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta (ACCase subunit beta) (Acetyl-CoA carboxylase carboxyltransferase subunit beta) (EC 2.1.3.15)
[HFA1 C1Q_02929] Acetyl-CoA carboxylase, mitochondrial (ACC) (EC 6.4.1.2) [Includes: Biotin carboxylase (EC 6.3.4.14)]
[pccA accA2 HFX_2490 BM92_13250 C439_14249] Propionyl-CoA carboxylase, biotin carboxylase and biotin-carboxyl carrier subunit (PCC) (EC 6.4.1.3) [Includes: Biotin carboxylase (BC) (EC 6.3.4.14); Biotin-carboxyl carrier protein (BCCP)]
[HFA1 SCRG_02101] Acetyl-CoA carboxylase, mitochondrial (ACC) (EC 6.4.1.2) [Includes: Biotin carboxylase (EC 6.3.4.14)]
[Gcnt3] Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 3 (EC 2.4.1.102) (EC 2.4.1.148) (EC 2.4.1.150) (C2GnT-mucin type) (C2GnT-M) (Mucus-type core 2 beta-1,6-N-acetylglucosaminyltransferase)
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[HFA1 SCY_4385] Acetyl-CoA carboxylase, mitochondrial (ACC) (EC 6.4.1.2) [Includes: Biotin carboxylase (EC 6.3.4.14)]
[Prkaa2] 5'-AMP-activated protein kinase catalytic subunit alpha-2 (AMPK subunit alpha-2) (EC 2.7.11.1) (Acetyl-CoA carboxylase kinase) (ACACA kinase) (EC 2.7.11.27) (Hydroxymethylglutaryl-CoA reductase kinase) (HMGCR kinase) (EC 2.7.11.31)
[Prkaa1] 5'-AMP-activated protein kinase catalytic subunit alpha-1 (AMPK subunit alpha-1) (EC 2.7.11.1) (Acetyl-CoA carboxylase kinase) (ACACA kinase) (EC 2.7.11.27) (Hydroxymethylglutaryl-CoA reductase kinase) (HMGCR kinase) (EC 2.7.11.31) (Tau-protein kinase PRKAA1) (EC 2.7.11.26)
[pyrG A6592_02570 A8M42_16405 A9R57_06965 AC067_22330 AC789_1c31020 ACN002_2797 ACN77_07080 ACN81_20385 ACU57_24415 ACU90_23015 AJ318_22735 AKG99_03555 AM270_00945 AM446_06950 AM464_05605 AM465_10605 AML07_12460 AML35_05300 APT94_17890 APU18_18535 APZ14_09290 ARC77_10140 AU473_08010 AUQ13_17535 AUS26_15660 AW059_10675 AW106_00665 AWP75_20610 AZZ83_003241 B1K96_20050 B7C53_10055 B9M99_21725 B9N33_09475 B9T59_19685 BB545_13920 BE963_03670 BEN53_16995 BET08_07180 BH694_13410 BHF46_05050 BHS81_16640 BHS87_15735 BIQ87_15835 BIU72_09520 BIZ41_16885 BJJ90_05265 BK248_12970 BK292_23205 BK334_11935 BK373_15870 BK375_10085 BK383_11680 BK400_05820 BMT49_17330 BMT53_21250 BMT91_11105 BN17_26661 BTQ04_11510 BTQ06_23845 BUE81_06975 BVL39_12970 BW690_04975 BWP17_05185 BXT93_24405 BZL31_00820 BZL69_02125 C1I57_04860 C2M16_17770 C2U48_20025 C3K24_08940 C4J69_11655 C4K41_05275 C4M78_00835 C5715_23540 C5N07_06155 C5P01_05005 C5P43_15935 C5P44_09340 C6669_14670 C6986_17750 C6B13_03370 C7235_05745 C7B02_19400 C7B06_11630 C7B07_14530 C7B08_01430 C9E25_03325 CA593_12975 CCZ14_04445 CCZ17_10850 CDL37_13440 CG691_07365 CG692_07005 CG705_05530 CG706_07860 CIJ94_12220 COD30_01795 COD46_07095 CR538_05495 CR539_18815 CRE06_03485 CRM83_26360 CSB64_15850 CT143_09630 CT146_00680 CV83915_03339 CVH05_06295 CWM24_00790 CWS33_03125 CXB56_08765 D0X26_06660 D1900_12730 D2183_19100 D2F89_14380 D3I61_16000 DD762_13665 DIV22_29760 DIV25_29790 DL545_05995 DL800_20505 DNQ41_18960 DNR41_08670 DQE83_04685 DS732_20695 DS966_06010 DTL43_09355 DTL84_00105 DTL90_02675 DTM10_03745 DTM25_22630 DTM27_13675 DTM45_13530 EC1094V2_904 EC3234A_48c00890 EC95NR1_02021 ECONIH1_15890 ECs3640 EL75_0914 EL79_0915 EL80_0918 ERS085365_02427 ERS085366_03042 ERS085374_03279 ERS085386_03410 ERS085416_02898 ERS139211_02072 ERS150873_02003 ERS150876_01467 FORC28_1110 GJ11_18025 HMPREF3040_01161 HW43_18180 JD73_16335 MJ49_17095 MS6198_30910 MS8345_02965 NCTC10082_03473 NCTC10090_04050 NCTC10418_01701 NCTC10764_00296 NCTC10766_00690 NCTC10767_02309 NCTC11022_02860 NCTC11112_00121 NCTC11181_03277 NCTC12950_01251 NCTC13125_04353 NCTC13127_01436 NCTC13462_04807 NCTC13846_01212 NCTC7152_00995 NCTC7927_01209 NCTC8500_01090 NCTC8960_03783 NCTC9007_03892 NCTC9010_01168 NCTC9036_01135 NCTC9037_01243 NCTC9045_01221 NCTC9050_04166 NCTC9058_00847 NCTC9062_02131 NCTC9075_01630 NCTC9077_01409 NCTC9081_05851 NCTC9117_01609 NCTC9119_01271 NCTC9434_01004 NCTC9706_03296 NCTC9775_04845 NCTC9777_02704 NCTC9969_01292 PU06_02080 RG28_07675 RK56_023165 SAMEA3472033_01264 SAMEA3472044_02272 SAMEA3472047_00339 SAMEA3472056_05455 SAMEA3472067_02540 SAMEA3472070_01673 SAMEA3472080_03155 SAMEA3472090_00131 SAMEA3472108_00527 SAMEA3472110_03462 SAMEA3472112_03722 SAMEA3472114_02432 SAMEA3472147_03296 SAMEA3484427_03298 SAMEA3484429_03415 SAMEA3484433_01660 SAMEA3484434_01581 SAMEA3485101_02257 SAMEA3485113_02257 SAMEA3752372_03639 SAMEA3752557_03040 SAMEA3752559_02995 SAMEA3752620_01282 SAMEA3753064_02287 SAMEA3753097_02219 SAMEA3753106_03183 SAMEA3753164_01192 SAMEA3753290_02847 SAMEA3753300_01107 SAMEA3753391_02580 SAMEA3753397_04005 SK85_03024 SY51_15605 UC41_20365 UN91_03645 WM48_14990 WQ89_10170 WR15_06090 YDC107_1339] CTP synthase (EC 6.3.4.2) (Cytidine 5'-triphosphate synthase) (Cytidine triphosphate synthetase) (CTP synthetase) (CTPS) (UTP--ammonia ligase)
[mcl1 RHOS4_03500 RSP_1771] L-malyl-CoA/beta-methylmalyl-CoA lyase (EC 4.1.3.24) ((3S)-malyl-CoA/beta-methylmalyl-CoA lyase) ((S)-citramalyl-CoA lyase) (EC 4.1.3.25)
[PCCB] Propionyl-CoA carboxylase beta chain, mitochondrial (PCCase subunit beta) (EC 6.4.1.3) (Propanoyl-CoA:carbon dioxide ligase subunit beta)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]

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