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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.
27-SEP-2017, entry version 177.
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, ENZYME 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, 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).
[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: ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate
+ malonyl-CoA. {ECO:0000269|PubMed:16854592,
ECO:0000269|PubMed:20952656}.
-!- CATALYTIC ACTIVITY: ATP + biotin-[carboxyl-carrier-protein] +
HCO(3)(-) = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-
protein]. {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};
-!- ENZYME 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:
P50747:HLCS; NbExp=4; IntAct=EBI-2211739, EBI-3915568;
-!- 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; 15.
DIP; DIP-51617N; -.
IntAct; O00763; 7.
MINT; MINT-6800190; -.
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; -.
MaxQB; O00763; -.
PaxDb; O00763; -.
PeptideAtlas; O00763; -.
PRIDE; O00763; -.
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; -.
MalaCards; ACACB; -.
MIM; 601557; gene.
neXtProt; NX_O00763; -.
OpenTargets; ENSG00000076555; -.
PharmGKB; PA24422; -.
eggNOG; KOG0368; Eukaryota.
eggNOG; COG0439; LUCA.
eggNOG; COG0511; LUCA.
eggNOG; COG4799; LUCA.
GeneTree; ENSGT00550000074703; -.
HOVERGEN; HBG005371; -.
InParanoid; O00763; -.
KO; K01946; -.
OMA; QAHYDKC; -.
OrthoDB; EOG091G02ND; -.
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; -.
CleanEx; HS_ACACB; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006084; P:acetyl-CoA metabolic process; IDA:UniProtKB.
GO; GO:0006768; P:biotin metabolic process; TAS:Reactome.
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.
InterPro; IPR011763; COA_CT_C.
InterPro; IPR011762; COA_CT_N.
InterPro; IPR016185; PreATP-grasp_dom.
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 200 200 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 207 207 Phosphothreonine.
{ECO:0000250|UniProtKB:E9Q4Z2}.
MOD_RES 222 222 Phosphoserine; by AMPK.
{ECO:0000269|PubMed:12488245}.
MOD_RES 469 469 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
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}.
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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