Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

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)

 MCCB_HUMAN              Reviewed;         563 AA.
Q9HCC0; A6NIY9; Q96C27; Q9Y4L7;
05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
27-SEP-2017, entry version 163.
RecName: Full=Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial;
Short=MCCase subunit beta;
EC=6.4.1.4;
AltName: Full=3-methylcrotonyl-CoA carboxylase 2;
AltName: Full=3-methylcrotonyl-CoA carboxylase non-biotin-containing subunit;
AltName: Full=3-methylcrotonyl-CoA:carbon dioxide ligase subunit beta;
Flags: Precursor;
Name=MCCC2; Synonyms=MCCB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
Fukuda T., Otsuka H., Morishita R., Takemoto Y., Sone M., Nakao M.,
Abe S., Kondo I.;
"Human non-biotin containing subunit gene of 3-methylcrotonyl-CoA
carboxylase (MCCB).";
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
VARIANTS MCC2D ARG-167 AND THR-218.
PubMed=11170888; DOI=10.1086/318202;
Gallardo M.E., Desviat L.R., Rodriguez J.M., Esparza-Gordillo J.,
Perez-Cerda C., Perez B., Rodriguez-Pombo P., Criado O., Sanz R.,
Morton D.H., Gibson K.M., Le T.P., Ribes A., Rodriguez de Cordoba S.,
Ugarte M., Penalva M.A.;
"The molecular basis of 3-methylcrotonylglycinuria, a disorder of
leucine catabolism.";
Am. J. Hum. Genet. 68:334-346(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS MCC2D GLN-99;
GLN-155; LEU-173; CYS-193; ARG-310 AND MET-339.
PubMed=11181649; DOI=10.1172/JCI11948;
Baumgartner M.R., Almashanu S., Suormala T., Obie C., Cole R.N.,
Packman S., Baumgartner E.R., Valle D.;
"The molecular basis of human 3-methylcrotonyl-CoA carboxylase
deficiency.";
J. Clin. Invest. 107:495-504(2001).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT MCC2D THR-268.
PubMed=11406611; DOI=10.1093/hmg/10.12.1299;
Holzinger A., Roeschinger W., Lagler F., Mayerhofer P.U., Lichtner P.,
Kattenfeld T., Thuy L.P., Nyhan W.L., Koch H.G., Muntau A.C.,
Roscher A.A.;
"Cloning of the human MCCA and MCCB genes and mutations therein reveal
the molecular cause of 3-methylcrotonyl-CoA: carboxylase deficiency.";
Hum. Mol. Genet. 10:1299-1306(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Testis, and Uterus;
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).
[8]
PROTEIN SEQUENCE OF 23-28, AND SUBCELLULAR LOCATION.
TISSUE=Kidney;
PubMed=16023992; DOI=10.1016/j.bbrc.2005.06.190;
Stadler S.C., Polanetz R., Meier S., Mayerhofer P.U., Herrmann J.M.,
Anslinger K., Roscher A.A., Roschinger W., Holzinger A.;
"Mitochondrial targeting signals and mature peptides of 3-
methylcrotonyl-CoA carboxylase.";
Biochem. Biophys. Res. Commun. 334:939-946(2005).
[9]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=17360195; DOI=10.1016/j.pep.2007.01.012;
Chu C.H., Cheng D.;
"Expression, purification, characterization of human 3-methylcrotonyl-
CoA carboxylase (MCCC).";
Protein Expr. Purif. 53:421-427(2007).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 469-563.
The European IMAGE consortium;
Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
[11]
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).
[12]
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]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[14]
VARIANTS MCC2D ARG-190; VAL-218 AND TYR-280.
PubMed=17968484; DOI=10.1007/s10038-007-0211-9;
Uematsu M., Sakamoto O., Sugawara N., Kumagai N., Morimoto T.,
Yamaguchi S., Hasegawa Y., Kobayashi H., Ihara K., Yoshino M.,
Watanabe Y., Inokuchi T., Yokoyama T., Kiwaki K., Nakamura K.,
Endo F., Tsuchiya S., Ohura T.;
"Novel mutations in five Japanese patients with 3-methylcrotonyl-CoA
carboxylase deficiency.";
J. Hum. Genet. 52:1040-1043(2007).
[15]
VARIANTS MCC2D GLN-99; TRP-155; GLN-155; TYR-190; THR-268; ARG-282;
ARG-310; PHE-375 AND VAL-456, AND CHARACTERIZATION OF VARIANTS TYR-190
AND ARG-352.
PubMed=16010683; DOI=10.1002/humu.9352;
Dantas M.F., Suormala T., Randolph A., Coelho D., Fowler B., Valle D.,
Baumgartner M.R.;
"3-Methylcrotonyl-CoA carboxylase deficiency: mutation analysis in 28
probands, 9 symptomatic and 19 detected by newborn screening.";
Hum. Mutat. 26:164-174(2005).
[16]
VARIANTS MCC2D PHE-355; ARG-477; ARG-517 AND SER-520.
PubMed=21071250; DOI=10.1016/j.ymgme.2010.10.008;
Nguyen K.V., Naviaux R.K., Patra S., Barshop B.A., Nyhan W.L.;
"Novel mutations in the human MCCA and MCCB gene causing
methylcrotonylglycinuria.";
Mol. Genet. Metab. 102:218-221(2011).
[17]
VARIANTS MCC2D TYR-280 AND SER-459.
PubMed=22150417; DOI=10.1111/j.1399-0004.2011.01704.x;
Cho S.Y., Park H.D., Lee Y.W., Ki C.S., Lee S.Y., Sohn Y.B.,
Park S.W., Kim S.H., Ji S., Kim S.J., Choi E.W., Kim C.H., Ko A.R.,
Paik K.H., Lee D.H., Jin D.K.;
"Mutational spectrum in eight Korean patients with 3-methylcrotonyl-
CoA carboxylase deficiency.";
Clin. Genet. 81:96-98(2012).
[18]
VARIANTS MCC2D VAL-218; MET-339 AND GLY-523.
PubMed=22264772; DOI=10.1016/j.ymgme.2011.12.018;
Morscher R.J., Grunert S.C., Burer C., Burda P., Suormala T.,
Fowler B., Baumgartner M.R.;
"A single mutation in MCCC1 or MCCC2 as a potential cause of positive
screening for 3-methylcrotonyl-CoA carboxylase deficiency.";
Mol. Genet. Metab. 105:602-606(2012).
[19]
VARIANTS MCC2D PHE-39; GLN-99; PHE-101; GLY-118 DEL; PHE-131; ASN-146;
THR-152; TRP-155; ARG-167; ASP-169; LEU-173; ARG-190; TYR-190;
CYS-193; HIS-193; ASN-200; THR-218; VAL-218; GLU-220; LEU-224;
ASP-237; LEU-266; TYR-280; ARG-282; ARG-310; MET-339; VAL-340 ARG-352;
PHE-355; PHE-375; THR-403; LEU-434; VAL-456; ARG-475; ARG-477;
ARG-517; SER-520; GLY-523 AND GLU-555, AND CHARACTERIZATION OF
VARIANTS MCC2D PHE-39; GLY-118 DEL; ASN-146; ARG-282; LEU-434;
VAL-456; ARG-475 AND GLY-523.
PubMed=22642865; DOI=10.1186/1750-1172-7-31;
Gruenert S.C., Stucki M., Morscher R.J., Suormala T., Buerer C.,
Burda P., Christensen E., Ficicioglu C., Herwig J., Koelker S.,
Moeslinger D., Pasquini E., Santer R., Schwab K.O., Wilcken B.,
Fowler B., Yue W.W., Baumgartner M.R.;
"3-methylcrotonyl-CoA carboxylase deficiency: clinical, biochemical,
enzymatic and molecular studies in 88 individuals.";
Orphanet J. Rare Dis. 7:31-54(2012).
[20]
VARIANTS MCC2D ILE-139 AND ARG-319.
PubMed=25382614; DOI=10.1111/cge.12535;
Yang L., Yang J., Zhang T., Weng C., Hong F., Tong F., Yang R.,
Yin X., Yu P., Huang X., Qi M.;
"Identification of eight novel mutations and transcript analysis of
two splicing mutations in Chinese newborns with MCC deficiency.";
Clin. Genet. 88:484-488(2015).
[21]
VARIANTS MCC2D VAL-68; ARG-105; TRP-155; ASP-163; ASN-200; ALA-214;
TRP-216; THR-218; ASP-230; CYS-318; MET-339; VAL-387; PRO-393;
ARG-410; ASP-410; THR-441; VAL-461; ARG-475 AND THR-524.
PubMed=27601257; DOI=10.1016/j.gene.2016.09.003;
Fonseca H., Azevedo L., Serrano C., Sousa C., Marcao A., Vilarinho L.;
"3-Methylcrotonyl-CoA carboxylase deficiency: Mutational spectrum
derived from comprehensive newborn screening.";
Gene 594:203-210(2016).
-!- FUNCTION: Carboxyltransferase subunit of the 3-methylcrotonyl-CoA
carboxylase, an enzyme that catalyzes the conversion of 3-
methylcrotonyl-CoA to 3-methylglutaconyl-CoA, a critical step for
leucine and isovaleric acid catabolism.
{ECO:0000269|PubMed:17360195}.
-!- CATALYTIC ACTIVITY: ATP + 3-methylcrotonoyl-CoA + HCO(3)(-) = ADP
+ phosphate + 3-methylglutaconyl-CoA.
{ECO:0000269|PubMed:17360195}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=45 uM for ATP {ECO:0000269|PubMed:17360195};
KM=74 uM for 3-methylcrotonyl-CoA {ECO:0000269|PubMed:17360195};
Note=kcat is 4.0 sec(-1).;
-!- PATHWAY: Amino-acid degradation; L-leucine degradation; (S)-3-
hydroxy-3-methylglutaryl-CoA from 3-isovaleryl-CoA: step 2/3.
-!- SUBUNIT: Probably a dodecamer composed of six biotin-containing
alpha subunits (MCCC1) and six beta (MCCC2) subunits.
-!- SUBCELLULAR LOCATION: Mitochondrion matrix
{ECO:0000269|PubMed:11170888, ECO:0000269|PubMed:16023992}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9HCC0-1; Sequence=Displayed;
Name=2;
IsoId=Q9HCC0-2; Sequence=VSP_000069;
Note=No experimental confirmation available.;
-!- DISEASE: 3-methylcrotonoyl-CoA carboxylase 2 deficiency (MCC2D)
[MIM:210210]: An autosomal recessive disorder of leucine
catabolism. The phenotype is variable, ranging from neonatal onset
with severe neurological involvement to asymptomatic adults. There
is a characteristic organic aciduria with massive excretion of 3-
hydroxyisovaleric acid and 3-methylcrotonylglycine, usually in
combination with a severe secondary carnitine deficiency.
{ECO:0000269|PubMed:11170888, ECO:0000269|PubMed:11181649,
ECO:0000269|PubMed:11406611, ECO:0000269|PubMed:16010683,
ECO:0000269|PubMed:17968484, ECO:0000269|PubMed:21071250,
ECO:0000269|PubMed:22150417, ECO:0000269|PubMed:22264772,
ECO:0000269|PubMed:22642865, ECO:0000269|PubMed:25382614,
ECO:0000269|PubMed:27601257}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH14897.1; Type=Frameshift; Positions=359; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB050049; BAB16880.1; -; mRNA.
EMBL; AB050050; BAB41121.1; -; Genomic_DNA.
EMBL; AF310971; AAG53094.1; -; mRNA.
EMBL; AF301000; AAK16404.1; -; mRNA.
EMBL; AF261884; AAK49409.1; -; mRNA.
EMBL; AC138832; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471084; EAW95693.1; -; Genomic_DNA.
EMBL; BC014897; AAH14897.1; ALT_FRAME; mRNA.
EMBL; BC065027; AAH65027.1; -; mRNA.
EMBL; AL079298; CAB45194.1; -; mRNA.
CCDS; CCDS34184.1; -. [Q9HCC0-1]
RefSeq; NP_071415.1; NM_022132.4. [Q9HCC0-1]
RefSeq; XP_005248624.1; XM_005248567.1. [Q9HCC0-2]
UniGene; Hs.604789; -.
ProteinModelPortal; Q9HCC0; -.
SMR; Q9HCC0; -.
BioGrid; 122050; 35.
IntAct; Q9HCC0; 19.
MINT; MINT-8051924; -.
STRING; 9606.ENSP00000343657; -.
DrugBank; DB00121; Biotin.
iPTMnet; Q9HCC0; -.
PhosphoSitePlus; Q9HCC0; -.
BioMuta; MCCC2; -.
DMDM; 20138731; -.
REPRODUCTION-2DPAGE; IPI00784044; -.
EPD; Q9HCC0; -.
MaxQB; Q9HCC0; -.
PaxDb; Q9HCC0; -.
PeptideAtlas; Q9HCC0; -.
PRIDE; Q9HCC0; -.
Ensembl; ENST00000340941; ENSP00000343657; ENSG00000131844. [Q9HCC0-1]
GeneID; 64087; -.
KEGG; hsa:64087; -.
UCSC; uc003kbs.5; human. [Q9HCC0-1]
CTD; 64087; -.
DisGeNET; 64087; -.
EuPathDB; HostDB:ENSG00000131844.15; -.
GeneCards; MCCC2; -.
HGNC; HGNC:6937; MCCC2.
HPA; HPA038300; -.
HPA; HPA038301; -.
HPA; HPA061546; -.
MalaCards; MCCC2; -.
MIM; 210210; phenotype.
MIM; 609014; gene.
neXtProt; NX_Q9HCC0; -.
OpenTargets; ENSG00000131844; -.
Orphanet; 6; Isolated 3-methylcrotonyl-CoA carboxylase deficiency.
PharmGKB; PA30681; -.
eggNOG; KOG0540; Eukaryota.
eggNOG; COG4799; LUCA.
GeneTree; ENSGT00530000063337; -.
HOGENOM; HOG000218692; -.
HOVERGEN; HBG052424; -.
InParanoid; Q9HCC0; -.
KO; K01969; -.
OMA; MCGKAYD; -.
OrthoDB; EOG091G05B5; -.
PhylomeDB; Q9HCC0; -.
TreeFam; TF300446; -.
BioCyc; MetaCyc:ENSG00000131844-MONOMER; -.
Reactome; R-HSA-196780; Biotin transport and metabolism.
Reactome; R-HSA-3371599; Defective HLCS causes multiple carboxylase deficiency.
Reactome; R-HSA-70895; Branched-chain amino acid catabolism.
UniPathway; UPA00363; UER00861.
GenomeRNAi; 64087; -.
PRO; PR:Q9HCC0; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000131844; -.
CleanEx; HS_MCCC2; -.
ExpressionAtlas; Q9HCC0; baseline and differential.
Genevisible; Q9HCC0; HS.
GO; GO:0002169; C:3-methylcrotonyl-CoA carboxylase complex, mitochondrial; TAS:ParkinsonsUK-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:1905202; C:methylcrotonoyl-CoA carboxylase complex; IDA:ParkinsonsUK-UCL.
GO; GO:0005759; C:mitochondrial matrix; IDA:ParkinsonsUK-UCL.
GO; GO:0005739; C:mitochondrion; IDA:ParkinsonsUK-UCL.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004485; F:methylcrotonoyl-CoA carboxylase activity; IEA:UniProtKB-EC.
GO; GO:0006768; P:biotin metabolic process; TAS:Reactome.
GO; GO:0009083; P:branched-chain amino acid catabolic process; TAS:Reactome.
GO; GO:0015936; P:coenzyme A metabolic process; IEA:Ensembl.
GO; GO:0006552; P:leucine catabolic process; TAS:UniProtKB.
GO; GO:0051291; P:protein heterooligomerization; NAS:ParkinsonsUK-UCL.
InterPro; IPR034733; AcCoA_carboxyl.
InterPro; IPR029045; ClpP/crotonase-like_dom.
InterPro; IPR011763; COA_CT_C.
InterPro; IPR011762; COA_CT_N.
Pfam; PF01039; Carboxyl_trans; 1.
SUPFAM; SSF52096; SSF52096; 2.
PROSITE; PS50989; COA_CT_CTER; 1.
PROSITE; PS50980; COA_CT_NTER; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; ATP-binding; Complete proteome;
Direct protein sequencing; Disease mutation; Ligase; Mitochondrion;
Nucleotide-binding; Reference proteome; Transit peptide.
TRANSIT 1 22 Mitochondrion.
{ECO:0000269|PubMed:16023992}.
CHAIN 23 563 Methylcrotonoyl-CoA carboxylase beta
chain, mitochondrial.
/FTId=PRO_0000000291.
DOMAIN 49 306 CoA carboxyltransferase N-terminal.
{ECO:0000255|PROSITE-ProRule:PRU01136}.
DOMAIN 309 555 CoA carboxyltransferase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU01137}.
REGION 49 555 Carboxyltransferase.
{ECO:0000255|PROSITE-ProRule:PRU01138}.
REGION 343 372 Acyl-CoA binding. {ECO:0000255}.
MOD_RES 70 70 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q3ULD5}.
MOD_RES 70 70 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q3ULD5}.
MOD_RES 141 141 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q3ULD5}.
MOD_RES 495 495 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q3ULD5}.
MOD_RES 495 495 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q3ULD5}.
MOD_RES 511 511 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q3ULD5}.
VAR_SEQ 209 246 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_000069.
VARIANT 39 39 S -> F (in MCC2D; has some wild-type
residual activity; dbSNP:rs398124371).
{ECO:0000269|PubMed:22642865}.
/FTId=VAR_072507.
VARIANT 68 68 G -> V (in MCC2D; unknown pathological
significance).
{ECO:0000269|PubMed:27601257}.
/FTId=VAR_077291.
VARIANT 99 99 E -> Q (in MCC2D; severe and mild form;
dbSNP:rs119103219).
{ECO:0000269|PubMed:11181649,
ECO:0000269|PubMed:16010683,
ECO:0000269|PubMed:22642865}.
/FTId=VAR_012792.
VARIANT 101 101 S -> F (in MCC2D; dbSNP:rs748028684).
{ECO:0000269|PubMed:22642865}.
/FTId=VAR_072508.
VARIANT 105 105 G -> R (in MCC2D; unknown pathological
significance).
{ECO:0000269|PubMed:27601257}.
/FTId=VAR_077292.
VARIANT 118 118 Missing (in MCC2D; has some wild-type
residual activity).
{ECO:0000269|PubMed:22642865}.
/FTId=VAR_072509.
VARIANT 131 131 C -> F (in MCC2D).
{ECO:0000269|PubMed:22642865}.
/FTId=VAR_072510.
VARIANT 139 139 T -> I (in MCC2D).
{ECO:0000269|PubMed:25382614}.
/FTId=VAR_077293.
VARIANT 146 146 Y -> N (in MCC2D; has some wild-type
residual activity).
{ECO:0000269|PubMed:22642865}.
/FTId=VAR_072511.
VARIANT 152 152 K -> T (in MCC2D).
{ECO:0000269|PubMed:22642865}.
/FTId=VAR_072512.
VARIANT 155 155 R -> Q (in MCC2D; mild form;
dbSNP:rs119103220).
{ECO:0000269|PubMed:11181649,
ECO:0000269|PubMed:16010683}.
/FTId=VAR_012793.
VARIANT 155 155 R -> W (in MCC2D; dbSNP:rs141030969).
{ECO:0000269|PubMed:16010683,
ECO:0000269|PubMed:22642865,
ECO:0000269|PubMed:27601257}.
/FTId=VAR_072513.
VARIANT 163 163 N -> D (in MCC2D; unknown pathological
significance).
{ECO:0000269|PubMed:27601257}.
/FTId=VAR_077294.
VARIANT 167 167 C -> R (in MCC2D; dbSNP:rs119103222).
{ECO:0000269|PubMed:11170888,
ECO:0000269|PubMed:22642865}.
/FTId=VAR_012794.
VARIANT 169 169 Y -> D (in MCC2D).
{ECO:0000269|PubMed:22642865}.
/FTId=VAR_072514.
VARIANT 173 173 S -> L (in MCC2D; severe form;
dbSNP:rs752866557).
{ECO:0000269|PubMed:11181649,
ECO:0000269|PubMed:22642865}.
/FTId=VAR_012795.
VARIANT 190 190 H -> R (in MCC2D; dbSNP:rs119103225).
{ECO:0000269|PubMed:17968484,
ECO:0000269|PubMed:22642865}.
/FTId=VAR_072515.
VARIANT 190 190 H -> Y (in MCC2D; produces severely
decreased wild-type residual activity;
dbSNP:rs773774134).
{ECO:0000269|PubMed:16010683,
ECO:0000269|PubMed:22642865}.
/FTId=VAR_072516.
VARIANT 193 193 R -> C (in MCC2D; mild form;
dbSNP:rs547662164).
{ECO:0000269|PubMed:11181649,
ECO:0000269|PubMed:22642865}.
/FTId=VAR_012796.
VARIANT 193 193 R -> H (in MCC2D; dbSNP:rs535519604).
{ECO:0000269|PubMed:22642865}.
/FTId=VAR_072517.
VARIANT 200 200 I -> N (in MCC2D; dbSNP:rs140806722).
{ECO:0000269|PubMed:22642865,
ECO:0000269|PubMed:27601257}.
/FTId=VAR_072518.
VARIANT 214 214 G -> A (in MCC2D; dbSNP:rs277995).
{ECO:0000269|PubMed:27601257}.
/FTId=VAR_077295.
VARIANT 216 216 C -> W (in MCC2D).
{ECO:0000269|PubMed:27601257}.
/FTId=VAR_077296.
VARIANT 218 218 A -> T (in MCC2D).
{ECO:0000269|PubMed:11170888,
ECO:0000269|PubMed:22642865,
ECO:0000269|PubMed:27601257}.
/FTId=VAR_012797.
VARIANT 218 218 A -> V (in MCC2D; dbSNP:rs760420191).
{ECO:0000269|PubMed:17968484,
ECO:0000269|PubMed:22264772,
ECO:0000269|PubMed:22642865}.
/FTId=VAR_072519.
VARIANT 220 220 G -> E (in MCC2D).
{ECO:0000269|PubMed:22642865}.
/FTId=VAR_072520.
VARIANT 224 224 P -> L (in MCC2D).
{ECO:0000269|PubMed:22642865}.
/FTId=VAR_072521.
VARIANT 230 230 N -> D (in MCC2D; dbSNP:rs766753795).
{ECO:0000269|PubMed:27601257}.
/FTId=VAR_077297.
VARIANT 237 237 G -> D (in MCC2D).
{ECO:0000269|PubMed:22642865}.
/FTId=VAR_072522.
VARIANT 266 266 H -> L (in MCC2D).
{ECO:0000269|PubMed:22642865}.
/FTId=VAR_072523.
VARIANT 268 268 R -> T (in MCC2D; asymptomatic form;
dbSNP:rs119103223).
{ECO:0000269|PubMed:11406611,
ECO:0000269|PubMed:16010683}.
/FTId=VAR_012798.
VARIANT 268 268 Missing (in MCC2D).
{ECO:0000269|PubMed:16010683}.
/FTId=VAR_072524.
VARIANT 280 280 D -> Y (in MCC2D; dbSNP:rs119103226).
{ECO:0000269|PubMed:17968484,
ECO:0000269|PubMed:22150417,
ECO:0000269|PubMed:22642865}.
/FTId=VAR_067199.
VARIANT 282 282 H -> R (in MCC2D; has some wild-type
residual activity).
{ECO:0000269|PubMed:16010683,
ECO:0000269|PubMed:22642865}.
/FTId=VAR_072525.
VARIANT 310 310 P -> R (in MCC2D; mild form;
dbSNP:rs119103221).
{ECO:0000269|PubMed:11181649,
ECO:0000269|PubMed:16010683,
ECO:0000269|PubMed:22642865}.
/FTId=VAR_012799.
VARIANT 318 318 Y -> C (in MCC2D; dbSNP:rs773115035).
{ECO:0000269|PubMed:27601257}.
/FTId=VAR_077298.
VARIANT 319 319 G -> R (in MCC2D).
{ECO:0000269|PubMed:25382614}.
/FTId=VAR_077299.
VARIANT 339 339 V -> M (in MCC2D; severe form;
dbSNP:rs150591260).
{ECO:0000269|PubMed:11181649,
ECO:0000269|PubMed:22264772,
ECO:0000269|PubMed:22642865,
ECO:0000269|PubMed:27601257}.
/FTId=VAR_012800.
VARIANT 340 340 D -> V (in MCC2D; dbSNP:rs398124370).
{ECO:0000269|PubMed:22642865}.
/FTId=VAR_072526.
VARIANT 352 352 G -> R (in MCC2D; produces severely
decreased wild-type residual activity;
dbSNP:rs765438239).
{ECO:0000269|PubMed:22642865}.
/FTId=VAR_072527.
VARIANT 355 355 L -> F (in MCC2D; dbSNP:rs757052602).
{ECO:0000269|PubMed:21071250,
ECO:0000269|PubMed:22642865}.
/FTId=VAR_072528.
VARIANT 375 375 V -> F (in MCC2D).
{ECO:0000269|PubMed:16010683,
ECO:0000269|PubMed:22642865}.
/FTId=VAR_072529.
VARIANT 387 387 F -> V (in MCC2D; unknown pathological
significance).
{ECO:0000269|PubMed:27601257}.
/FTId=VAR_077300.
VARIANT 393 393 Q -> P (in MCC2D).
{ECO:0000269|PubMed:27601257}.
/FTId=VAR_077301.
VARIANT 403 403 N -> T (in MCC2D).
{ECO:0000269|PubMed:22642865}.
/FTId=VAR_072530.
VARIANT 410 410 G -> D (in MCC2D; dbSNP:rs771440617).
{ECO:0000269|PubMed:27601257}.
/FTId=VAR_077302.
VARIANT 410 410 G -> R (in MCC2D).
{ECO:0000269|PubMed:27601257}.
/FTId=VAR_077303.
VARIANT 434 434 V -> L (in MCC2D; has some wild-type
residual activity; dbSNP:rs758506791).
{ECO:0000269|PubMed:22642865}.
/FTId=VAR_072531.
VARIANT 437 437 I -> V (in MCC2D; mild form;
dbSNP:rs119103224).
/FTId=VAR_012801.
VARIANT 441 441 I -> T (in MCC2D; unknown pathological
significance; dbSNP:rs139852818).
{ECO:0000269|PubMed:27601257}.
/FTId=VAR_077304.
VARIANT 456 456 A -> V (in MCC2D; shows virtually no
enzyme activity; dbSNP:rs727504011).
{ECO:0000269|PubMed:16010683,
ECO:0000269|PubMed:22642865}.
/FTId=VAR_072532.
VARIANT 459 459 P -> S (in MCC2D; dbSNP:rs754741111).
{ECO:0000269|PubMed:22150417}.
/FTId=VAR_067200.
VARIANT 461 461 F -> V (in MCC2D).
{ECO:0000269|PubMed:27601257}.
/FTId=VAR_077305.
VARIANT 475 475 G -> R (in MCC2D; has some wild-type
residual activity; dbSNP:rs148773718).
{ECO:0000269|PubMed:22642865,
ECO:0000269|PubMed:27601257}.
/FTId=VAR_072533.
VARIANT 477 477 Q -> R (in MCC2D; dbSNP:rs769558016).
{ECO:0000269|PubMed:21071250,
ECO:0000269|PubMed:22642865}.
/FTId=VAR_072534.
VARIANT 478 478 A -> G (in dbSNP:rs35068278).
/FTId=VAR_038630.
VARIANT 517 517 G -> R (in MCC2D).
{ECO:0000269|PubMed:21071250,
ECO:0000269|PubMed:22642865}.
/FTId=VAR_072535.
VARIANT 520 520 Y -> S (in MCC2D; dbSNP:rs150327768).
{ECO:0000269|PubMed:21071250,
ECO:0000269|PubMed:22642865}.
/FTId=VAR_072536.
VARIANT 523 523 S -> G (in MCC2D; has some wild-type
residual activity).
{ECO:0000269|PubMed:22264772,
ECO:0000269|PubMed:22642865}.
/FTId=VAR_072537.
VARIANT 524 524 A -> T (in MCC2D; dbSNP:rs774241918).
{ECO:0000269|PubMed:27601257}.
/FTId=VAR_077306.
VARIANT 555 555 K -> E (in MCC2D).
{ECO:0000269|PubMed:22642865}.
/FTId=VAR_072538.
SEQUENCE 563 AA; 61333 MW; 8E3D401AF52DC7D2 CRC64;
MWAVLRLALR PCARASPAGP RAYHGDSVAS LGTQPDLGSA LYQENYKQMK ALVNQLHERV
EHIKLGGGEK ARALHISRGK LLPRERIDNL IDPGSPFLEL SQFAGYQLYD NEEVPGGGII
TGIGRVSGVE CMIIANDATV KGGAYYPVTV KKQLRAQEIA MQNRLPCIYL VDSGGAYLPR
QADVFPDRDH FGRTFYNQAI MSSKNIAQIA VVMGSCTAGG AYVPAMADEN IIVRKQGTIF
LAGPPLVKAA TGEEVSAEDL GGADLHCRKS GVSDHWALDD HHALHLTRKV VRNLNYQKKL
DVTIEPSEEP LFPADELYGI VGANLKRSFD VREVIARIVD GSRFTEFKAF YGDTLVTGFA
RIFGYPVGIV GNNGVLFSES AKKGTHFVQL CCQRNIPLLF LQNITGFMVG REYEAEGIAK
DGAKMVAAVA CAQVPKITLI IGGSYGAGNY GMCGRAYSPR FLYIWPNARI SVMGGEQAAN
VLATITKDQR AREGKQFSSA DEAALKEPII KKFEEEGNPY YSSARVWDDG IIDPADTRLV
LGLSFSAALN APIEKTDFGI FRM


Related products :

Catalog number Product name Quantity
EIAAB30046 PCCase subunit beta,PCCB,Pig,Propanoyl-CoA carbon dioxide ligase subunit beta,Propionyl-CoA carboxylase beta chain, mitochondrial,Sus scrofa
EIAAB30045 Bos taurus,Bovine,PCCase subunit beta,PCCB,Propanoyl-CoA carbon dioxide ligase subunit beta,Propionyl-CoA carboxylase beta chain, mitochondrial
EIAAB30044 PCCase subunit beta,Pccb,Propanoyl-CoA carbon dioxide ligase subunit beta,Propionyl-CoA carboxylase beta chain, mitochondrial,Rat,Rattus norvegicus
EIAAB30047 Mouse,Mus musculus,PCCase subunit beta,Pccb,Propanoyl-CoA carbon dioxide ligase subunit beta,Propionyl-CoA carboxylase beta chain, mitochondrial
EIAAB30043 Homo sapiens,Human,PCCase subunit beta,PCCB,Propanoyl-CoA carbon dioxide ligase subunit beta,Propionyl-CoA carboxylase beta chain, mitochondrial
15-288-21224 Propionyl-CoA carboxylase alpha chain. mitochondrial - EC 6.4.1.3; PCCase subunit alpha; Propanoyl-CoA carbon dioxide ligase subunit alpha Polyclonal 0.1 mg
15-288-21224 Propionyl-CoA carboxylase alpha chain. mitochondrial - EC 6.4.1.3; PCCase subunit alpha; Propanoyl-CoA carbon dioxide ligase subunit alpha Polyclonal 0.05 mg
EIAAB30042 Mouse,Mus musculus,Pcca,PCCase subunit alpha,Propanoyl-CoA carbon dioxide ligase subunit alpha,Propionyl-CoA carboxylase alpha chain, mitochondrial
EIAAB30041 Pcca,PCCase subunit alpha,Propanoyl-CoA carbon dioxide ligase subunit alpha,Propionyl-CoA carboxylase alpha chain, mitochondrial,Rat,Rattus norvegicus
EIAAB30040 Homo sapiens,Human,PCCA,PCCase subunit alpha,Propanoyl-CoA carbon dioxide ligase subunit alpha,Propionyl-CoA carboxylase alpha chain, mitochondrial
SPAG7_HUMAN Mouse ELISA Kit FOR Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial 96T
CSB-EL013573RA Rat Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial(MCCC2) ELISA kit 96T
E1570h Human ELISA Kit FOR Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial 96T
E0703r Mouse ELISA Kit FOR Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial 96T
CSB-EL013573MO Mouse Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial(MCCC2) ELISA kit 96T
CSB-EL013573RA Rat Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial(MCCC2) ELISA kit SpeciesRat 96T
CSB-EL013573HU Human Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial(MCCC2) ELISA kit 96T
CSB-EL013573MO Mouse Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial(MCCC2) ELISA kit SpeciesMouse 96T
CSB-EL013573HU Human Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial(MCCC2) ELISA kit SpeciesHuman 96T
MCCB_MOUSE ELISA Kit FOR Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial; organism: Mouse; gene name: Mccc2 96T
E0195h Human ELISA Kit FOR Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial 96T
STOX1_HUMAN Human ELISA Kit FOR Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial 96T
HCST_MOUSE Human ELISA Kit FOR Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial 96T
CSB-EL013572RA Rat Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial(MCCC1) ELISA kit 96T
CSB-EL013572RA Rat Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial(MCCC1) ELISA kit SpeciesRat 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur