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Protein

Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial

Gene

MCCC2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

ATP + 3-methylcrotonoyl-CoA + HCO3- = ADP + phosphate + 3-methylglutaconyl-CoA.1 Publication

Kineticsi

kcat is 4.0 sec(-1).

  1. KM=45 µM for ATP1 Publication
  2. KM=74 µM for 3-methylcrotonyl-CoA1 Publication

Pathwayi

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. methylcrotonoyl-CoA carboxylase activity Source: UniProtKB

GO - Biological processi

  1. biotin metabolic process Source: Reactome
  2. branched-chain amino acid catabolic process Source: Reactome
  3. cellular nitrogen compound metabolic process Source: Reactome
  4. coenzyme A metabolic process Source: Ensembl
  5. leucine catabolic process Source: UniProtKB
  6. small molecule metabolic process Source: Reactome
  7. vitamin metabolic process Source: Reactome
  8. water-soluble vitamin metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000131844-MONOMER.
ReactomeiREACT_11153. Biotin transport and metabolism.
REACT_169312. Defective HLCS causes multiple carboxylase deficiency.
REACT_197. Branched-chain amino acid catabolism.
UniPathwayiUPA00363; UER00861.

Names & Taxonomyi

Protein namesi
Recommended name:
Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial (EC:6.4.1.4)
Short name:
MCCase subunit beta
Alternative name(s):
3-methylcrotonyl-CoA carboxylase 2
3-methylcrotonyl-CoA carboxylase non-biotin-containing subunit
3-methylcrotonyl-CoA:carbon dioxide ligase subunit beta
Gene namesi
Name:MCCC2
Synonyms:MCCB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:6937. MCCC2.

Subcellular locationi

Mitochondrion matrix 2 Publications

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. mitochondrial matrix Source: Reactome
  3. mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Methylcrotonoyl-CoA carboxylase 2 deficiency9 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn 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.

See also OMIM:210210
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti39 – 391S → F in MCC2D; has some wild-type residual activity. 1 Publication
VAR_072507
Natural varianti99 – 991E → Q in MCC2D; severe and mild form. 3 Publications
Corresponds to variant rs28934883 [ dbSNP | Ensembl ].
VAR_012792
Natural varianti101 – 1011S → F in MCC2D. 1 Publication
VAR_072508
Natural varianti118 – 1181Missing in MCC2D; has some wild-type residual activity. 1 Publication
VAR_072509
Natural varianti131 – 1311C → F in MCC2D. 1 Publication
VAR_072510
Natural varianti146 – 1461Y → N in MCC2D; has some wild-type residual activity. 1 Publication
VAR_072511
Natural varianti152 – 1521K → T in MCC2D. 1 Publication
VAR_072512
Natural varianti155 – 1551R → Q in MCC2D; mild form. 2 Publications
VAR_012793
Natural varianti155 – 1551R → W in MCC2D. 2 Publications
VAR_072513
Natural varianti167 – 1671C → R in MCC2D. 2 Publications
Corresponds to variant rs28934884 [ dbSNP | Ensembl ].
VAR_012794
Natural varianti169 – 1691Y → D in MCC2D. 1 Publication
VAR_072514
Natural varianti173 – 1731S → L in MCC2D; severe form. 2 Publications
VAR_012795
Natural varianti190 – 1901H → R in MCC2D. 2 Publications
VAR_072515
Natural varianti190 – 1901H → Y in MCC2D; produces severely decreased wild-type residual activity. 2 Publications
VAR_072516
Natural varianti193 – 1931R → C in MCC2D; mild form. 2 Publications
VAR_012796
Natural varianti193 – 1931R → H in MCC2D. 1 Publication
VAR_072517
Natural varianti200 – 2001I → N in MCC2D. 1 Publication
VAR_072518
Natural varianti218 – 2181A → T in MCC2D. 2 Publications
VAR_012797
Natural varianti218 – 2181A → V in MCC2D. 3 Publications
VAR_072519
Natural varianti220 – 2201G → E in MCC2D. 1 Publication
VAR_072520
Natural varianti224 – 2241P → L in MCC2D. 1 Publication
VAR_072521
Natural varianti237 – 2371G → D in MCC2D. 1 Publication
VAR_072522
Natural varianti266 – 2661H → L in MCC2D. 1 Publication
VAR_072523
Natural varianti268 – 2681R → T in MCC2D; asymptomatic form. 2 Publications
VAR_012798
Natural varianti268 – 2681Missing in MCC2D. 1 Publication
VAR_072524
Natural varianti280 – 2801D → Y in MCC2D. 3 Publications
Corresponds to variant rs119103226 [ dbSNP | Ensembl ].
VAR_067199
Natural varianti282 – 2821H → R in MCC2D; has some wild-type residual activity. 2 Publications
VAR_072525
Natural varianti310 – 3101P → R in MCC2D; mild form. 3 Publications
VAR_012799
Natural varianti339 – 3391V → M in MCC2D; severe form. 3 Publications
VAR_012800
Natural varianti340 – 3401D → V in MCC2D. 1 Publication
VAR_072526
Natural varianti352 – 3521G → R in MCC2D; produces severely decreased wild-type residual activity. 1 Publication
VAR_072527
Natural varianti355 – 3551L → F in MCC2D. 2 Publications
VAR_072528
Natural varianti375 – 3751V → F in MCC2D. 2 Publications
VAR_072529
Natural varianti403 – 4031N → T in MCC2D. 1 Publication
VAR_072530
Natural varianti434 – 4341V → L in MCC2D; has some wild-type residual activity. 1 Publication
VAR_072531
Natural varianti437 – 4371I → V in MCC2D; mild form.
VAR_012801
Natural varianti456 – 4561A → V in MCC2D; shows virtually no enzyme activity. 2 Publications
VAR_072532
Natural varianti459 – 4591P → S in MCC2D. 1 Publication
VAR_067200
Natural varianti475 – 4751G → R in MCC2D; has some wild-type residual activity. 1 Publication
VAR_072533
Natural varianti477 – 4771Q → R in MCC2D. 2 Publications
VAR_072534
Natural varianti517 – 5171G → R in MCC2D. 2 Publications
VAR_072535
Natural varianti520 – 5201Y → S in MCC2D. 2 Publications
VAR_072536
Natural varianti523 – 5231S → G in MCC2D; has some wild-type residual activity. 2 Publications
VAR_072537
Natural varianti555 – 5551K → E in MCC2D. 1 Publication
VAR_072538

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi210210. phenotype.
Orphaneti6. Isolated 3-methylcrotonyl-CoA carboxylase deficiency.
PharmGKBiPA30681.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2222Mitochondrion1 PublicationAdd
BLAST
Chaini23 – 563541Methylcrotonoyl-CoA carboxylase beta chain, mitochondrialPRO_0000000291Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei70 – 701N6-acetyllysine; alternateBy similarity
Modified residuei70 – 701N6-succinyllysine; alternateBy similarity
Modified residuei141 – 1411N6-succinyllysineBy similarity
Modified residuei495 – 4951N6-acetyllysine; alternateBy similarity
Modified residuei495 – 4951N6-succinyllysine; alternateBy similarity
Modified residuei511 – 5111N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9HCC0.
PaxDbiQ9HCC0.
PRIDEiQ9HCC0.

2D gel databases

REPRODUCTION-2DPAGEIPI00784044.

PTM databases

PhosphoSiteiQ9HCC0.

Expressioni

Gene expression databases

BgeeiQ9HCC0.
CleanExiHS_MCCC2.
ExpressionAtlasiQ9HCC0. baseline and differential.
GenevestigatoriQ9HCC0.

Organism-specific databases

HPAiHPA038300.
HPA038301.
HPA061546.

Interactioni

Subunit structurei

Probably a dodecamer composed of six biotin-containing alpha subunits (MCCC1) and six beta (MCCC2) subunits.

Protein-protein interaction databases

BioGridi122050. 20 interactions.
IntActiQ9HCC0. 12 interactions.
MINTiMINT-8051924.
STRINGi9606.ENSP00000343657.

Structurei

3D structure databases

ProteinModelPortaliQ9HCC0.
SMRiQ9HCC0. Positions 28-563.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini55 – 557503CarboxyltransferaseAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni343 – 37230Acyl-CoA bindingSequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the AccD/PCCB family.Curated
Contains 1 carboxyltransferase domain.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG4799.
GeneTreeiENSGT00530000063337.
HOGENOMiHOG000218692.
HOVERGENiHBG052424.
InParanoidiQ9HCC0.
KOiK01969.
OMAiCKTSGVT.
PhylomeDBiQ9HCC0.
TreeFamiTF300446.

Family and domain databases

Gene3Di3.90.226.10. 2 hits.
InterProiIPR000022. Carboxyl_trans.
IPR029045. ClpP/crotonase-like_dom.
IPR011763. COA_CT_C.
IPR011762. COA_CT_N.
[Graphical view]
PfamiPF01039. Carboxyl_trans. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 2 hits.
PROSITEiPS50989. COA_CT_CTER. 1 hit.
PS50980. COA_CT_NTER. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9HCC0-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MWAVLRLALR PCARASPAGP RAYHGDSVAS LGTQPDLGSA LYQENYKQMK
60 70 80 90 100
ALVNQLHERV EHIKLGGGEK ARALHISRGK LLPRERIDNL IDPGSPFLEL
110 120 130 140 150
SQFAGYQLYD NEEVPGGGII TGIGRVSGVE CMIIANDATV KGGAYYPVTV
160 170 180 190 200
KKQLRAQEIA MQNRLPCIYL VDSGGAYLPR QADVFPDRDH FGRTFYNQAI
210 220 230 240 250
MSSKNIAQIA VVMGSCTAGG AYVPAMADEN IIVRKQGTIF LAGPPLVKAA
260 270 280 290 300
TGEEVSAEDL GGADLHCRKS GVSDHWALDD HHALHLTRKV VRNLNYQKKL
310 320 330 340 350
DVTIEPSEEP LFPADELYGI VGANLKRSFD VREVIARIVD GSRFTEFKAF
360 370 380 390 400
YGDTLVTGFA RIFGYPVGIV GNNGVLFSES AKKGTHFVQL CCQRNIPLLF
410 420 430 440 450
LQNITGFMVG REYEAEGIAK DGAKMVAAVA CAQVPKITLI IGGSYGAGNY
460 470 480 490 500
GMCGRAYSPR FLYIWPNARI SVMGGEQAAN VLATITKDQR AREGKQFSSA
510 520 530 540 550
DEAALKEPII KKFEEEGNPY YSSARVWDDG IIDPADTRLV LGLSFSAALN
560
APIEKTDFGI FRM
Length:563
Mass (Da):61,333
Last modified:March 1, 2001 - v1
Checksum:i8E3D401AF52DC7D2
GO
Isoform 2 (identifier: Q9HCC0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     209-246: Missing.

Note: No experimental confirmation available.

Show »
Length:525
Mass (Da):57,519
Checksum:i344050ABB7A9DE8A
GO

Sequence cautioni

The sequence AAH14897.1 differs from that shown. Reason: Frameshift at position 359. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti39 – 391S → F in MCC2D; has some wild-type residual activity. 1 Publication
VAR_072507
Natural varianti99 – 991E → Q in MCC2D; severe and mild form. 3 Publications
Corresponds to variant rs28934883 [ dbSNP | Ensembl ].
VAR_012792
Natural varianti101 – 1011S → F in MCC2D. 1 Publication
VAR_072508
Natural varianti118 – 1181Missing in MCC2D; has some wild-type residual activity. 1 Publication
VAR_072509
Natural varianti131 – 1311C → F in MCC2D. 1 Publication
VAR_072510
Natural varianti146 – 1461Y → N in MCC2D; has some wild-type residual activity. 1 Publication
VAR_072511
Natural varianti152 – 1521K → T in MCC2D. 1 Publication
VAR_072512
Natural varianti155 – 1551R → Q in MCC2D; mild form. 2 Publications
VAR_012793
Natural varianti155 – 1551R → W in MCC2D. 2 Publications
VAR_072513
Natural varianti167 – 1671C → R in MCC2D. 2 Publications
Corresponds to variant rs28934884 [ dbSNP | Ensembl ].
VAR_012794
Natural varianti169 – 1691Y → D in MCC2D. 1 Publication
VAR_072514
Natural varianti173 – 1731S → L in MCC2D; severe form. 2 Publications
VAR_012795
Natural varianti190 – 1901H → R in MCC2D. 2 Publications
VAR_072515
Natural varianti190 – 1901H → Y in MCC2D; produces severely decreased wild-type residual activity. 2 Publications
VAR_072516
Natural varianti193 – 1931R → C in MCC2D; mild form. 2 Publications
VAR_012796
Natural varianti193 – 1931R → H in MCC2D. 1 Publication
VAR_072517
Natural varianti200 – 2001I → N in MCC2D. 1 Publication
VAR_072518
Natural varianti218 – 2181A → T in MCC2D. 2 Publications
VAR_012797
Natural varianti218 – 2181A → V in MCC2D. 3 Publications
VAR_072519
Natural varianti220 – 2201G → E in MCC2D. 1 Publication
VAR_072520
Natural varianti224 – 2241P → L in MCC2D. 1 Publication
VAR_072521
Natural varianti237 – 2371G → D in MCC2D. 1 Publication
VAR_072522
Natural varianti266 – 2661H → L in MCC2D. 1 Publication
VAR_072523
Natural varianti268 – 2681R → T in MCC2D; asymptomatic form. 2 Publications
VAR_012798
Natural varianti268 – 2681Missing in MCC2D. 1 Publication
VAR_072524
Natural varianti280 – 2801D → Y in MCC2D. 3 Publications
Corresponds to variant rs119103226 [ dbSNP | Ensembl ].
VAR_067199
Natural varianti282 – 2821H → R in MCC2D; has some wild-type residual activity. 2 Publications
VAR_072525
Natural varianti310 – 3101P → R in MCC2D; mild form. 3 Publications
VAR_012799
Natural varianti339 – 3391V → M in MCC2D; severe form. 3 Publications
VAR_012800
Natural varianti340 – 3401D → V in MCC2D. 1 Publication
VAR_072526
Natural varianti352 – 3521G → R in MCC2D; produces severely decreased wild-type residual activity. 1 Publication
VAR_072527
Natural varianti355 – 3551L → F in MCC2D. 2 Publications
VAR_072528
Natural varianti375 – 3751V → F in MCC2D. 2 Publications
VAR_072529
Natural varianti403 – 4031N → T in MCC2D. 1 Publication
VAR_072530
Natural varianti434 – 4341V → L in MCC2D; has some wild-type residual activity. 1 Publication
VAR_072531
Natural varianti437 – 4371I → V in MCC2D; mild form.
VAR_012801
Natural varianti456 – 4561A → V in MCC2D; shows virtually no enzyme activity. 2 Publications
VAR_072532
Natural varianti459 – 4591P → S in MCC2D. 1 Publication
VAR_067200
Natural varianti475 – 4751G → R in MCC2D; has some wild-type residual activity. 1 Publication
VAR_072533
Natural varianti477 – 4771Q → R in MCC2D. 2 Publications
VAR_072534
Natural varianti478 – 4781A → G.
Corresponds to variant rs35068278 [ dbSNP | Ensembl ].
VAR_038630
Natural varianti517 – 5171G → R in MCC2D. 2 Publications
VAR_072535
Natural varianti520 – 5201Y → S in MCC2D. 2 Publications
VAR_072536
Natural varianti523 – 5231S → G in MCC2D; has some wild-type residual activity. 2 Publications
VAR_072537
Natural varianti555 – 5551K → E in MCC2D. 1 Publication
VAR_072538

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei209 – 24638Missing in isoform 2. 1 PublicationVSP_000069Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB050049 mRNA. Translation: BAB16880.1.
AB050050 Genomic DNA. Translation: BAB41121.1.
AF310971 mRNA. Translation: AAG53094.1.
AF301000 mRNA. Translation: AAK16404.1.
AF261884 mRNA. Translation: AAK49409.1.
AC138832 Genomic DNA. No translation available.
CH471084 Genomic DNA. Translation: EAW95693.1.
BC014897 mRNA. Translation: AAH14897.1. Frameshift.
BC065027 mRNA. Translation: AAH65027.1.
AL079298 mRNA. Translation: CAB45194.1.
CCDSiCCDS34184.1. [Q9HCC0-1]
RefSeqiNP_071415.1. NM_022132.4. [Q9HCC0-1]
XP_005248624.1. XM_005248567.1. [Q9HCC0-2]
UniGeneiHs.604789.

Genome annotation databases

EnsembliENST00000340941; ENSP00000343657; ENSG00000131844. [Q9HCC0-1]
GeneIDi64087.
KEGGihsa:64087.
UCSCiuc003kbs.4. human. [Q9HCC0-1]

Polymorphism databases

DMDMi20138731.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB050049 mRNA. Translation: BAB16880.1.
AB050050 Genomic DNA. Translation: BAB41121.1.
AF310971 mRNA. Translation: AAG53094.1.
AF301000 mRNA. Translation: AAK16404.1.
AF261884 mRNA. Translation: AAK49409.1.
AC138832 Genomic DNA. No translation available.
CH471084 Genomic DNA. Translation: EAW95693.1.
BC014897 mRNA. Translation: AAH14897.1. Frameshift.
BC065027 mRNA. Translation: AAH65027.1.
AL079298 mRNA. Translation: CAB45194.1.
CCDSiCCDS34184.1. [Q9HCC0-1]
RefSeqiNP_071415.1. NM_022132.4. [Q9HCC0-1]
XP_005248624.1. XM_005248567.1. [Q9HCC0-2]
UniGeneiHs.604789.

3D structure databases

ProteinModelPortaliQ9HCC0.
SMRiQ9HCC0. Positions 28-563.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122050. 20 interactions.
IntActiQ9HCC0. 12 interactions.
MINTiMINT-8051924.
STRINGi9606.ENSP00000343657.

Chemistry

DrugBankiDB00121. Biotin.

PTM databases

PhosphoSiteiQ9HCC0.

Polymorphism databases

DMDMi20138731.

2D gel databases

REPRODUCTION-2DPAGEIPI00784044.

Proteomic databases

MaxQBiQ9HCC0.
PaxDbiQ9HCC0.
PRIDEiQ9HCC0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000340941; ENSP00000343657; ENSG00000131844. [Q9HCC0-1]
GeneIDi64087.
KEGGihsa:64087.
UCSCiuc003kbs.4. human. [Q9HCC0-1]

Organism-specific databases

CTDi64087.
GeneCardsiGC05P070883.
HGNCiHGNC:6937. MCCC2.
HPAiHPA038300.
HPA038301.
HPA061546.
MIMi210210. phenotype.
609014. gene.
neXtProtiNX_Q9HCC0.
Orphaneti6. Isolated 3-methylcrotonyl-CoA carboxylase deficiency.
PharmGKBiPA30681.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG4799.
GeneTreeiENSGT00530000063337.
HOGENOMiHOG000218692.
HOVERGENiHBG052424.
InParanoidiQ9HCC0.
KOiK01969.
OMAiCKTSGVT.
PhylomeDBiQ9HCC0.
TreeFamiTF300446.

Enzyme and pathway databases

UniPathwayiUPA00363; UER00861.
BioCyciMetaCyc:ENSG00000131844-MONOMER.
ReactomeiREACT_11153. Biotin transport and metabolism.
REACT_169312. Defective HLCS causes multiple carboxylase deficiency.
REACT_197. Branched-chain amino acid catabolism.

Miscellaneous databases

GenomeRNAii64087.
NextBioi65884.
PROiQ9HCC0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9HCC0.
CleanExiHS_MCCC2.
ExpressionAtlasiQ9HCC0. baseline and differential.
GenevestigatoriQ9HCC0.

Family and domain databases

Gene3Di3.90.226.10. 2 hits.
InterProiIPR000022. Carboxyl_trans.
IPR029045. ClpP/crotonase-like_dom.
IPR011763. COA_CT_C.
IPR011762. COA_CT_N.
[Graphical view]
PfamiPF01039. Carboxyl_trans. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 2 hits.
PROSITEiPS50989. COA_CT_CTER. 1 hit.
PS50980. COA_CT_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human non-biotin containing subunit gene of 3-methylcrotonyl-CoA carboxylase (MCCB)."
    Fukuda T., Otsuka H., Morishita R., Takemoto Y., Sone M., Nakao M., Abe S., Kondo I.
    Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, VARIANTS MCC2D ARG-167 AND THR-218.
  3. "The molecular basis of human 3-methylcrotonyl-CoA carboxylase deficiency."
    Baumgartner M.R., Almashanu S., Suormala T., Obie C., Cole R.N., Packman S., Baumgartner E.R., Valle D.
    J. Clin. Invest. 107:495-504(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS MCC2D GLN-99; GLN-155; LEU-173; CYS-193; ARG-310 AND MET-339.
  4. "Cloning of the human MCCA and MCCB genes and mutations therein reveal the molecular cause of 3-methylcrotonyl-CoA: carboxylase deficiency."
    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.
    Hum. Mol. Genet. 10:1299-1306(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT MCC2D THR-268.
  5. "The DNA sequence and comparative analysis of human chromosome 5."
    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.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Testis and Uterus.
  8. Cited for: PROTEIN SEQUENCE OF 23-28, SUBCELLULAR LOCATION.
    Tissue: Kidney.
  9. "Expression, purification, characterization of human 3-methylcrotonyl-CoA carboxylase (MCCC)."
    Chu C.H., Cheng D.
    Protein Expr. Purif. 53:421-427(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
  10. The European IMAGE consortium
    Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 469-563.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. Cited for: VARIANTS MCC2D ARG-190; VAL-218 AND TYR-280.
  14. "3-Methylcrotonyl-CoA carboxylase deficiency: mutation analysis in 28 probands, 9 symptomatic and 19 detected by newborn screening."
    Dantas M.F., Suormala T., Randolph A., Coelho D., Fowler B., Valle D., Baumgartner M.R.
    Hum. Mutat. 26:164-174(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MCC2D GLN-99; TRP-155; GLN-155; TYR-190; THR-268; ARG-282; ARG-310; PHE-375 AND VAL-456, CHARACTERIZATION OF VARIANTS TYR-190 AND ARG-352.
  15. "Novel mutations in the human MCCA and MCCB gene causing methylcrotonylglycinuria."
    Nguyen K.V., Naviaux R.K., Patra S., Barshop B.A., Nyhan W.L.
    Mol. Genet. Metab. 102:218-221(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MCC2D PHE-355; ARG-477; ARG-517 AND SER-520.
  16. "Mutational spectrum in eight Korean patients with 3-methylcrotonyl-CoA carboxylase deficiency."
    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.
    Clin. Genet. 81:96-98(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MCC2D TYR-280 AND SER-459.
  17. "A single mutation in MCCC1 or MCCC2 as a potential cause of positive screening for 3-methylcrotonyl-CoA carboxylase deficiency."
    Morscher R.J., Grunert S.C., Burer C., Burda P., Suormala T., Fowler B., Baumgartner M.R.
    Mol. Genet. Metab. 105:602-606(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MCC2D VAL-218; MET-339 AND GLY-523.
  18. Cited for: 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, CHARACTERIZATION OF VARIANTS MCC2D PHE-39; GLY-118 DEL; ASN-146; ARG-282; LEU-434; VAL-456; ARG-475 AND GLY-523.

Entry informationi

Entry nameiMCCB_HUMAN
AccessioniPrimary (citable) accession number: Q9HCC0
Secondary accession number(s): A6NIY9, Q96C27, Q9Y4L7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: March 1, 2001
Last modified: March 4, 2015
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.