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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

    Pathway:iL-leucine degradation

    This protein is involved in step 2 of the subpathway that synthesizes (S)-3-hydroxy-3-methylglutaryl-CoA from 3-isovaleryl-CoA.
    Proteins known to be involved in the 3 steps of the subpathway in this organism are:
    1. Isovaleryl-CoA dehydrogenase, mitochondrial (IVD)
    2. Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial (MCCC1), Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial (MCCC2)
    3. Methylglutaconyl-CoA hydratase, mitochondrial (AUH)
    This subpathway is part of the pathway L-leucine degradation, which is itself part of Amino-acid degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-3-hydroxy-3-methylglutaryl-CoA from 3-isovaleryl-CoA, the pathway L-leucine degradation and in Amino-acid degradation.

    GO - Molecular functioni

    • ATP binding Source: UniProtKB-KW
    • methylcrotonoyl-CoA carboxylase activity Source: UniProtKB

    GO - Biological processi

    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 Componenti: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:6937. MCCC2.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: Reactome
    • mitochondrial matrix Source: Reactome
    • mitochondrion Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    3-methylcrotonoyl-CoA carboxylase 2 deficiency (MCC2D)9 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.

    Chemistry

    DrugBankiDB00121. Biotin.

    Polymorphism and mutation databases

    BioMutaiMCCC2.
    DMDMi20138731.

    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.
    GenevisibleiQ9HCC0. HS.

    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. 18 interactions.
    IntActiQ9HCC0. 15 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.
    OMAiFRNNAVM.
    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.
    GeneIDi64087.
    KEGGihsa:64087.
    UCSCiuc003kbs.4. human. [Q9HCC0-1]

    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. 18 interactions.
    IntActiQ9HCC0. 15 interactions.
    MINTiMINT-8051924.
    STRINGi9606.ENSP00000343657.

    Chemistry

    DrugBankiDB00121. Biotin.

    PTM databases

    PhosphoSiteiQ9HCC0.

    Polymorphism and mutation databases

    BioMutaiMCCC2.
    DMDMi20138731.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00784044.

    Proteomic databases

    MaxQBiQ9HCC0.
    PaxDbiQ9HCC0.
    PRIDEiQ9HCC0.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000340941; ENSP00000343657; ENSG00000131844.
    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.
    OMAiFRNNAVM.
    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.
    GenevisibleiQ9HCC0. HS.

    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: July 22, 2015
    This is version 143 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.