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Q96RQ3

- MCCA_HUMAN

UniProt

Q96RQ3 - MCCA_HUMAN

Protein

Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial

Gene

MCCC1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 3 (30 May 2006)
      Previous versions | rss
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    Functioni

    Biotin-attachment 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

    Cofactori

    Biotin.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei163 – 1631ATPBy similarity
    Binding sitei247 – 2471ATPBy similarity
    Binding sitei282 – 2821ATPBy similarity
    Active sitei339 – 3391By similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. biotin binding Source: UniProtKB
    3. biotin carboxylase activity Source: InterPro
    4. metal ion binding Source: InterPro
    5. methylcrotonoyl-CoA carboxylase activity Source: UniProtKB
    6. protein binding Source: UniProtKB

    GO - Biological processi

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

    Keywords - Molecular functioni

    Ligase

    Keywords - Ligandi

    ATP-binding, Biotin, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:ENSG00000078070-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 subunit alpha, mitochondrial (EC:6.4.1.4)
    Short name:
    MCCase subunit alpha
    Alternative name(s):
    3-methylcrotonyl-CoA carboxylase 1
    3-methylcrotonyl-CoA carboxylase biotin-containing subunit
    3-methylcrotonyl-CoA:carbon dioxide ligase subunit alpha
    Gene namesi
    Name:MCCC1
    Synonyms:MCCA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:6936. MCCC1.

    Subcellular locationi

    Mitochondrion matrix 1 Publication

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. mitochondrial inner membrane Source: Ensembl
    3. mitochondrial matrix Source: UniProtKB
    4. mitochondrion Source: HPA

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Methylcrotonoyl-CoA carboxylase 1 deficiency (MCC1D) [MIM:210200]: 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.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti276 – 2761C → R in MCC1D. 1 Publication
    VAR_067197
    Natural varianti281 – 2811R → Q in MCC1D. 1 Publication
    VAR_067198
    Natural varianti289 – 2891A → V in MCC1D; mild form. 1 Publication
    VAR_012785
    Natural varianti325 – 3251M → R in MCC1D. 1 Publication
    VAR_012786
    Natural varianti385 – 3851R → S in MCC1D; severe form. 2 Publications
    Corresponds to variant rs28934881 [ dbSNP | Ensembl ].
    VAR_012787
    Natural varianti437 – 4371L → P in MCC1D; severe form. 1 Publication
    Corresponds to variant rs28934882 [ dbSNP | Ensembl ].
    VAR_012788
    Natural varianti532 – 5321D → H in MCC1D; severe form. 1 Publication
    VAR_012790
    Natural varianti535 – 5351S → F in MCC1D; asymptomatic form. 1 Publication
    VAR_012791

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi210200. phenotype.
    Orphaneti6. Isolated 3-methylcrotonyl-CoA carboxylase deficiency.
    PharmGKBiPA30680.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4141Mitochondrion1 PublicationAdd
    BLAST
    Chaini42 – 725684Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrialPRO_0000002833Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei237 – 2371N6-acetyllysineBy similarity
    Modified residuei494 – 4941N6-acetyllysineBy similarity
    Modified residuei581 – 5811N6-acetyllysine; alternateBy similarity
    Modified residuei581 – 5811N6-succinyllysine; alternateBy similarity
    Modified residuei681 – 6811N6-biotinyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ96RQ3.
    PaxDbiQ96RQ3.
    PRIDEiQ96RQ3.

    PTM databases

    PhosphoSiteiQ96RQ3.

    Expressioni

    Gene expression databases

    ArrayExpressiQ96RQ3.
    BgeeiQ96RQ3.
    CleanExiHS_MCCC1.
    GenevestigatoriQ96RQ3.

    Organism-specific databases

    HPAiHPA008310.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi121249. 9 interactions.
    IntActiQ96RQ3. 3 interactions.
    STRINGi9606.ENSP00000265594.

    Structurei

    Secondary structure

    1
    725
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi652 – 6609
    Beta strandi666 – 6683
    Beta strandi673 – 68715
    Beta strandi692 – 6987
    Beta strandi703 – 7053
    Beta strandi712 – 7143

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2EJMNMR-A640-725[»]
    ProteinModelPortaliQ96RQ3.
    SMRiQ96RQ3. Positions 47-725.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ96RQ3.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini48 – 494447Biotin carboxylationAdd
    BLAST
    Domaini167 – 364198ATP-graspPROSITE-ProRule annotationAdd
    BLAST
    Domaini629 – 71486Biotinyl-bindingAdd
    BLAST

    Sequence similaritiesi

    Contains 1 ATP-grasp domain.PROSITE-ProRule annotation
    Contains 1 biotin carboxylation domain.Curated
    Contains 1 biotinyl-binding domain.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG4770.
    HOGENOMiHOG000008989.
    HOVERGENiHBG000555.
    InParanoidiQ96RQ3.
    KOiK01968.
    OMAiVDNPRHV.
    OrthoDBiEOG7RZ5PH.
    PhylomeDBiQ96RQ3.
    TreeFamiTF105650.

    Family and domain databases

    Gene3Di3.30.1490.20. 1 hit.
    3.30.470.20. 1 hit.
    3.40.50.20. 1 hit.
    InterProiIPR011761. ATP-grasp.
    IPR013815. ATP_grasp_subdomain_1.
    IPR013816. ATP_grasp_subdomain_2.
    IPR001882. Biotin_BS.
    IPR011764. Biotin_carboxylation_dom.
    IPR005482. Biotin_COase_C.
    IPR000089. Biotin_lipoyl.
    IPR005481. CarbamoylP_synth_lsu_N.
    IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
    IPR016185. PreATP-grasp_dom.
    IPR011054. Rudment_hybrid_motif.
    IPR011053. Single_hybrid_motif.
    [Graphical view]
    PfamiPF02785. Biotin_carb_C. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    PF00289. CPSase_L_chain. 1 hit.
    PF02786. CPSase_L_D2. 1 hit.
    [Graphical view]
    SMARTiSM00878. Biotin_carb_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF51230. SSF51230. 1 hit.
    SSF51246. SSF51246. 1 hit.
    SSF52440. SSF52440. 1 hit.
    PROSITEiPS50975. ATP_GRASP. 1 hit.
    PS50979. BC. 1 hit.
    PS00188. BIOTIN. 1 hit.
    PS50968. BIOTINYL_LIPOYL. 1 hit.
    PS00867. CPSASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q96RQ3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAASAVSVL LVAAERNRWH RLPSLLLPPR TWVWRQRTMK YTTATGRNIT    50
    KVLIANRGEI ACRVMRTAKK LGVQTVAVYS EADRNSMHVD MADEAYSIGP 100
    APSQQSYLSM EKIIQVAKTS AAQAIHPGCG FLSENMEFAE LCKQEGIIFI 150
    GPPPSAIRDM GIKSTSKSIM AAAGVPVVEG YHGEDQSDQC LKEHARRIGY 200
    PVMIKAVRGG GGKGMRIVRS EQEFQEQLES ARREAKKSFN DDAMLIEKFV 250
    DTPRHVEVQV FGDHHGNAVY LFERDCSVQR RHQKIIEEAP APGIKSEVRK 300
    KLGEAAVRAA KAVNYVGAGT VEFIMDSKHN FCFMEMNTRL QVEHPVTEMI 350
    TGTDLVEWQL RIAAGEKIPL SQEEITLQGH AFEARIYAED PSNNFMPVAG 400
    PLVHLSTPRA DPSTRIETGV RQGDEVSVHY DPMIAKLVVW AADRQAALTK 450
    LRYSLRQYNI VGLHTNIDFL LNLSGHPEFE AGNVHTDFIP QHHKQLLLSR 500
    KAAAKESLCQ AALGLILKEK AMTDTFTLQA HDQFSPFSSS SGRRLNISYT 550
    RNMTLKDGKN NVAIAVTYNH DGSYSMQIED KTFQVLGNLY SEGDCTYLKC 600
    SVNGVASKAK LIILENTIYL FSKEGSIEID IPVPKYLSSV SSQETQGGPL 650
    APMTGTIEKV FVKAGDKVKA GDSLMVMIAM KMEHTIKSPK DGTVKKVFYR 700
    EGAQANRHTP LVEFEEEESD KRESE 725
    Length:725
    Mass (Da):80,473
    Last modified:May 30, 2006 - v3
    Checksum:iB84AD23806035A40
    GO

    Sequence cautioni

    The sequence BAD92974.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti232 – 2321R → W in BAD92974. 1 PublicationCurated
    Sequence conflicti469 – 4691F → L in AAK67986. (PubMed:11406611)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti276 – 2761C → R in MCC1D. 1 Publication
    VAR_067197
    Natural varianti281 – 2811R → Q in MCC1D. 1 Publication
    VAR_067198
    Natural varianti289 – 2891A → V in MCC1D; mild form. 1 Publication
    VAR_012785
    Natural varianti325 – 3251M → R in MCC1D. 1 Publication
    VAR_012786
    Natural varianti385 – 3851R → S in MCC1D; severe form. 2 Publications
    Corresponds to variant rs28934881 [ dbSNP | Ensembl ].
    VAR_012787
    Natural varianti437 – 4371L → P in MCC1D; severe form. 1 Publication
    Corresponds to variant rs28934882 [ dbSNP | Ensembl ].
    VAR_012788
    Natural varianti464 – 4641H → P.5 Publications
    Corresponds to variant rs2270968 [ dbSNP | Ensembl ].
    VAR_012789
    Natural varianti532 – 5321D → H in MCC1D; severe form. 1 Publication
    VAR_012790
    Natural varianti535 – 5351S → F in MCC1D; asymptomatic form. 1 Publication
    VAR_012791
    Natural varianti560 – 5601N → T.
    Corresponds to variant rs35219417 [ dbSNP | Ensembl ].
    VAR_038631

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF310972 mRNA. Translation: AAG53095.1.
    AB029826 mRNA. Translation: BAA99407.1.
    AF297332 mRNA. Translation: AAK67986.1.
    AF310339 mRNA. Translation: AAG50245.1.
    AK023051 mRNA. Translation: BAB14377.1.
    AB209737 mRNA. Translation: BAD92974.1. Different initiation.
    BC004214 mRNA. Translation: AAH04214.1.
    BC004187 mRNA. Translation: AAH04187.1.
    CCDSiCCDS3241.1.
    RefSeqiNP_064551.3. NM_020166.4.
    UniGeneiHs.47649.

    Genome annotation databases

    EnsembliENST00000265594; ENSP00000265594; ENSG00000078070.
    GeneIDi56922.
    KEGGihsa:56922.
    UCSCiuc003fle.3. human.

    Polymorphism databases

    DMDMi108861983.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF310972 mRNA. Translation: AAG53095.1 .
    AB029826 mRNA. Translation: BAA99407.1 .
    AF297332 mRNA. Translation: AAK67986.1 .
    AF310339 mRNA. Translation: AAG50245.1 .
    AK023051 mRNA. Translation: BAB14377.1 .
    AB209737 mRNA. Translation: BAD92974.1 . Different initiation.
    BC004214 mRNA. Translation: AAH04214.1 .
    BC004187 mRNA. Translation: AAH04187.1 .
    CCDSi CCDS3241.1.
    RefSeqi NP_064551.3. NM_020166.4.
    UniGenei Hs.47649.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2EJM NMR - A 640-725 [» ]
    ProteinModelPortali Q96RQ3.
    SMRi Q96RQ3. Positions 47-725.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121249. 9 interactions.
    IntActi Q96RQ3. 3 interactions.
    STRINGi 9606.ENSP00000265594.

    Chemistry

    DrugBanki DB00121. Biotin.

    PTM databases

    PhosphoSitei Q96RQ3.

    Polymorphism databases

    DMDMi 108861983.

    Proteomic databases

    MaxQBi Q96RQ3.
    PaxDbi Q96RQ3.
    PRIDEi Q96RQ3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265594 ; ENSP00000265594 ; ENSG00000078070 .
    GeneIDi 56922.
    KEGGi hsa:56922.
    UCSCi uc003fle.3. human.

    Organism-specific databases

    CTDi 56922.
    GeneCardsi GC03M182733.
    HGNCi HGNC:6936. MCCC1.
    HPAi HPA008310.
    MIMi 210200. phenotype.
    609010. gene.
    neXtProti NX_Q96RQ3.
    Orphaneti 6. Isolated 3-methylcrotonyl-CoA carboxylase deficiency.
    PharmGKBi PA30680.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4770.
    HOGENOMi HOG000008989.
    HOVERGENi HBG000555.
    InParanoidi Q96RQ3.
    KOi K01968.
    OMAi VDNPRHV.
    OrthoDBi EOG7RZ5PH.
    PhylomeDBi Q96RQ3.
    TreeFami TF105650.

    Enzyme and pathway databases

    UniPathwayi UPA00363 ; UER00861 .
    BioCyci MetaCyc:ENSG00000078070-MONOMER.
    Reactomei REACT_11153. Biotin transport and metabolism.
    REACT_169312. Defective HLCS causes multiple carboxylase deficiency.
    REACT_197. Branched-chain amino acid catabolism.

    Miscellaneous databases

    ChiTaRSi MCCC1. human.
    EvolutionaryTracei Q96RQ3.
    GenomeRNAii 56922.
    NextBioi 62428.
    PROi Q96RQ3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96RQ3.
    Bgeei Q96RQ3.
    CleanExi HS_MCCC1.
    Genevestigatori Q96RQ3.

    Family and domain databases

    Gene3Di 3.30.1490.20. 1 hit.
    3.30.470.20. 1 hit.
    3.40.50.20. 1 hit.
    InterProi IPR011761. ATP-grasp.
    IPR013815. ATP_grasp_subdomain_1.
    IPR013816. ATP_grasp_subdomain_2.
    IPR001882. Biotin_BS.
    IPR011764. Biotin_carboxylation_dom.
    IPR005482. Biotin_COase_C.
    IPR000089. Biotin_lipoyl.
    IPR005481. CarbamoylP_synth_lsu_N.
    IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
    IPR016185. PreATP-grasp_dom.
    IPR011054. Rudment_hybrid_motif.
    IPR011053. Single_hybrid_motif.
    [Graphical view ]
    Pfami PF02785. Biotin_carb_C. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    PF00289. CPSase_L_chain. 1 hit.
    PF02786. CPSase_L_D2. 1 hit.
    [Graphical view ]
    SMARTi SM00878. Biotin_carb_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51230. SSF51230. 1 hit.
    SSF51246. SSF51246. 1 hit.
    SSF52440. SSF52440. 1 hit.
    PROSITEi PS50975. ATP_GRASP. 1 hit.
    PS50979. BC. 1 hit.
    PS00188. BIOTIN. 1 hit.
    PS50968. BIOTINYL_LIPOYL. 1 hit.
    PS00867. CPSASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS MCC1D ARG-325 AND SER-385.
    2. "Human biotin-containing subunit of 3-methylcrotonyl-CoA carboxylase gene (MCCA): cDNA sequence, genomic organization, localization to chromosomal band 3q27, and expression."
      Obata K., Fukuda T., Morishita R., Abe S., Asakawa S., Yamaguchi S., Yoshino M., Ihara K., Murayama K., Shigemoto K., Shimizu N., Kondo I.
      Genomics 72:145-152(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "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], VARIANT MCC1D PHE-535, VARIANT PRO-464.
    4. "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], VARIANTS MCC1D VAL-289; SER-385; PRO-437 AND HIS-532, VARIANT PRO-464.
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT PRO-464.
    6. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT PRO-464.
      Tissue: Aorta.
    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], VARIANT PRO-464.
      Tissue: Skeletal muscle.
    8. Cited for: PROTEIN SEQUENCE OF 42-47, 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.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Solution structure of RSGI RUH-072, an apo-biotinyl domain from human acetyl coenzyme A carboxylase."
      RIKEN structural genomics initiative (RSGI)
      Submitted (SEP-2007) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 640-725.
    12. "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 MCC1D ARG-276 AND GLN-281.

    Entry informationi

    Entry nameiMCCA_HUMAN
    AccessioniPrimary (citable) accession number: Q96RQ3
    Secondary accession number(s): Q59ES4, Q9H959, Q9NS97
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 5, 2002
    Last sequence update: May 30, 2006
    Last modified: October 1, 2014
    This is version 149 of the entry and version 3 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3