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Q96RQ3

- MCCA_HUMAN

UniProt

Q96RQ3 - MCCA_HUMAN

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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

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

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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ96RQ3.
CleanExiHS_MCCC1.
ExpressionAtlasiQ96RQ3. baseline and differential.
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. 14 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.
GeneTreeiENSGT00550000074675.
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

        10         20         30         40         50
MAAASAVSVL LVAAERNRWH RLPSLLLPPR TWVWRQRTMK YTTATGRNIT
60 70 80 90 100
KVLIANRGEI ACRVMRTAKK LGVQTVAVYS EADRNSMHVD MADEAYSIGP
110 120 130 140 150
APSQQSYLSM EKIIQVAKTS AAQAIHPGCG FLSENMEFAE LCKQEGIIFI
160 170 180 190 200
GPPPSAIRDM GIKSTSKSIM AAAGVPVVEG YHGEDQSDQC LKEHARRIGY
210 220 230 240 250
PVMIKAVRGG GGKGMRIVRS EQEFQEQLES ARREAKKSFN DDAMLIEKFV
260 270 280 290 300
DTPRHVEVQV FGDHHGNAVY LFERDCSVQR RHQKIIEEAP APGIKSEVRK
310 320 330 340 350
KLGEAAVRAA KAVNYVGAGT VEFIMDSKHN FCFMEMNTRL QVEHPVTEMI
360 370 380 390 400
TGTDLVEWQL RIAAGEKIPL SQEEITLQGH AFEARIYAED PSNNFMPVAG
410 420 430 440 450
PLVHLSTPRA DPSTRIETGV RQGDEVSVHY DPMIAKLVVW AADRQAALTK
460 470 480 490 500
LRYSLRQYNI VGLHTNIDFL LNLSGHPEFE AGNVHTDFIP QHHKQLLLSR
510 520 530 540 550
KAAAKESLCQ AALGLILKEK AMTDTFTLQA HDQFSPFSSS SGRRLNISYT
560 570 580 590 600
RNMTLKDGKN NVAIAVTYNH DGSYSMQIED KTFQVLGNLY SEGDCTYLKC
610 620 630 640 650
SVNGVASKAK LIILENTIYL FSKEGSIEID IPVPKYLSSV SSQETQGGPL
660 670 680 690 700
APMTGTIEKV FVKAGDKVKA GDSLMVMIAM KMEHTIKSPK DGTVKKVFYR
710 720
EGAQANRHTP LVEFEEEESD KRESE
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_001280202.1. NM_001293273.1.
NP_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_001280202.1. NM_001293273.1.
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. 14 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.
GeneTreei ENSGT00550000074675.
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

Bgeei Q96RQ3.
CleanExi HS_MCCC1.
ExpressionAtlasi Q96RQ3. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 150 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