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Protein

Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial

Gene

MCCC1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

Pathwayi: L-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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei163ATPBy similarity1
Binding sitei247ATPBy similarity1
Binding sitei282ATPBy similarity1
Active sitei339By similarity1

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • biotin binding Source: UniProtKB
  • biotin carboxylase activity Source: ParkinsonsUK-UCL
  • metal ion binding Source: InterPro
  • methylcrotonoyl-CoA carboxylase activity Source: CACAO

GO - Biological processi

  • biotin metabolic process Source: UniProtKB
  • branched-chain amino acid catabolic process Source: Reactome
  • leucine catabolic process Source: UniProtKB
  • protein heterooligomerization Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Biotin, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000078070-MONOMER.
ZFISH:ENSG00000078070-MONOMER.
ReactomeiR-HSA-196780. Biotin transport and metabolism.
R-HSA-3371599. Defective HLCS causes multiple carboxylase deficiency.
R-HSA-70895. 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
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:6936. MCCC1.

Subcellular locationi

GO - Cellular componenti

  • 3-methylcrotonyl-CoA carboxylase complex, mitochondrial Source: ParkinsonsUK-UCL
  • cytosol Source: Reactome
  • methylcrotonoyl-CoA carboxylase complex Source: ParkinsonsUK-UCL
  • mitochondrial inner membrane Source: Ensembl
  • mitochondrial matrix Source: UniProtKB
  • mitochondrion Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

3-methylcrotonoyl-CoA carboxylase 1 deficiency (MCC1D)10 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:210200
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07248646G → E in MCC1D. 2 PublicationsCorresponds to variant rs199517715dbSNPEnsembl.1
Natural variantiVAR_07248756N → K in MCC1D. 2 Publications1
Natural variantiVAR_07248865M → L in MCC1D. 1 Publication1
Natural variantiVAR_072489123Q → H in MCC1D. 1 Publication1
Natural variantiVAR_072490125I → M in MCC1D. 1 Publication1
Natural variantiVAR_072491134E → K in MCC1D. 2 Publications1
Natural variantiVAR_072492160M → R in MCC1D. 1 Publication1
Natural variantiVAR_072493180G → V in MCC1D. 1 Publication1
Natural variantiVAR_072494187S → P in MCC1D. 2 PublicationsCorresponds to variant rs757362635dbSNPEnsembl.1
Natural variantiVAR_072495232R → W in MCC1D. 2 PublicationsCorresponds to variant rs727504004dbSNPEnsembl.1
Natural variantiVAR_072496268A → D in MCC1D. 1 Publication1
Natural variantiVAR_067197276C → R in MCC1D. 1 PublicationCorresponds to variant rs773433541dbSNPEnsembl.1
Natural variantiVAR_067198281R → Q in MCC1D. 3 PublicationsCorresponds to variant rs754437245dbSNPEnsembl.1
Natural variantiVAR_072497288E → G in MCC1D; shows no residual activity. 1 PublicationCorresponds to variant rs746500530dbSNPEnsembl.1
Natural variantiVAR_012785289A → V in MCC1D; mild form. 2 Publications1
Natural variantiVAR_072498291A → V in MCC1D; associated with a reduction of wild-type residual activity. 2 PublicationsCorresponds to variant rs201041864dbSNPEnsembl.1
Natural variantiVAR_012786325M → R in MCC1D. 2 PublicationsCorresponds to variant rs119103212dbSNPEnsembl.1
Natural variantiVAR_072499372Q → P in MCC1D. 1 PublicationCorresponds to variant rs755328329dbSNPEnsembl.1
Natural variantiVAR_072500379G → D in MCC1D. 1 Publication1
Natural variantiVAR_072501379G → S in MCC1D. 1 Publication1
Natural variantiVAR_072502380H → P in MCC1D. 2 PublicationsCorresponds to variant rs794727036dbSNPEnsembl.1
Natural variantiVAR_012787385R → S in MCC1D; severe form. 5 PublicationsCorresponds to variant rs28934881dbSNPEnsembl.1
Natural variantiVAR_072503434I → M in MCC1D; shows some wild-type residual activity. 1 PublicationCorresponds to variant rs376289130dbSNPEnsembl.1
Natural variantiVAR_012788437L → P in MCC1D; severe form. 1 PublicationCorresponds to variant rs28934882dbSNPEnsembl.1
Natural variantiVAR_072504439V → M in MCC1D. 1 PublicationCorresponds to variant rs398124352dbSNPEnsembl.1
Natural variantiVAR_072505460I → M in MCC1D. 2 PublicationsCorresponds to variant rs119103218dbSNPEnsembl.1
Natural variantiVAR_012790532D → H in MCC1D; severe form. 2 PublicationsCorresponds to variant rs119103214dbSNPEnsembl.1
Natural variantiVAR_012791535S → F in MCC1D; asymptomatic form. 2 PublicationsCorresponds to variant rs119103216dbSNPEnsembl.1
Natural variantiVAR_072506566 – 567Missing in MCC1D. 1 Publication2

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi56922.
MalaCardsiMCCC1.
MIMi210200. phenotype.
OpenTargetsiENSG00000078070.
Orphaneti6. Isolated 3-methylcrotonyl-CoA carboxylase deficiency.
PharmGKBiPA30680.

Chemistry databases

DrugBankiDB00121. Biotin.

Polymorphism and mutation databases

BioMutaiMCCC1.
DMDMi108861983.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 41Mitochondrion1 PublicationAdd BLAST41
ChainiPRO_000000283342 – 725Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrialAdd BLAST684

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei237N6-acetyllysineBy similarity1
Modified residuei494N6-acetyllysineBy similarity1
Modified residuei581N6-acetyllysine; alternateBy similarity1
Modified residuei581N6-succinyllysine; alternateBy similarity1
Modified residuei681N6-biotinyllysinePROSITE-ProRule annotationBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ96RQ3.
MaxQBiQ96RQ3.
PaxDbiQ96RQ3.
PeptideAtlasiQ96RQ3.
PRIDEiQ96RQ3.

PTM databases

iPTMnetiQ96RQ3.
PhosphoSitePlusiQ96RQ3.
SwissPalmiQ96RQ3.

Expressioni

Gene expression databases

BgeeiENSG00000078070.
CleanExiHS_MCCC1.
ExpressionAtlasiQ96RQ3. baseline and differential.
GenevisibleiQ96RQ3. HS.

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. 32 interactors.
IntActiQ96RQ3. 7 interactors.
STRINGi9606.ENSP00000265594.

Structurei

Secondary structure

1725
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi652 – 660Combined sources9
Beta strandi666 – 668Combined sources3
Beta strandi673 – 687Combined sources15
Beta strandi692 – 698Combined sources7
Beta strandi703 – 705Combined sources3
Beta strandi712 – 714Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2EJMNMR-A640-725[»]
ProteinModelPortaliQ96RQ3.
SMRiQ96RQ3.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96RQ3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini48 – 494Biotin carboxylationAdd BLAST447
Domaini167 – 364ATP-graspPROSITE-ProRule annotationAdd BLAST198
Domaini643 – 715Biotinyl-bindingPROSITE-ProRule annotationAdd BLAST73

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0238. Eukaryota.
COG4770. LUCA.
GeneTreeiENSGT00550000074675.
HOGENOMiHOG000008989.
HOVERGENiHBG000555.
InParanoidiQ96RQ3.
KOiK01968.
OMAiYQLCARK.
OrthoDBiEOG091G06RG.
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.
IPR005481. BC-like_N.
IPR001882. Biotin_BS.
IPR011764. Biotin_carboxylation_dom.
IPR005482. Biotin_COase_C.
IPR000089. Biotin_lipoyl.
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.
PF00289. Biotin_carb_N. 1 hit.
PF00364. Biotin_lipoyl. 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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti469F → L in AAK67986 (PubMed:11406611).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07248646G → E in MCC1D. 2 PublicationsCorresponds to variant rs199517715dbSNPEnsembl.1
Natural variantiVAR_07248756N → K in MCC1D. 2 Publications1
Natural variantiVAR_07248865M → L in MCC1D. 1 Publication1
Natural variantiVAR_072489123Q → H in MCC1D. 1 Publication1
Natural variantiVAR_072490125I → M in MCC1D. 1 Publication1
Natural variantiVAR_072491134E → K in MCC1D. 2 Publications1
Natural variantiVAR_072492160M → R in MCC1D. 1 Publication1
Natural variantiVAR_072493180G → V in MCC1D. 1 Publication1
Natural variantiVAR_072494187S → P in MCC1D. 2 PublicationsCorresponds to variant rs757362635dbSNPEnsembl.1
Natural variantiVAR_072495232R → W in MCC1D. 2 PublicationsCorresponds to variant rs727504004dbSNPEnsembl.1
Natural variantiVAR_072496268A → D in MCC1D. 1 Publication1
Natural variantiVAR_067197276C → R in MCC1D. 1 PublicationCorresponds to variant rs773433541dbSNPEnsembl.1
Natural variantiVAR_067198281R → Q in MCC1D. 3 PublicationsCorresponds to variant rs754437245dbSNPEnsembl.1
Natural variantiVAR_072497288E → G in MCC1D; shows no residual activity. 1 PublicationCorresponds to variant rs746500530dbSNPEnsembl.1
Natural variantiVAR_012785289A → V in MCC1D; mild form. 2 Publications1
Natural variantiVAR_072498291A → V in MCC1D; associated with a reduction of wild-type residual activity. 2 PublicationsCorresponds to variant rs201041864dbSNPEnsembl.1
Natural variantiVAR_012786325M → R in MCC1D. 2 PublicationsCorresponds to variant rs119103212dbSNPEnsembl.1
Natural variantiVAR_072499372Q → P in MCC1D. 1 PublicationCorresponds to variant rs755328329dbSNPEnsembl.1
Natural variantiVAR_072500379G → D in MCC1D. 1 Publication1
Natural variantiVAR_072501379G → S in MCC1D. 1 Publication1
Natural variantiVAR_072502380H → P in MCC1D. 2 PublicationsCorresponds to variant rs794727036dbSNPEnsembl.1
Natural variantiVAR_012787385R → S in MCC1D; severe form. 5 PublicationsCorresponds to variant rs28934881dbSNPEnsembl.1
Natural variantiVAR_072503434I → M in MCC1D; shows some wild-type residual activity. 1 PublicationCorresponds to variant rs376289130dbSNPEnsembl.1
Natural variantiVAR_012788437L → P in MCC1D; severe form. 1 PublicationCorresponds to variant rs28934882dbSNPEnsembl.1
Natural variantiVAR_072504439V → M in MCC1D. 1 PublicationCorresponds to variant rs398124352dbSNPEnsembl.1
Natural variantiVAR_072505460I → M in MCC1D. 2 PublicationsCorresponds to variant rs119103218dbSNPEnsembl.1
Natural variantiVAR_012789464H → P.5 PublicationsCorresponds to variant rs2270968dbSNPEnsembl.1
Natural variantiVAR_012790532D → H in MCC1D; severe form. 2 PublicationsCorresponds to variant rs119103214dbSNPEnsembl.1
Natural variantiVAR_012791535S → F in MCC1D; asymptomatic form. 2 PublicationsCorresponds to variant rs119103216dbSNPEnsembl.1
Natural variantiVAR_038631560N → T.Corresponds to variant rs35219417dbSNPEnsembl.1
Natural variantiVAR_072506566 – 567Missing in MCC1D. 1 Publication2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2EJMNMR-A640-725[»]
ProteinModelPortaliQ96RQ3.
SMRiQ96RQ3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121249. 32 interactors.
IntActiQ96RQ3. 7 interactors.
STRINGi9606.ENSP00000265594.

Chemistry databases

DrugBankiDB00121. Biotin.

PTM databases

iPTMnetiQ96RQ3.
PhosphoSitePlusiQ96RQ3.
SwissPalmiQ96RQ3.

Polymorphism and mutation databases

BioMutaiMCCC1.
DMDMi108861983.

Proteomic databases

EPDiQ96RQ3.
MaxQBiQ96RQ3.
PaxDbiQ96RQ3.
PeptideAtlasiQ96RQ3.
PRIDEiQ96RQ3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265594; ENSP00000265594; ENSG00000078070.
GeneIDi56922.
KEGGihsa:56922.
UCSCiuc003fle.4. human.

Organism-specific databases

CTDi56922.
DisGeNETi56922.
GeneCardsiMCCC1.
HGNCiHGNC:6936. MCCC1.
HPAiHPA008310.
MalaCardsiMCCC1.
MIMi210200. phenotype.
609010. gene.
neXtProtiNX_Q96RQ3.
OpenTargetsiENSG00000078070.
Orphaneti6. Isolated 3-methylcrotonyl-CoA carboxylase deficiency.
PharmGKBiPA30680.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0238. Eukaryota.
COG4770. LUCA.
GeneTreeiENSGT00550000074675.
HOGENOMiHOG000008989.
HOVERGENiHBG000555.
InParanoidiQ96RQ3.
KOiK01968.
OMAiYQLCARK.
OrthoDBiEOG091G06RG.
PhylomeDBiQ96RQ3.
TreeFamiTF105650.

Enzyme and pathway databases

UniPathwayiUPA00363; UER00861.
BioCyciMetaCyc:ENSG00000078070-MONOMER.
ZFISH:ENSG00000078070-MONOMER.
ReactomeiR-HSA-196780. Biotin transport and metabolism.
R-HSA-3371599. Defective HLCS causes multiple carboxylase deficiency.
R-HSA-70895. Branched-chain amino acid catabolism.

Miscellaneous databases

ChiTaRSiMCCC1. human.
EvolutionaryTraceiQ96RQ3.
GenomeRNAii56922.
PROiQ96RQ3.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000078070.
CleanExiHS_MCCC1.
ExpressionAtlasiQ96RQ3. baseline and differential.
GenevisibleiQ96RQ3. HS.

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.
IPR005481. BC-like_N.
IPR001882. Biotin_BS.
IPR011764. Biotin_carboxylation_dom.
IPR005482. Biotin_COase_C.
IPR000089. Biotin_lipoyl.
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.
PF00289. Biotin_carb_N. 1 hit.
PF00364. Biotin_lipoyl. 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]
ProtoNetiSearch...

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: November 30, 2016
This is version 173 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

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 one 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.