H0YCA8 · H0YCA8_HUMAN

  • Protein
    Adenine DNA glycosylase
  • Gene
    MUTYH
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    2/5

Function

function

Adenine glycosylase active on G-A mispairs.

Catalytic activity

  • Hydrolyzes free adenine bases from 7,8-dihydro-8-oxoguanine:adenine mismatched double-stranded DNA, leaving an apurinic site.
    EC:3.2.2.31 (UniProtKB | ENZYME | Rhea)

Cofactor

[4Fe-4S] cluster (UniProtKB | Rhea| CHEBI:49883 )

Note: Binds 1 [4Fe-4S] cluster.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Molecular Function4 iron, 4 sulfur cluster binding
Molecular FunctionDNA binding
Molecular Functionhydrolase activity, acting on glycosyl bonds
Molecular Functionmetal ion binding
Biological Processbase-excision repair

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Adenine DNA glycosylase
  • EC number

Gene names

    • Name
      MUTYH

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    H0YCA8

Proteomes

Organism-specific databases

Disease & Variants

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 1,235 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Genetic variation databases

PTM/Processing

Expression

Gene expression databases

Structure

3D structure databases

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region1-38Disordered
Compositional bias22-36Polar residues
Domain339-470Nudix hydrolase

Sequence similarities

Belongs to the Nth/MutY family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    478
  • Mass (Da)
    52,719
  • Last updated
    2024-01-24 v2
  • Checksum
    E1AC718C027FB8BD
MRKPRAAVGSGHRKQAASQEGRQKHAKNNSQAKPSACDGLARQPEEVVLQASVSSYHLFRDVAEVTAFRGSLLSWYDQEKRDLPWRRRAEDEMDLDRRAYAVWVSEVMLQQTQVATVINYYTGWMQKWPTLQDLASASLEEVNQLWAGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQLLPGVGRYTAGAIASIAFGQATGVVDGNVARVLCRVRAIGADPSSTLVSQQLWGLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSQCPVESLCRARQRVEQEQLLASGSLSGSPDVEECAPNTGQCHLCLPPSEPWDQTLGVVNFPRKASRKPPREESSATCVLEQPGALGAQILLVQRPNSGLLAGLWEFPSVTWEPSEQLQRKALLQELQRWAGPLPATHLRHLGEVVHTFSHIKLTYQVYGLALEGQTPVTTVPPGARWLTQEEFHTAAVSTAMKKVFRVYQGQQPGTCM

Computationally mapped potential isoform sequences

There are 21 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
Q9UIF7MUTYH_HUMANMUTYH546
A0AAQ5BGW7A0AAQ5BGW7_HUMANMUTYH528
A0A6Q8PF38A0A6Q8PF38_HUMANMUTYH47
H0YEI2H0YEI2_HUMANMUTYH386
H0YER6H0YER6_HUMANMUTYH97
H0YCY5H0YCY5_HUMANMUTYH472
Q5T413Q5T413_HUMANMUTYH291
Q5T418Q5T418_HUMANMUTYH393
E5KP25E5KP25_HUMANMUTYH549
A0A5F9ZHI2A0A5F9ZHI2_HUMANMUTYH212
A0A5F9ZI14A0A5F9ZI14_HUMANMUTYH466
A0A5F9ZI60A0A5F9ZI60_HUMANMUTYH209
E9PNY0E9PNY0_HUMANMUTYH216
E9PP30E9PP30_HUMANMUTYH45
E9PP34E9PP34_HUMANMUTYH527
E9PLT4E9PLT4_HUMANMUTYH62
E9PM53E9PM53_HUMANMUTYH535
E9PMH1E9PMH1_HUMANMUTYH185
E9PIW5E9PIW5_HUMANMUTYH40
E9PKM9E9PKM9_HUMANMUTYH55
E9PI11E9PI11_HUMANMUTYH54

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias22-36Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AL359540
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Genome annotation databases

Similar Proteins

Disclaimer

Any 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. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp