B1APR7 · B1APR7_HUMAN

  • Protein
    Eyes absent homolog
  • Gene
    EYA3
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    3/5

Function

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 1 Mg2+ ion per subunit.

Features

Showing features for active site, binding site.

141650100150200250300350400
TypeIDPosition(s)Description
Active site152Nucleophile
Binding site152Mg2+ (UniProtKB | ChEBI)
Active site154Proton donor
Binding site154Mg2+ (UniProtKB | ChEBI)
Binding site380Mg2+ (UniProtKB | ChEBI)

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
Cellular Componentcentrosome
Cellular Componentnucleoplasm
Molecular Functionmetal ion binding
Molecular Functionprotein tyrosine phosphatase activity

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Eyes absent homolog
  • EC number

Gene names

    • Name
      EYA3

Organism names

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

Accessions

  • Primary accession
    B1APR7

Proteomes

Organism-specific databases

Subcellular Location

Keywords

  • Cellular component

Disease & Variants

Variants

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

The viewer provides 344 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Genetic variation databases

PTM/Processing

Features

Showing features for modified residue (large scale data).

TypeIDPosition(s)SourceDescription
Modified residue (large scale data)140PRIDEPhosphoserine
Modified residue (large scale data)281PRIDEPhosphoserine

Proteomic databases

Expression

Gene expression databases

Structure

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region81-139Disordered
Compositional bias97-115Polar residues
Compositional bias116-139Basic and acidic residues

Sequence similarities

Belongs to the HAD-like hydrolase superfamily. EYA family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    416
  • Mass (Da)
    45,549
  • Last updated
    2008-04-08 v1
  • Checksum
    EAA05A439BC4D0B0
MIIPHKCILQTSSTNASLISTSSTIANIPAAAVASISNQDYPTYTILGQNQYQACYPSSSFGVTGQTNSDAESTTLAATTYQSEKPSVMAPAPAAQRLSSDPSTSPSLSQTTPSKDTDDQSRKNMTSKNRGKRKADATSSQDSELERVFLWDLDETIIIFHSLLTGSYAQKYGKDPTVVIGSGLTMEEMIFEVADTHLFFNDLEECDQVHVEDVASDDNGQDLSNYSFSTDGFSGSGGSGSHGSSVGVQGGVDWMRKLAFRYRKVREIYDKHKSNVGGLLSPQRKEALQRLRAEIEVLTDSWLGTALKSLLLIQSRKNCVNVLITTTQLVPALAKVLLYGLGEIFPIENIYSATKIGKESCFERIVSRFGKKVTYVVIGDGRDEEIAAKQHNMPFWRITNHGDLVSLHQALELDFL

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
Q99504EYA3_HUMANEYA3573

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias97-115Polar residues
Compositional bias116-139Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AL137792
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AL512288
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Genome annotation databases

Similar Proteins

Disclaimer

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