E9PLN6 · E9PLN6_HUMAN

  • Protein
    Eyes absent homolog
  • Gene
    EYA4
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    2/5

Function

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 1 Mg2+ ion per subunit.

Features

Showing features for active site, binding site.

161650100150200250300350400450500550600
TypeIDPosition(s)Description
Active site352Nucleophile
Binding site352Mg2+ (UniProtKB | ChEBI)
Active site354Proton donor
Binding site354Mg2+ (UniProtKB | ChEBI)
Binding site580Mg2+ (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 Componentnucleus
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
      EYA4

Organism names

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

Accessions

  • Primary accession
    E9PLN6

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 879 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)4PRIDEPhosphoserine
Modified residue (large scale data)29PRIDEPhosphoserine
Modified residue (large scale data)37PRIDEPhosphoserine
Modified residue (large scale data)47PRIDEPhosphothreonine
Modified residue (large scale data)108PRIDEPhosphoserine
Modified residue (large scale data)111PRIDEPhosphoserine
Modified residue (large scale data)116PRIDEPhosphoserine
Modified residue (large scale data)338PRIDEPhosphoserine

Proteomic databases

Expression

Gene expression databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region1-66Disordered
Compositional bias10-34Polar residues
Compositional bias50-66Polar residues
Compositional bias277-314Polar residues
Region277-345Disordered

Sequence similarities

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    616
  • Mass (Da)
    66,977
  • Last updated
    2011-04-05 v1
  • Checksum
    FCAEBEDDD6E4EC20
MEDSQDLNEQSVKKTCTESDVSQSQNSRSMEMQDLASPHTLVGGGDTPGSSKLEKSNLSSTSVTTNGTGVSLLAVKTEPLNSSETTATTGDGALDTFTGSVITSSGYSPRSAHQYSPQLYPSKPYPHILSTPAAQTMSAYAGQTQYSGMQQPAVYTAYSQTGQPYSLPTYDLGVMLPAIKTESGLSQTQSPLQSGCLSYSPGFSTPQPGQTPYSYQMPGSSFAPSSTIYANNSVSNSTNFSGSQQDYPSYTAFGQNQYAQYYSASTYGAYMTSNNTADGTPSSTSTYQLQESLPGLTNQPGEFDTMQSPSTPIKDLDERTCRSSGSKSRGRGRKNNPSPPPDSDLERVFVWDLDETIIVFHSLLTGSYAQKYGKDPPMAVTLGLRMEEMIFNLADTHLFFNDLEECDQVHIDDVSSDDNGQDLSTYSFATDGFHAAASSANLCLPTGVRGGVDWMRKLAFRYRRVKELYNTYKNNVGGLLGPAKRDAWLQLRAEIEGLTDSWLTNALKSLSIISTRSNCINVLVTTTQLIPALAKVLLYSLGGAFPIENIYSATKIGKESCFERIVSRFGTNITYVVIGDGRDEEHAANQHNMPFWRISSHSDLLALHQALELEYL

Computationally mapped potential isoform sequences

There are 6 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
O95677EYA4_HUMANEYA4639
E7ESD5E7ESD5_HUMANEYA4570
A0A8C8KDW0A0A8C8KDW0_HUMANEYA4591
A0A804HHY3A0A804HHY3_HUMANEYA4415
A0A804HL00A0A804HL00_HUMANEYA4293
F2Z2Y1F2Z2Y1_HUMANEYA4645

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias10-34Polar residues
Compositional bias50-66Polar residues
Compositional bias277-314Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AL024497
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AL121959
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AL356242
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AL450270
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
KF458286
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
KF458290
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Genome annotation databases

Similar Proteins

Disclaimer

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