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Protein

Eyes absent homolog 4

Gene

EYA4

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Tyrosine phosphatase that specifically dephosphorylates 'Tyr-142' of histone H2AX (H2AXY142ph). 'Tyr-142' phosphorylation of histone H2AX plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress. Promotes efficient DNA repair by dephosphorylating H2AX, promoting the recruitment of DNA repair complexes containing MDC1. Its function as histone phosphatase probably explains its role in transcription regulation during organogenesis. May be involved in development of the eye (By similarity).By similarity

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator, Developmental protein, Hydrolase, Protein phosphatase

Keywords - Biological processi

DNA damage, DNA repair, Transcription, Transcription regulation

Keywords - Ligandi

Magnesium

Names & Taxonomyi

Protein namesi
Recommended name:
Eyes absent homolog 4 (EC:3.1.3.48)
Gene namesi
Name:EYA4
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – ›119›119Eyes absent homolog 4PRO_0000218653Add
BLAST

Proteomic databases

PaxDbiQ9YH98.

Structurei

3D structure databases

ProteinModelPortaliQ9YH98.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG297494.
HOGENOMiHOG000045156.
InParanoidiQ9YH98.
PhylomeDBiQ9YH98.

Family and domain databases

InterProiIPR028478. EYA4.
IPR028472. EYA_fam.
[Graphical view]
PANTHERiPTHR10190. PTHR10190. 1 hit.
PTHR10190:SF17. PTHR10190:SF17. 1 hit.

Sequencei

Sequence statusi: Fragment.

Q9YH98-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
RKLAFRYRRV KELYNTYKNN IGGLLGPAKR DAWLQLRAEI EALTDSWLTN
60 70 80 90 100
ALKSLSIIST RSNCVNVLVT TTQLIPALAK VLLYSLGGAF PIENIYSATK
110
IGKESCFERI VSRFGTNIT
Length:119
Mass (Da):13,340
Last modified:May 1, 1999 - v1
Checksum:i9E6BC4F6F8D0679D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Non-terminal residuei119 – 1191

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ008004 mRNA. Translation: CAA07824.1.
RefSeqiNP_001292106.1. NM_001305177.1.
UniGeneiGga.25747.

Genome annotation databases

GeneIDi395716.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ008004 mRNA. Translation: CAA07824.1.
RefSeqiNP_001292106.1. NM_001305177.1.
UniGeneiGga.25747.

3D structure databases

ProteinModelPortaliQ9YH98.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PaxDbiQ9YH98.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi395716.

Phylogenomic databases

eggNOGiNOG297494.
HOGENOMiHOG000045156.
InParanoidiQ9YH98.
PhylomeDBiQ9YH98.

Family and domain databases

InterProiIPR028478. EYA4.
IPR028472. EYA_fam.
[Graphical view]
PANTHERiPTHR10190. PTHR10190. 1 hit.
PTHR10190:SF17. PTHR10190:SF17. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Embryo.

Entry informationi

Entry nameiEYA4_CHICK
AccessioniPrimary (citable) accession number: Q9YH98
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: July 22, 2015
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.