Q9YHA0 (EYA1_CHICK) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Eyes absent homolog 1
EC=3.1.3.48

Gene names

Name:

EYA1

Organism

Gallus gallus (Chicken) [Reference proteome]

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Sauropsida › Sauria › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	119 AA.
Sequence status	Fragment.
Protein existence	Inferred from homology

General annotation (Comments)

Function	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.
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
Cofactor	Binds 1 Mg2+ ion per subunit By similarity.
Subcellular location	Cytoplasm By similarity. Nucleus By similarity.
Sequence similarities	Belongs to the HAD-like hydrolase superfamily. EYA family.

Ontologies

Keywords
Biological process	DNA damage DNA repair Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Ligand	Magnesium
Molecular function	Activator Chromatin regulator Developmental protein Hydrolase Protein phosphatase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	aorta morphogenesis Inferred from electronic annotation. Source: Compara branching involved in ureteric bud morphogenesis Inferred from electronic annotation. Source: Compara cell fate commitment Inferred from electronic annotation. Source: Compara cellular protein localization Inferred from electronic annotation. Source: Compara cochlea morphogenesis Inferred from electronic annotation. Source: Compara double-strand break repair Inferred from sequence or structural similarity. Source: UniProtKB embryonic skeletal system morphogenesis Inferred from electronic annotation. Source: Compara establishment of mitotic spindle orientation Inferred from electronic annotation. Source: Compara establishment or maintenance of apical/basal cell polarity Inferred from electronic annotation. Source: Compara histone dephosphorylation Inferred from sequence or structural similarity. Source: UniProtKB lung epithelial cell differentiation Inferred from electronic annotation. Source: Compara metanephros development Inferred from electronic annotation. Source: Compara middle ear morphogenesis Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara otic vesicle morphogenesis Inferred from electronic annotation. Source: Compara outer ear morphogenesis Inferred from electronic annotation. Source: Compara outflow tract morphogenesis Inferred from electronic annotation. Source: Compara pattern specification process Inferred from electronic annotation. Source: Compara pharyngeal system development Inferred from electronic annotation. Source: Compara positive regulation of DNA repair Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of Notch signaling pathway Inferred from electronic annotation. Source: Compara positive regulation of epithelial cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of secondary heart field cardioblast proliferation Inferred from electronic annotation. Source: Compara positive regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara protein sumoylation Inferred from sequence or structural similarity. Source: UniProtKB regulation of neuron differentiation Inferred from electronic annotation. Source: Compara response to ionizing radiation Inferred from sequence or structural similarity. Source: UniProtKB semicircular canal morphogenesis Inferred from electronic annotation. Source: Compara striated muscle tissue development Inferred from electronic annotation. Source: Compara transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	protein tyrosine phosphatase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	‹1 – ›119	›119	Eyes absent homolog 1		PRO_0000218645
Experimental info
	Non-terminal residue	1	1
	Non-terminal residue	119	1

Sequences

	Sequence		Length	Mass (Da)
	Q9YHA0 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: DD24DF364AD166E6	FASTA	119	13,549
	10 20 30 40 50 60 RKLAFRYRRV KEIYNTYKNN VGGLLGPAKR EAWLQLRAEI EALTDSWLTL ALKALTLIHS 70 80 90 100 110 RTNCVNILVT TTQLIPALAK VLLYGLGVVF PIENIYSATK IGKESCFERI IQRFGRKVV

References

[1]

"EYA4, a novel vertebrate gene related to Drosophila eyes absent." Borsani G., DeGrandi A., Ballabio A., Bulfone A., Bernard L., Banfi S., Gattuso C., Mariani M., Dixon M., Donnai D., Metcalfe K., Winter R., Robertson M., Axton R., Brown A., van Heyningen V., Hanson I. Hum. Mol. Genet. 8:11-23(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Embryo.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ008002 mRNA. Translation: CAA07822.1.
IPI	IPI00602564.
UniGene	Gga.2329.
3D structure databases
ProteinModelPortal	Q9YHA0.
ModBase	Search...
Protein-protein interaction databases
STRING	9031.ENSGALP00000025135.
Proteomic databases
PaxDb	Q9YHA0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
eggNOG	NOG297494.
HOGENOM	HOG000293149.
InParanoid	Q9YHA0.
OrthoDB	EOG4XH000.
Family and domain databases
ProtoNet	Search...

Entry information

Entry name

EYA1_CHICK

Accession

Primary (citable) accession number: Q9YHA0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 1, 1999
Last modified:	April 3, 2013
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program