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Eyes absent homolog 1 (EC 3.1.3.16) (EC 3.1.3.48)

 EYA1_HUMAN              Reviewed;         592 AA.
Q99502; A6NHQ0; G5E9R4; Q0P516; Q8WX80;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
15-JUL-1998, sequence version 2.
18-JUL-2018, entry version 163.
RecName: Full=Eyes absent homolog 1;
EC=3.1.3.16 {ECO:0000269|PubMed:19234442};
EC=3.1.3.48 {ECO:0000269|PubMed:19234442};
Name=EYA1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, AND VARIANTS BOR1
PRO-487 AND ARG-505.
TISSUE=Embryo;
PubMed=9361030; DOI=10.1093/hmg/6.13.2247;
Abdelhak S., Kalatzis V., Heilig R., Compain S., Samson D.,
Vincent C., Levi-Acobas F., Cruaud C., le Merrer M., Mathieu M.,
Koenig R., Vigneron J., Weissenbach J., Petit C., Weil D.;
"Clustering of mutations responsible for branchio-oto-renal (BOR)
syndrome in the eyes absent homologous region (eyaHR) of EYA1.";
Hum. Mol. Genet. 6:2247-2255(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM EYA1A).
TISSUE=Embryo;
PubMed=9020840; DOI=10.1038/ng0297-157;
Abdelhak S., Kalatzis V., Heilig R., Compain S., Samson D.,
Vincent C., Weil D., Cruaud C., Sahly I., Leibovici M.,
Bitner-Glindzicz M., Francis M., Lacombe D., Vigneron J.,
Charachon R., Boven K., Bedbeder P., van Regemorter N.,
Weissenbach J., Petit C.;
"A human homologue of the Drosophila eyes absent gene underlies
branchio-oto-renal (BOR) syndrome and identifies a novel gene
family.";
Nat. Genet. 15:157-164(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM EYA1D), AND ALTERNATIVE SPLICING.
TISSUE=Kidney;
Vervoort V.S., Schwartz C.E.;
"EYA1D, a novel EYA1 isoform.";
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
INVOLVEMENT IN BOS1.
PubMed=9359046;
Vincent C., Kalatzis V., Abdelhak S., Chaib H., Compain S., Helias J.,
Vaneecloo F.M., Petit C.;
"BOR and BO syndromes are allelic defects of EYA1.";
Eur. J. Hum. Genet. 5:242-246(1997).
[8]
INVOLVEMENT IN OTFCS1.
PubMed=11409867; DOI=10.1007/s004390100495;
Rickard S., Parker M., van't Hoff W., Barnicoat A., Russell-Eggitt I.,
Winter R.M., Bitner-Glindzicz M.;
"Oto-facio-cervical (OFC) syndrome is a contiguous gene deletion
syndrome involving EYA1: molecular analysis confirms allelism with BOR
syndrome and further narrows the Duane syndrome critical region to 1
cM.";
Hum. Genet. 108:398-403(2001).
[9]
SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
PubMed=12500905; DOI=10.1023/A:1020990825644;
Fougerousse F., Durand M., Lopez S., Suel L., Demignon J.,
Thornton C., Ozaki H., Kawakami K., Barbet P., Beckmann J.S.,
Maire P.;
"Six and Eya expression during human somitogenesis and MyoD gene
family activation.";
J. Muscle Res. Cell Motil. 23:255-264(2002).
[10]
INVOLVEMENT IN OTFCS1.
PubMed=16441263; DOI=10.1111/j.1529-8817.2005.00204.x;
Estefania E., Ramirez-Camacho R., Gomar M., Trinidad A., Arellano B.,
Garcia-Berrocal J.R., Verdaguer J.M., Vilches C.;
"Point mutation of an EYA1-gene splice site in a patient with oto-
facio-cervical syndrome.";
Ann. Hum. Genet. 70:140-144(2006).
[11]
INVOLVEMENT IN BOS1.
PubMed=16691597; DOI=10.1002/ajmg.a.31285;
Spruijt L., Hoefsloot L.H., van Schaijk G.H.W.H., van Waardenburg D.,
Kremer B., Brackel H.J.L., de Die-Smulders C.E.M.;
"Identification of a novel EYA1 mutation presenting in a newborn with
laryngomalacia, glossoptosis, retrognathia, and pectus excavatum.";
Am. J. Med. Genet. A 140:1343-1345(2006).
[12]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
ASP-328.
PubMed=19234442; DOI=10.1038/nature07849;
Cook P.J., Ju B.G., Telese F., Wang X., Glass C.K., Rosenfeld M.G.;
"Tyrosine dephosphorylation of H2AX modulates apoptosis and survival
decisions.";
Nature 458:591-596(2009).
[13]
VARIANT BOR1 GLN-440.
PubMed=10464653; DOI=10.1089/gte.1997.1.243;
Kumar S., Deffenbacher K., Cremers C.W.R.J., Van Camp G.,
Kimberling W.J.;
"Branchio-oto-renal syndrome: identification of novel mutations,
molecular characterization, mutation distribution, and prospects for
genetic testing.";
Genet. Test. 1:243-251(1997).
[14]
VARIANTS ASA LYS-363 AND GLY-547, AND VARIANT BOR1 SER-426.
PubMed=10655545; DOI=10.1093/hmg/9.3.363;
Azuma N., Hirakiyama A., Inoue T., Asaka A., Yamada M.;
"Mutations of a human homologue of the Drosophila eyes absent gene
(EYA1) detected in patients with congenital cataracts and ocular
anterior segment anomalies.";
Hum. Mol. Genet. 9:363-366(2000).
[15]
VARIANT BOR1 PRO-583.
PubMed=10991693; DOI=10.1136/jmg.37.8.623;
Rickard S., Boxer M., Trompeter R., Bitner-Glindzicz M.;
"Importance of clinical evaluation and molecular testing in the
branchio-oto-renal (BOR) syndrome and overlapping phenotypes.";
J. Med. Genet. 37:623-627(2000).
[16]
VARIANT BOR1 GLY-429.
PubMed=11558900; DOI=10.1007/s100380170033;
Namba A., Abe S., Shinkawa H., Kimberling W.J., Usami S.;
"Genetic features of hearing loss associated with ear anomalies: PDS
and EYA1 mutation analysis.";
J. Hum. Genet. 46:518-521(2001).
[17]
VARIANT BOS1 GLY-242.
PubMed=12701758; DOI=10.1080/0036554021000028103;
Yashima T., Noguchi Y., Ishikawa K., Mizusawa H., Kitamura K.;
"Mutation of the EYA1 gene in patients with branchio-oto syndrome.";
Acta Oto-Laryngol. 123:279-282(2003).
[18]
VARIANTS BOR1 SER-95; SER-140; VAL-363; GLN-440; PRO-514; CYS-527 AND
THR-569.
PubMed=21280147; DOI=10.1002/humu.21402;
Krug P., Moriniere V., Marlin S., Koubi V., Gabriel H.D., Colin E.,
Bonneau D., Salomon R., Antignac C., Heidet L.;
"Mutation screening of the EYA1, SIX1, and SIX5 genes in a large
cohort of patients harboring branchio-oto-renal syndrome calls into
question the pathogenic role of SIX5 mutations.";
Hum. Mutat. 32:183-190(2011).
[19]
VARIANT LYS-41.
PubMed=23508780; DOI=10.1007/s00439-013-1289-0;
Reis L.M., Tyler R.C., Muheisen S., Raggio V., Salviati L., Han D.P.,
Costakos D., Yonath H., Hall S., Power P., Semina E.V.;
"Whole exome sequencing in dominant cataract identifies a new
causative factor, CRYBA2, and a variety of novel alleles in known
genes.";
Hum. Genet. 132:761-770(2013).
-!- FUNCTION: Functions both as protein phosphatase and as
transcriptional coactivator for SIX1, and probably also for SIX2,
SIX4 and SIX5 (By similarity). Tyrosine phosphatase that
dephosphorylates 'Tyr-142' of histone H2AX (H2AXY142ph) and
promotes efficient DNA repair via the recruitment of DNA repair
complexes containing MDC1. '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 (PubMed:19234442). Its function as histone phosphatase may
contribute to its function in transcription regulation during
organogenesis (By similarity). Has also phosphatase activity with
proteins phosphorylated on Ser and Thr residues (in vitro) (By
similarity). Required for normal embryonic development of the
craniofacial and trunk skeleton, kidneys and ears (By similarity).
Together with SIX1, it plays an important role in hypaxial muscle
development; in this it is functionally redundant with EYA2 (By
similarity). {ECO:0000250|UniProtKB:P97767,
ECO:0000269|PubMed:19234442}.
-!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
tyrosine + phosphate. {ECO:0000269|PubMed:19234442}.
-!- CATALYTIC ACTIVITY: [a protein]-serine/threonine phosphate + H(2)O
= [a protein]-serine/threonine + phosphate.
{ECO:0000269|PubMed:19234442}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:O00167};
Note=Binds 1 Mg(2+) ion per subunit.
{ECO:0000250|UniProtKB:O00167};
-!- SUBUNIT: Probably interacts with SIX2, SIX4 and SIX5. Interacts
with H2AX in response to DNA damage. Interacts with SIX3; promotes
EYA1 translocation to the nucleus. {ECO:0000250|UniProtKB:P97767}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12500905}.
Nucleus {ECO:0000269|PubMed:12500905,
ECO:0000269|PubMed:19234442}. Note=Localizes at sites of DNA
damage at double-strand breaks (DSBs).
{ECO:0000269|PubMed:19234442}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=EYA1A;
IsoId=Q99502-1; Sequence=Displayed;
Name=EYA1B;
IsoId=Q99502-2; Sequence=VSP_001486;
Name=EYA1D;
IsoId=Q99502-3; Sequence=VSP_045793, VSP_045794;
-!- TISSUE SPECIFICITY: In the embryo, highly expressed in kidney with
lower levels in brain. Weakly expressed in lung. In the adult,
highly expressed in heart and skeletal muscle. Weakly expressed in
brain and liver. No expression in eye or kidney.
-!- DEVELOPMENTAL STAGE: Detected in cytoplasm of somite cells at the
beginning of fourth week of development. Detected in cytoplasm of
limb bud cell between the sixth and eighth week of development.
{ECO:0000269|PubMed:12500905}.
-!- PTM: Sumoylated with SUMO1. {ECO:0000250}.
-!- DISEASE: Branchiootorenal syndrome 1 (BOR1) [MIM:113650]: A
syndrome characterized by branchial cleft fistulas or cysts,
sensorineural and/or conductive hearing loss, pre-auricular pits,
structural defects of the outer, middle or inner ear, and renal
malformations. {ECO:0000269|PubMed:10464653,
ECO:0000269|PubMed:10655545, ECO:0000269|PubMed:10991693,
ECO:0000269|PubMed:11558900, ECO:0000269|PubMed:21280147,
ECO:0000269|PubMed:9361030}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Otofaciocervical syndrome 1 (OTFCS1) [MIM:166780]: A
disorder characterized by facial dysmorphism, cup-shaped low-set
ears, preauricular fistulas, hearing loss, branchial defects,
skeletal anomalies including vertebral defects, low-set clavicles,
winged scapulae, sloping shoulders, and mild intellectual
disability. {ECO:0000269|PubMed:11409867,
ECO:0000269|PubMed:16441263}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Branchiootic syndrome 1 (BOS1) [MIM:602588]: A syndrome
characterized by usually bilateral branchial cleft fistulas or
cysts, sensorineural and/or conductive hearing loss, pre-auricular
pits, and structural defects of the outer, middle or inner ear.
Otic defects include malformed and hypoplastic pinnae, a narrowed
external ear canal, bulbous internal auditory canal, stapes
fixation, malformed and hypoplastic cochlea. Branchial and otic
anomalies overlap with those seen in individuals with the
branchiootorenal syndrome. However renal anomalies are absent in
branchiootic syndrome patients. {ECO:0000269|PubMed:12701758,
ECO:0000269|PubMed:16691597, ECO:0000269|PubMed:9359046}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Anterior segment anomalies with or without cataract (ASA)
[MIM:602588]: A disease characterized by various types of
developmental eye anomalies, in the absence of other
abnormalities. The phenotypic spectrum of anterior segment
anomalies include central corneal opacity, Peters anomaly, and
bilateral persistence of the pupillary membrane. Some patients
have cataract. {ECO:0000269|PubMed:10655545}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. EYA
family. {ECO:0000305}.
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EMBL; Y10260; CAA71309.1; -; Genomic_DNA.
EMBL; AJ000097; CAA03922.1; -; mRNA.
EMBL; AJ000098; CAA03923.1; -; mRNA.
EMBL; AF467247; AAL73437.1; -; mRNA.
EMBL; AC016465; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC022858; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471068; EAW86976.1; -; Genomic_DNA.
EMBL; BC121799; AAI21800.1; -; mRNA.
CCDS; CCDS34906.1; -. [Q99502-1]
RefSeq; NP_000494.2; NM_000503.5. [Q99502-1]
RefSeq; NP_001275503.1; NM_001288574.1.
RefSeq; NP_001275504.1; NM_001288575.1.
RefSeq; NP_742055.1; NM_172058.3. [Q99502-1]
RefSeq; NP_742056.1; NM_172059.3.
RefSeq; NP_742057.1; NM_172060.3.
RefSeq; XP_016868695.1; XM_017013206.1. [Q99502-1]
RefSeq; XP_016868701.1; XM_017013212.1. [Q99502-2]
UniGene; Hs.444971; -.
UniGene; Hs.491997; -.
UniGene; Hs.612611; -.
ProteinModelPortal; Q99502; -.
SMR; Q99502; -.
BioGrid; 108439; 20.
DIP; DIP-60446N; -.
IntAct; Q99502; 3.
STRING; 9606.ENSP00000342626; -.
DEPOD; Q99502; -.
iPTMnet; Q99502; -.
PhosphoSitePlus; Q99502; -.
DMDM; 3183005; -.
MaxQB; Q99502; -.
PaxDb; Q99502; -.
PeptideAtlas; Q99502; -.
PRIDE; Q99502; -.
ProteomicsDB; 78303; -.
ProteomicsDB; 78304; -. [Q99502-2]
Ensembl; ENST00000340726; ENSP00000342626; ENSG00000104313. [Q99502-1]
Ensembl; ENST00000388740; ENSP00000373392; ENSG00000104313. [Q99502-2]
Ensembl; ENST00000388742; ENSP00000373394; ENSG00000104313. [Q99502-1]
Ensembl; ENST00000419131; ENSP00000410176; ENSG00000104313. [Q99502-3]
Ensembl; ENST00000644427; ENSP00000496702; ENSG00000104313. [Q99502-1]
Ensembl; ENST00000645793; ENSP00000496255; ENSG00000104313. [Q99502-1]
Ensembl; ENST00000647540; ENSP00000494438; ENSG00000104313. [Q99502-1]
GeneID; 2138; -.
KEGG; hsa:2138; -.
UCSC; uc003xyr.6; human. [Q99502-1]
CTD; 2138; -.
DisGeNET; 2138; -.
EuPathDB; HostDB:ENSG00000104313.17; -.
GeneCards; EYA1; -.
GeneReviews; EYA1; -.
HGNC; HGNC:3519; EYA1.
HPA; HPA028917; -.
MalaCards; EYA1; -.
MIM; 113650; phenotype.
MIM; 166780; phenotype.
MIM; 601653; gene.
MIM; 602588; phenotype.
neXtProt; NX_Q99502; -.
OpenTargets; ENSG00000104313; -.
Orphanet; 107; BOR syndrome.
Orphanet; 52429; Branchio-otic syndrome.
Orphanet; 2792; Otofaciocervical syndrome.
PharmGKB; PA27931; -.
eggNOG; KOG3107; Eukaryota.
eggNOG; ENOG410XT12; LUCA.
GeneTree; ENSGT00390000008860; -.
HOGENOM; HOG000293149; -.
HOVERGEN; HBG002447; -.
InParanoid; Q99502; -.
KO; K15616; -.
OMA; YATYPQP; -.
OrthoDB; EOG091G04YD; -.
PhylomeDB; Q99502; -.
TreeFam; TF319337; -.
Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
SIGNOR; Q99502; -.
ChiTaRS; EYA1; human.
GeneWiki; EYA1; -.
GenomeRNAi; 2138; -.
PRO; PR:Q99502; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000104313; -.
CleanEx; HS_EYA1; -.
ExpressionAtlas; Q99502; baseline and differential.
Genevisible; Q99502; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0032993; C:protein-DNA complex; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IEA:Ensembl.
GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
GO; GO:0035909; P:aorta morphogenesis; IEA:Ensembl.
GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IEA:Ensembl.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0090103; P:cochlea morphogenesis; IEA:Ensembl.
GO; GO:0006302; P:double-strand break repair; IMP:UniProtKB.
GO; GO:0048704; P:embryonic skeletal system morphogenesis; IEA:Ensembl.
GO; GO:0016576; P:histone dephosphorylation; IDA:UniProtKB.
GO; GO:0007501; P:mesodermal cell fate specification; IEA:Ensembl.
GO; GO:0001656; P:metanephros development; IEA:Ensembl.
GO; GO:0042474; P:middle ear morphogenesis; IEA:Ensembl.
GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IBA:GO_Central.
GO; GO:0048665; P:neuron fate specification; IEA:Ensembl.
GO; GO:0071600; P:otic vesicle morphogenesis; IEA:Ensembl.
GO; GO:0042473; P:outer ear morphogenesis; IEA:Ensembl.
GO; GO:0003151; P:outflow tract morphogenesis; IEA:Ensembl.
GO; GO:0007389; P:pattern specification process; IEA:Ensembl.
GO; GO:0060037; P:pharyngeal system development; IEA:Ensembl.
GO; GO:0045739; P:positive regulation of DNA repair; IMP:UniProtKB.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IEA:Ensembl.
GO; GO:0072513; P:positive regulation of secondary heart field cardioblast proliferation; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0016925; P:protein sumoylation; ISS:UniProtKB.
GO; GO:0045664; P:regulation of neuron differentiation; IEA:Ensembl.
GO; GO:0010212; P:response to ionizing radiation; IDA:UniProtKB.
GO; GO:0048752; P:semicircular canal morphogenesis; IEA:Ensembl.
GO; GO:0007605; P:sensory perception of sound; TAS:ProtInc.
GO; GO:0014706; P:striated muscle tissue development; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd02601; HAD_Eya; 1.
Gene3D; 3.40.50.12350; -; 1.
InterPro; IPR006545; EYA_dom.
InterPro; IPR038102; EYA_dom_sf.
InterPro; IPR028472; EYA_fam.
InterPro; IPR028471; Eyes_absent_h1.
PANTHER; PTHR10190; PTHR10190; 1.
PANTHER; PTHR10190:SF11; PTHR10190:SF11; 1.
TIGRFAMs; TIGR01658; EYA-cons_domain; 1.
1: Evidence at protein level;
Activator; Alternative splicing; Chromatin regulator;
Complete proteome; Cytoplasm; Deafness; Developmental protein;
Disease mutation; DNA damage; DNA repair; Hydrolase; Magnesium;
Mental retardation; Metal-binding; Nucleus; Polymorphism;
Protein phosphatase; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 592 Eyes absent homolog 1.
/FTId=PRO_0000218643.
ACT_SITE 328 328 Nucleophile.
{ECO:0000250|UniProtKB:O00167}.
ACT_SITE 330 330 Proton donor.
{ECO:0000250|UniProtKB:O00167}.
METAL 328 328 Magnesium.
{ECO:0000250|UniProtKB:O00167}.
METAL 330 330 Magnesium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:O00167}.
METAL 556 556 Magnesium.
{ECO:0000250|UniProtKB:O00167}.
VAR_SEQ 1 41 MEMQDLTSPHSRLSGSSESPSGPKLGNSHINSNSMTPNGTE
-> MLLFPQVA (in isoform EYA1B).
{ECO:0000305}.
/FTId=VSP_001486.
VAR_SEQ 140 144 Missing (in isoform EYA1D).
{ECO:0000303|Ref.3}.
/FTId=VSP_045793.
VAR_SEQ 351 380 Missing (in isoform EYA1D).
{ECO:0000303|Ref.3}.
/FTId=VSP_045794.
VARIANT 20 20 P -> A (in dbSNP:rs1445404).
/FTId=VAR_024439.
VARIANT 41 41 E -> K (found in a patient with
congenital cataract; dbSNP:rs561111097).
{ECO:0000269|PubMed:23508780}.
/FTId=VAR_070033.
VARIANT 95 95 P -> S (in BOR1).
{ECO:0000269|PubMed:21280147}.
/FTId=VAR_064942.
VARIANT 140 140 G -> S (in BOR1).
{ECO:0000269|PubMed:21280147}.
/FTId=VAR_064943.
VARIANT 242 242 S -> G (in BOS1; dbSNP:rs191838840).
{ECO:0000269|PubMed:12701758}.
/FTId=VAR_044452.
VARIANT 363 363 E -> K (in ASA; dbSNP:rs121909198).
{ECO:0000269|PubMed:10655545}.
/FTId=VAR_016864.
VARIANT 363 363 E -> V (in BOR1).
{ECO:0000269|PubMed:21280147}.
/FTId=VAR_064944.
VARIANT 426 426 G -> S (in BOR1; with cataract;
dbSNP:rs121909199).
{ECO:0000269|PubMed:10655545}.
/FTId=VAR_016865.
VARIANT 429 429 D -> G (in BOR1).
{ECO:0000269|PubMed:11558900}.
/FTId=VAR_016866.
VARIANT 440 440 R -> Q (in BOR1; dbSNP:rs121909196).
{ECO:0000269|PubMed:10464653,
ECO:0000269|PubMed:21280147}.
/FTId=VAR_016867.
VARIANT 487 487 S -> P (in BOR1; dbSNP:rs121909200).
{ECO:0000269|PubMed:9361030}.
/FTId=VAR_005203.
VARIANT 505 505 L -> R (in BOR1; dbSNP:rs121909201).
{ECO:0000269|PubMed:9361030}.
/FTId=VAR_005204.
VARIANT 514 514 L -> P (in BOR1; dbSNP:rs112340154).
{ECO:0000269|PubMed:21280147}.
/FTId=VAR_064945.
VARIANT 527 527 Y -> C (in BOR1).
{ECO:0000269|PubMed:21280147}.
/FTId=VAR_064946.
VARIANT 547 547 R -> G (in ASA; with cataract;
dbSNP:rs121909197).
{ECO:0000269|PubMed:10655545}.
/FTId=VAR_016868.
VARIANT 569 569 M -> T (in BOR1).
{ECO:0000269|PubMed:21280147}.
/FTId=VAR_064947.
VARIANT 583 583 L -> P (in BOR1; dbSNP:rs397517920).
{ECO:0000269|PubMed:10991693}.
/FTId=VAR_016869.
MUTAGEN 328 328 D->A: Loss of tyrosine phosphatase
activity toward H2AX.
{ECO:0000269|PubMed:19234442}.
CONFLICT 33 33 N -> D (in Ref. 3; AAL73437).
{ECO:0000305}.
SEQUENCE 592 AA; 64593 MW; D62365F81EB692E2 CRC64;
MEMQDLTSPH SRLSGSSESP SGPKLGNSHI NSNSMTPNGT EVKTEPMSSS ETASTTADGS
LNNFSGSAIG SSSFSPRPTH QFSPPQIYPS NRPYPHILPT PSSQTMAAYG QTQFTTGMQQ
ATAYATYPQP GQPYGISSYG ALWAGIKTEG GLSQSQSPGQ TGFLSYGTSF STPQPGQAPY
SYQMQGSSFT TSSGIYTGNN SLTNSSGFNS SQQDYPSYPS FGQGQYAQYY NSSPYPAHYM
TSSNTSPTTP STNATYQLQE PPSGITSQAV TDPTAEYSTI HSPSTPIKDS DSDRLRRGSD
GKSRGRGRRN NNPSPPPDSD LERVFIWDLD ETIIVFHSLL TGSYANRYGR DPPTSVSLGL
RMEEMIFNLA DTHLFFNDLE ECDQVHIDDV SSDDNGQDLS TYNFGTDGFP AAATSANLCL
ATGVRGGVDW MRKLAFRYRR VKEIYNTYKN NVGGLLGPAK REAWLQLRAE IEALTDSWLT
LALKALSLIH SRTNCVNILV TTTQLIPALA KVLLYGLGIV FPIENIYSAT KIGKESCFER
IIQRFGRKVV YVVIGDGVEE EQGAKKHAMP FWRISSHSDL MALHHALELE YL


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