EYA1_HUMAN
ID EYA1_HUMAN Reviewed; 592 AA.
AC Q99502; A6NHQ0; G5E9R4; Q0P516; Q8WX80;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Eyes absent homolog 1;
DE EC=3.1.3.16 {ECO:0000269|PubMed:19234442};
DE EC=3.1.3.48 {ECO:0000269|PubMed:19234442};
GN Name=EYA1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, AND VARIANTS BOR1 PRO-487
RP AND ARG-505.
RC TISSUE=Embryo;
RX PubMed=9361030; DOI=10.1093/hmg/6.13.2247;
RA Abdelhak S., Kalatzis V., Heilig R., Compain S., Samson D., Vincent C.,
RA Levi-Acobas F., Cruaud C., le Merrer M., Mathieu M., Koenig R.,
RA Vigneron J., Weissenbach J., Petit C., Weil D.;
RT "Clustering of mutations responsible for branchio-oto-renal (BOR) syndrome
RT in the eyes absent homologous region (eyaHR) of EYA1.";
RL Hum. Mol. Genet. 6:2247-2255(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM EYA1A).
RC TISSUE=Embryo;
RX PubMed=9020840; DOI=10.1038/ng0297-157;
RA Abdelhak S., Kalatzis V., Heilig R., Compain S., Samson D., Vincent C.,
RA Weil D., Cruaud C., Sahly I., Leibovici M., Bitner-Glindzicz M.,
RA Francis M., Lacombe D., Vigneron J., Charachon R., Boven K., Bedbeder P.,
RA van Regemorter N., Weissenbach J., Petit C.;
RT "A human homologue of the Drosophila eyes absent gene underlies branchio-
RT oto-renal (BOR) syndrome and identifies a novel gene family.";
RL Nat. Genet. 15:157-164(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM EYA1D), AND ALTERNATIVE SPLICING.
RC TISSUE=Kidney;
RA Vervoort V.S., Schwartz C.E.;
RT "EYA1D, a novel EYA1 isoform.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP INVOLVEMENT IN BOS1.
RX PubMed=9359046;
RA Vincent C., Kalatzis V., Abdelhak S., Chaib H., Compain S., Helias J.,
RA Vaneecloo F.M., Petit C.;
RT "BOR and BO syndromes are allelic defects of EYA1.";
RL Eur. J. Hum. Genet. 5:242-246(1997).
RN [8]
RP INVOLVEMENT IN OTFCS1.
RX PubMed=11409867; DOI=10.1007/s004390100495;
RA Rickard S., Parker M., van't Hoff W., Barnicoat A., Russell-Eggitt I.,
RA Winter R.M., Bitner-Glindzicz M.;
RT "Oto-facio-cervical (OFC) syndrome is a contiguous gene deletion syndrome
RT involving EYA1: molecular analysis confirms allelism with BOR syndrome and
RT further narrows the Duane syndrome critical region to 1 cM.";
RL Hum. Genet. 108:398-403(2001).
RN [9]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=12500905; DOI=10.1023/a:1020990825644;
RA Fougerousse F., Durand M., Lopez S., Suel L., Demignon J., Thornton C.,
RA Ozaki H., Kawakami K., Barbet P., Beckmann J.S., Maire P.;
RT "Six and Eya expression during human somitogenesis and MyoD gene family
RT activation.";
RL J. Muscle Res. Cell Motil. 23:255-264(2002).
RN [10]
RP INVOLVEMENT IN OTFCS1.
RX PubMed=16441263; DOI=10.1111/j.1529-8817.2005.00204.x;
RA Estefania E., Ramirez-Camacho R., Gomar M., Trinidad A., Arellano B.,
RA Garcia-Berrocal J.R., Verdaguer J.M., Vilches C.;
RT "Point mutation of an EYA1-gene splice site in a patient with oto-facio-
RT cervical syndrome.";
RL Ann. Hum. Genet. 70:140-144(2006).
RN [11]
RP INVOLVEMENT IN BOS1.
RX PubMed=16691597; DOI=10.1002/ajmg.a.31285;
RA Spruijt L., Hoefsloot L.H., van Schaijk G.H.W.H., van Waardenburg D.,
RA Kremer B., Brackel H.J.L., de Die-Smulders C.E.M.;
RT "Identification of a novel EYA1 mutation presenting in a newborn with
RT laryngomalacia, glossoptosis, retrognathia, and pectus excavatum.";
RL Am. J. Med. Genet. A 140:1343-1345(2006).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP ASP-328.
RX PubMed=19234442; DOI=10.1038/nature07849;
RA Cook P.J., Ju B.G., Telese F., Wang X., Glass C.K., Rosenfeld M.G.;
RT "Tyrosine dephosphorylation of H2AX modulates apoptosis and survival
RT decisions.";
RL Nature 458:591-596(2009).
RN [13]
RP VARIANT BOR1 GLN-440.
RX PubMed=10464653; DOI=10.1089/gte.1997.1.243;
RA Kumar S., Deffenbacher K., Cremers C.W.R.J., Van Camp G., Kimberling W.J.;
RT "Branchio-oto-renal syndrome: identification of novel mutations, molecular
RT characterization, mutation distribution, and prospects for genetic
RT testing.";
RL Genet. Test. 1:243-251(1997).
RN [14]
RP VARIANTS ASA LYS-363 AND GLY-547, AND VARIANT BOR1 SER-426.
RX PubMed=10655545; DOI=10.1093/hmg/9.3.363;
RA Azuma N., Hirakiyama A., Inoue T., Asaka A., Yamada M.;
RT "Mutations of a human homologue of the Drosophila eyes absent gene (EYA1)
RT detected in patients with congenital cataracts and ocular anterior segment
RT anomalies.";
RL Hum. Mol. Genet. 9:363-366(2000).
RN [15]
RP VARIANT BOR1 PRO-583.
RX PubMed=10991693; DOI=10.1136/jmg.37.8.623;
RA Rickard S., Boxer M., Trompeter R., Bitner-Glindzicz M.;
RT "Importance of clinical evaluation and molecular testing in the branchio-
RT oto-renal (BOR) syndrome and overlapping phenotypes.";
RL J. Med. Genet. 37:623-627(2000).
RN [16]
RP VARIANT BOR1 GLY-429.
RX PubMed=11558900; DOI=10.1007/s100380170033;
RA Namba A., Abe S., Shinkawa H., Kimberling W.J., Usami S.;
RT "Genetic features of hearing loss associated with ear anomalies: PDS and
RT EYA1 mutation analysis.";
RL J. Hum. Genet. 46:518-521(2001).
RN [17]
RP VARIANT BOS1 GLY-242.
RX PubMed=12701758; DOI=10.1080/0036554021000028103;
RA Yashima T., Noguchi Y., Ishikawa K., Mizusawa H., Kitamura K.;
RT "Mutation of the EYA1 gene in patients with branchio-oto syndrome.";
RL Acta Oto-Laryngol. 123:279-282(2003).
RN [18]
RP VARIANTS BOR1 SER-95; SER-140; VAL-363; GLN-440; PRO-514; CYS-527 AND
RP THR-569.
RX PubMed=21280147; DOI=10.1002/humu.21402;
RA Krug P., Moriniere V., Marlin S., Koubi V., Gabriel H.D., Colin E.,
RA Bonneau D., Salomon R., Antignac C., Heidet L.;
RT "Mutation screening of the EYA1, SIX1, and SIX5 genes in a large cohort of
RT patients harboring branchio-oto-renal syndrome calls into question the
RT pathogenic role of SIX5 mutations.";
RL Hum. Mutat. 32:183-190(2011).
RN [19]
RP VARIANT LYS-41.
RX PubMed=23508780; DOI=10.1007/s00439-013-1289-0;
RA Reis L.M., Tyler R.C., Muheisen S., Raggio V., Salviati L., Han D.P.,
RA Costakos D., Yonath H., Hall S., Power P., Semina E.V.;
RT "Whole exome sequencing in dominant cataract identifies a new causative
RT factor, CRYBA2, and a variety of novel alleles in known genes.";
RL Hum. Genet. 132:761-770(2013).
CC -!- FUNCTION: Functions both as protein phosphatase and as transcriptional
CC coactivator for SIX1, and probably also for SIX2, SIX4 and SIX5 (By
CC similarity). Tyrosine phosphatase that dephosphorylates 'Tyr-142' of
CC histone H2AX (H2AXY142ph) and promotes efficient DNA repair via the
CC recruitment of DNA repair complexes containing MDC1. 'Tyr-142'
CC phosphorylation of histone H2AX plays a central role in DNA repair and
CC acts as a mark that distinguishes between apoptotic and repair
CC responses to genotoxic stress (PubMed:19234442). Its function as
CC histone phosphatase may contribute to its function in transcription
CC regulation during organogenesis (By similarity). Has also phosphatase
CC activity with proteins phosphorylated on Ser and Thr residues (in
CC vitro) (By similarity). Required for normal embryonic development of
CC the craniofacial and trunk skeleton, kidneys and ears (By similarity).
CC Together with SIX1, it plays an important role in hypaxial muscle
CC development; in this it is functionally redundant with EYA2 (By
CC similarity). {ECO:0000250|UniProtKB:P97767,
CC ECO:0000269|PubMed:19234442}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48;
CC Evidence={ECO:0000269|PubMed:19234442};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC Evidence={ECO:0000269|PubMed:19234442};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC Evidence={ECO:0000269|PubMed:19234442};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O00167};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:O00167};
CC -!- SUBUNIT: Probably interacts with SIX2, SIX4 and SIX5. Interacts with
CC H2AX in response to DNA damage. Interacts with SIX3; promotes EYA1
CC translocation to the nucleus. {ECO:0000250|UniProtKB:P97767}.
CC -!- INTERACTION:
CC Q99502; Q15475: SIX1; NbExp=4; IntAct=EBI-12244764, EBI-743675;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12500905}. Nucleus
CC {ECO:0000269|PubMed:12500905, ECO:0000269|PubMed:19234442}.
CC Note=Localizes at sites of DNA damage at double-strand breaks (DSBs).
CC {ECO:0000269|PubMed:19234442}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=EYA1A;
CC IsoId=Q99502-1; Sequence=Displayed;
CC Name=EYA1B;
CC IsoId=Q99502-2; Sequence=VSP_001486;
CC Name=EYA1D;
CC IsoId=Q99502-3; Sequence=VSP_045793, VSP_045794;
CC -!- TISSUE SPECIFICITY: In the embryo, highly expressed in kidney with
CC lower levels in brain. Weakly expressed in lung. In the adult, highly
CC expressed in heart and skeletal muscle. Weakly expressed in brain and
CC liver. No expression in eye or kidney.
CC -!- DEVELOPMENTAL STAGE: Detected in cytoplasm of somite cells at the
CC beginning of fourth week of development. Detected in cytoplasm of limb
CC bud cell between the sixth and eighth week of development.
CC {ECO:0000269|PubMed:12500905}.
CC -!- PTM: Sumoylated with SUMO1. {ECO:0000250}.
CC -!- DISEASE: Branchiootorenal syndrome 1 (BOR1) [MIM:113650]: A syndrome
CC characterized by branchial cleft fistulas or cysts, sensorineural
CC and/or conductive hearing loss, pre-auricular pits, structural defects
CC of the outer, middle or inner ear, and renal malformations.
CC {ECO:0000269|PubMed:10464653, ECO:0000269|PubMed:10655545,
CC ECO:0000269|PubMed:10991693, ECO:0000269|PubMed:11558900,
CC ECO:0000269|PubMed:21280147, ECO:0000269|PubMed:9361030}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Otofaciocervical syndrome 1 (OTFCS1) [MIM:166780]: A disorder
CC characterized by facial dysmorphism, cup-shaped low-set ears,
CC preauricular fistulas, hearing loss, branchial defects, skeletal
CC anomalies including vertebral defects, low-set clavicles, winged
CC scapulae, sloping shoulders, and mild intellectual disability.
CC {ECO:0000269|PubMed:11409867, ECO:0000269|PubMed:16441263}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Branchiootic syndrome 1 (BOS1) [MIM:602588]: A syndrome
CC characterized by usually bilateral branchial cleft fistulas or cysts,
CC sensorineural and/or conductive hearing loss, pre-auricular pits, and
CC structural defects of the outer, middle or inner ear. Otic defects
CC include malformed and hypoplastic pinnae, a narrowed external ear
CC canal, bulbous internal auditory canal, stapes fixation, malformed and
CC hypoplastic cochlea. Branchial and otic anomalies overlap with those
CC seen in individuals with the branchiootorenal syndrome. However renal
CC anomalies are absent in branchiootic syndrome patients.
CC {ECO:0000269|PubMed:12701758, ECO:0000269|PubMed:16691597,
CC ECO:0000269|PubMed:9359046}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Anterior segment anomalies with or without cataract (ASA)
CC [MIM:602588]: A disease characterized by various types of developmental
CC eye anomalies, in the absence of other abnormalities. The phenotypic
CC spectrum of anterior segment anomalies include central corneal opacity,
CC Peters anomaly, and bilateral persistence of the pupillary membrane.
CC Some patients have cataract. {ECO:0000269|PubMed:10655545}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. EYA family.
CC {ECO:0000305}.
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DR EMBL; Y10260; CAA71309.1; -; Genomic_DNA.
DR EMBL; AJ000097; CAA03922.1; -; mRNA.
DR EMBL; AJ000098; CAA03923.1; -; mRNA.
DR EMBL; AF467247; AAL73437.1; -; mRNA.
DR EMBL; AC016465; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC022858; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471068; EAW86976.1; -; Genomic_DNA.
DR EMBL; BC121799; AAI21800.1; -; mRNA.
DR CCDS; CCDS34906.1; -. [Q99502-1]
DR RefSeq; NP_000494.2; NM_000503.5. [Q99502-1]
DR RefSeq; NP_001275503.1; NM_001288574.1.
DR RefSeq; NP_001275504.1; NM_001288575.1.
DR RefSeq; NP_742055.1; NM_172058.3. [Q99502-1]
DR RefSeq; NP_742056.1; NM_172059.3.
DR RefSeq; NP_742057.1; NM_172060.3.
DR RefSeq; XP_016868695.1; XM_017013206.1.
DR RefSeq; XP_016868701.1; XM_017013212.1. [Q99502-2]
DR AlphaFoldDB; Q99502; -.
DR SMR; Q99502; -.
DR BioGRID; 108439; 43.
DR CORUM; Q99502; -.
DR DIP; DIP-60446N; -.
DR IntAct; Q99502; 17.
DR MINT; Q99502; -.
DR STRING; 9606.ENSP00000342626; -.
DR DEPOD; EYA1; -.
DR iPTMnet; Q99502; -.
DR PhosphoSitePlus; Q99502; -.
DR BioMuta; EYA1; -.
DR DMDM; 3183005; -.
DR EPD; Q99502; -.
DR MassIVE; Q99502; -.
DR MaxQB; Q99502; -.
DR PaxDb; Q99502; -.
DR PeptideAtlas; Q99502; -.
DR PRIDE; Q99502; -.
DR ProteomicsDB; 34020; -.
DR ProteomicsDB; 78303; -. [Q99502-1]
DR ProteomicsDB; 78304; -. [Q99502-2]
DR Antibodypedia; 25098; 234 antibodies from 31 providers.
DR DNASU; 2138; -.
DR Ensembl; ENST00000340726.8; ENSP00000342626.3; ENSG00000104313.20. [Q99502-1]
DR Ensembl; ENST00000388740.4; ENSP00000373392.3; ENSG00000104313.20. [Q99502-2]
DR Ensembl; ENST00000388742.8; ENSP00000373394.4; ENSG00000104313.20. [Q99502-1]
DR Ensembl; ENST00000419131.6; ENSP00000410176.1; ENSG00000104313.20. [Q99502-3]
DR Ensembl; ENST00000645793.1; ENSP00000496255.1; ENSG00000104313.20. [Q99502-1]
DR Ensembl; ENST00000647540.1; ENSP00000494438.1; ENSG00000104313.20. [Q99502-1]
DR GeneID; 2138; -.
DR KEGG; hsa:2138; -.
DR MANE-Select; ENST00000340726.8; ENSP00000342626.3; NM_000503.6; NP_000494.2.
DR UCSC; uc003xyr.6; human. [Q99502-1]
DR CTD; 2138; -.
DR DisGeNET; 2138; -.
DR GeneCards; EYA1; -.
DR GeneReviews; EYA1; -.
DR HGNC; HGNC:3519; EYA1.
DR HPA; ENSG00000104313; Tissue enhanced (choroid plexus, parathyroid gland).
DR MalaCards; EYA1; -.
DR MIM; 113650; phenotype.
DR MIM; 166780; phenotype.
DR MIM; 601653; gene.
DR MIM; 602588; phenotype.
DR neXtProt; NX_Q99502; -.
DR OpenTargets; ENSG00000104313; -.
DR Orphanet; 107; BOR syndrome.
DR Orphanet; 52429; Branchiootic syndrome.
DR Orphanet; 2792; Otofaciocervical syndrome.
DR PharmGKB; PA27931; -.
DR VEuPathDB; HostDB:ENSG00000104313; -.
DR eggNOG; KOG3107; Eukaryota.
DR GeneTree; ENSGT00950000182978; -.
DR InParanoid; Q99502; -.
DR OMA; FTAGMQQ; -.
DR OrthoDB; 1030296at2759; -.
DR PhylomeDB; Q99502; -.
DR TreeFam; TF319337; -.
DR PathwayCommons; Q99502; -.
DR Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR SignaLink; Q99502; -.
DR SIGNOR; Q99502; -.
DR BioGRID-ORCS; 2138; 8 hits in 1072 CRISPR screens.
DR ChiTaRS; EYA1; human.
DR GeneWiki; EYA1; -.
DR GenomeRNAi; 2138; -.
DR Pharos; Q99502; Tbio.
DR PRO; PR:Q99502; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q99502; protein.
DR Bgee; ENSG00000104313; Expressed in choroid plexus epithelium and 148 other tissues.
DR ExpressionAtlas; Q99502; baseline and differential.
DR Genevisible; Q99502; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032993; C:protein-DNA complex; IEA:Ensembl.
DR GO; GO:0140793; F:histone tyrosine phosphatase activity (H2-Y142 specific); IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:Ensembl.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
DR GO; GO:0035909; P:aorta morphogenesis; IEA:Ensembl.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0090103; P:cochlea morphogenesis; IEA:Ensembl.
DR GO; GO:0006302; P:double-strand break repair; IMP:UniProtKB.
DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; IEA:Ensembl.
DR GO; GO:0050673; P:epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
DR GO; GO:0007501; P:mesodermal cell fate specification; IEA:Ensembl.
DR GO; GO:0001656; P:metanephros development; IEA:Ensembl.
DR GO; GO:0042474; P:middle ear morphogenesis; IEA:Ensembl.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IBA:GO_Central.
DR GO; GO:0048665; P:neuron fate specification; IEA:Ensembl.
DR GO; GO:0071600; P:otic vesicle morphogenesis; IEA:Ensembl.
DR GO; GO:0042473; P:outer ear morphogenesis; IEA:Ensembl.
DR GO; GO:0003151; P:outflow tract morphogenesis; IEA:Ensembl.
DR GO; GO:0007389; P:pattern specification process; IEA:Ensembl.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IEA:InterPro.
DR GO; GO:0060037; P:pharyngeal system development; IEA:Ensembl.
DR GO; GO:0045739; P:positive regulation of DNA repair; IMP:UniProtKB.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0072513; P:positive regulation of secondary heart field cardioblast proliferation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0016925; P:protein sumoylation; ISS:UniProtKB.
DR GO; GO:0045664; P:regulation of neuron differentiation; IEA:Ensembl.
DR GO; GO:0010212; P:response to ionizing radiation; IDA:UniProtKB.
DR GO; GO:0048752; P:semicircular canal morphogenesis; IEA:Ensembl.
DR GO; GO:0007605; P:sensory perception of sound; TAS:ProtInc.
DR GO; GO:0014706; P:striated muscle tissue development; IEA:Ensembl.
DR CDD; cd02601; HAD_Eya; 1.
DR Gene3D; 3.40.50.12350; -; 1.
DR InterPro; IPR006545; EYA_dom.
DR InterPro; IPR042577; EYA_dom_metazoan.
DR InterPro; IPR038102; EYA_dom_sf.
DR InterPro; IPR028472; EYA_fam.
DR InterPro; IPR028471; Eyes_absent_h1.
DR PANTHER; PTHR10190; PTHR10190; 1.
DR PANTHER; PTHR10190:SF11; PTHR10190:SF11; 1.
DR TIGRFAMs; TIGR01658; EYA-cons_domain; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Chromatin regulator; Cytoplasm; Deafness;
KW Developmental protein; Disease variant; DNA damage; DNA repair; Hydrolase;
KW Intellectual disability; Magnesium; Metal-binding; Nucleus;
KW Protein phosphatase; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..592
FT /note="Eyes absent homolog 1"
FT /id="PRO_0000218643"
FT REGION 1..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 328
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O00167"
FT ACT_SITE 330
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O00167"
FT BINDING 328
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O00167"
FT BINDING 330
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O00167"
FT BINDING 556
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O00167"
FT VAR_SEQ 1..41
FT /note="MEMQDLTSPHSRLSGSSESPSGPKLGNSHINSNSMTPNGTE -> MLLFPQV
FT A (in isoform EYA1B)"
FT /evidence="ECO:0000305"
FT /id="VSP_001486"
FT VAR_SEQ 140..144
FT /note="Missing (in isoform EYA1D)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_045793"
FT VAR_SEQ 351..380
FT /note="Missing (in isoform EYA1D)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_045794"
FT VARIANT 20
FT /note="P -> A (in dbSNP:rs1445404)"
FT /id="VAR_024439"
FT VARIANT 41
FT /note="E -> K (found in a patient with congenital cataract;
FT dbSNP:rs561111097)"
FT /evidence="ECO:0000269|PubMed:23508780"
FT /id="VAR_070033"
FT VARIANT 95
FT /note="P -> S (in BOR1)"
FT /evidence="ECO:0000269|PubMed:21280147"
FT /id="VAR_064942"
FT VARIANT 140
FT /note="G -> S (in BOR1)"
FT /evidence="ECO:0000269|PubMed:21280147"
FT /id="VAR_064943"
FT VARIANT 242
FT /note="S -> G (in BOS1; dbSNP:rs191838840)"
FT /evidence="ECO:0000269|PubMed:12701758"
FT /id="VAR_044452"
FT VARIANT 363
FT /note="E -> K (in ASA; dbSNP:rs121909198)"
FT /evidence="ECO:0000269|PubMed:10655545"
FT /id="VAR_016864"
FT VARIANT 363
FT /note="E -> V (in BOR1)"
FT /evidence="ECO:0000269|PubMed:21280147"
FT /id="VAR_064944"
FT VARIANT 426
FT /note="G -> S (in BOR1; with cataract; dbSNP:rs121909199)"
FT /evidence="ECO:0000269|PubMed:10655545"
FT /id="VAR_016865"
FT VARIANT 429
FT /note="D -> G (in BOR1)"
FT /evidence="ECO:0000269|PubMed:11558900"
FT /id="VAR_016866"
FT VARIANT 440
FT /note="R -> Q (in BOR1; dbSNP:rs121909196)"
FT /evidence="ECO:0000269|PubMed:10464653,
FT ECO:0000269|PubMed:21280147"
FT /id="VAR_016867"
FT VARIANT 487
FT /note="S -> P (in BOR1; dbSNP:rs121909200)"
FT /evidence="ECO:0000269|PubMed:9361030"
FT /id="VAR_005203"
FT VARIANT 505
FT /note="L -> R (in BOR1; dbSNP:rs121909201)"
FT /evidence="ECO:0000269|PubMed:9361030"
FT /id="VAR_005204"
FT VARIANT 514
FT /note="L -> P (in BOR1; dbSNP:rs112340154)"
FT /evidence="ECO:0000269|PubMed:21280147"
FT /id="VAR_064945"
FT VARIANT 527
FT /note="Y -> C (in BOR1)"
FT /evidence="ECO:0000269|PubMed:21280147"
FT /id="VAR_064946"
FT VARIANT 547
FT /note="R -> G (in ASA; with cataract; dbSNP:rs121909197)"
FT /evidence="ECO:0000269|PubMed:10655545"
FT /id="VAR_016868"
FT VARIANT 569
FT /note="M -> T (in BOR1)"
FT /evidence="ECO:0000269|PubMed:21280147"
FT /id="VAR_064947"
FT VARIANT 583
FT /note="L -> P (in BOR1; dbSNP:rs397517920)"
FT /evidence="ECO:0000269|PubMed:10991693"
FT /id="VAR_016869"
FT MUTAGEN 328
FT /note="D->A: Loss of tyrosine phosphatase activity toward
FT H2AX."
FT /evidence="ECO:0000269|PubMed:19234442"
FT CONFLICT 33
FT /note="N -> D (in Ref. 3; AAL73437)"
FT /evidence="ECO:0000305"
SQ 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
