EYA3_HUMAN
ID EYA3_HUMAN Reviewed; 573 AA.
AC Q99504; A8K190; B4DIR7; B4DNZ7; O95463; Q8IVX7; Q99813;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 3.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Eyes absent homolog 3;
DE EC=3.1.3.48 {ECO:0000269|PubMed:19234442, ECO:0000269|PubMed:19351884};
GN Name=EYA3;
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 [GENOMIC DNA] (ISOFORM 1).
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Retina;
RX PubMed=9049631; DOI=10.1101/gr.7.2.128;
RA Zimmerman J.E., Bui Q.T., Steingrimsson E., Nagle D.L., Fu W., Genin A.,
RA Spinner N.B., Copeland N.G., Jenkins N.A., Bucan M., Bonini N.M.;
RT "Cloning and characterization of two vertebrate homologs of the Drosophila
RT eyes absent gene.";
RL Genome Res. 7:128-141(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 4 AND 5).
RC TISSUE=Brain, and Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 413-531.
RX PubMed=9887327; DOI=10.1093/hmg/8.1.11;
RA Borsani G., DeGrandi A., Ballabio A., Bulfone A., Bernard L., Banfi S.,
RA Gattuso C., Mariani M., Dixon M., Donnai D., Metcalfe K., Winter R.,
RA Robertson M., Axton R., Brown A., van Heyningen V., Hanson I.;
RT "EYA4, a novel vertebrate gene related to Drosophila eyes absent.";
RL Hum. Mol. Genet. 8:11-23(1999).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19351884; DOI=10.1074/jbc.c900032200;
RA Krishnan N., Jeong D.G., Jung S.-K., Ryu S.E., Xiao A., Allis C.D.,
RA Kim S.J., Tonks N.K.;
RT "Dephosphorylation of the C-terminal tyrosyl residue of the DNA damage-
RT related histone H2A.X is mediated by the protein phosphatase eyes absent.";
RL J. Biol. Chem. 284:16066-16070(2009).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, PHOSPHORYLATION AT
RP SER-266, AND MUTAGENESIS OF SER-266 AND ASP-309.
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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-472, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-262 AND SER-438, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Tyrosine phosphatase that specifically dephosphorylates 'Tyr-
CC 142' of histone H2AX (H2AXY142ph). 'Tyr-142' phosphorylation of histone
CC H2AX plays a central role in DNA repair and acts as a mark that
CC distinguishes between apoptotic and repair responses to genotoxic
CC stress. Promotes efficient DNA repair by dephosphorylating H2AX,
CC promoting the recruitment of DNA repair complexes containing MDC1
CC (PubMed:19234442, PubMed:19351884). Its function as histone phosphatase
CC probably explains its role in transcription regulation during
CC organogenesis. Coactivates SIX1, and seems to coactivate SIX2, SIX4 and
CC SIX5. The repression of precursor cell proliferation in myoblasts by
CC SIX1 is switched to activation through recruitment of EYA3 to the SIX1-
CC DACH1 complex and seems to be dependent on EYA3 phosphatase activity
CC (By similarity). May be involved in development of the eye.
CC {ECO:0000250|UniProtKB:P97480, ECO:0000269|PubMed:19234442,
CC ECO:0000269|PubMed:19351884}.
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, ECO:0000269|PubMed:19351884};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.8 uM for H2AXY142ph {ECO:0000269|PubMed:19351884};
CC KM=72 uM for H2AXS139ph {ECO:0000269|PubMed:19351884};
CC -!- SUBUNIT: Interacts with SIX1 and DACH1, and probably SIX2, SIX4, SIX5.
CC {ECO:0000250|UniProtKB:P97480}.
CC -!- INTERACTION:
CC Q99504; Q92870-2: APBB2; NbExp=3; IntAct=EBI-9089567, EBI-21535880;
CC Q99504; P13637: ATP1A3; NbExp=3; IntAct=EBI-9089567, EBI-948169;
CC Q99504; P50570-2: DNM2; NbExp=3; IntAct=EBI-9089567, EBI-10968534;
CC Q99504; P26378-2: ELAVL4; NbExp=3; IntAct=EBI-9089567, EBI-21603100;
CC Q99504; P10809: HSPD1; NbExp=3; IntAct=EBI-9089567, EBI-352528;
CC Q99504; P42858: HTT; NbExp=6; IntAct=EBI-9089567, EBI-466029;
CC Q99504; O60333-2: KIF1B; NbExp=3; IntAct=EBI-9089567, EBI-10975473;
CC Q99504; P51608: MECP2; NbExp=3; IntAct=EBI-9089567, EBI-1189067;
CC Q99504; P07196: NEFL; NbExp=3; IntAct=EBI-9089567, EBI-475646;
CC Q99504; P16284: PECAM1; NbExp=3; IntAct=EBI-9089567, EBI-716404;
CC Q99504; D3DTS7: PMP22; NbExp=3; IntAct=EBI-9089567, EBI-25882629;
CC Q99504; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-9089567, EBI-396669;
CC Q99504; O76024: WFS1; NbExp=3; IntAct=EBI-9089567, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P97480}. Nucleus
CC {ECO:0000269|PubMed:19234442}. Note=Localizes at sites of DNA damage at
CC double-strand breaks (DSBs) (PubMed:19234442). With decreasing
CC efficiency, translocalized to the nucleus by SIX2 and SIX5, and SIX4,
CC respectively (By similarity). {ECO:0000250|UniProtKB:P97480,
CC ECO:0000269|PubMed:19234442}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q99504-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99504-2; Sequence=VSP_001493;
CC Name=3;
CC IsoId=Q99504-3; Sequence=VSP_054518, VSP_054519;
CC Name=4;
CC IsoId=Q99504-4; Sequence=VSP_054530;
CC Name=5;
CC IsoId=Q99504-5; Sequence=VSP_054518;
CC -!- PTM: Ser-266 phosphorylation is required for localization at sites of
CC DNA damage and directing interaction with H2AX.
CC {ECO:0000269|PubMed:19234442}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. EYA family.
CC {ECO:0000305}.
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DR EMBL; Y10262; CAA71311.1; -; Genomic_DNA.
DR EMBL; U81602; AAB42066.1; -; mRNA.
DR EMBL; AK289805; BAF82494.1; -; mRNA.
DR EMBL; AK295745; BAG58579.1; -; mRNA.
DR EMBL; AK298129; BAG60409.1; -; mRNA.
DR EMBL; AL137792; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL512288; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07713.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07714.1; -; Genomic_DNA.
DR EMBL; BC041667; AAH41667.1; -; mRNA.
DR EMBL; AJ007991; CAA07814.1; -; mRNA.
DR CCDS; CCDS316.1; -. [Q99504-1]
DR CCDS; CCDS60050.1; -. [Q99504-4]
DR CCDS; CCDS60051.1; -. [Q99504-5]
DR CCDS; CCDS60052.1; -. [Q99504-3]
DR RefSeq; NP_001269489.1; NM_001282560.1. [Q99504-3]
DR RefSeq; NP_001269490.1; NM_001282561.1. [Q99504-5]
DR RefSeq; NP_001269491.1; NM_001282562.1. [Q99504-4]
DR RefSeq; NP_001981.2; NM_001990.3. [Q99504-1]
DR AlphaFoldDB; Q99504; -.
DR SMR; Q99504; -.
DR BioGRID; 108441; 54.
DR DIP; DIP-60448N; -.
DR IntAct; Q99504; 23.
DR STRING; 9606.ENSP00000362978; -.
DR BindingDB; Q99504; -.
DR ChEMBL; CHEMBL4296245; -.
DR DEPOD; EYA3; -.
DR GlyGen; Q99504; 3 sites, 2 O-linked glycans (3 sites).
DR iPTMnet; Q99504; -.
DR PhosphoSitePlus; Q99504; -.
DR BioMuta; EYA3; -.
DR DMDM; 239938901; -.
DR EPD; Q99504; -.
DR jPOST; Q99504; -.
DR MassIVE; Q99504; -.
DR MaxQB; Q99504; -.
DR PaxDb; Q99504; -.
DR PeptideAtlas; Q99504; -.
DR PRIDE; Q99504; -.
DR ProteomicsDB; 4324; -.
DR ProteomicsDB; 4738; -.
DR ProteomicsDB; 70790; -.
DR ProteomicsDB; 78305; -. [Q99504-1]
DR ProteomicsDB; 78306; -. [Q99504-2]
DR TopDownProteomics; Q99504-2; -. [Q99504-2]
DR Antibodypedia; 16480; 166 antibodies from 27 providers.
DR DNASU; 2140; -.
DR Ensembl; ENST00000373863.3; ENSP00000362970.3; ENSG00000158161.16. [Q99504-3]
DR Ensembl; ENST00000373871.8; ENSP00000362978.3; ENSG00000158161.16. [Q99504-1]
DR Ensembl; ENST00000436342.6; ENSP00000405587.3; ENSG00000158161.16. [Q99504-4]
DR Ensembl; ENST00000540618.5; ENSP00000442558.1; ENSG00000158161.16. [Q99504-5]
DR GeneID; 2140; -.
DR KEGG; hsa:2140; -.
DR MANE-Select; ENST00000373871.8; ENSP00000362978.3; NM_001990.4; NP_001981.2.
DR UCSC; uc001bpi.3; human. [Q99504-1]
DR CTD; 2140; -.
DR DisGeNET; 2140; -.
DR GeneCards; EYA3; -.
DR HGNC; HGNC:3521; EYA3.
DR HPA; ENSG00000158161; Low tissue specificity.
DR MIM; 601655; gene.
DR neXtProt; NX_Q99504; -.
DR OpenTargets; ENSG00000158161; -.
DR PharmGKB; PA27933; -.
DR VEuPathDB; HostDB:ENSG00000158161; -.
DR eggNOG; KOG3107; Eukaryota.
DR GeneTree; ENSGT00950000182978; -.
DR HOGENOM; CLU_021184_2_1_1; -.
DR InParanoid; Q99504; -.
DR OMA; XLLSPQR; -.
DR OrthoDB; 1030296at2759; -.
DR PhylomeDB; Q99504; -.
DR TreeFam; TF319337; -.
DR PathwayCommons; Q99504; -.
DR Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR SABIO-RK; Q99504; -.
DR SignaLink; Q99504; -.
DR SIGNOR; Q99504; -.
DR BioGRID-ORCS; 2140; 13 hits in 1086 CRISPR screens.
DR ChiTaRS; EYA3; human.
DR GenomeRNAi; 2140; -.
DR Pharos; Q99504; Tbio.
DR PRO; PR:Q99504; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q99504; protein.
DR Bgee; ENSG00000158161; Expressed in esophagus squamous epithelium and 181 other tissues.
DR ExpressionAtlas; Q99504; baseline and differential.
DR Genevisible; Q99504; HS.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IEA:InterPro.
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:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006302; P:double-strand break repair; IMP:UniProtKB.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IBA:GO_Central.
DR GO; GO:0045739; P:positive regulation of DNA repair; IMP:UniProtKB.
DR GO; GO:0010212; P:response to ionizing radiation; IDA:UniProtKB.
DR GO; GO:0007601; P:visual perception; TAS:ProtInc.
DR CDD; cd02601; HAD_Eya; 1.
DR Gene3D; 3.40.50.12350; -; 1.
DR InterPro; IPR028479; EYA3.
DR InterPro; IPR006545; EYA_dom.
DR InterPro; IPR042577; EYA_dom_metazoan.
DR InterPro; IPR038102; EYA_dom_sf.
DR InterPro; IPR028472; EYA_fam.
DR PANTHER; PTHR10190; PTHR10190; 1.
DR PANTHER; PTHR10190:SF5; PTHR10190:SF5; 1.
DR TIGRFAMs; TIGR01658; EYA-cons_domain; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Alternative splicing; Chromatin regulator;
KW Cytoplasm; Developmental protein; DNA damage; DNA repair; Hydrolase;
KW Magnesium; Metal-binding; Nucleus; Phosphoprotein; Protein phosphatase;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..573
FT /note="Eyes absent homolog 3"
FT /id="PRO_0000218648"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 309
FT /note="Nucleophile"
FT /evidence="ECO:0000305"
FT ACT_SITE 311
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O00167"
FT BINDING 309
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O00167"
FT BINDING 311
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O00167"
FT BINDING 537
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O00167"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 262
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19234442"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 472
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT VAR_SEQ 1..126
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9049631"
FT /id="VSP_001493"
FT VAR_SEQ 1..53
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054530"
FT VAR_SEQ 121..166
FT /note="Missing (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_054518"
FT VAR_SEQ 548..572
FT /note="HNMPFWRITNHGDLVSLHQALELDF -> QLYFLDMEALGCQLEPTALILFI
FT QLSGNLSNYNK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054519"
FT MUTAGEN 266
FT /note="S->A: Fails to form damage-dependent nuclear foci or
FT interact with H2AX."
FT /evidence="ECO:0000269|PubMed:19234442"
FT MUTAGEN 309
FT /note="D->A: Loss of tyrosine phosphatase activity toward
FT H2AX."
FT /evidence="ECO:0000269|PubMed:19234442"
FT CONFLICT 105
FT /note="Y -> D (in Ref. 1; CAA71311)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="H -> R (in Ref. 2; AAB42066)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="L -> V (in Ref. 2; AAB42066)"
FT /evidence="ECO:0000305"
FT CONFLICT 253
FT /note="R -> K (in Ref. 1; CAA71311)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="T -> S (in Ref. 2; AAB42066)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="T -> N (in Ref. 1; CAA71311)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="R -> K (in Ref. 1; CAA71311)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="V -> L (in Ref. 2; AAB42066)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="E -> K (in Ref. 1; CAA71311)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="F -> S (in Ref. 1; CAA71311)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="E -> K (in Ref. 1; CAA71311)"
FT /evidence="ECO:0000305"
FT CONFLICT 373..381
FT /note="SDDNGQDLS -> PNDKGQNLN (in Ref. 1; CAA71311)"
FT /evidence="ECO:0000305"
FT CONFLICT 388
FT /note="D -> N (in Ref. 1; CAA71311)"
FT /evidence="ECO:0000305"
FT CONFLICT 447..449
FT /note="RLR -> KLK (in Ref. 1; CAA71311)"
FT /evidence="ECO:0000305"
FT CONFLICT 457
FT /note="D -> N (in Ref. 1; CAA71311)"
FT /evidence="ECO:0000305"
FT CONFLICT 473
FT /note="R -> K (in Ref. 1; CAA71311)"
FT /evidence="ECO:0000305"
FT CONFLICT 480
FT /note="L -> P (in Ref. 2; AAB42066)"
FT /evidence="ECO:0000305"
FT CONFLICT 487
FT /note="V -> L (in Ref. 1; CAA71311)"
FT /evidence="ECO:0000305"
FT CONFLICT 500
FT /note="E -> K (in Ref. 1; CAA71311)"
FT /evidence="ECO:0000305"
FT CONFLICT 524..526
FT /note="SRF -> TSL (in Ref. 1; CAA71311)"
FT /evidence="ECO:0000305"
FT CONFLICT 530
FT /note="V -> L (in Ref. 1; CAA71311)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 573 AA; 62663 MW; 684B961B1E630371 CRC64;
MEEEQDLPEQ PVKKAKMQES GEQTISQVSN PDVSDQKPET SSLASNLPMS EEIMTCTDYI
PRSSNDYTSQ MYSAKPYAHI LSVPVSETAY PGQTQYQTLQ QTQPYAVYPQ ATQTYGLPPF
GALWPGMKPE SGLIQTPSPS QHSVLTCTTG LTTSQPSPAH YSYPIQASST NASLISTSST
IANIPAAAVA SISNQDYPTY TILGQNQYQA CYPSSSFGVT GQTNSDAEST TLAATTYQSE
KPSVMAPAPA AQRLSSGDPS TSPSLSQTTP SKDTDDQSRK NMTSKNRGKR KADATSSQDS
ELERVFLWDL DETIIIFHSL LTGSYAQKYG KDPTVVIGSG LTMEEMIFEV ADTHLFFNDL
EECDQVHVED VASDDNGQDL SNYSFSTDGF SGSGGSGSHG SSVGVQGGVD WMRKLAFRYR
KVREIYDKHK SNVGGLLSPQ RKEALQRLRA EIEVLTDSWL GTALKSLLLI QSRKNCVNVL
ITTTQLVPAL AKVLLYGLGE IFPIENIYSA TKIGKESCFE RIVSRFGKKV TYVVIGDGRD
EEIAAKQHNM PFWRITNHGD LVSLHQALEL DFL
