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Protein

Eyes absent homolog 3

Gene

EYA3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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. Coactivates SIX1, and seems to coactivate SIX2, SIX4 and SIX5. The repression of precursor cell proliferation in myoblasts by SIX1 is switched to activation through recruitment of EYA3 to the SIX1-DACH1 complex and seems to be dependent on EYA3 phosphatase activity (By similarity). May be involved in development of the eye.By similarity2 Publications

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.2 Publications

Cofactori

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

Kineticsi

  1. KM=1.8 µM for H2AXY142ph1 Publication
  2. KM=72 µM for H2AXS139ph1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei309 – 3091NucleophileCurated
    Metal bindingi309 – 3091Magnesium
    Active sitei311 – 3111Proton donorBy similarity
    Metal bindingi311 – 3111MagnesiumBy similarity
    Metal bindingi537 – 5371MagnesiumBy similarity

    GO - Molecular functioni

    GO - Biological processi

    • anatomical structure morphogenesis Source: ProtInc
    • double-strand break repair Source: UniProtKB
    • histone dephosphorylation Source: UniProtKB
    • multicellular organismal development Source: UniProtKB-KW
    • peptidyl-tyrosine dephosphorylation Source: GOC
    • positive regulation of DNA repair Source: UniProtKB
    • regulation of transcription, DNA-templated Source: UniProtKB-KW
    • response to ionizing radiation Source: UniProtKB
    • transcription, DNA-templated Source: UniProtKB-KW
    • visual perception Source: ProtInc
    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, Metal-binding

    Enzyme and pathway databases

    SABIO-RKQ99504.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Eyes absent homolog 3 (EC:3.1.3.48)
    Gene namesi
    Name:EYA3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:3521. EYA3.

    Subcellular locationi

    • Cytoplasm By similarity
    • Nucleus 1 Publication

    • Note: Localizes at sites of DNA damage at double-strand breaks (DSBs). With decreasing efficiency, translocalized to the nucleus by SIX2 and SIX5, and SIX4, respectively (By similarity).By similarity

    GO - Cellular componenti

    • centrosome Source: HPA
    • cytoplasm Source: UniProtKB-SubCell
    • nucleoplasm Source: HPA
    • nucleus Source: UniProtKB
    • transcription factor complex Source: Ensembl
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi266 – 2661S → A: Fails to form damage-dependent nuclear foci or interact with H2AX. 1 Publication
    Mutagenesisi309 – 3091D → A: Loss of tyrosine phosphatase activity toward H2AX. 1 Publication

    Organism-specific databases

    PharmGKBiPA27933.

    Polymorphism and mutation databases

    BioMutaiEYA3.
    DMDMi239938901.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 573573Eyes absent homolog 3PRO_0000218648Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei266 – 2661Phosphoserine1 Publication
    Modified residuei472 – 4721Phosphoserine1 Publication

    Post-translational modificationi

    Ser-266 phosphorylation is required for localization at sites of DNA damage and directing interaction with H2AX.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ99504.
    PaxDbiQ99504.
    PRIDEiQ99504.

    PTM databases

    DEPODiQ99504.
    PhosphoSiteiQ99504.

    Expressioni

    Gene expression databases

    BgeeiQ99504.
    CleanExiHS_EYA3.
    ExpressionAtlasiQ99504. baseline and differential.
    GenevisibleiQ99504. HS.

    Organism-specific databases

    HPAiHPA052432.
    HPA062889.

    Interactioni

    Subunit structurei

    Interacts with SIX1 and DACH1, and probably SIX2, SIX4, SIX5.By similarity

    Protein-protein interaction databases

    BioGridi108441. 7 interactions.
    DIPiDIP-60448N.
    IntActiQ99504. 2 interactions.
    STRINGi9606.ENSP00000362978.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99504.
    SMRiQ99504. Positions 300-573.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG297494.
    GeneTreeiENSGT00390000008860.
    HOGENOMiHOG000293149.
    HOVERGENiHBG002447.
    InParanoidiQ99504.
    KOiK17621.
    OMAiSQYQACY.
    OrthoDBiEOG7DNNTZ.
    PhylomeDBiQ99504.
    TreeFamiTF319337.

    Family and domain databases

    InterProiIPR028479. EYA3.
    IPR006545. EYA_dom.
    IPR028472. EYA_fam.
    [Graphical view]
    PANTHERiPTHR10190. PTHR10190. 1 hit.
    PTHR10190:SF5. PTHR10190:SF5. 1 hit.
    TIGRFAMsiTIGR01658. EYA-cons_domain. 1 hit.

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q99504-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    MEEEQDLPEQ PVKKAKMQES GEQTISQVSN PDVSDQKPET SSLASNLPMS
    60 70 80 90 100
    EEIMTCTDYI PRSSNDYTSQ MYSAKPYAHI LSVPVSETAY PGQTQYQTLQ
    110 120 130 140 150
    QTQPYAVYPQ ATQTYGLPPF GALWPGMKPE SGLIQTPSPS QHSVLTCTTG
    160 170 180 190 200
    LTTSQPSPAH YSYPIQASST NASLISTSST IANIPAAAVA SISNQDYPTY
    210 220 230 240 250
    TILGQNQYQA CYPSSSFGVT GQTNSDAEST TLAATTYQSE KPSVMAPAPA
    260 270 280 290 300
    AQRLSSGDPS TSPSLSQTTP SKDTDDQSRK NMTSKNRGKR KADATSSQDS
    310 320 330 340 350
    ELERVFLWDL DETIIIFHSL LTGSYAQKYG KDPTVVIGSG LTMEEMIFEV
    360 370 380 390 400
    ADTHLFFNDL EECDQVHVED VASDDNGQDL SNYSFSTDGF SGSGGSGSHG
    410 420 430 440 450
    SSVGVQGGVD WMRKLAFRYR KVREIYDKHK SNVGGLLSPQ RKEALQRLRA
    460 470 480 490 500
    EIEVLTDSWL GTALKSLLLI QSRKNCVNVL ITTTQLVPAL AKVLLYGLGE
    510 520 530 540 550
    IFPIENIYSA TKIGKESCFE RIVSRFGKKV TYVVIGDGRD EEIAAKQHNM
    560 570
    PFWRITNHGD LVSLHQALEL DFL
    Length:573
    Mass (Da):62,663
    Last modified:June 16, 2009 - v3
    Checksum:i684B961B1E630371
    GO
    Isoform 2 (identifier: Q99504-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-126: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:447
    Mass (Da):48,652
    Checksum:i129E0A20B4A7BA2F
    GO
    Isoform 3 (identifier: Q99504-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         121-166: Missing.
         548-572: HNMPFWRITNHGDLVSLHQALELDF → QLYFLDMEALGCQLEPTALILFIQLSGNLSNYNK

    Note: No experimental confirmation available.
    Show »
    Length:536
    Mass (Da):58,697
    Checksum:i7F502740058138F7
    GO
    Isoform 4 (identifier: Q99504-4) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-53: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:520
    Mass (Da):56,805
    Checksum:iEE85E9F3F4E00708
    GO
    Isoform 5 (identifier: Q99504-5) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         121-166: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:527
    Mass (Da):57,827
    Checksum:i33DA17379017618E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti105 – 1051Y → D in CAA71311 (PubMed:9020840).Curated
    Sequence conflicti142 – 1421H → R in AAB42066 (PubMed:9049631).Curated
    Sequence conflicti151 – 1511L → V in AAB42066 (PubMed:9049631).Curated
    Sequence conflicti253 – 2531R → K in CAA71311 (PubMed:9020840).Curated
    Sequence conflicti268 – 2681T → S in AAB42066 (PubMed:9049631).Curated
    Sequence conflicti283 – 2831T → N in CAA71311 (PubMed:9020840).Curated
    Sequence conflicti290 – 2901R → K in CAA71311 (PubMed:9020840).Curated
    Sequence conflicti305 – 3051V → L in AAB42066 (PubMed:9049631).Curated
    Sequence conflicti345 – 3451E → K in CAA71311 (PubMed:9020840).Curated
    Sequence conflicti357 – 3571F → S in CAA71311 (PubMed:9020840).Curated
    Sequence conflicti361 – 3611E → K in CAA71311 (PubMed:9020840).Curated
    Sequence conflicti373 – 3819SDDNGQDLS → PNDKGQNLN in CAA71311 (PubMed:9020840).Curated
    Sequence conflicti388 – 3881D → N in CAA71311 (PubMed:9020840).Curated
    Sequence conflicti447 – 4493RLR → KLK in CAA71311 (PubMed:9020840).Curated
    Sequence conflicti457 – 4571D → N in CAA71311 (PubMed:9020840).Curated
    Sequence conflicti473 – 4731R → K in CAA71311 (PubMed:9020840).Curated
    Sequence conflicti480 – 4801L → P in AAB42066 (PubMed:9049631).Curated
    Sequence conflicti487 – 4871V → L in CAA71311 (PubMed:9020840).Curated
    Sequence conflicti500 – 5001E → K in CAA71311 (PubMed:9020840).Curated
    Sequence conflicti524 – 5263SRF → TSL in CAA71311 (PubMed:9020840).Curated
    Sequence conflicti530 – 5301V → L in CAA71311 (PubMed:9020840).Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 126126Missing in isoform 2. 1 PublicationVSP_001493Add
    BLAST
    Alternative sequencei1 – 5353Missing in isoform 4. 1 PublicationVSP_054530Add
    BLAST
    Alternative sequencei121 – 16646Missing in isoform 3 and isoform 5. 2 PublicationsVSP_054518Add
    BLAST
    Alternative sequencei548 – 57225HNMPF…LELDF → QLYFLDMEALGCQLEPTALI LFIQLSGNLSNYNK in isoform 3. 1 PublicationVSP_054519Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Y10262 Genomic DNA. Translation: CAA71311.1.
    U81602 mRNA. Translation: AAB42066.1.
    AK289805 mRNA. Translation: BAF82494.1.
    AK295745 mRNA. Translation: BAG58579.1.
    AK298129 mRNA. Translation: BAG60409.1.
    AL512288, AL137792 Genomic DNA. Translation: CAI14297.1.
    CH471059 Genomic DNA. Translation: EAX07713.1.
    CH471059 Genomic DNA. Translation: EAX07714.1.
    BC041667 mRNA. Translation: AAH41667.1.
    AJ007991 mRNA. Translation: CAA07814.1.
    CCDSiCCDS316.1. [Q99504-1]
    CCDS60050.1. [Q99504-4]
    CCDS60051.1. [Q99504-5]
    CCDS60052.1. [Q99504-3]
    RefSeqiNP_001269489.1. NM_001282560.1. [Q99504-3]
    NP_001269490.1. NM_001282561.1. [Q99504-5]
    NP_001269491.1. NM_001282562.1. [Q99504-4]
    NP_001981.2. NM_001990.3. [Q99504-1]
    UniGeneiHs.185774.

    Genome annotation databases

    EnsembliENST00000373863; ENSP00000362970; ENSG00000158161. [Q99504-3]
    ENST00000373871; ENSP00000362978; ENSG00000158161. [Q99504-1]
    ENST00000436342; ENSP00000405587; ENSG00000158161. [Q99504-4]
    ENST00000540618; ENSP00000442558; ENSG00000158161. [Q99504-5]
    GeneIDi2140.
    KEGGihsa:2140.
    UCSCiuc001bpi.2. human. [Q99504-1]
    uc001bpj.3. human.
    uc010oft.2. human.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Y10262 Genomic DNA. Translation: CAA71311.1.
    U81602 mRNA. Translation: AAB42066.1.
    AK289805 mRNA. Translation: BAF82494.1.
    AK295745 mRNA. Translation: BAG58579.1.
    AK298129 mRNA. Translation: BAG60409.1.
    AL512288, AL137792 Genomic DNA. Translation: CAI14297.1.
    CH471059 Genomic DNA. Translation: EAX07713.1.
    CH471059 Genomic DNA. Translation: EAX07714.1.
    BC041667 mRNA. Translation: AAH41667.1.
    AJ007991 mRNA. Translation: CAA07814.1.
    CCDSiCCDS316.1. [Q99504-1]
    CCDS60050.1. [Q99504-4]
    CCDS60051.1. [Q99504-5]
    CCDS60052.1. [Q99504-3]
    RefSeqiNP_001269489.1. NM_001282560.1. [Q99504-3]
    NP_001269490.1. NM_001282561.1. [Q99504-5]
    NP_001269491.1. NM_001282562.1. [Q99504-4]
    NP_001981.2. NM_001990.3. [Q99504-1]
    UniGeneiHs.185774.

    3D structure databases

    ProteinModelPortaliQ99504.
    SMRiQ99504. Positions 300-573.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi108441. 7 interactions.
    DIPiDIP-60448N.
    IntActiQ99504. 2 interactions.
    STRINGi9606.ENSP00000362978.

    PTM databases

    DEPODiQ99504.
    PhosphoSiteiQ99504.

    Polymorphism and mutation databases

    BioMutaiEYA3.
    DMDMi239938901.

    Proteomic databases

    MaxQBiQ99504.
    PaxDbiQ99504.
    PRIDEiQ99504.

    Protocols and materials databases

    DNASUi2140.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000373863; ENSP00000362970; ENSG00000158161. [Q99504-3]
    ENST00000373871; ENSP00000362978; ENSG00000158161. [Q99504-1]
    ENST00000436342; ENSP00000405587; ENSG00000158161. [Q99504-4]
    ENST00000540618; ENSP00000442558; ENSG00000158161. [Q99504-5]
    GeneIDi2140.
    KEGGihsa:2140.
    UCSCiuc001bpi.2. human. [Q99504-1]
    uc001bpj.3. human.
    uc010oft.2. human.

    Organism-specific databases

    CTDi2140.
    GeneCardsiGC01M028296.
    HGNCiHGNC:3521. EYA3.
    HPAiHPA052432.
    HPA062889.
    MIMi601655. gene.
    neXtProtiNX_Q99504.
    PharmGKBiPA27933.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiNOG297494.
    GeneTreeiENSGT00390000008860.
    HOGENOMiHOG000293149.
    HOVERGENiHBG002447.
    InParanoidiQ99504.
    KOiK17621.
    OMAiSQYQACY.
    OrthoDBiEOG7DNNTZ.
    PhylomeDBiQ99504.
    TreeFamiTF319337.

    Enzyme and pathway databases

    SABIO-RKQ99504.

    Miscellaneous databases

    ChiTaRSiEYA3. human.
    GenomeRNAii2140.
    NextBioi35472340.
    PROiQ99504.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ99504.
    CleanExiHS_EYA3.
    ExpressionAtlasiQ99504. baseline and differential.
    GenevisibleiQ99504. HS.

    Family and domain databases

    InterProiIPR028479. EYA3.
    IPR006545. EYA_dom.
    IPR028472. EYA_fam.
    [Graphical view]
    PANTHERiPTHR10190. PTHR10190. 1 hit.
    PTHR10190:SF5. PTHR10190:SF5. 1 hit.
    TIGRFAMsiTIGR01658. EYA-cons_domain. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "A human homologue of the Drosophila eyes absent gene underlies branchio-oto-renal (BOR) syndrome and identifies a novel gene family."
      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.
      Nat. Genet. 15:157-164(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
      Tissue: Embryo.
    2. "Cloning and characterization of two vertebrate homologs of the Drosophila eyes absent gene."
      Zimmerman J.E., Bui Q.T., Steingrimsson E., Nagle D.L., Fu W., Genin A., Spinner N.B., Copeland N.G., Jenkins N.A., Bucan M., Bonini N.M.
      Genome Res. 7:128-141(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Retina.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 4 AND 5).
      Tissue: Brain and Hippocampus.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Brain.
    7. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 413-531.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Dephosphorylation of the C-terminal tyrosyl residue of the DNA damage-related histone H2A.X is mediated by the protein phosphatase eyes absent."
      Krishnan N., Jeong D.G., Jung S.-K., Ryu S.E., Xiao A., Allis C.D., Kim S.J., Tonks N.K.
      J. Biol. Chem. 284:16066-16070(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    11. "Tyrosine dephosphorylation of H2AX modulates apoptosis and survival decisions."
      Cook P.J., Ju B.G., Telese F., Wang X., Glass C.K., Rosenfeld M.G.
      Nature 458:591-596(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-266, MUTAGENESIS OF SER-266 AND ASP-309.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-472, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiEYA3_HUMAN
    AccessioniPrimary (citable) accession number: Q99504
    Secondary accession number(s): A8K190
    , B4DIR7, B4DNZ7, O95463, Q8IVX7, Q99813
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: June 16, 2009
    Last modified: June 24, 2015
    This is version 134 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. 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.