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Q99504

- EYA3_HUMAN

UniProt

Q99504 - EYA3_HUMAN

Protein

Eyes absent homolog 3

Gene

EYA3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 3 (16 Jun 2009)
      Previous versions | rss
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    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

    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

    1. chromatin binding Source: Ensembl
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: UniProtKB
    4. protein tyrosine/serine/threonine phosphatase activity Source: Ensembl
    5. protein tyrosine phosphatase activity Source: UniProtKB

    GO - Biological processi

    1. anatomical structure morphogenesis Source: ProtInc
    2. double-strand break repair Source: UniProtKB
    3. histone dephosphorylation Source: UniProtKB
    4. multicellular organismal development Source: UniProtKB-KW
    5. peptidyl-tyrosine dephosphorylation Source: GOC
    6. positive regulation of DNA repair Source: UniProtKB
    7. regulation of transcription, DNA-templated Source: UniProtKB-KW
    8. response to ionizing radiation Source: UniProtKB
    9. transcription, DNA-templated Source: UniProtKB-KW
    10. visual perception Source: ProtInc

    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: 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

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB
    3. transcription factor complex Source: Ensembl

    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.

    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.2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ99504.
    PaxDbiQ99504.
    PRIDEiQ99504.

    PTM databases

    PhosphoSiteiQ99504.

    Expressioni

    Gene expression databases

    ArrayExpressiQ99504.
    BgeeiQ99504.
    CleanExiHS_EYA3.
    GenevestigatoriQ99504.

    Organism-specific databases

    HPAiHPA052432.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi108441. 4 interactions.
    DIPiDIP-60448N.
    IntActiQ99504. 1 interaction.
    STRINGi9606.ENSP00000362978.

    Structurei

    3D structure databases

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

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG297494.
    HOGENOMiHOG000293149.
    HOVERGENiHBG002447.
    InParanoidiQ99504.
    KOiK17621.
    OMAiYTILGQS.
    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. Align

    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

    MEEEQDLPEQ PVKKAKMQES GEQTISQVSN PDVSDQKPET SSLASNLPMS    50
    EEIMTCTDYI PRSSNDYTSQ MYSAKPYAHI LSVPVSETAY PGQTQYQTLQ 100
    QTQPYAVYPQ ATQTYGLPPF GALWPGMKPE SGLIQTPSPS QHSVLTCTTG 150
    LTTSQPSPAH YSYPIQASST NASLISTSST IANIPAAAVA SISNQDYPTY 200
    TILGQNQYQA CYPSSSFGVT GQTNSDAEST TLAATTYQSE KPSVMAPAPA 250
    AQRLSSGDPS TSPSLSQTTP SKDTDDQSRK NMTSKNRGKR KADATSSQDS 300
    ELERVFLWDL DETIIIFHSL LTGSYAQKYG KDPTVVIGSG LTMEEMIFEV 350
    ADTHLFFNDL EECDQVHVED VASDDNGQDL SNYSFSTDGF SGSGGSGSHG 400
    SSVGVQGGVD WMRKLAFRYR KVREIYDKHK SNVGGLLSPQ RKEALQRLRA 450
    EIEVLTDSWL GTALKSLLLI QSRKNCVNVL ITTTQLVPAL AKVLLYGLGE 500
    IFPIENIYSA TKIGKESCFE RIVSRFGKKV TYVVIGDGRD EEIAAKQHNM 550
    PFWRITNHGD LVSLHQALEL DFL 573
    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:
    EMBL
    GenBank
    DDBJ
    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. [Q99504-2]
    ENST00000540618; ENSP00000442558; ENSG00000158161. [Q99504-5]
    GeneIDi2140.
    KEGGihsa:2140.
    UCSCiuc001bpi.2. human. [Q99504-1]
    uc001bpj.3. human.

    Polymorphism databases

    DMDMi239938901.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS316.1. [Q99504-1 ]
    CCDS60050.1. [Q99504-4 ]
    CCDS60051.1. [Q99504-5 ]
    CCDS60052.1. [Q99504-3 ]
    RefSeqi NP_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 ]
    UniGenei Hs.185774.

    3D structure databases

    ProteinModelPortali Q99504.
    SMRi Q99504. Positions 300-573.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108441. 4 interactions.
    DIPi DIP-60448N.
    IntActi Q99504. 1 interaction.
    STRINGi 9606.ENSP00000362978.

    PTM databases

    PhosphoSitei Q99504.

    Polymorphism databases

    DMDMi 239938901.

    Proteomic databases

    MaxQBi Q99504.
    PaxDbi Q99504.
    PRIDEi Q99504.

    Protocols and materials databases

    DNASUi 2140.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000373863 ; ENSP00000362970 ; ENSG00000158161 . [Q99504-3 ]
    ENST00000373871 ; ENSP00000362978 ; ENSG00000158161 . [Q99504-1 ]
    ENST00000436342 ; ENSP00000405587 ; ENSG00000158161 . [Q99504-2 ]
    ENST00000540618 ; ENSP00000442558 ; ENSG00000158161 . [Q99504-5 ]
    GeneIDi 2140.
    KEGGi hsa:2140.
    UCSCi uc001bpi.2. human. [Q99504-1 ]
    uc001bpj.3. human.

    Organism-specific databases

    CTDi 2140.
    GeneCardsi GC01M028296.
    HGNCi HGNC:3521. EYA3.
    HPAi HPA052432.
    MIMi 601655. gene.
    neXtProti NX_Q99504.
    PharmGKBi PA27933.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG297494.
    HOGENOMi HOG000293149.
    HOVERGENi HBG002447.
    InParanoidi Q99504.
    KOi K17621.
    OMAi YTILGQS.
    OrthoDBi EOG7DNNTZ.
    PhylomeDBi Q99504.
    TreeFami TF319337.

    Enzyme and pathway databases

    SABIO-RK Q99504.

    Miscellaneous databases

    GenomeRNAii 2140.
    NextBioi 35472340.
    PROi Q99504.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99504.
    Bgeei Q99504.
    CleanExi HS_EYA3.
    Genevestigatori Q99504.

    Family and domain databases

    InterProi IPR028479. EYA3.
    IPR006545. EYA_dom.
    IPR028472. EYA_fam.
    [Graphical view ]
    PANTHERi PTHR10190. PTHR10190. 1 hit.
    PTHR10190:SF5. PTHR10190:SF5. 1 hit.
    TIGRFAMsi TIGR01658. EYA-cons_domain. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 126 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