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O00167

- EYA2_HUMAN

UniProt

O00167 - EYA2_HUMAN

Protein

Eyes absent homolog 2

Gene

EYA2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 2 (02 May 2002)
      Previous versions | rss
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    Functioni

    Functions both as protein phosphatase and as transcriptional coactivator for SIX1, and probably also for SIX2, SIX4 and SIX5. Tyrosine phosphatase that dephosphorylates 'Tyr-142' of histone H2AX (H2AXY142ph) and promotes efficient DNA repair via the recruitment of DNA repair complexes containing MDC1. 'Tyr-142' phosphorylation of histone H2AX plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress. Its function as histone phosphatase may contribute to its function in transcription regulation during organogenesis. Plays an important role in hypaxial muscle development together with SIX1 and DACH2; in this it is functionally redundant with EYA1.2 Publications

    Catalytic activityi

    Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.1 Publication

    Cofactori

    Binds 1 Mg2+ ion per subunit.1 Publication

    Kineticsi

    1. KM=1.9 µM for H2AXY142ph1 Publication
    2. KM=80 µM for H2AXS139ph1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei274 – 2741Nucleophile1 Publication
    Metal bindingi274 – 2741Magnesium1 Publication
    Active sitei276 – 2761Proton donor1 Publication
    Metal bindingi276 – 2761Magnesium; via carbonyl oxygen1 Publication
    Metal bindingi502 – 5021Magnesium1 Publication

    GO - Molecular functioni

    1. magnesium ion binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. protein tyrosine phosphatase activity Source: UniProtKB

    GO - Biological processi

    1. DNA repair Source: UniProtKB-KW
    2. extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
    3. histone dephosphorylation Source: UniProtKB
    4. mesodermal cell fate specification Source: ProtInc
    5. mitochondrial outer membrane permeabilization Source: Ensembl
    6. peptidyl-tyrosine dephosphorylation Source: GOC
    7. regulation of transcription, DNA-templated Source: UniProtKB-KW
    8. striated muscle tissue development Source: Ensembl
    9. transcription, DNA-templated Source: UniProtKB-KW

    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-RKO00167.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Eyes absent homolog 2 (EC:3.1.3.48)
    Gene namesi
    Name:EYA2
    Synonyms:EAB1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:3520. EYA2.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: Retained in the cytoplasm via interaction with GNAZ and GNAI2. Interaction with SIX1, SIX2, SIX4 or SIX5 is required for translocation to the nucleus.

    GO - Cellular componenti

    1. centrosome Source: HPA
    2. cytoplasm Source: HPA
    3. mitochondrion Source: GOC
    4. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi516 – 5161P → R: Strongly reduces SIX1 binding. 1 Publication
    Mutagenesisi532 – 5321A → R: Abolishes interaction with SIX1. 1 Publication

    Organism-specific databases

    PharmGKBiPA27932.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 538538Eyes absent homolog 2PRO_0000218646Add
    BLAST

    Proteomic databases

    PaxDbiO00167.
    PRIDEiO00167.

    PTM databases

    PhosphoSiteiO00167.

    Expressioni

    Tissue specificityi

    Highest expression in muscle with lower levels in kidney, placenta, pancreas, brain and heart.

    Developmental stagei

    At the begin of fourth week of development detected in cytoplasm of somite cells. Between the sixth and eighth week of development detected in cytoplasm of limb bud cells.1 Publication

    Gene expression databases

    ArrayExpressiO00167.
    BgeeiO00167.
    GenevestigatoriO00167.

    Organism-specific databases

    HPAiHPA027024.

    Interactioni

    Subunit structurei

    Interacts with DACH2 and SIX1, and probably with SIX2, SIX4 and SIX5. Interacts with CAPN8 By similarity. Interacts with GNAZ and GNAI2; this precludes interaction with SIX1.By similarity5 Publications

    Protein-protein interaction databases

    BioGridi108440. 7 interactions.
    DIPiDIP-40707N.
    IntActiO00167. 2 interactions.
    MINTiMINT-139839.

    Structurei

    Secondary structure

    1
    538
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi269 – 2735
    Turni277 – 2793
    Helixi283 – 2875
    Helixi289 – 2946
    Helixi298 – 31922
    Helixi322 – 3254
    Helixi326 – 3283
    Turni333 – 3364
    Helixi337 – 3393
    Helixi350 – 3523
    Helixi374 – 39421
    Helixi398 – 4025
    Helixi406 – 42015
    Turni421 – 4233
    Helixi424 – 43613
    Beta strandi441 – 4499
    Helixi451 – 46010
    Turni464 – 4663
    Helixi469 – 4713
    Beta strandi472 – 4743
    Turni476 – 4783
    Helixi480 – 49112
    Beta strandi493 – 50311
    Helixi504 – 5129
    Beta strandi517 – 5193
    Helixi523 – 53412

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3GEBX-ray2.40A/B/C/D268-538[»]
    3HB0X-ray2.50A/B/C/D268-538[»]
    3HB1X-ray2.51A/B/C/D268-538[»]
    4EGCX-ray1.99B253-538[»]
    ProteinModelPortaliO00167.
    SMRiO00167. Positions 268-538.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO00167.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG297494.
    HOVERGENiHBG002447.
    InParanoidiO00167.
    KOiK17620.
    OMAiIHSRPNC.
    OrthoDBiEOG7DNNTZ.
    PhylomeDBiO00167.
    TreeFamiTF319337.

    Family and domain databases

    InterProiIPR028473. EYA2.
    IPR006545. EYA_dom.
    IPR028472. EYA_fam.
    IPR023214. HAD-like_dom.
    [Graphical view]
    PANTHERiPTHR10190. PTHR10190. 1 hit.
    PTHR10190:SF7. PTHR10190:SF7. 1 hit.
    SUPFAMiSSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR01658. EYA-cons_domain. 1 hit.

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Note: Experimental confirmation may be lacking for some isoforms.

    Isoform 1 (identifier: O00167-1) [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

    MVELVISPSL TVNSDCLDKL KFNRADAAVW TLSDRQGITK SAPLRVSQLF    50
    SRSCPRVLPR QPSTAMAAYG QTQYSAGIQQ ATPYTAYPPP AQAYGIPSYS 100
    IKTEDSLNHS PGQSGFLSYG SSFSTSPTGQ SPYTYQMHGT TGFYQGGNGL 150
    GNAAGFGSVH QDYPSYPGFP QSQYPQYYGS SYNPPYVPAS SICPSPLSTS 200
    TYVLQEASHN VPNQSSESLA GEYNTHNGPS TPAKEGDTDR PHRASDGKLR 250
    GRSKRSSDPS PAGDNEIERV FVWDLDETII IFHSLLTGTF ASRYGKDTTT 300
    SVRIGLMMEE MIFNLADTHL FFNDLEDCDQ IHVDDVSSDD NGQDLSTYNF 350
    SADGFHSSAP GANLCLGSGV HGGVDWMRKL AFRYRRVKEM YNTYKNNVGG 400
    LIGTPKRETW LQLRAELEAL TDLWLTHSLK ALNLINSRPN CVNVLVTTTQ 450
    LIPALAKVLL YGLGSVFPIE NIYSATKTGK ESCFERIMQR FGRKAVYVVI 500
    GDGVEEEQGA KKHNMPFWRI SCHADLEALR HALELEYL 538
    Length:538
    Mass (Da):59,232
    Last modified:May 2, 2002 - v2
    Checksum:i3DBFC31D8BE1E85D
    GO
    Isoform 2 (identifier: O00167-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         99-122: Missing.

    Show »
    Length:514
    Mass (Da):56,688
    Checksum:i970E63DB345E484A
    GO
    Isoform 3 (identifier: O00167-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         401-479: Missing.

    Show »
    Length:459
    Mass (Da):50,533
    Checksum:i774885A6F04CA6B2
    GO

    Sequence cautioni

    The sequence AAH13882.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti296 – 2961K → E in AAB42065. (PubMed:9049631)Curated
    Sequence conflicti361 – 3611G → A in AAP35328. 1 PublicationCurated
    Sequence conflicti361 – 3611G → A in AAH08803. (PubMed:15489334)Curated
    Sequence conflicti381 – 3811A → S in AAB42065. (PubMed:9049631)Curated
    Sequence conflicti419 – 4191A → V in CAA07815. (PubMed:9887327)Curated
    Sequence conflicti525 – 5251D → N in AAB51120. (PubMed:9195991)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti83 – 831P → S.
    Corresponds to variant rs2275596 [ dbSNP | Ensembl ].
    VAR_048964
    Natural varianti238 – 2381T → A.
    Corresponds to variant rs866936 [ dbSNP | Ensembl ].
    VAR_048965

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei99 – 12224Missing in isoform 2. 2 PublicationsVSP_001490Add
    BLAST
    Alternative sequencei401 – 47979Missing in isoform 3. 1 PublicationVSP_001491Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U71207 mRNA. Translation: AAB51120.1.
    Y10261 Genomic DNA. Translation: CAA71310.1.
    BT006682 mRNA. Translation: AAP35328.1.
    AL049540
    , AL121776, AL359434, AL022342 Genomic DNA. Translation: CAI23166.1.
    AL121776
    , AL049540, AL359434, AL022342 Genomic DNA. Translation: CAI42150.1.
    AL359434
    , AL049540, AL121776, AL022342 Genomic DNA. Translation: CAI40099.1.
    BC000289 mRNA. Translation: AAH00289.2.
    BC008803 mRNA. Translation: AAH08803.1.
    BC013882 mRNA. Translation: AAH13882.2. Different initiation.
    U81601 mRNA. Translation: AAB42065.1.
    AJ007992 mRNA. Translation: CAA07815.1.
    CCDSiCCDS13403.1. [O00167-1]
    CCDS54471.1. [O00167-3]
    RefSeqiNP_005235.3. NM_005244.4. [O00167-1]
    NP_742108.2. NM_172110.3. [O00167-3]
    UniGeneiHs.472877.
    Hs.722040.
    Hs.722415.
    Hs.722416.

    Genome annotation databases

    EnsembliENST00000327619; ENSP00000333640; ENSG00000064655. [O00167-1]
    ENST00000357410; ENSP00000349986; ENSG00000064655. [O00167-3]
    GeneIDi2139.
    KEGGihsa:2139.
    UCSCiuc002xsm.3. human. [O00167-1]
    uc010ghp.3. human. [O00167-3]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U71207 mRNA. Translation: AAB51120.1 .
    Y10261 Genomic DNA. Translation: CAA71310.1 .
    BT006682 mRNA. Translation: AAP35328.1 .
    AL049540
    , AL121776 , AL359434 , AL022342 Genomic DNA. Translation: CAI23166.1 .
    AL121776
    , AL049540 , AL359434 , AL022342 Genomic DNA. Translation: CAI42150.1 .
    AL359434
    , AL049540 , AL121776 , AL022342 Genomic DNA. Translation: CAI40099.1 .
    BC000289 mRNA. Translation: AAH00289.2 .
    BC008803 mRNA. Translation: AAH08803.1 .
    BC013882 mRNA. Translation: AAH13882.2 . Different initiation.
    U81601 mRNA. Translation: AAB42065.1 .
    AJ007992 mRNA. Translation: CAA07815.1 .
    CCDSi CCDS13403.1. [O00167-1 ]
    CCDS54471.1. [O00167-3 ]
    RefSeqi NP_005235.3. NM_005244.4. [O00167-1 ]
    NP_742108.2. NM_172110.3. [O00167-3 ]
    UniGenei Hs.472877.
    Hs.722040.
    Hs.722415.
    Hs.722416.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3GEB X-ray 2.40 A/B/C/D 268-538 [» ]
    3HB0 X-ray 2.50 A/B/C/D 268-538 [» ]
    3HB1 X-ray 2.51 A/B/C/D 268-538 [» ]
    4EGC X-ray 1.99 B 253-538 [» ]
    ProteinModelPortali O00167.
    SMRi O00167. Positions 268-538.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108440. 7 interactions.
    DIPi DIP-40707N.
    IntActi O00167. 2 interactions.
    MINTi MINT-139839.

    Chemistry

    ChEMBLi CHEMBL1293275.

    PTM databases

    PhosphoSitei O00167.

    Proteomic databases

    PaxDbi O00167.
    PRIDEi O00167.

    Protocols and materials databases

    DNASUi 2139.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000327619 ; ENSP00000333640 ; ENSG00000064655 . [O00167-1 ]
    ENST00000357410 ; ENSP00000349986 ; ENSG00000064655 . [O00167-3 ]
    GeneIDi 2139.
    KEGGi hsa:2139.
    UCSCi uc002xsm.3. human. [O00167-1 ]
    uc010ghp.3. human. [O00167-3 ]

    Organism-specific databases

    CTDi 2139.
    GeneCardsi GC20P045523.
    HGNCi HGNC:3520. EYA2.
    HPAi HPA027024.
    MIMi 601654. gene.
    neXtProti NX_O00167.
    PharmGKBi PA27932.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG297494.
    HOVERGENi HBG002447.
    InParanoidi O00167.
    KOi K17620.
    OMAi IHSRPNC.
    OrthoDBi EOG7DNNTZ.
    PhylomeDBi O00167.
    TreeFami TF319337.

    Enzyme and pathway databases

    SABIO-RK O00167.

    Miscellaneous databases

    EvolutionaryTracei O00167.
    GeneWikii EYA2.
    GenomeRNAii 2139.
    NextBioi 8649.
    PROi O00167.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O00167.
    Bgeei O00167.
    Genevestigatori O00167.

    Family and domain databases

    InterProi IPR028473. EYA2.
    IPR006545. EYA_dom.
    IPR028472. EYA_fam.
    IPR023214. HAD-like_dom.
    [Graphical view ]
    PANTHERi PTHR10190. PTHR10190. 1 hit.
    PTHR10190:SF7. PTHR10190:SF7. 1 hit.
    SUPFAMi SSF56784. SSF56784. 1 hit.
    TIGRFAMsi TIGR01658. EYA-cons_domain. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Eyes absent: a gene family found in several metazoan phyla."
      Duncan M.K., Kos L., Jenkins N.A., Gilbert D.J., Copeland N.G., Tomarev S.I.
      Mamm. Genome 8:479-485(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Embryonic brain.
    2. Erratum
      Duncan M.K., Kos L., Jenkins N.A., Gilbert D.J., Copeland N.G., Tomarev S.I.
      Mamm. Genome 8:877-877(1997)
    3. "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].
      Tissue: Embryo.
    4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    5. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      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] (ISOFORMS 2 AND 3).
      Tissue: Lung.
    7. "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] OF 295-538.
      Tissue: Brain.
    8. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 378-496.
      Tissue: Lens epithelium.
    9. "The alpha subunits of Gz and Gi interact with the eyes absent transcription cofactor Eya2, preventing its interaction with the six class of homeodomain-containing proteins."
      Fan X., Brass L.F., Poncz M., Spitz F., Maire P., Manning D.R.
      J. Biol. Chem. 275:32129-32134(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH GNAZ AND GNAI2.
    10. Cited for: SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
    11. "Biochemical and functional characterization of six SIX1 Branchio-oto-renal syndrome mutations."
      Patrick A.N., Schiemann B.J., Yang K., Zhao R., Ford H.L.
      J. Biol. Chem. 284:20781-20790(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SIX1.
    12. "Eya2 is required to mediate the pro-metastatic functions of Six1 via the induction of TGF-beta signaling, epithelial-mesenchymal transition, and cancer stem cell properties."
      Farabaugh S.M., Micalizzi D.S., Jedlicka P., Zhao R., Ford H.L.
      Oncogene 31:552-562(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "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: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 268-538 IN COMPLEX WITH MAGNESIUM, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    14. "Crystal structure of ED-Eya2: insight into dual roles as a protein tyrosine phosphatase and a transcription factor."
      Jung S.K., Jeong D.G., Chung S.J., Kim J.H., Park B.C., Tonks N.K., Ryu S.E., Kim S.J.
      FASEB J. 24:560-569(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 268-538 IN COMPLEX WITH MAGNESIUM IONS AND TRANSITION STATE ANALOGS, COFACTOR, ACTIVE SITE.
    15. "Structure-function analyses of the human SIX1-EYA2 complex reveal insights into metastasis and BOR syndrome."
      Patrick A.N., Cabrera J.H., Smith A.L., Chen X.S., Ford H.L., Zhao R.
      Nat. Struct. Mol. Biol. 20:447-453(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 253-538 IN COMPLEX WITH SIX1, SUBUNIT, MUTAGENESIS OF PRO-516 AND ALA-532.

    Entry informationi

    Entry nameiEYA2_HUMAN
    AccessioniPrimary (citable) accession number: O00167
    Secondary accession number(s): Q5JSW8
    , Q86U84, Q96CV6, Q96H97, Q99503, Q99812, Q9BWF6, Q9H4S3, Q9H4S9, Q9NPZ4, Q9UIX7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: May 2, 2002
    Last modified: October 1, 2014
    This is version 139 of the entry and version 2 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3