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O00167

- EYA2_HUMAN

UniProt

O00167 - EYA2_HUMAN

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Protein

Eyes absent homolog 2

Gene
EYA2, EAB1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 H2AXS139ph

Sites

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

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
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-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.3 Publications

GO - Cellular componenti

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

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 SIX1.3 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.

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.

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. VSP_001490Add
BLAST
Alternative sequencei401 – 47979Missing in isoform 3. VSP_001491Add
BLAST

Sequence conflict

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

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 138 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

Similar proteinsi