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Q99504

- EYA3_HUMAN

UniProt

Q99504 - EYA3_HUMAN

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Protein

Eyes absent homolog 3

Gene

EYA3

Organism
Homo sapiens (Human)
Status
Reviewed - 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

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 tyrosine/serine/threonine phosphatase activity Source: Ensembl
  4. 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
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: 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-KW
  2. nucleus Source: UniProtKB
  3. 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.

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

BgeeiQ99504.
CleanExiHS_EYA3.
ExpressionAtlasiQ99504. baseline and differential.
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. 5 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.
GeneTreeiENSGT00390000008860.
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

        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:
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. [Q99504-4]
ENST00000540618; ENSP00000442558; ENSG00000158161. [Q99504-5]
GeneIDi2140.
KEGGihsa:2140.
UCSCiuc001bpi.2. human. [Q99504-1]
uc001bpj.3. human.
uc010oft.2. 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. 5 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 . [Q99504-4 ]
ENST00000540618 ; ENSP00000442558 ; ENSG00000158161 . [Q99504-5 ]
GeneIDi 2140.
KEGGi hsa:2140.
UCSCi uc001bpi.2. human. [Q99504-1 ]
uc001bpj.3. human.
uc010oft.2. 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.
GeneTreei ENSGT00390000008860.
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

Bgeei Q99504.
CleanExi HS_EYA3.
ExpressionAtlasi Q99504. baseline and differential.
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

« 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: October 29, 2014
This is version 127 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