CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019720
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Eyes absent homolog 3 
Protein Synonyms/Alias
  
Gene Name
 EYA3 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
272LSQTTPSKDTDDQSRubiquitination[1]
515YSATKIGKESCFERIubiquitination[1]
546RDEEIAAKQHNMPFWubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961
Functional Description
 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. 
Sequence Annotation
 ACT_SITE 309 309 Nucleophile (Probable).
 ACT_SITE 311 311 Proton donor (By similarity).
 METAL 309 309 Magnesium.
 METAL 311 311 Magnesium (By similarity).
 METAL 537 537 Magnesium (By similarity).
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 266 266 Phosphoserine.
 MOD_RES 472 472 Phosphoserine.  
Keyword
 Acetylation; Activator; Alternative splicing; Chromatin regulator; Complete proteome; Cytoplasm; Developmental protein; DNA damage; DNA repair; Hydrolase; Magnesium; Metal-binding; Nucleus; Phosphoprotein; Protein phosphatase; Reference proteome; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 573 AA 
Protein Sequence
MEEEQDLPEQ PVKKAKMQES GEQTISQVSN PDVSDQKPET SSLASNLPMS EEIMTCTDYI 60
PRSSNDYTSQ MYSAKPYAHI LSVPVSETAY PGQTQYQTLQ QTQPYAVYPQ ATQTYGLPPF 120
GALWPGMKPE SGLIQTPSPS QHSVLTCTTG LTTSQPSPAH YSYPIQASST NASLISTSST 180
IANIPAAAVA SISNQDYPTY TILGQNQYQA CYPSSSFGVT GQTNSDAEST TLAATTYQSE 240
KPSVMAPAPA AQRLSSGDPS TSPSLSQTTP SKDTDDQSRK NMTSKNRGKR KADATSSQDS 300
ELERVFLWDL DETIIIFHSL LTGSYAQKYG KDPTVVIGSG LTMEEMIFEV ADTHLFFNDL 360
EECDQVHVED VASDDNGQDL SNYSFSTDGF SGSGGSGSHG SSVGVQGGVD WMRKLAFRYR 420
KVREIYDKHK SNVGGLLSPQ RKEALQRLRA EIEVLTDSWL GTALKSLLLI QSRKNCVNVL 480
ITTTQLVPAL AKVLLYGLGE IFPIENIYSA TKIGKESCFE RIVSRFGKKV TYVVIGDGRD 540
EEIAAKQHNM PFWRITNHGD LVSLHQALEL DFL 573 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0005667; C:transcription factor complex; IEA:Compara.
 GO:0003682; F:chromatin binding; IEA:Compara.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB.
 GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:Compara.
 GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
 GO:0006302; P:double-strand break repair; IMP:UniProtKB.
 GO:0016576; P:histone dephosphorylation; IDA:UniProtKB.
 GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
 GO:0045739; P:positive regulation of DNA repair; IMP:UniProtKB.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0010212; P:response to ionizing radiation; IDA:UniProtKB.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0007601; P:visual perception; TAS:ProtInc. 
Interpro
 IPR006545; EYA. 
Pfam
  
SMART
  
PROSITE
  
PRINTS