Search Results

Overview

Uniprot ID	Q99504
Protein Name	Protein phosphatase EYA3
Gene Name	EYA3
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
291	SKNRGKRKADATSSQ

Function

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 (PubMed:19234442, PubMed:19351884). 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

Protein Sequence

10 MEEEQDLPEQ 20 PVKKAKMQES 30 GEQTISQVSN 40 PDVSDQKPET 50 SSLASNLPMS 60 EEIMTCTDYI 70 PRSSNDYTSQ 80 MYSAKPYAHI 90 LSVPVSETAY 100 PGQTQYQTLQ 110 QTQPYAVYPQ 120 ATQTYGLPPF 130 GALWPGMKPE 140 SGLIQTPSPS 150 QHSVLTCTTG 160 LTTSQPSPAH 170 YSYPIQASST 180 NASLISTSST 190 IANIPAAAVA 200 SISNQDYPTY 210 TILGQNQYQA 220 CYPSSSFGVT 230 GQTNSDAEST 240 TLAATTYQSE 250 KPSVMAPAPA 260 AQRLSSGDPS 270 TSPSLSQTTP 280 SKDTDDQSRK 290 NMTSKNRGKR 300 KADATSSQDS 310 ELERVFLWDL 320 DETIIIFHSL 330 LTGSYAQKYG 340 KDPTVVIGSG 350 LTMEEMIFEV 360 ADTHLFFNDL 370 EECDQVHVED 380 VASDDNGQDL 390 SNYSFSTDGF 400 SGSGGSGSHG 410 SSVGVQGGVD 420 WMRKLAFRYR 430 KVREIYDKHK 440 SNVGGLLSPQ 450 RKEALQRLRA 460 EIEVLTDSWL 470 GTALKSLLLI 480 QSRKNCVNVL 490 ITTTQLVPAL 500 AKVLLYGLGE 510 IFPIENIYSA 520 TKIGKESCFE 530 RIVSRFGKKV 540 TYVVIGDGRD 550 EEIAAKQHNM 560 PFWRITNHGD 570 LVSLHQALEL DFL

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0005737	cytoplasm
Cellular Component	GO:0005654	nucleoplasm
Cellular Component	GO:0005634	nucleus
Molecular Function	GO:0140793	histone H2AXY142 phosphatase activity
Molecular Function	GO:0046872	metal ion binding
Molecular Function	GO:0004725	protein tyrosine phosphatase activity
Biological Process	GO:0009653	anatomical structure morphogenesis
Biological Process	GO:0030154	cell differentiation
Biological Process	GO:0006351	DNA-templated transcription
Biological Process	GO:0006302	double-strand break repair
Biological Process	GO:2001240	negative regulation of extrinsic apoptotic signaling pathway in absence of ligand
Biological Process	GO:0045739	positive regulation of DNA repair
Biological Process	GO:0010212	response to ionizing radiation
Biological Process	GO:0007601	visual perception

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[3] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[4] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.