3hb1
From Proteopedia
Contents |
Crystal structure of ed-eya2 complexed with Alf3
Template:ABSTRACT PUBMED 19858093
Function
[EYA2_HUMAN] 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. Seems to coactivate SIX2, SIX4 and SIX5. Together with SIX1 and DACH2 seem to be involved in myogenesis. May be involved in development of the eye. Interaction with GNAZ and GNAI2 prevents nuclear translocation and transcriptional activity.[1]
About this Structure
3hb1 is a 4 chain structure with sequence from Human. Full crystallographic information is available from OCA.
Reference
- Jung SK, Jeong DG, Chung SJ, Kim JH, Park BC, Tonks NK, Ryu SE, Kim SJ. Crystal structure of ED-Eya2: insight into dual roles as a protein tyrosine phosphatase and a transcription factor. FASEB J. 2010 Feb;24(2):560-9. Epub 2009 Oct 26. PMID:19858093 doi:10.1096/fj.09-143891
- ↑ Krishnan N, Jeong DG, Jung SK, Ryu SE, Xiao A, Allis CD, Kim SJ, Tonks NK. Dephosphorylation of the C-terminal tyrosyl residue of the DNA damage-related histone H2A.X is mediated by the protein phosphatase eyes absent. J Biol Chem. 2009 Jun 12;284(24):16066-70. Epub 2009 Apr 7. PMID:19351884 doi:C900032200
