H2AX_XENLA - dbPTM
H2AX_XENLA - PTM Information in dbPTM
Basic Information of Protein
UniProt ID H2AX_XENLA
UniProt AC Q6GM86
Protein Name Histone H2AX
Gene Name h2afx
Organism Xenopus laevis (African clawed frog).
Sequence Length 139
Subcellular Localization Nucleus. Chromosome.
Protein Description Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Required for checkpoint-mediated arrest of cell cycle progression in response to low doses of ionizing radiation and for efficient repair of DNA double strand breaks (DSBs) specifically when modified by C-terminal phosphorylation (By similarity)..
Protein Sequence MSGRGKAVSKTRAKAKTRSSRAGLQFPVGRVHRLLRKGNYAHRVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKSRIIPRHLQLAVRNDEELNKLLGGVTIAQGGVLPNIQAVLLPKKSSGGVSTSGKKSSQQSQEY
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MSGRGKAVS
------CCCCCCHHH
36.88-
2Phosphorylation------MSGRGKAVS
------CCCCCCHHH
36.88-
10LactoylationGRGKAVSKTRAKAKT
CCCCHHHHHHHHHHH
35.12-
136PhosphorylationGKKSSQQSQEY----
CCCCCCCCCCC----
19.8310477747
139PhosphorylationSSQQSQEY-------
CCCCCCCC-------
19.0619092802

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
139YPhosphorylationKinaseWSTFA8DZJ1
Uniprot
139YPhosphorylationKinaseBAZ1B-GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of H2AX_XENLA !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of H2AX_XENLA !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of H2AX_XENLA !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of H2AX_XENLA

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Megabase chromatin domains involved in DNA double-strand breaks invivo.";
Rogakou E.P., Boon C., Redon C., Bonner W.M.;
J. Cell Biol. 146:905-916(1999).
Cited for: PHOSPHORYLATION AT SER-136.
"WSTF regulates the H2A.X DNA damage response via a novel tyrosinekinase activity.";
Xiao A., Li H., Shechter D., Ahn S.H., Fabrizio L.A.,Erdjument-Bromage H., Ishibe-Murakami S., Wang B., Tempst P.,Hofmann K., Patel D.J., Elledge S.J., Allis C.D.;
Nature 457:57-62(2009).
Cited for: PHOSPHORYLATION AT TYR-139.

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