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Protein Page:
H2AX (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
H2AX a histone that replaces conventional H2A in a subset of nucleosomes. 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. Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an octamer, around which approximately 146 bp of DNA is wrapped in repeating units, called 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. Phosphorylated on S139 by ATM and DNA-PK in response to DNA double strand breaks (DSBs) generated by exogenous genotoxic agents and by stalled replication forks, and may also occur during meiotic recombination events and immunoglobulin class switching in lymphocytes. Phosphorylation can extend up to several thousand nucleosomes from the actual site of the DSB and may mark the surrounding chromatin for recruitment of proteins required for DNA damage signaling and repair. Widespread phosphorylation may also serve to amplify the damage signal or aid repair of persistent lesions. Dephosphorylation of S139 by PP2A is required for DNA DSB repair. Apparently phosphorylated on Y143 by WSTF, determining the relative recruitment of either DNA repair or pro-apoptotic factors. H2AXpY142 favors the recruitment of pro-apoptotic factors APBB1 and JNK1. In contrast, dephosphorylation of pY143 by EYA phosphatases favors the recruitment of MDC1-containing DNA repair complexes to the tail of phosphorylated pS139. Monoubiquitination of K119 by RING1 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'K63' linkages by the E2 ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the recruitment of repair proteins to sites of DNA damage. Note: This description may include information from UniProtKB.
Protein type: DNA binding protein; Helicase; DNA repair, damage
Cellular Component: nucleoplasm; XY body; male germ cell nucleus; chromosome, telomeric region; condensed nuclear chromosome; nuclear chromatin; replication fork; nucleosome; nucleus
Molecular Function: protein binding; enzyme binding; DNA binding; histone binding; protein heterodimerization activity; damaged DNA binding
Biological Process: meiosis; nucleosome assembly; positive regulation of DNA repair; double-strand break repair; DNA damage checkpoint; spermatogenesis; response to ionizing radiation; DNA repair; response to DNA damage stimulus; double-strand break repair via homologous recombination
Reference #:  P16104 (UniProtKB)
Alt. Names/Synonyms: H2A histone family, member X; H2A.X; H2a/x; H2AFX; H2AX; H2AX histone; Histone H2A.x
Gene Symbols: H2AFX
Molecular weight: 15,145 Da
Basal Isoelectric point: 10.74  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

H2AX

Protein Structure Not Found.


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Sites Implicated In
apoptosis, altered: S140‑p
apoptosis, induced: Y143‑p
cell cycle regulation: S140‑p
cytoskeletal reorganization: S140‑p
DNA repair, altered: S140‑p, Y143‑p
intracellular localization: T137‑p, S140‑p
molecular association, regulation: T137‑p, S140‑p, Y143‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
3 52 K6-ac __MSGRGkTGGkARA
1 52 K10-ac GRGkTGGkARAKAKS
2 1 K37-ac RVHRLLRkGHyAERV
0 3 Y40-p RLLRkGHyAERVGAG
0 20 K96-ub RNDEELNkLLGGVtI
1 5 T102-p NkLLGGVtIAQGGVL
0 41 K119-ac IQAVLLPkktsAtVG
2 176 K119-ub IQAVLLPkktsAtVG
0 19 K120-ac QAVLLPkktsAtVGP
2 162 K120-ub QAVLLPkktsAtVGP
0 4 T121-p AVLLPkktsAtVGPk
0 5 S122-p VLLPkktsAtVGPkA
0 2 T124-p LPkktsAtVGPkAPs
0 1 K128 tsAtVGPKAPsGGkk
0 112 K128-ub tsAtVGPkAPsGGkk
0 1 S131-p tVGPkAPsGGkkAtQ
0 3 K134-ac PkAPsGGkkAtQAsQ
0 5 K134-ub PkAPsGGkkAtQAsQ
0 11 K135-ub kAPsGGkkAtQAsQE
5 15 T137-p PsGGkkAtQAsQEy_
153 28 S140-p GkkAtQAsQEy____
4 2 Y143-p AtQAsQEy_______
2577 : Phospho-Histone H2A.X (Ser139) Antibody
4309 : Phospho-Histone H2A.X (Ser139) (20E3) Rabbit mAb (Biotinylated)
5438 : Phospho-Histone H2A.X (Ser139/Tyr142) Antibody
5763 : Phospho-Histone H2A.X (Ser139) (20E3) Rabbit mAb (PE Conjugate)
8228 : Phospho-Histone H2A.X (Ser139) (20E3) Rabbit mAb (Alexa Fluor(R) 555 Conjugate)
9718 : Phospho-Histone H2A.X (Ser139) (20E3) Rabbit mAb
9719 : Phospho-Histone H2A.X (Ser139) (20E3) Rabbit mAb (Alexa Fluor(R) 488 Conjugate)
9720 : Phospho-Histone H2A.X (Ser139) (20E3) Rabbit mAb (Alexa Fluor(R) 647 Conjugate)
5438 : Phospho-Histone H2A.X (Ser139/Tyr142) Antibody
  mouse

 
K6-ac __MSGRGkTGGkARA
K10-ac GRGkTGGkARAKAKS
K37 RVHRLLRKGHYAERV
Y40 RLLRKGHYAERVGAG
K96-ub RNDEELNkLLGGVtI
T102-p NkLLGGVtIAQGGVL
K119-ac IQAVLLPkkssAtVG
K119-ub IQAVLLPkkssAtVG
K120-ac QAVLLPkkssAtVGP
K120-ub QAVLLPkkssAtVGP
S121-p AVLLPkkssAtVGPk
S122-p VLLPkkssAtVGPkA
T124-p LPkkssAtVGPkAPA
K128-ac ssAtVGPkAPAVGkK
K128-ub ssAtVGPkAPAVGkK
A131 tVGPkAPAVGkKAsQ
K134-ac PkAPAVGkKAsQAsQ
K134 PkAPAVGKKAsQAsQ
K135 kAPAVGkKAsQAsQE
S137-p PAVGkKAsQAsQEy_
S140-p GkKAsQAsQEy____
Y143-p AsQAsQEy_______
2577 : Phospho-Histone H2A.X (Ser139) Antibody
4309 : Phospho-Histone H2A.X (Ser139) (20E3) Rabbit mAb (Biotinylated)
5438 : Phospho-Histone H2A.X (Ser139/Tyr142) Antibody
5763 : Phospho-Histone H2A.X (Ser139) (20E3) Rabbit mAb (PE Conjugate)
8228 : Phospho-Histone H2A.X (Ser139) (20E3) Rabbit mAb (Alexa Fluor(R) 555 Conjugate)
9718 : Phospho-Histone H2A.X (Ser139) (20E3) Rabbit mAb
9719 : Phospho-Histone H2A.X (Ser139) (20E3) Rabbit mAb (Alexa Fluor(R) 488 Conjugate)
9720 : Phospho-Histone H2A.X (Ser139) (20E3) Rabbit mAb (Alexa Fluor(R) 647 Conjugate)
5438 : Phospho-Histone H2A.X (Ser139/Tyr142) Antibody
  rat

 
K6 __MSGRGKTGGKARA
K10 GRGKTGGKARAKAKS
K37 RVHRLLRKGHYAERV
Y40 RLLRKGHYAERVGAG
K96 RNDEELNKLLGGVTI
T102 NKLLGGVTIAQGGVL
K119-ac IQAVLLPkkTSATVG
K119-ub IQAVLLPkkTSATVG
K120-ac QAVLLPkkTSATVGP
K120-ub QAVLLPkkTSATVGP
T121 AVLLPkkTSATVGPk
S122 VLLPkkTSATVGPkA
T124 LPkkTSATVGPkAPA
K128 TSATVGPKAPAGGKK
K128-ub TSATVGPkAPAGGKK
A131 TVGPkAPAGGKKASQ
K134 PkAPAGGKKASQAsQ
K134 PkAPAGGKKASQAsQ
K135 kAPAGGKKASQAsQE
S137 PAGGKKASQAsQEY_
S140-p GKKASQAsQEY____
Y143 ASQAsQEY_______
2577 : Phospho-Histone H2A.X (Ser139) Antibody
4309 : Phospho-Histone H2A.X (Ser139) (20E3) Rabbit mAb (Biotinylated)
5438 : Phospho-Histone H2A.X (Ser139/Tyr142) Antibody
5763 : Phospho-Histone H2A.X (Ser139) (20E3) Rabbit mAb (PE Conjugate)
8228 : Phospho-Histone H2A.X (Ser139) (20E3) Rabbit mAb (Alexa Fluor(R) 555 Conjugate)
9718 : Phospho-Histone H2A.X (Ser139) (20E3) Rabbit mAb
9719 : Phospho-Histone H2A.X (Ser139) (20E3) Rabbit mAb (Alexa Fluor(R) 488 Conjugate)
9720 : Phospho-Histone H2A.X (Ser139) (20E3) Rabbit mAb (Alexa Fluor(R) 647 Conjugate)
5438 : Phospho-Histone H2A.X (Ser139/Tyr142) Antibody
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