dbPTM

H2AX_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	H2AX_HUMAN
UniProt AC	P16104
Protein Name	Histone H2AX
Gene Name	H2AFX
Organism	Homo sapiens (Human).
Sequence Length	143
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..
Protein Sequence	MSGRGKTGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGHYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGGVTIAQGGVLPNIQAVLLPKKTSATVGPKAPSGGKKATQASQEY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSGRGKTGG ------CCCCCCCCC	36.88	9488723
6	Acetylation	--MSGRGKTGGKARA --CCCCCCCCCHHHH	42.51	19608861
6	Lactylation	--MSGRGKTGGKARA --CCCCCCCCCHHHH	42.51	31645732
10	Lactoylation	GRGKTGGKARAKAKS CCCCCCCHHHHHHHH	35.72	-
10	Lactylation	GRGKTGGKARAKAKS CCCCCCCHHHHHHHH	35.72	31645732
10	Acetylation	GRGKTGGKARAKAKS CCCCCCCHHHHHHHH	35.72	26051181
14	Ubiquitination	TGGKARAKAKSRSSR CCCHHHHHHHHHHHC	51.28	22980979
16	Acetylation	GKARAKAKSRSSRAG CHHHHHHHHHHHCCC	45.77	19666589
16	Ubiquitination	GKARAKAKSRSSRAG CHHHHHHHHHHHCCC	45.77	22980979
17	Phosphorylation	KARAKAKSRSSRAGL HHHHHHHHHHHCCCC	42.10	24247654
19	Phosphorylation	RAKAKSRSSRAGLQF HHHHHHHHHCCCCCC	31.13	30622161
20	Phosphorylation	AKAKSRSSRAGLQFP HHHHHHHHCCCCCCC	25.66	27966365
21	Methylation	KAKSRSSRAGLQFPV HHHHHHHCCCCCCCH	33.64	-
30	Methylation	GLQFPVGRVHRLLRK CCCCCHHHHHHHHHC	22.69	-
37	Acetylation	RVHRLLRKGHYAERV HHHHHHHCCCHHHHC	50.43	-
40	Phosphorylation	RLLRKGHYAERVGAG HHHHCCCHHHHCCCC	20.87	22817900
58	Phosphorylation	YLAAVLEYLTAEILE HHHHHHHHHHHHHHH	12.75	-
77	Phosphorylation	AARDNKKTRIIPRHL HHHCCCCCCEEHHHH	28.80	23882029
82	Methylation	KKTRIIPRHLQLAIR CCCCEEHHHHHHHHC	32.51	-
89	Methylation	RHLQLAIRNDEELNK HHHHHHHCCHHHHHH	38.65	-
96	Ubiquitination	RNDEELNKLLGGVTI CCHHHHHHHHCCEEE	58.68	22817900
96	Acetylation	RNDEELNKLLGGVTI CCHHHHHHHHCCEEE	58.68	25038526
102	O-linked_Glycosylation	NKLLGGVTIAQGGVL HHHHCCEEEECCCCC	17.55	27458206
102	Phosphorylation	NKLLGGVTIAQGGVL HHHHCCEEEECCCCC	17.55	20703100
119	Ubiquitination	IQAVLLPKKTSATVG EEEEECCCCCCCCCC	69.52	25015289
119	Sumoylation	IQAVLLPKKTSATVG EEEEECCCCCCCCCC	69.52	-
119	Neddylation	IQAVLLPKKTSATVG EEEEECCCCCCCCCC	69.52	32015554
119	Acetylation	IQAVLLPKKTSATVG EEEEECCCCCCCCCC	69.52	164041
120	Neddylation	QAVLLPKKTSATVGP EEEECCCCCCCCCCC	45.86	32015554
120	Ubiquitination	QAVLLPKKTSATVGP EEEECCCCCCCCCCC	45.86	23000965
120	Lactylation	QAVLLPKKTSATVGP EEEECCCCCCCCCCC	45.86	31645732
121	Phosphorylation	AVLLPKKTSATVGPK EEECCCCCCCCCCCC	29.71	30266825
122	Phosphorylation	VLLPKKTSATVGPKA EECCCCCCCCCCCCC	30.72	30266825
124	Phosphorylation	LPKKTSATVGPKAPS CCCCCCCCCCCCCCC	26.26	30266825
128	Lactylation	TSATVGPKAPSGGKK CCCCCCCCCCCCCHH	67.98	31645732
128	Ubiquitination	TSATVGPKAPSGGKK CCCCCCCCCCCCCHH	67.98	32142685
128	Sumoylation	TSATVGPKAPSGGKK CCCCCCCCCCCCCHH	67.98	28112733
131	Phosphorylation	TVGPKAPSGGKKATQ CCCCCCCCCCHHCCH	66.10	26074081
134	"N6,N6-dimethyllysine"	PKAPSGGKKATQASQ CCCCCCCHHCCHHHH	42.64	-
134	Acetylation	PKAPSGGKKATQASQ CCCCCCCHHCCHHHH	42.64	26051181
134	Methylation	PKAPSGGKKATQASQ CCCCCCCHHCCHHHH	42.64	-
134	Ubiquitination	PKAPSGGKKATQASQ CCCCCCCHHCCHHHH	42.64	27667366
135	Methylation	KAPSGGKKATQASQE CCCCCCHHCCHHHHC	61.00	-
135	Acetylation	KAPSGGKKATQASQE CCCCCCHHCCHHHHC	61.00	26051181
135	Lactylation	KAPSGGKKATQASQE CCCCCCHHCCHHHHC	61.00	31645732
135	Sumoylation	KAPSGGKKATQASQE CCCCCCHHCCHHHHC	61.00	28112733
135	Ubiquitination	KAPSGGKKATQASQE CCCCCCHHCCHHHHC	61.00	21906983
137	Phosphorylation	PSGGKKATQASQEY- CCCCHHCCHHHHCC-	33.28	28176443
140	O-linked_Glycosylation	GKKATQASQEY---- CHHCCHHHHCC----	17.46	27458206
140	Phosphorylation	GKKATQASQEY---- CHHCCHHHHCC----	17.46	21151168
140	Dephosphorylation	GKKATQASQEY---- CHHCCHHHHCC----	17.46	12926989
143	Phosphorylation	ATQASQEY------- CCHHHHCC-------	19.06	28176443

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
16	S	Phosphorylation	Kinase	RSK2	P51812	PSP
17	S	Phosphorylation	Kinase	RPS6KA3	P51812	GPS
39	Y	Phosphorylation	Kinase	JMJD6	Q6NYC1	PSP
57	Y	Phosphorylation	Kinase	CK2A1	P68400	PSP
136	T	Phosphorylation	Kinase	PRKDC	P78527	GPS
139	S	Phosphorylation	Kinase	ATM	Q13315	PSP
139	S	Phosphorylation	Kinase	PRKDC	P78527	GPS
139	S	Phosphorylation	Kinase	STK4	Q13043	GPS
140	S	Phosphorylation	Kinase	ATM	Q13315	Uniprot
140	S	Phosphorylation	Kinase	ATR	Q13535	Uniprot
140	S	Phosphorylation	Kinase	RPS6KA3	P51812	GPS
140	S	Phosphorylation	Kinase	PRKDC	P78527	Uniprot
142	Y	Phosphorylation	Kinase	BAZ1B	Q9UIG0	GPS
143	Y	Phosphorylation	Kinase	WSTF	Q9UIG0	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	BMI1	P35226	PMID:21676867
-	K	Ubiquitination	E3 ubiquitin ligase	RNF2	Q99496	PMID:21676867
-	K	Ubiquitination	E3 ubiquitin ligase	TOPORS	Q9NS56	PMID:22972498
-	K	Ubiquitination	E3 ubiquitin ligase	RNF8	O76064	PMID:18001824
-	K	Ubiquitination	E3 ubiquitin ligase	BRCA1	P38398	PMID:11927591
-	K	Ubiquitination	E3 ubiquitin ligase	BARD1	Q99728	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	PRC1	O43663	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	RNF168	Q8IYW5	PMID:22980979
-	K	Ubiquitination	E3 ubiquitin ligase	BMI1#RNF2	P35226#Q99496	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
14	K	ubiquitylation	22980979
Ubiquitination at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage is initiated by RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-linked ubiquitin are then conjugated to monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin chains in vitro.
16	K	ubiquitylation	22980979
Ubiquitination at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage is initiated by RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-linked ubiquitin are then conjugated to monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin chains in vitro.
37	K	Acetylation	-
Acetylation at Lys-37 increases in S and G2 phases.
63	K	ubiquitylation	18001824
Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the recruitment of repair proteins to sites of DNA damage.
120	K	ubiquitylation	18001824
Monoubiquitination of Lys-120 (H2AXK119ub) by RING1 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression (By similarity).
140	S	Phosphorylation	9488723
Dephosphorylation of Ser-140 by PP2A is required for DNA DSB repair.
140	S	Phosphorylation	9488723
During immunoglobulin class switch recombination in lymphocytes, Ser-140 phosphorylation (H2AX139ph) may occur at sites of DNA-recombination subsequent to activation of the activation-induced cytidine deaminase AICDA.
140	S	Phosphorylation	9488723
In contrast, dephosphorylation of Tyr-143 by EYA proteins (EYA1, EYA2, EYA3 or EYA4) favors the recruitment of MDC1-containing DNA repair complexes to the tail of phosphorylated Ser-140 (H2AX139ph).
140	S	Phosphorylation	9488723
In meiosis, Ser-140 phosphorylation (H2AX139ph) may occur at synaptonemal complexes during leptotene as an ATM-dependent response to the formation of programmed DSBs by SPO11.
140	S	Phosphorylation	9488723
Phosphorylated on Ser-140 (to form gamma-H2AX or H2AX139ph) 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.
140	S	Phosphorylation	9488723
Phosphorylation of Ser-140 (H2AX139ph) in response to ionizing radiation is mediated by both ATM and PRKDC while defects in DNA replication induce Ser-140 phosphorylation (H2AX139ph) subsequent to activation of ATR and PRKDC.
140	S	Phosphorylation	9488723
Ser-140 phosphorylation (H2AX139ph) may also be required for transcriptional repression of unsynapsed chromatin and meiotic sex chromosome inactivation (MSCI), whereby the X and Y chromosomes condense in pachytene to form the heterochromatic XY-body.
140	S	Phosphorylation	9488723
Ser-140 phosphorylation (H2AX139ph) may subsequently occurs at unsynapsed regions of both autosomes and the XY bivalent during zygotene, downstream of ATR and BRCA1 activation.

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BRCA1_HUMAN	BRCA1	physical	10959836
RAD50_HUMAN	RAD50	physical	10959836
RAD51_HUMAN	RAD51	physical	10959836
BRCA1_HUMAN	BRCA1	physical	19805520
EYA1_HUMAN	EYA1	physical	19234442
EYA3_HUMAN	EYA3	physical	19234442
SMCA4_HUMAN	SMARCA4	physical	16932743
SMCA2_HUMAN	SMARCA2	physical	16932743
NBN_HUMAN	NBN	physical	16932743
H2B2E_HUMAN	HIST2H2BE	physical	16522924
CALR_HUMAN	CALR	physical	16522924
NPM_HUMAN	NPM1	physical	16522924
GRP78_HUMAN	HSPA5	physical	16522924
SSRP1_HUMAN	SSRP1	physical	16522924
SP16H_HUMAN	SUPT16H	physical	16522924
HNRPR_HUMAN	HNRNPR	physical	16522924
LA_HUMAN	SSB	physical	16522924
EIF3L_HUMAN	EIF3L	physical	16522924
PABP1_HUMAN	PABPC1	physical	16522924
PARP1_HUMAN	PARP1	physical	16522924
DHX30_HUMAN	DHX30	physical	16522924
H2B1M_HUMAN	HIST1H2BM	physical	16522924
PAPP1_HUMAN	PAPPA	physical	16522924
PTCD3_HUMAN	PTCD3	physical	16522924
P53_HUMAN	TP53	physical	16322227
WRN_HUMAN	WRN	physical	15733840
NBN_HUMAN	NBN	physical	15733840
RPB1_HUMAN	POLR2A	physical	15613478
DHX9_HUMAN	DHX9	physical	15613478
XRCC6_HUMAN	XRCC6	physical	15613478
SP16H_HUMAN	SUPT16H	physical	18406329
BRCA2_HUMAN	BRCA2	physical	18406329
PARP1_HUMAN	PARP1	physical	18406329
XRCC5_HUMAN	XRCC5	physical	18406329
XRCC6_HUMAN	XRCC6	physical	18406329
KAT5_HUMAN	KAT5	physical	18406329
EF1A1_HUMAN	EEF1A1	physical	18406329
PPM1G_HUMAN	PPM1G	physical	18406329
PRKDC_HUMAN	PRKDC	physical	18406329
SSRP1_HUMAN	SSRP1	physical	18406329
ATM_HUMAN	ATM	physical	18344987
BRCA1_HUMAN	BRCA1	physical	18344987
RAD17_HUMAN	RAD17	physical	18344987
FOXO3_HUMAN	FOXO3	physical	18344987
MDC1_HUMAN	MDC1	physical	15201865
RAD50_HUMAN	RAD50	physical	15201865
NBN_HUMAN	NBN	physical	15201865
MRE11_HUMAN	MRE11A	physical	15201865
FACD2_HUMAN	FANCD2	physical	17304220
SMCA4_HUMAN	SMARCA4	physical	20224553
SMCA2_HUMAN	SMARCA2	physical	20224553
XRCC6_HUMAN	XRCC6	physical	20224553
H31_HUMAN	HIST1H3A	physical	20224553
H2B2E_HUMAN	HIST2H2BE	physical	20224553
H2A2C_HUMAN	HIST2H2AC	physical	20224553
BRD1_HUMAN	BRD1	physical	20224553
KAT2A_HUMAN	KAT2A	physical	20224553
KAT8_HUMAN	KAT8	physical	20224553
KAT5_HUMAN	KAT5	physical	20224553
KAT2B_HUMAN	KAT2B	physical	20224553
HAT1_HUMAN	HAT1	physical	20224553
PPM1D_HUMAN	PPM1D	physical	20118229
QORX_HUMAN	TP53I3	physical	20023697
BRCA2_HUMAN	BRCA2	physical	20936109
COF1_HUMAN	CFL1	physical	20000738
CLUS_HUMAN	CLU	physical	20000738
ENPL_HUMAN	HSP90B1	physical	20000738
ANXA4_HUMAN	ANXA4	physical	20000738
ANXA5_HUMAN	ANXA5	physical	20000738
PDCD6_HUMAN	PDCD6	physical	20000738
TMX1_HUMAN	TMX1	physical	20000738
ADT3_HUMAN	SLC25A6	physical	20000738
TOR1B_HUMAN	TOR1B	physical	20000738
HS90A_HUMAN	HSP90AA1	physical	20000738
HS71L_HUMAN	HSPA1L	physical	20000738
TRAP1_HUMAN	TRAP1	physical	20000738
PRDX6_HUMAN	PRDX6	physical	20000738
PLOD1_HUMAN	PLOD1	physical	20000738
SODM_HUMAN	SOD2	physical	20000738
AIFM1_HUMAN	AIFM1	physical	20000738
NONO_HUMAN	NONO	physical	20000738
PARP1_HUMAN	PARP1	physical	20000738
CALR_HUMAN	CALR	physical	20000738
1433Z_HUMAN	YWHAZ	physical	20000738
1433E_HUMAN	YWHAE	physical	20000738
TOR1A_HUMAN	TOR1A	physical	20000738
HYOU1_HUMAN	HYOU1	physical	20000738
SSBP_HUMAN	SSBP1	physical	20000738
PGK1_HUMAN	PGK1	physical	20000738
MOES_HUMAN	MSN	physical	20000738
IF4A1_HUMAN	EIF4A1	physical	20000738
RS10_HUMAN	RPS10	physical	20000738
CPSM_HUMAN	CPS1	physical	20000738
ILF2_HUMAN	ILF2	physical	20000738
ANXA2_HUMAN	ANXA2	physical	20000738
S10A4_HUMAN	S100A4	physical	20000738
PEF1_HUMAN	PEF1	physical	20000738
ANXA6_HUMAN	ANXA6	physical	20000738
1433B_HUMAN	YWHAB	physical	20000738
MATR3_HUMAN	MATR3	physical	20000738
ALDOA_HUMAN	ALDOA	physical	20000738
KPYM_HUMAN	PKM	physical	20000738
ENOA_HUMAN	ENO1	physical	20000738
OFUT1_HUMAN	POFUT1	physical	20000738
LDHB_HUMAN	LDHB	physical	20000738
ELAV1_HUMAN	ELAVL1	physical	20000738
HNRPD_HUMAN	HNRNPD	physical	20000738
HNRDL_HUMAN	HNRNPDL	physical	20000738
HNRH3_HUMAN	HNRNPH3	physical	20000738
HNRPR_HUMAN	HNRNPR	physical	20000738
ROAA_HUMAN	HNRNPAB	physical	20000738
PCBP2_HUMAN	PCBP2	physical	20000738
PABP1_HUMAN	PABPC1	physical	20000738
BTF3_HUMAN	BTF3	physical	20000738
MSI2H_HUMAN	MSI2	physical	20000738
THOC4_HUMAN	ALYREF	physical	20000738
HNRPQ_HUMAN	SYNCRIP	physical	20000738
ROA1_HUMAN	HNRNPA1	physical	20000738
ROA2_HUMAN	HNRNPA2B1	physical	20000738
HNRPC_HUMAN	HNRNPC	physical	20000738
VPS35_HUMAN	VPS35	physical	20000738
ERP29_HUMAN	ERP29	physical	20000738
VAT1_HUMAN	VAT1	physical	20000738
LMNA_HUMAN	LMNA	physical	20000738
P3H1_HUMAN	P3H1	physical	20000738
PDIA4_HUMAN	PDIA4	physical	20000738
RB11B_HUMAN	RAB11B	physical	20000738
NACAM_HUMAN	NACA	physical	20000738
NACA_HUMAN	NACA	physical	20000738
IF2B_HUMAN	EIF2S2	physical	20000738
EF1B_HUMAN	EEF1B2	physical	20000738
PDIA6_HUMAN	PDIA6	physical	20000738
TCPE_HUMAN	CCT5	physical	20000738
CATD_HUMAN	CTSD	physical	20000738
ERO1A_HUMAN	ERO1L	physical	20000738
PDIA1_HUMAN	P4HB	physical	20000738
PRDX4_HUMAN	PRDX4	physical	20000738
PPIA_HUMAN	PPIA	physical	20000738
PSB3_HUMAN	PSMB3	physical	20000738
RLA2_HUMAN	RPLP2	physical	20000738
PSB4_HUMAN	PSMB4	physical	20000738
FKB10_HUMAN	FKBP10	physical	20000738
SUMF2_HUMAN	SUMF2	physical	20000738
P4HA2_HUMAN	P4HA2	physical	20000738
RPN2_HUMAN	RPN2	physical	20000738
TXD12_HUMAN	TXNDC12	physical	20000738
PGES2_HUMAN	PTGES2	physical	20000738
HCD2_HUMAN	HSD17B10	physical	20000738
TKT_HUMAN	TKT	physical	20000738
GANAB_HUMAN	GANAB	physical	20000738
BGAL_HUMAN	GLB1	physical	20000738
CMBL_HUMAN	CMBL	physical	20000738
GLU2B_HUMAN	PRKCSH	physical	20000738
LG3BP_HUMAN	LGALS3BP	physical	20000738
HEXA_HUMAN	HEXA	physical	20000738
ABHDA_HUMAN	ABHD10	physical	20000738
NNRE_HUMAN	APOA1BP	physical	20000738
CFA45_HUMAN	CFAP45	physical	20000738
RMD1_HUMAN	RMDN1	physical	20000738
GRP75_HUMAN	HSPA9	physical	20000738
PRDX3_HUMAN	PRDX3	physical	20000738
HIBCH_HUMAN	HIBCH	physical	20000738
OTUB1_HUMAN	OTUB1	physical	21900206
SYQ_HUMAN	QARS	physical	21900206
TAF1C_HUMAN	TAF1C	physical	21900206
A2MG_HUMAN	A2M	physical	21900206
ACTB_HUMAN	ACTB	physical	21900206
TAF5L_HUMAN	TAF5L	physical	21900206
TNR16_HUMAN	NGFR	physical	21900206
MASP1_HUMAN	MASP1	physical	21900206
TIAM2_HUMAN	TIAM2	physical	21900206
COPG1_HUMAN	COPG1	physical	21900206
BMI1_HUMAN	BMI1	physical	21383063
CBX2_HUMAN	CBX2	physical	21383063
TP53B_HUMAN	TP53BP1	physical	21566653
MDC1_HUMAN	MDC1	physical	12607005
TP53B_HUMAN	TP53BP1	physical	12607005
MRE11_HUMAN	MRE11A	physical	12419185
NBN_HUMAN	NBN	physical	12419185
EGFR_HUMAN	EGFR	physical	21704408
ATM_HUMAN	ATM	physical	21704408
TIF1B_HUMAN	TRIM28	physical	21704408
PML_HUMAN	PML	physical	21704408
H32_HUMAN	HIST2H3C	physical	21704408
CBX5_HUMAN	CBX5	physical	21704408
RING2_HUMAN	RNF2	physical	21676867
BMI1_HUMAN	BMI1	physical	21676867
ATM_HUMAN	ATM	physical	21676867
MDC1_HUMAN	MDC1	physical	21676867
NBN_HUMAN	NBN	physical	21676867
TOPRS_HUMAN	TOPORS	physical	22972498
NUCL_HUMAN	NCL	physical	23145133
NBN_HUMAN	NBN	physical	23145133
XRCC6_HUMAN	XRCC6	physical	23145133
DDX21_HUMAN	DDX21	physical	23145133
UBC_HUMAN	UBC	physical	24196443
CSK21_HUMAN	CSNK2A1	physical	25252977
UBP11_HUMAN	USP11	physical	26507658
WAP53_HUMAN	WRAP53	physical	26734725
H2B1O_HUMAN	HIST1H2BO	physical	28514442
H2B1D_HUMAN	HIST1H2BD	physical	28514442
H2B1C_HUMAN	HIST1H2BD	physical	28514442
GON4L_HUMAN	GON4L	physical	28514442
TONSL_HUMAN	TONSL	physical	28514442
H12_HUMAN	HIST1H1C	physical	28514442
PHF14_HUMAN	PHF14	physical	28514442
MMS22_HUMAN	MMS22L	physical	28514442
H1T_HUMAN	HIST1H1T	physical	28514442
IPO9_HUMAN	IPO9	physical	28514442
CRML_HUMAN	CRAMP1L	physical	28514442
PARP2_HUMAN	PARP2	physical	28514442
MIER1_HUMAN	MIER1	physical	28514442
SP16H_HUMAN	SUPT16H	physical	28514442
XPC_HUMAN	XPC	physical	28514442
YBOX2_HUMAN	YBX2	physical	28514442
S18L2_HUMAN	SS18L2	physical	28514442
H2A2B_HUMAN	HIST2H2AB	physical	28514442
MIER3_HUMAN	MIER3	physical	28514442
DNLI3_HUMAN	LIG3	physical	28514442
SSRP1_HUMAN	SSRP1	physical	28514442
CP087_HUMAN	C16orf87	physical	28514442
PPM1G_HUMAN	PPM1G	physical	28514442
ZCCHV_HUMAN	ZC3HAV1	physical	28514442
NPAT_HUMAN	NPAT	physical	28514442
RS27A_HUMAN	RPS27A	physical	28514442
XRCC6_HUMAN	XRCC6	physical	28514442
CETN2_HUMAN	CETN2	physical	28514442
MCM2_HUMAN	MCM2	physical	28514442
NPM_HUMAN	NPM1	physical	28514442
CHD1L_HUMAN	CHD1L	physical	28514442
GAN_HUMAN	GAN	physical	28514442
MCM4_HUMAN	MCM4	physical	28514442
RL26L_HUMAN	RPL26L1	physical	28514442
TIM_HUMAN	TIMELESS	physical	28514442
PARP1_HUMAN	PARP1	physical	28514442
RS2_HUMAN	RPS2	physical	28514442
RS3_HUMAN	RPS3	physical	28514442
SPT6H_HUMAN	SUPT6H	physical	28514442
RS15_HUMAN	RPS15	physical	28514442
ILF2_HUMAN	ILF2	physical	28514442
CCD86_HUMAN	CCDC86	physical	28514442
NP1L1_HUMAN	NAP1L1	physical	28514442
CTCF_HUMAN	CTCF	physical	28514442
H2AY_HUMAN	H2AFY	physical	28514442
YBOX1_HUMAN	YBX1	physical	28514442
PSF2_HUMAN	GINS2	physical	28514442
ANKH1_HUMAN	ANKHD1	physical	28514442
RS16_HUMAN	RPS16	physical	28514442
MCM6_HUMAN	MCM6	physical	28514442
KRR1_HUMAN	KRR1	physical	28514442
CXXC1_HUMAN	CXXC1	physical	28514442
ZCHC9_HUMAN	ZCCHC9	physical	28514442
PSF3_HUMAN	GINS3	physical	28514442
RS3A_HUMAN	RPS3A	physical	28514442
RS10_HUMAN	RPS10	physical	28514442
ZBT24_HUMAN	ZBTB24	physical	28514442
LAR1B_HUMAN	LARP1B	physical	28514442
RENT1_HUMAN	UPF1	physical	28514442
RS18_HUMAN	RPS18	physical	28514442
RBM19_HUMAN	RBM19	physical	28514442
ZNF22_HUMAN	ZNF22	physical	28514442
RS6_HUMAN	RPS6	physical	28514442
ELAV2_HUMAN	ELAVL2	physical	28514442
SLD5_HUMAN	GINS4	physical	28514442
RS28_HUMAN	RPS28	physical	28514442
DKC1_HUMAN	DKC1	physical	28514442
RL8_HUMAN	RPL8	physical	28514442
ZSC25_HUMAN	ZSCAN25	physical	28514442
RS9_HUMAN	RPS9	physical	28514442
YBOX3_HUMAN	YBX3	physical	28514442
RL23A_HUMAN	RPL23A	physical	28514442
RS5_HUMAN	RPS5	physical	28514442
RT35_HUMAN	MRPS35	physical	28514442
RL19_HUMAN	RPL19	physical	28514442
ZN574_HUMAN	ZNF574	physical	28514442
HIF1A_HUMAN	HIF1A	physical	27918549
TRAF6_HUMAN	TRAF6	physical	27918549
RNF8_HUMAN	RNF8	physical	28983621

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of H2AX_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-6 AND LYS-10, AND MASSSPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, AND MASSSPECTROMETRY.	19007248 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140, AND MASSSPECTROMETRY.	17525332 [Abstract]
"Actinomycin D induces histone gamma-H2AX foci and complex formationof gamma-H2AX with Ku70 and nuclear DNA helicase II."; Mischo H.E., Hemmerich P., Grosse F., Zhang S.; J. Biol. Chem. 280:9586-9594(2005). Cited for: INTERACTION WITH DHX9, SUBCELLULAR LOCATION, AND PHOSPHORYLATION ATSER-140.	15613478 [Abstract]
"Doxorubicin activates ATM-dependent phosphorylation of multipledownstream targets in part through the generation of reactive oxygenspecies."; Kurz E.U., Douglas P., Lees-Miller S.P.; J. Biol. Chem. 279:53272-53281(2004). Cited for: PHOSPHORYLATION AT SER-140.	15489221 [Abstract]
"ATM and DNA-PK function redundantly to phosphorylate H2AX afterexposure to ionizing radiation."; Stiff T., O'Driscoll M., Rief N., Iwabuchi K., Loebrich M.,Jeggo P.A.; Cancer Res. 64:2390-2396(2004). Cited for: SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-140.	15059890 [Abstract]
"DNA-PK is activated by nucleosomes and phosphorylates H2AX within thenucleosomes in an acetylation-dependent manner."; Park E.-J., Chan D.W., Park J.-H., Oettinger M.A., Kwon J.; Nucleic Acids Res. 31:6819-6827(2003). Cited for: PHOSPHORYLATION AT SER-140.	14627815 [Abstract]
"MDC1 is a mediator of the mammalian DNA damage checkpoint."; Stewart G.S., Wang B., Bignell C.R., Taylor A.M.R., Elledge S.J.; Nature 421:961-966(2003). Cited for: FUNCTION, INTERACTION WITH MDC1 AND TP53BP1, SUBCELLULAR LOCATION, ANDPHOSPHORYLATION AT SER-140.	12607005 [Abstract]
"Phosphorylation of histone H2AX and activation of Mre11, Rad50, andNbs1 in response to replication-dependent DNA double-strand breaksinduced by mammalian DNA topoisomerase I cleavage complexes."; Furuta T., Takemura H., Liao Z.-Y., Aune G.J., Redon C.,Sedelnikova O.A., Pilch D.R., Rogakou E.P., Celeste A., Chen H.T.,Nussenzweig A., Aladjem M.I., Bonner W.M., Pommier Y.; J. Biol. Chem. 278:20303-20312(2003). Cited for: SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-140.	12660252 [Abstract]
"Accumulation of checkpoint protein 53BP1 at DNA breaks involves itsbinding to phosphorylated histone H2AX."; Ward I.M., Minn K., Jorda K.G., Chen J.; J. Biol. Chem. 278:19579-19582(2003). Cited for: SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-140.	12697768 [Abstract]
"NBS1 localizes to gamma-H2AX foci through interaction with theFHA/BRCT domain."; Kobayashi J., Tauchi H., Sakamoto S., Nakamura A., Morishima K.,Matsuura S., Kobayashi T., Tamai K., Tanimoto K., Komatsu K.; Curr. Biol. 12:1846-1851(2002). Cited for: FUNCTION, INTERACTION WITH NBN AND BRCA1, SUBCELLULAR LOCATION, ANDPHOSPHORYLATION AT SER-140.	12419185 [Abstract]
"Histone H2AX is phosphorylated in an ATR-dependent manner in responseto replicational stress."; Ward I.M., Chen J.; J. Biol. Chem. 276:47759-47762(2001). Cited for: SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-140.	11673449 [Abstract]
"Initiation of DNA fragmentation during apoptosis inducesphosphorylation of H2AX histone at serine 139."; Rogakou E.P., Nieves-Neira W., Boon C., Pommier Y., Bonner W.M.; J. Biol. Chem. 275:9390-9395(2000). Cited for: PHOSPHORYLATION AT SER-140.	10734083 [Abstract]
"A critical role for histone H2AX in recruitment of repair factors tonuclear foci after DNA damage."; Paull T.T., Rogakou E.P., Yamazaki V., Kirchgessner C.U., Gellert M.,Bonner W.M.; Curr. Biol. 10:886-895(2000). Cited for: FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-140.	10959836 [Abstract]
"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: SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-140.	10477747 [Abstract]
"DNA double-stranded breaks induce histone H2AX phosphorylation onserine 139."; Rogakou E.P., Pilch D.R., Orr A.H., Ivanova V.S., Bonner W.M.; J. Biol. Chem. 273:5858-5868(1998). Cited for: PHOSPHORYLATION AT SER-140, AND MUTAGENESIS OF GLN-141.	9488723 [Abstract]
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells."; Kim J.-E., Tannenbaum S.R., White F.M.; J. Proteome Res. 4:1339-1346(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-121, AND MASSSPECTROMETRY.	16083285 [Abstract]
"Tyrosine dephosphorylation of H2AX modulates apoptosis and survivaldecisions."; Cook P.J., Ju B.G., Telese F., Wang X., Glass C.K., Rosenfeld M.G.; Nature 458:591-596(2009). Cited for: PHOSPHORYLATION AT TYR-143, AND MUTAGENESIS OF TYR-143.	19234442 [Abstract]
"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-143, AND MUTAGENESIS OF TYR-143.	19092802 [Abstract]

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