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Histone H2AX (H2a/x) (Histone H2A.X)

 H2AX_HUMAN              Reviewed;         143 AA.
P16104; Q4ZGJ7; Q6IAS5;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
27-SEP-2017, entry version 185.
RecName: Full=Histone H2AX;
Short=H2a/x;
AltName: Full=Histone H2A.X;
Name=H2AFX; Synonyms=H2AX;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2587254; DOI=10.1093/nar/17.22.9113;
Mannironi C., Bonner W.M., Hatch C.L.;
"H2A.X. a histone isoprotein with a conserved C-terminal sequence, is
encoded by a novel mRNA with both DNA replication type and polyA 3'
processing signals.";
Nucleic Acids Res. 17:9113-9126(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung, and Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PHOSPHORYLATION AT SER-140, AND MUTAGENESIS OF GLN-141.
PubMed=9488723; DOI=10.1074/jbc.273.10.5858;
Rogakou E.P., Pilch D.R., Orr A.H., Ivanova V.S., Bonner W.M.;
"DNA double-stranded breaks induce histone H2AX phosphorylation on
serine 139.";
J. Biol. Chem. 273:5858-5868(1998).
[6]
SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-140.
PubMed=10477747; DOI=10.1083/jcb.146.5.905;
Rogakou E.P., Boon C., Redon C., Bonner W.M.;
"Megabase chromatin domains involved in DNA double-strand breaks in
vivo.";
J. Cell Biol. 146:905-916(1999).
[7]
FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-140.
PubMed=10959836; DOI=10.1016/S0960-9822(00)00610-2;
Paull T.T., Rogakou E.P., Yamazaki V., Kirchgessner C.U., Gellert M.,
Bonner W.M.;
"A critical role for histone H2AX in recruitment of repair factors to
nuclear foci after DNA damage.";
Curr. Biol. 10:886-895(2000).
[8]
PHOSPHORYLATION AT SER-140.
PubMed=10734083; DOI=10.1074/jbc.275.13.9390;
Rogakou E.P., Nieves-Neira W., Boon C., Pommier Y., Bonner W.M.;
"Initiation of DNA fragmentation during apoptosis induces
phosphorylation of H2AX histone at serine 139.";
J. Biol. Chem. 275:9390-9395(2000).
[9]
SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-140.
PubMed=11673449; DOI=10.1074/jbc.C100569200;
Ward I.M., Chen J.;
"Histone H2AX is phosphorylated in an ATR-dependent manner in response
to replicational stress.";
J. Biol. Chem. 276:47759-47762(2001).
[10]
FUNCTION, INTERACTION WITH NBN AND BRCA1, SUBCELLULAR LOCATION, AND
PHOSPHORYLATION AT SER-140.
PubMed=12419185; DOI=10.1016/S0960-9822(02)01259-9;
Kobayashi J., Tauchi H., Sakamoto S., Nakamura A., Morishima K.,
Matsuura S., Kobayashi T., Tamai K., Tanimoto K., Komatsu K.;
"NBS1 localizes to gamma-H2AX foci through interaction with the
FHA/BRCT domain.";
Curr. Biol. 12:1846-1851(2002).
[11]
SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-140.
PubMed=12697768; DOI=10.1074/jbc.C300117200;
Ward I.M., Minn K., Jorda K.G., Chen J.;
"Accumulation of checkpoint protein 53BP1 at DNA breaks involves its
binding to phosphorylated histone H2AX.";
J. Biol. Chem. 278:19579-19582(2003).
[12]
SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-140.
PubMed=12660252; DOI=10.1074/jbc.M300198200;
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.;
"Phosphorylation of histone H2AX and activation of Mre11, Rad50, and
Nbs1 in response to replication-dependent DNA double-strand breaks
induced by mammalian DNA topoisomerase I cleavage complexes.";
J. Biol. Chem. 278:20303-20312(2003).
[13]
FUNCTION, INTERACTION WITH MDC1 AND TP53BP1, SUBCELLULAR LOCATION, AND
PHOSPHORYLATION AT SER-140.
PubMed=12607005; DOI=10.1038/nature01446;
Stewart G.S., Wang B., Bignell C.R., Taylor A.M.R., Elledge S.J.;
"MDC1 is a mediator of the mammalian DNA damage checkpoint.";
Nature 421:961-966(2003).
[14]
PHOSPHORYLATION AT SER-140.
PubMed=14627815; DOI=10.1093/nar/gkg921;
Park E.-J., Chan D.W., Park J.-H., Oettinger M.A., Kwon J.;
"DNA-PK is activated by nucleosomes and phosphorylates H2AX within the
nucleosomes in an acetylation-dependent manner.";
Nucleic Acids Res. 31:6819-6827(2003).
[15]
SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-140.
PubMed=15059890; DOI=10.1158/0008-5472.CAN-03-3207;
Stiff T., O'Driscoll M., Rief N., Iwabuchi K., Loebrich M.,
Jeggo P.A.;
"ATM and DNA-PK function redundantly to phosphorylate H2AX after
exposure to ionizing radiation.";
Cancer Res. 64:2390-2396(2004).
[16]
FUNCTION, INTERACTION WITH MDC1 AND NBN, AND SUBCELLULAR LOCATION.
PubMed=15201865; DOI=10.1038/sj.emboj.7600269;
Lukas C., Melander F., Stucki M., Falck J., Bekker-Jensen S.,
Goldberg M., Lerenthal Y., Jackson S.P., Bartek J., Lukas J.;
"Mdc1 couples DNA double-strand break recognition by Nbs1 with its
H2AX-dependent chromatin retention.";
EMBO J. 23:2674-2683(2004).
[17]
PHOSPHORYLATION AT SER-140.
PubMed=15489221; DOI=10.1074/jbc.M406879200;
Kurz E.U., Douglas P., Lees-Miller S.P.;
"Doxorubicin activates ATM-dependent phosphorylation of multiple
downstream targets in part through the generation of reactive oxygen
species.";
J. Biol. Chem. 279:53272-53281(2004).
[18]
INTERACTION WITH DHX9, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT
SER-140.
PubMed=15613478; DOI=10.1074/jbc.M411444200;
Mischo H.E., Hemmerich P., Grosse F., Zhang S.;
"Actinomycin D induces histone gamma-H2AX foci and complex formation
of gamma-H2AX with Ku70 and nuclear DNA helicase II.";
J. Biol. Chem. 280:9586-9594(2005).
[19]
DEPHOSPHORYLATION.
PubMed=16310392; DOI=10.1016/j.molcel.2005.10.003;
Chowdhury D., Keogh M.-C., Ishii H., Peterson C.L., Buratowski S.,
Lieberman J.;
"gamma-H2AX dephosphorylation by protein phosphatase 2A facilitates
DNA double-strand break repair.";
Mol. Cell 20:801-809(2005).
[20]
INTERACTION WITH ARRB2.
PubMed=16820410; DOI=10.1242/jcs.03046;
Neuhaus E.M., Mashukova A., Barbour J., Wolters D., Hatt H.;
"Novel function of beta-arrestin2 in the nucleus of mature
spermatozoa.";
J. Cell Sci. 119:3047-3056(2006).
[21]
UBIQUITINATION.
PubMed=18001824; DOI=10.1016/j.cell.2007.09.040;
Mailand N., Bekker-Jensen S., Faustrup H., Melander F., Bartek J.,
Lukas C., Lukas J.;
"RNF8 ubiquitylates histones at DNA double-strand breaks and promotes
assembly of repair proteins.";
Cell 131:887-900(2007).
[22]
UBIQUITINATION.
PubMed=18001825; DOI=10.1016/j.cell.2007.09.041;
Huen M.S.Y., Grant R., Manke I., Minn K., Yu X., Yaffe M.B., Chen J.;
"RNF8 transduces the DNA-damage signal via histone ubiquitylation and
checkpoint protein assembly.";
Cell 131:901-914(2007).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
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.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[24]
UBIQUITINATION.
PubMed=19203578; DOI=10.1016/j.cell.2008.12.042;
Stewart G.S., Panier S., Townsend K., Al-Hakim A.K., Kolas N.K.,
Miller E.S., Nakada S., Ylanko J., Olivarius S., Mendez M.,
Oldreive C., Wildenhain J., Tagliaferro A., Pelletier L.,
Taubenheim N., Durandy A., Byrd P.J., Stankovic T., Taylor A.M.R.,
Durocher D.;
"The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling
cascade at sites of DNA damage.";
Cell 136:420-434(2009).
[25]
UBIQUITINATION.
PubMed=19203579; DOI=10.1016/j.cell.2008.12.041;
Doil C., Mailand N., Bekker-Jensen S., Menard P., Larsen D.H.,
Pepperkok R., Ellenberg J., Panier S., Durocher D., Bartek J.,
Lukas J., Lukas C.;
"RNF168 binds and amplifies ubiquitin conjugates on damaged
chromosomes to allow accumulation of repair proteins.";
Cell 136:435-446(2009).
[26]
PHOSPHORYLATION AT TYR-143, AND MUTAGENESIS OF TYR-143.
PubMed=19092802; DOI=10.1038/nature07668;
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.;
"WSTF regulates the H2A.X DNA damage response via a novel tyrosine
kinase activity.";
Nature 457:57-62(2009).
[27]
PHOSPHORYLATION AT TYR-143, AND MUTAGENESIS OF TYR-143.
PubMed=19234442; DOI=10.1038/nature07849;
Cook P.J., Ju B.G., Telese F., Wang X., Glass C.K., Rosenfeld M.G.;
"Tyrosine dephosphorylation of H2AX modulates apoptosis and survival
decisions.";
Nature 458:591-596(2009).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[30]
UBIQUITINATION AT LYS-14 AND LYS-16 BY RNF168.
PubMed=22980979; DOI=10.1016/j.cell.2012.08.005;
Mattiroli F., Vissers J.H., van Dijk W.J., Ikpa P., Citterio E.,
Vermeulen W., Marteijn J.A., Sixma T.K.;
"RNF168 ubiquitinates K13-15 on H2A/H2AX to drive DNA Damage
signaling.";
Cell 150:1182-1195(2012).
[31]
INTERACTION WITH EPSTEIN-BARR VIRUS PROTEIN EBNA6, AND SUBCELLULAR
LOCATION.
PubMed=24429368; DOI=10.1128/JVI.03568-13;
Jha H.C., Aj M.P., Saha A., Banerjee S., Lu J., Robertson E.S.;
"Epstein-Barr virus essential antigen EBNA3C attenuates H2AX
expression.";
J. Virol. 88:3776-3788(2014).
[32]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-135, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[33]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-128 AND LYS-135, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[34]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 134-143, AND PHOSPHORYLATION
AT SER-140.
PubMed=22154951; DOI=10.1016/j.jsb.2011.11.022;
Shao Z., Li F., Sy S.M., Yan W., Zhang Z., Gong D., Wen B., Huen M.S.,
Gong Q., Wu J., Shi Y.;
"Specific recognition of phosphorylated tail of H2AX by the tandem
BRCT domains of MCPH1 revealed by complex structure.";
J. Struct. Biol. 177:459-468(2012).
-!- FUNCTION: 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. {ECO:0000269|PubMed:10959836,
ECO:0000269|PubMed:12419185, ECO:0000269|PubMed:12607005,
ECO:0000269|PubMed:15201865}.
-!- SUBUNIT: The nucleosome is a histone octamer containing two
molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4
heterotetramer and two H2A-H2B heterodimers. The octamer wraps
approximately 147 bp of DNA. Interacts with numerous proteins
required for DNA damage signaling and repair when phosphorylated
on Ser-140. These include MDC1, TP53BP1, BRCA1 and the MRN
complex, composed of MRE11, RAD50, and NBN. Interaction with the
MRN complex is mediated at least in part by NBN. Also interacts
with DHX9/NDHII when phosphorylated on Ser-140 and MCPH1 when
phosphorylated at Ser-140 or Tyr-143. Interacts with ARRB2; the
interaction is detected in the nucleus upon OR1D2 stimulation.
Interacts with Epstein-Barr virus protein EBNA6.
{ECO:0000269|PubMed:12419185, ECO:0000269|PubMed:12607005,
ECO:0000269|PubMed:15201865, ECO:0000269|PubMed:15613478,
ECO:0000269|PubMed:16820410, ECO:0000269|PubMed:24429368}.
-!- INTERACTION:
Q9Z0X1:Aifm1 (xeno); NbExp=2; IntAct=EBI-494830, EBI-5326677;
P38398:BRCA1; NbExp=4; IntAct=EBI-494830, EBI-349905;
Q16695:HIST3H3; NbExp=11; IntAct=EBI-494830, EBI-358900;
P02545:LMNA; NbExp=3; IntAct=EBI-494830, EBI-351935;
Q14676:MDC1; NbExp=16; IntAct=EBI-494830, EBI-495644;
P49959:MRE11; NbExp=6; IntAct=EBI-494830, EBI-396513;
O60934:NBN; NbExp=14; IntAct=EBI-494830, EBI-494844;
Q6ZW49-1:PAXIP1; NbExp=7; IntAct=EBI-494830, EBI-7521368;
O15297:PPM1D; NbExp=3; IntAct=EBI-494830, EBI-1551512;
P67775:PPP2CA; NbExp=2; IntAct=EBI-494830, EBI-712311;
P51532:SMARCA4; NbExp=9; IntAct=EBI-494830, EBI-302489;
Q15554:TERF2; NbExp=4; IntAct=EBI-494830, EBI-706637;
Q12888:TP53BP1; NbExp=6; IntAct=EBI-494830, EBI-396540;
Q99986:VRK1; NbExp=3; IntAct=EBI-494830, EBI-1769146;
Q14191:WRN; NbExp=6; IntAct=EBI-494830, EBI-368417;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12419185,
ECO:0000269|PubMed:12660252, ECO:0000269|PubMed:12697768,
ECO:0000269|PubMed:15613478, ECO:0000269|PubMed:24429368}.
Chromosome {ECO:0000269|PubMed:10959836,
ECO:0000269|PubMed:11673449, ECO:0000269|PubMed:12607005,
ECO:0000269|PubMed:12660252, ECO:0000269|PubMed:15059890,
ECO:0000269|PubMed:15201865, ECO:0000269|PubMed:15613478}.
-!- DEVELOPMENTAL STAGE: Synthesized in G1 as well as in S-phase.
-!- DOMAIN: The [ST]-Q motif constitutes a recognition sequence for
kinases from the PI3/PI4-kinase family.
-!- PTM: 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. 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. 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. Dephosphorylation of Ser-140 by PP2A is required for DNA
DSB repair. 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.
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. 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. 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. Phosphorylation at Tyr-143 (H2AXY142ph)
by BAZ1B/WSTF determines the relative recruitment of either DNA
repair or pro-apoptotic factors. Phosphorylation at Tyr-143
(H2AXY142ph) favors the recruitment of APBB1/FE65 and pro-
apoptosis factors such as MAPK8/JNK1, triggering apoptosis. 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). {ECO:0000269|PubMed:10477747,
ECO:0000269|PubMed:10734083, ECO:0000269|PubMed:10959836,
ECO:0000269|PubMed:11673449, ECO:0000269|PubMed:12419185,
ECO:0000269|PubMed:12607005, ECO:0000269|PubMed:12660252,
ECO:0000269|PubMed:12697768, ECO:0000269|PubMed:14627815,
ECO:0000269|PubMed:15059890, ECO:0000269|PubMed:15489221,
ECO:0000269|PubMed:15613478, ECO:0000269|PubMed:19092802,
ECO:0000269|PubMed:19234442, ECO:0000269|PubMed:22154951,
ECO:0000269|PubMed:9488723}.
-!- PTM: Monoubiquitination of Lys-120 (H2AXK119ub) by RING1 and
RNF2/RING2 complex gives a specific tag for epigenetic
transcriptional repression (By similarity). 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. 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.
H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked
ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events.
{ECO:0000250, ECO:0000269|PubMed:18001824,
ECO:0000269|PubMed:18001825, ECO:0000269|PubMed:19203578,
ECO:0000269|PubMed:19203579, ECO:0000269|PubMed:22980979}.
-!- PTM: Acetylation at Lys-37 increases in S and G2 phases. This
modification has been proposed to play a role in DNA double-strand
break repair (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/h2afx/";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/H2AFXID40783ch11q23.html";
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EMBL; X14850; CAA32968.1; -; mRNA.
EMBL; CR457079; CAG33360.1; -; mRNA.
EMBL; DQ015918; AAY22178.1; -; Genomic_DNA.
EMBL; BC004915; AAH04915.1; -; mRNA.
EMBL; BC011694; AAH11694.1; -; mRNA.
EMBL; BC013416; AAH13416.1; -; mRNA.
CCDS; CCDS8410.1; -.
PIR; S07631; S07631.
RefSeq; NP_002096.1; NM_002105.2.
UniGene; Hs.477879; -.
PDB; 1YDP; X-ray; 1.90 A; P=78-86.
PDB; 2AZM; X-ray; 2.41 A; C/D=134-143.
PDB; 2D31; X-ray; 3.20 A; C/F=78-86.
PDB; 2DYP; X-ray; 2.50 A; C=78-86.
PDB; 3SHV; X-ray; 2.10 A; C/D=134-143.
PDB; 3SQD; X-ray; 2.15 A; C/D=134-143.
PDB; 3SZM; X-ray; 2.63 A; I/J/K/L/M/N/O/P=134-143.
PDB; 3U3Z; X-ray; 1.50 A; B=140-143.
PDBsum; 1YDP; -.
PDBsum; 2AZM; -.
PDBsum; 2D31; -.
PDBsum; 2DYP; -.
PDBsum; 3SHV; -.
PDBsum; 3SQD; -.
PDBsum; 3SZM; -.
PDBsum; 3U3Z; -.
ProteinModelPortal; P16104; -.
SMR; P16104; -.
BioGrid; 109268; 304.
CORUM; P16104; -.
DIP; DIP-33604N; -.
ELM; P16104; -.
IntAct; P16104; 173.
MINT; MINT-1338182; -.
STRING; 9606.ENSP00000364310; -.
iPTMnet; P16104; -.
PhosphoSitePlus; P16104; -.
SwissPalm; P16104; -.
BioMuta; H2AFX; -.
DMDM; 121992; -.
EPD; P16104; -.
MaxQB; P16104; -.
PaxDb; P16104; -.
PeptideAtlas; P16104; -.
PRIDE; P16104; -.
TopDownProteomics; P16104; -.
Ensembl; ENST00000375167; ENSP00000364310; ENSG00000188486.
Ensembl; ENST00000530167; ENSP00000434024; ENSG00000188486.
GeneID; 3014; -.
KEGG; hsa:3014; -.
UCSC; uc001pvg.4; human.
CTD; 3014; -.
DisGeNET; 3014; -.
EuPathDB; HostDB:ENSG00000188486.3; -.
GeneCards; H2AFX; -.
HGNC; HGNC:4739; H2AFX.
HPA; CAB012264; -.
HPA; HPA041189; -.
HPA; HPA051647; -.
MIM; 601772; gene.
neXtProt; NX_P16104; -.
OpenTargets; ENSG00000188486; -.
PharmGKB; PA29116; -.
eggNOG; KOG1756; Eukaryota.
eggNOG; COG5262; LUCA.
GeneTree; ENSGT00760000118934; -.
HOGENOM; HOG000234652; -.
HOVERGEN; HBG009342; -.
InParanoid; P16104; -.
KO; K11251; -.
OMA; MPNIHQT; -.
OrthoDB; EOG091G0XGD; -.
PhylomeDB; P16104; -.
TreeFam; TF300137; -.
Reactome; R-HSA-1221632; Meiotic synapsis.
Reactome; R-HSA-171306; Packaging Of Telomere Ends.
Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex.
Reactome; R-HSA-212300; PRC2 methylates histones and DNA.
Reactome; R-HSA-2299718; Condensation of Prophase Chromosomes.
Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-HSA-2559586; DNA Damage/Telomere Stress Induced Senescence.
Reactome; R-HSA-3214858; RMTs methylate histone arginines.
Reactome; R-HSA-427359; SIRT1 negatively regulates rRNA Expression.
Reactome; R-HSA-427389; ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression.
Reactome; R-HSA-5334118; DNA methylation.
Reactome; R-HSA-5578749; Transcriptional regulation by small RNAs.
Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
Reactome; R-HSA-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-HSA-5693571; Nonhomologous End-Joining (NHEJ).
Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
Reactome; R-HSA-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
Reactome; R-HSA-73728; RNA Polymerase I Promoter Opening.
Reactome; R-HSA-73777; RNA Polymerase I Chain Elongation.
Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
Reactome; R-HSA-912446; Meiotic recombination.
Reactome; R-HSA-977225; Amyloid fiber formation.
SIGNOR; P16104; -.
ChiTaRS; H2AFX; human.
EvolutionaryTrace; P16104; -.
GeneWiki; H2AFX; -.
GenomeRNAi; 3014; -.
PRO; PR:P16104; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000188486; -.
CleanEx; HS_H2AFX; -.
Genevisible; P16104; HS.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; IBA:GO_Central.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0035861; C:site of double-strand break; IDA:MGI.
GO; GO:0003677; F:DNA binding; IBA:GO_Central.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0042393; F:histone binding; IPI:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:BHF-UCL.
GO; GO:0071480; P:cellular response to gamma radiation; IEA:Ensembl.
GO; GO:0090398; P:cellular senescence; IEA:Ensembl.
GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
GO; GO:0006342; P:chromatin silencing; IBA:GO_Central.
GO; GO:0000077; P:DNA damage checkpoint; IDA:UniProtKB.
GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
GO; GO:0006302; P:double-strand break repair; NAS:UniProtKB.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; TAS:Reactome.
GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
GO; GO:0006334; P:nucleosome assembly; NAS:UniProtKB.
GO; GO:0045739; P:positive regulation of DNA repair; NAS:UniProtKB.
GO; GO:0010212; P:response to ionizing radiation; NAS:UniProtKB.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR009072; Histone-fold.
InterPro; IPR002119; Histone_H2A.
InterPro; IPR007125; Histone_H2A/H2B/H3.
InterPro; IPR032454; Histone_H2A_C.
InterPro; IPR032458; Histone_H2A_CS.
Pfam; PF00125; Histone; 1.
Pfam; PF16211; Histone_H2A_C; 1.
PRINTS; PR00620; HISTONEH2A.
SMART; SM00414; H2A; 1.
SUPFAM; SSF47113; SSF47113; 1.
PROSITE; PS00046; HISTONE_H2A; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Cell cycle; Chromosome; Complete proteome;
DNA damage; DNA recombination; DNA repair; DNA-binding;
Host-virus interaction; Isopeptide bond; Meiosis; Nucleosome core;
Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P27661}.
CHAIN 2 143 Histone H2AX.
/FTId=PRO_0000055242.
MOTIF 140 141 [ST]-Q motif.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:P27661}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000250|UniProtKB:P27661}.
MOD_RES 6 6 N6-acetyllysine.
{ECO:0000250|UniProtKB:P27661}.
MOD_RES 10 10 N6-acetyllysine.
{ECO:0000250|UniProtKB:P27661}.
MOD_RES 37 37 N6-acetyllysine.
{ECO:0000250|UniProtKB:P27661}.
MOD_RES 122 122 Phosphoserine.
{ECO:0000250|UniProtKB:P27661}.
MOD_RES 140 140 Phosphoserine; by ATM, ATR and PRKDC.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000269|PubMed:10477747,
ECO:0000269|PubMed:10734083,
ECO:0000269|PubMed:10959836,
ECO:0000269|PubMed:11673449,
ECO:0000269|PubMed:12419185,
ECO:0000269|PubMed:12607005,
ECO:0000269|PubMed:12660252,
ECO:0000269|PubMed:12697768,
ECO:0000269|PubMed:14627815,
ECO:0000269|PubMed:15059890,
ECO:0000269|PubMed:15489221,
ECO:0000269|PubMed:15613478,
ECO:0000269|PubMed:22154951,
ECO:0000269|PubMed:9488723}.
MOD_RES 143 143 Phosphotyrosine; by WSTF.
{ECO:0000269|PubMed:19092802,
ECO:0000269|PubMed:19234442}.
CROSSLNK 14 14 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:22980979}.
CROSSLNK 16 16 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:22980979}.
CROSSLNK 128 128 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 135 135 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
MUTAGEN 141 141 Q->N: Reduced phosphorylation of S-140 in
response to DNA damage.
{ECO:0000269|PubMed:9488723}.
MUTAGEN 143 143 Y->F: Displays a reduced apoptotic
response. S-140 phosphorylation is
reduced. {ECO:0000269|PubMed:19092802,
ECO:0000269|PubMed:19234442}.
CONFLICT 78 78 R -> L (in Ref. 2; CAG33360).
{ECO:0000305}.
SEQUENCE 143 AA; 15145 MW; D4683775C2E6C3A9 CRC64;
MSGRGKTGGK ARAKAKSRSS RAGLQFPVGR VHRLLRKGHY AERVGAGAPV YLAAVLEYLT
AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGG VTIAQGGVLP NIQAVLLPKK
TSATVGPKAP SGGKKATQAS QEY


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