H2AX_DICDI
ID H2AX_DICDI Reviewed; 154 AA.
AC Q54WG6;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Histone H2AX;
DE Short=H2a/x;
DE AltName: Full=Histone H2A.X;
GN Name=H2AX; ORFNames=DDB_G0279667;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP PHOSPHORYLATION, AND FUNCTION.
RX PubMed=16243037; DOI=10.1016/j.cub.2005.09.039;
RA Hudson J.J.R., Hsu D.-W., Guo K., Zhukovskaya N., Liu P.-H., Williams J.G.,
RA Pears C.J., Lakin N.D.;
RT "DNA-PKcs-dependent signaling of DNA damage in Dictyostelium discoideum.";
RL Curr. Biol. 15:1880-1885(2005).
CC -!- FUNCTION: Core component of nucleosome which plays a central role in
CC DNA double strand break (DSB) repair. Nucleosomes wrap and compact DNA
CC into chromatin, limiting DNA accessibility to the cellular machineries
CC which require DNA as a template. Histones thereby play a central role
CC in transcription regulation, DNA repair, DNA replication and
CC chromosomal stability. DNA accessibility is regulated via a complex set
CC of post-translational modifications of histones, also called histone
CC code, and nucleosome remodeling (By similarity). Phosphorylation of
CC H2AX seems to be performed by atr1 and/or possibly dnapkcs, as ATM
CC ortholog is absent in the genome of this organism. {ECO:0000250,
CC ECO:0000269|PubMed:16243037}.
CC -!- SUBUNIT: The nucleosome is a histone octamer containing two molecules
CC each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and
CC two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC -!- DOMAIN: The [ST]-Q motif constitutes a recognition sequence for kinases
CC from the PI3/PI4-kinase family. {ECO:0000250}.
CC -!- PTM: Phosphorylated at Ser-151 to form H2AS128ph (gamma-H2AX) in
CC response to DNA double-strand breaks (DSBs) generated by exogenous
CC genotoxic agents and by stalled replication forks. Phosphorylation is
CC dependent on the DNA damage checkpoint kinase atr1 and/or possibly
CC dnapkcs, spreads on either side of a detected DSB site and may mark the
CC surrounding chromatin for recruitment of proteins required for DNA
CC damage signaling and repair. Gamma-H2AX is removed from the DNA prior
CC to the strand invasion-primer extension step of the repair process and
CC subsequently dephosphorylated. Dephosphorylation is necessary for
CC efficient recovery from the DNA damage checkpoint (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
CC -!- CAUTION: To ensure consistency between histone entries, we follow the
CC 'Brno' nomenclature for histone modifications, with positions referring
CC to those used in the literature for the 'closest' model organism. Due
CC to slight variations in histone sequences between organisms and to the
CC presence of initiator methionine in UniProtKB/Swiss-Prot sequences, the
CC actual positions of modified amino acids in the sequence generally
CC differ. In this entry the following convention is used: H2AS128ph =
CC phosphorylated Ser-151. {ECO:0000305}.
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DR EMBL; AAFI02000032; EAL67608.1; -; Genomic_DNA.
DR RefSeq; XP_641587.1; XM_636495.1.
DR AlphaFoldDB; Q54WG6; -.
DR SMR; Q54WG6; -.
DR STRING; 44689.DDB0216271; -.
DR PaxDb; Q54WG6; -.
DR EnsemblProtists; EAL67608; EAL67608; DDB_G0279667.
DR GeneID; 8622161; -.
DR KEGG; ddi:DDB_G0279667; -.
DR dictyBase; DDB_G0279667; H2AX.
DR eggNOG; KOG1756; Eukaryota.
DR HOGENOM; CLU_062828_3_1_1; -.
DR InParanoid; Q54WG6; -.
DR OMA; VMPYIHP; -.
DR PhylomeDB; Q54WG6; -.
DR Reactome; R-DDI-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-DDI-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-DDI-3214815; HDACs deacetylate histones.
DR Reactome; R-DDI-3214858; RMTs methylate histone arginines.
DR Reactome; R-DDI-427359; SIRT1 negatively regulates rRNA expression.
DR Reactome; R-DDI-5689880; Ub-specific processing proteases.
DR Reactome; R-DDI-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-DDI-68616; Assembly of the ORC complex at the origin of replication.
DR Reactome; R-DDI-73772; RNA Polymerase I Promoter Escape.
DR PRO; PR:Q54WG6; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; ISS:dictyBase.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR CDD; cd00074; H2A; 1.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR002119; Histone_H2A.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR InterPro; IPR032454; Histone_H2A_C.
DR PANTHER; PTHR23430; PTHR23430; 1.
DR Pfam; PF00125; Histone; 1.
DR Pfam; PF16211; Histone_H2A_C; 1.
DR PRINTS; PR00620; HISTONEH2A.
DR SMART; SM00414; H2A; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW Chromosome; DNA damage; DNA repair; DNA-binding; Nucleosome core; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..154
FT /note="Histone H2AX"
FT /id="PRO_0000389153"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 151..152
FT /note="[ST]-Q motif"
FT COMPBIAS 22..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 154 AA; 16824 MW; 40E4CF5BDADC0397 CRC64;
MSETKPASSK PAAAAKPKKV IPRVSRTGEP KSKPESRSAR AGITFPVSRV DRLLREGRFA
PRVESTAPVY LAAVLEYLVF EILELAHNTC SISKKTRITP QHINWAVGND LELNSLFQHV
TIAYGGVLPT PQQSTGEKKK KPSKKAAEGS SQIY
