H2AX_TETTS
ID H2AX_TETTS Reviewed; 138 AA.
AC P35064; Q24DQ8;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Histone H2AX;
DE AltName: Full=Histone H2A.1;
DE Short=H2A1;
DE AltName: Full=Histone H2A.X;
GN Name=HTA1; ORFNames=TTHERM_00790790;
OS Tetrahymena thermophila (strain SB210).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC Tetrahymena.
OX NCBI_TaxID=312017;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=CU428;
RX PubMed=8177745; DOI=10.1093/nar/21.21.4954;
RA Liu X., Gorovsky M.A.;
RT "Mapping the 5' and 3' ends of Tetrahymena thermophila mRNAs using RNA
RT ligase mediated amplification of cDNA ends (RLM-RACE).";
RL Nucleic Acids Res. 21:4954-4960(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CU428;
RX PubMed=8760889; DOI=10.1093/nar/24.15.3023;
RA Liu X., Gorovsky M.A.;
RT "Cloning and characterization of the major histone H2A genes completes the
RT cloning and sequencing of known histone genes of Tetrahymena thermophila.";
RL Nucleic Acids Res. 24:3023-3030(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB210;
RX PubMed=16933976; DOI=10.1371/journal.pbio.0040286;
RA Eisen J.A., Coyne R.S., Wu M., Wu D., Thiagarajan M., Wortman J.R.,
RA Badger J.H., Ren Q., Amedeo P., Jones K.M., Tallon L.J., Delcher A.L.,
RA Salzberg S.L., Silva J.C., Haas B.J., Majoros W.H., Farzad M.,
RA Carlton J.M., Smith R.K. Jr., Garg J., Pearlman R.E., Karrer K.M., Sun L.,
RA Manning G., Elde N.C., Turkewitz A.P., Asai D.J., Wilkes D.E., Wang Y.,
RA Cai H., Collins K., Stewart B.A., Lee S.R., Wilamowska K., Weinberg Z.,
RA Ruzzo W.L., Wloga D., Gaertig J., Frankel J., Tsao C.-C., Gorovsky M.A.,
RA Keeling P.J., Waller R.F., Patron N.J., Cherry J.M., Stover N.A.,
RA Krieger C.J., del Toro C., Ryder H.F., Williamson S.C., Barbeau R.A.,
RA Hamilton E.P., Orias E.;
RT "Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a
RT model eukaryote.";
RL PLoS Biol. 4:1620-1642(2006).
RN [4]
RP ACETYLATION.
RC STRAIN=B;
RX PubMed=7061439; DOI=10.1016/s0021-9258(18)34965-2;
RA Vavra K.J., Allis C.D., Gorovsky M.A.;
RT "Regulation of histone acetylation in Tetrahymena macro- and micronuclei.";
RL J. Biol. Chem. 257:2591-2598(1982).
RN [5]
RP UBIQUITINATION.
RX PubMed=2713375; DOI=10.1021/bi00429a006;
RA Nickel B.E., Allis C.D., Davie J.R.;
RT "Ubiquitinated histone H2B is preferentially located in transcriptionally
RT active chromatin.";
RL Biochemistry 28:958-963(1989).
RN [6]
RP ACETYLATION AT SER-2; LYS-6; LYS-9; LYS-11; LYS-13 AND LYS-18.
RC STRAIN=B2086, CU427, and CU428;
RX PubMed=12665578; DOI=10.1128/mcb.23.8.2778-2789.2003;
RA Ren Q., Gorovsky M.A.;
RT "The nonessential H2A N-terminal tail can function as an essential charge
RT patch on the H2A.Z variant N-terminal tail.";
RL Mol. Cell. Biol. 23:2778-2789(2003).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-135, AND MUTAGENESIS
RP OF SER-135.
RX PubMed=17242195; DOI=10.1128/mcb.01910-06;
RA Song X., Gjoneska E., Ren Q., Taverna S.D., Allis C.D., Gorovsky M.A.;
RT "Phosphorylation of the SQ H2A.X motif is required for proper meiosis and
RT mitosis in Tetrahymena thermophila.";
RL Mol. Cell. Biol. 27:2648-2660(2007).
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. {ECO:0000269|PubMed:17242195}.
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
CC DNA.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17242195}. Chromosome
CC {ECO:0000269|PubMed:17242195}. Note=Localizes to both the large,
CC transcriptionally active, somatic macronucleus (MAC) and the small,
CC transcriptionally inert, germ line micronucleus (MIC).
CC -!- DOMAIN: The [ST]-Q motif constitutes a recognition sequence for kinases
CC from the PI3/PI4-kinase family.
CC -!- PTM: Monoubiquitination of Lys-124 gives a specific tag for epigenetic
CC transcriptional repression. {ECO:0000250}.
CC -!- PTM: Phosphorylated to form H2AX134ph (gamma-H2AX) in response to DNA
CC double-strand breaks (DSBs) generated by exogenous genotoxic agents in
CC both the mitotic MIC and the amitotic MAC. Gamma-H2AX is also found
CC when programmed DNA rearrangements occur, namely homologous
CC recombination in the MIC during prophase of meiosis, and chromosome
CC fragmentation and DNA elimination in developing MACs. Gamma-H2AX is
CC important to recover from exogenous DNA damage and to repair breaks
CC associated with normal micronuclear meiosis and mitosis and
CC macronuclear amitotic division. {ECO:0000269|PubMed:17242195}.
CC -!- PTM: Acetylation occurs almost exclusively in the MAC.
CC {ECO:0000269|PubMed:12665578, ECO:0000269|PubMed:7061439}.
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 conventions are used: H2AK5ac =
CC acetylated Lys-6; H2AK8ac = acetylated Lys-9; H2AK10ac = acetylated
CC Lys-11; H2AK12ac = acetylated Lys-13; H2AK17ac = acetylated Lys-18;
CC H2AS122ph = phosphorylated Ser-123; H2AK123ub1 = monoubiquitinated Lys-
CC 124; H2AS124ph = phosphorylated Ser-125; H2AS129ph = phosphorylated
CC Ser-130; H2AS134ph = phosphorylated Ser-135. {ECO:0000305}.
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DR EMBL; L18892; AAC37291.1; -; Unassigned_DNA.
DR EMBL; GG662316; EAS05932.1; -; Genomic_DNA.
DR PIR; S41471; S41471.
DR RefSeq; XP_001026177.1; XM_001026177.3.
DR AlphaFoldDB; P35064; -.
DR SMR; P35064; -.
DR STRING; 5911.EAS05932; -.
DR iPTMnet; P35064; -.
DR EnsemblProtists; EAS05932; EAS05932; TTHERM_00790790.
DR GeneID; 7837147; -.
DR KEGG; tet:TTHERM_00790790; -.
DR eggNOG; KOG1756; Eukaryota.
DR HOGENOM; CLU_062828_3_1_1; -.
DR InParanoid; P35064; -.
DR OMA; VMPYIHP; -.
DR OrthoDB; 1504122at2759; -.
DR Proteomes; UP000009168; Unassembled WGS sequence.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
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 InterPro; IPR032458; Histone_H2A_CS.
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.
DR PROSITE; PS00046; HISTONE_H2A; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chromosome; DNA-binding; Isopeptide bond; Nucleosome core;
KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..138
FT /note="Histone H2AX"
FT /id="PRO_0000055284"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 135..136
FT /note="[ST]-Q motif"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:12665578"
FT MOD_RES 6
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:12665578"
FT MOD_RES 9
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:12665578"
FT MOD_RES 11
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:12665578"
FT MOD_RES 13
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:12665578"
FT MOD_RES 18
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:12665578"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17242195"
FT CROSSLNK 124
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000305|PubMed:2713375"
FT MUTAGEN 135
FT /note="S->A: Causes DNA damage accumulation in both MACs
FT and MICs and leads to meiotic and mitotic defects."
FT /evidence="ECO:0000269|PubMed:17242195"
SQ SEQUENCE 138 AA; 14771 MW; 299D1442BC0658F0 CRC64;
MSTTGKGGKA KGKTASSKQV SRSARAGLQF PVGRISRFLK HGRYSERVGT GAPVYLAAVL
EYLAAEVLEL AGNAAKDNKK TRIVPRHILL AIRNDEELNK LMANTTIADG GVLPNINPML
LPSKSKKTES RGQASQDL
