H2AX_TETPY
ID H2AX_TETPY Reviewed; 138 AA.
AC P02273;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Histone H2AX;
DE AltName: Full=Histone H2A.1;
DE Short=H2A1;
DE AltName: Full=Histone H2A.X;
GN Name=HTA1;
OS Tetrahymena pyriformis.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC Tetrahymena.
OX NCBI_TaxID=5908;
RN [1]
RP PROTEIN SEQUENCE OF 2-138.
RX PubMed=6885734; DOI=10.1093/oxfordjournals.jbchem.a134286;
RA Fusauchi Y., Iwai K.;
RT "Tetrahymena histone H2A. Isolation and two variant sequences.";
RL J. Biochem. 93:1487-1497(1983).
RN [2]
RP ACETYLATION AT SER-2; LYS-6 AND LYS-13, AND PHOSPHORYLATION AT SER-123;
RP SER-125 AND SER-130.
RX PubMed=6706903; DOI=10.1093/oxfordjournals.jbchem.a134578;
RA Fusauchi Y., Iwai K.;
RT "Tetrahymena histone H2A. Acetylation in the N-terminal sequence and
RT phosphorylation in the C-terminal sequence.";
RL J. Biochem. 95:147-154(1984).
RN [3]
RP UBIQUITINATION, AND IDENTIFICATION OF PROBABLE UBIQUITINATION SITE.
RX PubMed=2993268; DOI=10.1093/oxfordjournals.jbchem.a135201;
RA Fusauchi Y., Iwai K.;
RT "Tetrahymena ubiquitin-histone conjugate uH2A. Isolation and structural
RT analysis.";
RL J. Biochem. 97:1467-1476(1985).
CC -!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact
CC DNA into chromatin, limiting DNA accessibility to the cellular
CC machineries which require DNA as a template. Histones thereby play a
CC central role in transcription regulation, DNA repair, DNA replication
CC and chromosomal stability. DNA accessibility is regulated via a complex
CC set of post-translational modifications of histones, also called
CC histone code, and nucleosome remodeling.
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. Chromosome. Note=Localizes to both the
CC large, transcriptionally active, somatic macronucleus (MAC) and the
CC small, transcriptionally inert, germ line micronucleus (MIC).
CC {ECO:0000250}.
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: Acetylation occurs almost exclusively in the MAC. {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 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 PIR; A02600; HSTE91.
DR AlphaFoldDB; P02273; -.
DR SMR; P02273; -.
DR iPTMnet; P02273; -.
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; Direct protein sequencing; DNA-binding;
KW Isopeptide bond; Nucleosome core; Nucleus; Phosphoprotein; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6706903,
FT ECO:0000269|PubMed:6885734"
FT CHAIN 2..138
FT /note="Histone H2AX"
FT /id="PRO_0000055283"
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:6706903"
FT MOD_RES 6
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:6706903"
FT MOD_RES 9
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 11
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 13
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:6706903"
FT MOD_RES 18
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:6706903"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:6706903"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:6706903"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT CROSSLNK 124
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000305|PubMed:2993268"
SQ SEQUENCE 138 AA; 14785 MW; A57D0AADA2F7B7EE CRC64;
MSTTGKGGKA KGKTASSKQV SRSARAGLQF PVGRISRFLK HGRYSERIGT GAPVYLAAVL
EYLAAEVLEL AGNAAKDNKK TRIVPRHILL AIRNDEELNK LMANTTIADG GVLPNINPML
LPSKSKKTES RGQASQDI
