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H2A1_TETPY
ID   H2A1_TETPY              Reviewed;         133 AA.
AC   P02274;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Histone H2A.1;
DE   AltName: Full=Histone H2A.2;
GN   Name=HTA2;
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 2-133.
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 AND
RP   SER-129.
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   -!- 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; H2AS127ph = phosphorylated Ser-128. {ECO:0000305}.
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DR   PIR; A02601; HSTE92.
DR   AlphaFoldDB; P02274; -.
DR   SMR; P02274; -.
DR   iPTMnet; P02274; -.
DR   PRIDE; P02274; -.
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..133
FT                   /note="Histone H2A.1"
FT                   /id="PRO_0000055285"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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         129
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:6706903"
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   133 AA;  14257 MW;  19FA68FA17F78677 CRC64;
     MSTTGKGGKA KGKTASSKQV SRSARAGLQF PVGRISRFLK NGRYSERIGT GAPVYLAAVL
     EYLAAEVLEL AGNAAKDNKK TRIVPRHILL AIRNDEELNK LMANTTIADG GVLPNINPML
     LPSKTKKTSE AEH
 
 
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