ID   H2A_TIGCA               Reviewed;         124 AA.
AC   P84057; P02267;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Histone H2A;
GN   Name=His2A;
OS   Tigriopus californicus (Marine copepod).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Hexanauplia; Copepoda; Harpacticoida; Harpacticidae; Tigriopus.
OX   NCBI_TaxID=6832;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1446074; DOI=10.3109/10425179209020818;
RA   Brown D., Cook A., Wagner M., Wells D.;
RT   "Closely linked H2B genes in the marine copepod, Tigriopus californicus
RT   indicate a recent gene duplication or gene conversion event.";
RL   DNA Seq. 2:387-396(1992).
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.
CC   -!- PTM: Monoubiquitination of Lys-119 gives a specific tag for epigenetic
CC       transcriptional repression. {ECO:0000250}.
CC   -!- PTM: Phosphorylation on Ser-2 is enhanced during mitosis.
CC       Phosphorylation on Ser-2 directly represses transcription (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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DR   EMBL; S49144; AAA12278.1; -; Genomic_DNA.
DR   EMBL; M84797; AAC41555.1; -; Genomic_DNA.
DR   PIR; C56612; C56612.
DR   AlphaFoldDB; P84057; -.
DR   SMR; P84057; -.
DR   EnsemblMetazoa; TCAL_03264-PA_mrna; TRY68716.1; TCAL_03264.
DR   EnsemblMetazoa; TCAL_07217-PA_mrna; TRY67727.1; TCAL_07217.
DR   EnsemblMetazoa; TCAL_12413-PA_mrna; TRY78826.1; TCAL_12413.
DR   EnsemblMetazoa; TCAL_12418-PA_mrna; TRY78830.1; TCAL_12418.
DR   EnsemblMetazoa; TCAL_12920-PA_mrna; TRY77834.1; TCAL_12920.
DR   EnsemblMetazoa; TCAL_13516-PA_mrna; TRY69112.1; TCAL_13516.
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   3: Inferred from homology;
KW   Acetylation; Chromosome; DNA-binding; Isopeptide bond; Methylation;
KW   Nucleosome core; Nucleus; Phosphoprotein; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..124
FT                   /note="Histone H2A"
FT                   /id="PRO_0000055226"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         104
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        119
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   124 AA;  13363 MW;  725BA63C393155F6 CRC64;
     MSGRGKGGKV KGKAKSRSNR AGLQFPVGRI HRLLRKGNYA ERVGAGAPVY LAAVMEYLAA
     EVLELAGNAA RDNKKTRIIP RHLQLAIRND EELNKLLSGV TIAQGGVLPN IQAVLLPKKT
     EKKA