H2A_EUPES
ID H2A_EUPES Reviewed; 153 AA.
AC Q9M531;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Histone H2A;
OS Euphorbia esula (Leafy spurge).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Euphorbioideae; Euphorbieae;
OC Euphorbia; Euphorbia subgen. Esula; Euphorbia sect. Esula.
OX NCBI_TaxID=3993;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Anderson J.V., Horvath D.P.;
RT "Identification of mRNAs expressed in underground adventitious buds of
RT Euphorbia esula (leafy spurge).";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
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 -!- DOMAIN: Contains one SPKK motif which may interact with the minor
CC groove of A/T-rich DNA sites. Phosphorylation of this motif may
CC regulate DNA binding. This motif is reiterated in both termini of
CC histone H1 and in the N-terminus of sea urchin histones H2B, but its
CC presence in the C-terminus seems to be unique to plant H2A.
CC -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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DR EMBL; AF242311; AAF65769.1; -; mRNA.
DR AlphaFoldDB; Q9M531; -.
DR SMR; Q9M531; -.
DR PRIDE; Q9M531; -.
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 2: Evidence at transcript level;
KW Chromosome; DNA-binding; Nucleosome core; Nucleus.
FT CHAIN 1..153
FT /note="Histone H2A"
FT /id="PRO_0000055229"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 149..152
FT /note="SPKK motif"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 153 AA; 16058 MW; DA1A9DF4B0806653 CRC64;
MDTGAKLKKG AGERKGGGPK KKPVSRSVKA GLQFPVGRIG RFLKKGRYAQ RVGSGAPVYL
AAVLEYLAAE VLELAGNAAR DNKKNRIIPR HVLLAVRNDE ELGKLLAGVT IAHGGVLPNI
NPVLLPKKAE KAAAAATKEP KSPAKATKSP KKA