H2A2_WHEAT
ID H2A2_WHEAT Reviewed; 151 AA.
AC P02276;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Histone H2A.2.1;
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP PROTEIN SEQUENCE, AND ACETYLATION AT MET-1.
RC TISSUE=Germ;
RX PubMed=3371346; DOI=10.1111/j.1432-1033.1988.tb14035.x;
RA Rodrigues J.A., Brandt W.F., von Holt C.;
RT "The primary structure of the histone H2A(2) type from wheat germ. A core
RT histone type with both, N-terminal and C-terminal extensions.";
RL Eur. J. Biochem. 173:555-560(1988).
RN [2]
RP PROTEIN SEQUENCE OF 1-37.
RC TISSUE=Germ;
RX PubMed=454665; DOI=10.1016/0005-2795(79)90127-2;
RA Rodrigues J.A., Brandt W.F., von Holt C.;
RT "Plant histone 2 from wheat germ, a family of histone H2a variants. Partial
RT amino acid sequences.";
RL Biochim. Biophys. Acta 578:196-206(1979).
RN [3]
RP PHOSPHORYLATION.
RX PubMed=16667585; DOI=10.1104/pp.93.3.1241;
RA Green G.R., Gustavsen L.C., Poccia D.L.;
RT "Phosphorylation of plant H2A histones.";
RL Plant Physiol. 93:1241-1245(1990).
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 2 SPKK motifs which may interact with the minor groove
CC of A/T-rich DNA sites. Phosphorylation of this motif may regulate DNA
CC binding. This motif is reiterated in both termini of histone H1 and in
CC the N-terminus of sea urchin histones H2B, but its presence in the C-
CC terminus seems to be unique to plant H2A.
CC -!- PTM: Phosphorylated within its C-terminal part, probably at the SPKK
CC motifs. {ECO:0000269|PubMed:16667585}.
CC -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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DR PIR; S00623; HSWT2A.
DR AlphaFoldDB; P02276; -.
DR SMR; P02276; -.
DR STRING; 4565.Traes_1AS_E774FAB9E.1; -.
DR iPTMnet; P02276; -.
DR PRIDE; P02276; -.
DR eggNOG; KOG1756; Eukaryota.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; P02276; baseline and differential.
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; IBA:GO_Central.
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 Nucleosome core; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..151
FT /note="Histone H2A.2.1"
FT /id="PRO_0000055292"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 140..143
FT /note="SPKK motif 1"
FT MOTIF 147..150
FT /note="SPKK motif 2"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:3371346"
SQ SEQUENCE 151 AA; 16013 MW; 968D4929D1C7669B CRC64;
MDGSKAKKVA AKKFGGPRKK SVTKSIKAGL QFPVGRIGRY LKKGRYAQRV GSGAPVYLAA
VLEYLAAEVL ELAGNAAKDN KKTRIVPRHL LLAIRNDQEL GRLLSGVTIA HGGVIPNINP
VLLPKKAAEK AEKAGAAPKS PKKTTKSPKK A
