H32_MAIZE
ID H32_MAIZE Reviewed; 136 AA.
AC P69246; P05203; P05329; P05330; Q53X03;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Histone H3.2;
GN Name=H3C2;
GN and
GN Name=H3C3;
GN and
GN Name=H3C4;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Chaubet N., Philipps G., Chaboute M.-E., Ehling M., Gigot C.;
RT "Nucleotide sequences of two corn histone H3 genes. Genomic organization of
RT the corn histone H3 and H4 genes.";
RL Plant Mol. Biol. 6:253-263(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Chaubet N., Chaboute M.-E., Philipps G., Gigot C.;
RT "Histone genes in higher plants: organization and expression.";
RL Dev. Genet. 8:461-473(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Gigot C., Chaubet N., Chaboute M.-E., Ehling M., Philipps G.;
RT "Nucleotide sequences of two histone H3 and H4 genes of corn. Further
RT insight into the structure and organization of the histone genes in higher
RT plants.";
RL Plant Physiol. Biochem. 25:235-247(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. B37N;
RA Tacchini P., Walbot W.;
RT "Nucleotide sequence of a new histone H3 gene in Zea mays.";
RL (er) Plant Gene Register PGR96-021(1996).
RN [5]
RP SUBCELLULAR LOCATION, AND METHYLATION AT LYS-5; LYS-10 AND LYS-28.
RX PubMed=16624902; DOI=10.1534/genetics.106.056853;
RA Shi J., Dawe R.K.;
RT "Partitioning of the maize epigenome by the number of methyl groups on
RT histone H3 lysines 9 and 27.";
RL Genetics 173:1571-1583(2006).
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 {ECO:0000269|PubMed:16624902}. Chromosome
CC {ECO:0000269|PubMed:16624902}.
CC -!- PTM: Acetylation is generally linked to gene activation. Can be
CC acetylated to form H3K9ac, H3K14ac, H3K18ac and H3K23ac. H3K9ac could
CC compete with H3K9me and prevent gene silencing. H3K9ac is restricted to
CC euchromatin (By similarity). {ECO:0000250}.
CC -!- PTM: Methylated to form mainly H3K4me, H3K9me, H3K18me, H3K23me,
CC H3K27me and H3K36me. H3K9 and H3K27 are predominantly under the form of
CC H3K9me1 and H3K27me1. H2BK143ub1 is probably prerequisite for H3K4me.
CC H3K4me2, H3K9me2 and H3K9me3 are restricted to euchromatin, including
CC centromeres. H3K27me2 is specifically enriched in heterochromatin,
CC including chromomeres, pericentromeres and knobs. H3K27me3 is limited
CC to several discrete euchromatic domains. H3K9me1 and H3K27me1 are
CC enriched in pericentromeric heterochromatin, but also found in
CC euchromatin between chromomeres. {ECO:0000269|PubMed:16624902}.
CC -!- PTM: Can be phosphorylated to form H3S10ph, H3T11ph and H3S28ph.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the histone H3 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: H3K4me1/2/3 =
CC mono-, di- and trimethylated Lys-5; H3K9ac = acetylated Lys-10;
CC H3K9me1/2/3 = mono-, di- and trimethylated Lys-10; H3S10ph =
CC phosphorylated Ser-11; H3T11ph = phosphorylated Thr-12; H3K14ac =
CC acetylated Lys-15; H3K18ac = acetylated Lys-19; H3K18me = methylated
CC Lys-19; H3K23ac = acetylated Lys-24; H3K23me = methylated Lys-24;
CC H3K27me1/2/3 = mono-, di- and trimethylated Lys-28; H3S28ph =
CC phosphorylated Ser-29; H3K36me = methylated Lys-37. {ECO:0000305}.
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DR EMBL; M13378; AAA33472.1; -; Genomic_DNA.
DR EMBL; M13379; AAA33473.1; -; Genomic_DNA.
DR EMBL; M35388; AAA66265.1; -; Genomic_DNA.
DR EMBL; M36658; AAA33471.1; -; Genomic_DNA.
DR EMBL; X84377; CAA59111.1; -; Genomic_DNA.
DR PIR; S57626; S57626.
DR RefSeq; NP_001131276.1; NM_001137804.1.
DR RefSeq; XP_008659267.1; XM_008661045.1.
DR RefSeq; XP_008663191.1; XM_008664969.1.
DR RefSeq; XP_008669428.1; XM_008671206.1.
DR RefSeq; XP_008678686.1; XM_008680464.1.
DR PDB; 7EF0; X-ray; 1.50 A; P=2-20.
DR PDB; 7EF1; X-ray; 1.90 A; P/Q=2-11.
DR PDB; 7EF2; X-ray; 2.00 A; P/Q=2-11.
DR PDB; 7EF3; X-ray; 2.10 A; P/Q=2-11.
DR PDBsum; 7EF0; -.
DR PDBsum; 7EF1; -.
DR PDBsum; 7EF2; -.
DR PDBsum; 7EF3; -.
DR AlphaFoldDB; P69246; -.
DR SMR; P69246; -.
DR STRING; 4577.GRMZM2G130079_P01; -.
DR iPTMnet; P69246; -.
DR PaxDb; P69246; -.
DR PRIDE; P69246; -.
DR EnsemblPlants; Zm00001eb083310_T001; Zm00001eb083310_P001; Zm00001eb083310.
DR EnsemblPlants; Zm00001eb083310_T002; Zm00001eb083310_P002; Zm00001eb083310.
DR EnsemblPlants; Zm00001eb083380_T001; Zm00001eb083380_P001; Zm00001eb083380.
DR EnsemblPlants; Zm00001eb123830_T001; Zm00001eb123830_P001; Zm00001eb123830.
DR EnsemblPlants; Zm00001eb137500_T001; Zm00001eb137500_P001; Zm00001eb137500.
DR EnsemblPlants; Zm00001eb181740_T001; Zm00001eb181740_P001; Zm00001eb181740.
DR EnsemblPlants; Zm00001eb271240_T001; Zm00001eb271240_P001; Zm00001eb271240.
DR EnsemblPlants; Zm00001eb376150_T001; Zm00001eb376150_P001; Zm00001eb376150.
DR EnsemblPlants; Zm00001eb422190_T001; Zm00001eb422190_P001; Zm00001eb422190.
DR EnsemblPlants; Zm00001eb422440_T001; Zm00001eb422440_P001; Zm00001eb422440.
DR GeneID; 100192589; -.
DR GeneID; 103638044; -.
DR GeneID; 103641629; -.
DR GeneID; 103646477; -.
DR GeneID; 103653610; -.
DR Gramene; Zm00001eb083310_T001; Zm00001eb083310_P001; Zm00001eb083310.
DR Gramene; Zm00001eb083310_T002; Zm00001eb083310_P002; Zm00001eb083310.
DR Gramene; Zm00001eb083380_T001; Zm00001eb083380_P001; Zm00001eb083380.
DR Gramene; Zm00001eb123830_T001; Zm00001eb123830_P001; Zm00001eb123830.
DR Gramene; Zm00001eb137500_T001; Zm00001eb137500_P001; Zm00001eb137500.
DR Gramene; Zm00001eb181740_T001; Zm00001eb181740_P001; Zm00001eb181740.
DR Gramene; Zm00001eb271240_T001; Zm00001eb271240_P001; Zm00001eb271240.
DR Gramene; Zm00001eb376150_T001; Zm00001eb376150_P001; Zm00001eb376150.
DR Gramene; Zm00001eb422190_T001; Zm00001eb422190_P001; Zm00001eb422190.
DR Gramene; Zm00001eb422440_T001; Zm00001eb422440_P001; Zm00001eb422440.
DR KEGG; zma:100192589; -.
DR KEGG; zma:103638044; -.
DR KEGG; zma:103641629; -.
DR KEGG; zma:103646477; -.
DR KEGG; zma:103653610; -.
DR MaizeGDB; 25143; -.
DR eggNOG; KOG1745; Eukaryota.
DR HOGENOM; CLU_078295_4_0_1; -.
DR OMA; MPRDINL; -.
DR OrthoDB; 1564596at2759; -.
DR Proteomes; UP000007305; Chromosome 10.
DR Proteomes; UP000007305; Chromosome 2.
DR Proteomes; UP000007305; Chromosome 3.
DR Proteomes; UP000007305; Chromosome 4.
DR Proteomes; UP000007305; Chromosome 6.
DR Proteomes; UP000007305; Chromosome 9.
DR ExpressionAtlas; P69246; baseline and differential.
DR Genevisible; P69246; ZM.
DR GO; GO:0010369; C:chromocenter; IEA:EnsemblPlants.
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 Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR InterPro; IPR000164; Histone_H3/CENP-A.
DR PANTHER; PTHR11426; PTHR11426; 1.
DR Pfam; PF00125; Histone; 1.
DR PRINTS; PR00622; HISTONEH3.
DR SMART; SM00428; H3; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR PROSITE; PS00322; HISTONE_H3_1; 1.
DR PROSITE; PS00959; HISTONE_H3_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chromosome; DNA-binding; Methylation;
KW Nucleosome core; Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..136
FT /note="Histone H3.2"
FT /id="PRO_0000221281"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 5
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 5
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:16624902"
FT MOD_RES 5
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 10
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 10
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:16624902"
FT MOD_RES 10
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 10
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 12
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 15
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 19
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 19
FT /note="N6-methylated lysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 24
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 24
FT /note="N6-methylated lysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 28
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:16624902"
FT MOD_RES 28
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:16624902"
FT MOD_RES 28
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 37
FT /note="N6-methylated lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 136 AA; 15268 MW; F1FB03A849777A61 CRC64;
MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RFRPGTVALR EIRKYQKSTE
LLIRKLPFQR LVREIAQDFK TDLRFQSSAV AALQEAAEAY LVGLFEDTNL CAIHAKRVTI
MPKDIQLARR IRGERA
