H32_TOBAC
ID H32_TOBAC Reviewed; 136 AA.
AC Q76MV0;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Histone H3.2;
GN Name=B34;
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Samsun;
RA Kyo M.;
RT "Cloning of cDNAs associated with embryogenic dedifferentiation of immature
RT pollen grains in Nicotiana tabacum.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP METHYLATION AT LYS-5 AND LYS-10, ACETYLATION, AND PHOSPHORYLATION AT
RP SER-11.
RX PubMed=15659094; DOI=10.1111/j.1365-313x.2004.02301.x;
RA Li Y., Butenko Y., Grafi G.;
RT "Histone deacetylation is required for progression through mitosis in
RT tobacco cells.";
RL Plant J. 41:346-352(2005).
RN [3]
RP PHOSPHORYLATION AT THR-4; THR-12 AND SER-29.
RX PubMed=17087760; DOI=10.1111/j.1365-313x.2006.02893.x;
RA Kurihara D., Matsunaga S., Kawabe A., Fujimoto S., Noda M., Uchiyama S.,
RA Fukui K.;
RT "Aurora kinase is required for chromosome segregation in tobacco BY-2
RT cells.";
RL Plant J. 48:572-580(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. Chromosome.
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). H3K9ac and H3K14ac are associated with
CC chromatin during interphase. Deacetylation at the metaphase-anaphase
CC transition and maintained up to telophase. {ECO:0000250,
CC ECO:0000269|PubMed:15659094}.
CC -!- PTM: Methylated to form mainly H3K4me, H3K9me, H3K18me, H3K23me,
CC H3K27me and H3K36me. H3K4me1/2/3, H3K9me3, H3K27me3 and H3K36me1/2/3
CC are typical marks for euchromatin, whereas heterochromatic
CC chromocenters are enriched in H3K9me1/2 and H3K27me1/2. H2BK143ub1 is
CC probably prerequisite for H3K4me (By similarity). H3K4me2 and H3K9me2
CC remain associated with chromosomes during interphase and mitosis.
CC Methylated in vitro by SET1 to form H3K9me and H3K27me. {ECO:0000250,
CC ECO:0000269|PubMed:15659094}.
CC -!- PTM: Phosphorylated to form H3T3ph, H3S10ph, H3T11ph and H3S28ph.
CC H3S10ph and H3S28ph found from prophase to telophase. Restricted to
CC chromocenters from prophase to early anaphase, but widespread along
CC chromosomes at late stages of mitosis, when H3 is deacetylated. No
CC phosphorylation detected during interphase. H3S28ph specifically formed
CC by AUR3 while H3T3ph and H3T11ph are not produced by Aurora.
CC {ECO:0000269|PubMed:15659094, ECO:0000269|PubMed:17087760}.
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: H3T3ph =
CC phosphorylated Thr-4; H3K4me1/2/3 = mono-, di- and trimethylated Lys-5;
CC H3K9ac = acetylated Lys-10; H3K9me1/2/3 = mono-, di- and trimethylated
CC Lys-10; H3S10ph = phosphorylated Ser-11; H3T11ph = phosphorylated Thr-
CC 12; H3K14ac = acetylated Lys-15; H3K18ac = acetylated Lys-19; H3K18me =
CC methylated Lys-19; H3K23ac = acetylated Lys-24; H3K23me = methylated
CC Lys-24; H3K27me = methylated Lys-28; H3S28ph = phosphorylated Ser-29;
CC H3K36me = methylated Lys-37. {ECO:0000305}.
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DR EMBL; AB032544; BAC53942.1; -; mRNA.
DR RefSeq; XP_016432553.1; XM_016577067.1.
DR RefSeq; XP_016432905.1; XM_016577419.1.
DR RefSeq; XP_016437038.1; XM_016581552.1.
DR RefSeq; XP_016438522.1; XM_016583036.1.
DR RefSeq; XP_016444277.1; XM_016588791.1.
DR RefSeq; XP_016472604.1; XM_016617118.1.
DR RefSeq; XP_016476898.1; XM_016621412.1.
DR RefSeq; XP_016497344.1; XM_016641858.1.
DR RefSeq; XP_016497746.1; XM_016642260.1.
DR RefSeq; XP_016498067.1; XM_016642581.1.
DR RefSeq; XP_016498068.1; XM_016642582.1.
DR RefSeq; XP_016500339.1; XM_016644853.1.
DR RefSeq; XP_016502252.1; XM_016646766.1.
DR RefSeq; XP_016506905.1; XM_016651419.1.
DR RefSeq; XP_016514570.1; XM_016659084.1.
DR AlphaFoldDB; Q76MV0; -.
DR SMR; Q76MV0; -.
DR STRING; 4097.Q76MV0; -.
DR iPTMnet; Q76MV0; -.
DR GeneID; 107759185; -.
DR GeneID; 107759464; -.
DR GeneID; 107763111; -.
DR GeneID; 107764469; -.
DR GeneID; 107769564; -.
DR GeneID; 107794615; -.
DR GeneID; 107798424; -.
DR GeneID; 107816172; -.
DR GeneID; 107816533; -.
DR GeneID; 107816835; -.
DR GeneID; 107816836; -.
DR GeneID; 107818805; -.
DR GeneID; 107820477; -.
DR GeneID; 107824614; -.
DR GeneID; 107831322; -.
DR KEGG; nta:107759185; -.
DR KEGG; nta:107759464; -.
DR KEGG; nta:107763111; -.
DR KEGG; nta:107764469; -.
DR KEGG; nta:107769564; -.
DR KEGG; nta:107794615; -.
DR KEGG; nta:107798424; -.
DR KEGG; nta:107816172; -.
DR KEGG; nta:107816533; -.
DR KEGG; nta:107816835; -.
DR KEGG; nta:107816836; -.
DR KEGG; nta:107818805; -.
DR KEGG; nta:107820477; -.
DR KEGG; nta:107824614; -.
DR KEGG; nta:107831322; -.
DR OrthoDB; 1564596at2759; -.
DR PhylomeDB; Q76MV0; -.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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 Acetylation; Chromosome; DNA-binding; Methylation; Nucleosome core;
KW 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_0000280821"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 4
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17087760"
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:15659094"
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:15659094"
FT MOD_RES 10
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P59226"
FT MOD_RES 10
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15659094"
FT MOD_RES 12
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17087760"
FT MOD_RES 15
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P59226"
FT MOD_RES 19
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P59226"
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|UniProtKB:P59226"
FT MOD_RES 24
FT /note="N6-methylated lysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 28
FT /note="N6-methylated lysine"
FT /evidence="ECO:0000250"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17087760"
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
