H32_MEDSA
ID H32_MEDSA Reviewed; 136 AA.
AC P68429; P02300;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Histone H3.2;
DE AltName: Full=Histone H3.1;
DE AltName: Full=Major histone H3;
GN Name=H3-1.1; Synonyms=ALH3-1.1;
GN and
GN Name=H3.1;
OS Medicago sativa (Alfalfa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3879;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=cv. Nagyszenasi, and cv. Regen S;
RX PubMed=2471147; DOI=10.1093/nar/17.8.3057;
RA Wu S.C., Gyoergyey J., Dudits D.;
RT "Polyadenylated H3 histone transcripts and H3 histone variants in
RT alfalfa.";
RL Nucleic Acids Res. 17:3057-3063(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Chief;
RA Robertson A.J.;
RT "Histone H3 genes in alfalfa.";
RL Thesis (1994), University of Missouri / Kansas City, United States.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Chief, and cv. Nagyszenasi;
RX AGRICOLA=IND92000009; DOI=10.1007/BF00017464;
RA Wu S.C., Boegre L., Vincze E., Kiss G.B., Dudits D.;
RT "Isolation of an alfalfa histone H3 gene: structure and expression.";
RL Plant Mol. Biol. 11:641-649(1988).
RN [4]
RP ACETYLATION.
RX PubMed=3606121; DOI=10.1016/0003-9861(87)90435-8;
RA Waterborg J.H., Winicov I., Harrington R.E.;
RT "Histone variants and acetylated species from the alfalfa plant Medicago
RT sativa.";
RL Arch. Biochem. Biophys. 256:167-178(1987).
RN [5]
RP ACETYLATION, AND LACK OF PHOSPHORYLATION.
RX PubMed=16666742; DOI=10.1104/pp.90.1.237;
RA Waterborg J.H., Harrington R.E., Winicov I.;
RT "Differential histone acetylation in alfalfa (Medicago sativa) due to
RT growth in NaCl: responses in salt stressed and salt tolerant callus
RT cultures.";
RL Plant Physiol. 90:237-245(1989).
RN [6]
RP PROTEIN SEQUENCE OF 2-45 AND 85-116, ACETYLATION AT LYS-15; LYS-19 AND
RP LYS-24, LACK OF ACETYLATION AT LYS-37 AND LYS-38, METHYLATION AT LYS-5;
RP LYS-10; LYS-15; LYS-19 AND LYS-28, AND LACK OF METHYLATION AT LYS-37 AND
RP LYS-38.
RC STRAIN=cv. R4;
RX PubMed=2211618; DOI=10.1016/s0021-9258(17)44882-4;
RA Waterborg J.H.;
RT "Sequence analysis of acetylation and methylation in two histone H3
RT variants of alfalfa.";
RL J. Biol. Chem. 265:17157-17161(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 -!- PTM: Acetylation is generally linked to gene activation. H3K14 is only
CC found as H3K14ac (20%) or H3K14me3 (14%) and H3K18 is only found as
CC H3K18ac (13%) or H3K18me3 (16%). When modified, H3K23 is exclusively
CC under the form of H3K23ac (5%). Pre-existing H3K9me or H3K27me limit
CC the possibility for histone acetylation. H3.1 shows a much lower level
CC of steady-state acetylation than H3.2. Increased multiacetylation after
CC exposure to NaCl. H3K9ac is restricted to euchromatin (By similarity).
CC {ECO:0000250}.
CC -!- PTM: 4% of H3K4 is found under the form of H3K4me1, 4% of H3K4me2 and
CC 16% of H3K4me3. H3K9 is found as H3K9me1 (73%) or H3K9me2 (15%) with no
CC detectable H3K9me3. H3K14 is only found as H3K14me3 (14%) or H3K14ac
CC (20%) and H3K18 is only found as H3K18me3 (16%) or H3K18ac (13%). 31%
CC of H3K27 is found under the form of H3K27me1, 22% of H3K27me2 and 42%
CC of H3K27me3. H3K4me1/2/3, H3K27me3 and H3K36me1/2/3 are typical marks
CC for euchromatin, whereas heterochromatic chromocenters are enriched in
CC H3K9me1/2 and H3K27me1/2. H2BK143ub1 is probably prerequisite for
CC H3K4me (By similarity). {ECO:0000250}.
CC -!- PTM: Can be phosphorylated to form H3S10ph, H3T11ph and H3S28ph (By
CC similarity). No phosphorylation detected during salt stress.
CC {ECO:0000250}.
CC -!- PTM: No modifications detected on H3K36 and H3K37.
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; H3K14me3 = trimethylated Lys-15; H3K18ac =
CC acetylated Lys-19; H3K18me3 = trimethylated Lys-19; H3K23ac =
CC acetylated Lys-24; H3K27me1/2/3 = mono-, di- and trimethylated Lys-28;
CC H3S28ph = phosphorylated Ser-29; H3K36 = Lys-37; H3K37 = Lys-38.
CC {ECO:0000305}.
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DR EMBL; X13673; CAA31964.1; -; Genomic_DNA.
DR EMBL; X13674; CAA31965.1; -; mRNA.
DR EMBL; X13675; CAA31966.1; -; mRNA.
DR EMBL; X13677; CAA31968.1; -; mRNA.
DR EMBL; U09459; AAB49545.1; -; Unassigned_DNA.
DR EMBL; M35867; AAA32655.1; -; Genomic_DNA.
DR PIR; A38309; A38309.
DR PIR; S04520; S04520.
DR AlphaFoldDB; P68429; -.
DR SMR; P68429; -.
DR iPTMnet; P68429; -.
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 Acetylation; Chromosome; Direct protein sequencing; DNA-binding;
KW Methylation; Nucleosome core; Nucleus; Phosphoprotein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2211618"
FT CHAIN 2..136
FT /note="Histone H3.2"
FT /id="PRO_0000221284"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 37
FT /note="Not N6-acetylated"
FT /evidence="ECO:0000269|PubMed:2211618"
FT SITE 37
FT /note="Not N6-methylated"
FT /evidence="ECO:0000269|PubMed:2211618"
FT SITE 38
FT /note="Not N6-acetylated"
FT /evidence="ECO:0000269|PubMed:2211618"
FT SITE 38
FT /note="Not N6-methylated"
FT /evidence="ECO:0000269|PubMed:2211618"
FT MOD_RES 5
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:2211618"
FT MOD_RES 5
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:2211618"
FT MOD_RES 5
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:2211618"
FT MOD_RES 10
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:2211618"
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:0000269|PubMed:2211618"
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,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:2211618"
FT MOD_RES 15
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:2211618"
FT MOD_RES 19
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:2211618"
FT MOD_RES 19
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:2211618"
FT MOD_RES 24
FT /note="N6-acetyllysine; partial"
FT /evidence="ECO:0000269|PubMed:2211618"
FT MOD_RES 28
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:2211618"
FT MOD_RES 28
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:2211618"
FT MOD_RES 28
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:2211618"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT CONFLICT 89
FT /note="A -> V (in Ref. 3; AAA32655)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 136 AA; 15284 MW; BE1B03A84960CCBA CRC64;
MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RFRPGTVALR EIRKYQKSTE
LLIRKLPFQR LVREIAQDFK TDLRFQSSAV SALQEAAEAY LVGLFEDTNL CAIHAKRVTI
MPKDIQLARR IRGERA
