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Histone H3.2

 H32_ENCAL               Reviewed;         136 AA.
P08903;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
10-MAY-2017, entry version 77.
RecName: Full=Histone H3.2;
Encephalartos altensteinii (Altenstein's bread tree) (Eastern Cape
giant cycad).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Cycadidae; Cycadales; Zamiaceae; Encephalartos.
NCBI_TaxID=3300;
[1]
PROTEIN SEQUENCE OF 2-136, AND METHYLATION AT LYS-5; LYS-10 AND
LYS-28.
TISSUE=Pollen;
Brandt W.F., von Holt C.;
"The primary structure of histone H3 from cycad pollen.";
FEBS Lett. 194:278-281(1986).
-!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and
compact DNA into chromatin, limiting DNA accessibility to the
cellular machineries which require DNA as a template. Histones
thereby play a central role in transcription regulation, DNA
repair, DNA replication and chromosomal stability. DNA
accessibility is regulated via a complex set of post-translational
modifications of histones, also called histone code, and
nucleosome remodeling.
-!- SUBUNIT: The nucleosome is a histone octamer containing two
molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4
heterotetramer and two H2A-H2B heterodimers. The octamer wraps
approximately 147 bp of DNA.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome
{ECO:0000250}.
-!- PTM: Acetylation is generally linked to gene activation. Can be
acetylated to form H3K9ac, H3K14ac, H3K18ac and H3K23ac. H3K9ac
could compete with H3K9me and prevent gene silencing. H3K9ac is
restricted to euchromatin (By similarity). {ECO:0000250}.
-!- PTM: Methylated to form mainly H3K4me, H3K9me, H3K18me, H3K23me,
H3K27me and H3K36me. H3K4me1/2/3, H3K9me3, H3K27me3 and
H3K36me1/2/3 are typical marks for euchromatin, whereas
heterochromatic chromocenters are enriched in H3K9me1/2 and
H3K27me1/2. H2BK143ub1 is probably prerequisite for H3K4me (By
similarity). {ECO:0000250}.
-!- PTM: Can be phosphorylated to form H3S10ph, H3T11ph and H3S28ph.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
-!- CAUTION: To ensure consistency between histone entries, we follow
the 'Brno' nomenclature for histone modifications, with positions
referring to those used in the literature for the 'closest' model
organism. Due to slight variations in histone sequences between
organisms and to the presence of initiator methionine in
UniProtKB/Swiss-Prot sequences, the actual positions of modified
amino acids in the sequence generally differ. In this entry the
following conventions are used: H3K4me = methylated Lys-5; H3K9ac
= acetylated Lys-10; H3K9me = methylated Lys-10; H3S10ph =
phosphorylated Ser-11; H3T11ph = phosphorylated Thr-12; H3K14ac =
acetylated Lys-15; H3K18ac = acetylated Lys-19; H3K18me =
methylated Lys-19; H3K23ac = acetylated Lys-24; H3K23me =
methylated Lys-24; H3K27me = methylated Lys-28; H3S28ph =
phosphorylated Ser-29; H3K36me = methylated Lys-37. {ECO:0000305}.
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PIR; A23604; HSEAH3.
ProteinModelPortal; P08903; -.
SMR; P08903; -.
GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
InterPro; IPR009072; Histone-fold.
InterPro; IPR007125; Histone_H2A/H2B/H3.
InterPro; IPR000164; Histone_H3/CENP-A.
PANTHER; PTHR11426; PTHR11426; 1.
Pfam; PF00125; Histone; 1.
PRINTS; PR00622; HISTONEH3.
SMART; SM00428; H3; 1.
SUPFAM; SSF47113; SSF47113; 1.
PROSITE; PS00322; HISTONE_H3_1; 1.
PROSITE; PS00959; HISTONE_H3_2; 1.
1: Evidence at protein level;
Acetylation; Chromosome; Direct protein sequencing; DNA-binding;
Methylation; Nucleosome core; Nucleus; Phosphoprotein.
INIT_MET 1 1 Removed. {ECO:0000269|Ref.1}.
CHAIN 2 136 Histone H3.2.
/FTId=PRO_0000221274.
MOD_RES 5 5 N6-methylated lysine.
{ECO:0000269|Ref.1}.
MOD_RES 10 10 N6-acetyllysine; alternate.
{ECO:0000250}.
MOD_RES 10 10 N6-methylated lysine; alternate.
{ECO:0000269|Ref.1}.
MOD_RES 11 11 Phosphoserine. {ECO:0000250}.
MOD_RES 12 12 Phosphothreonine. {ECO:0000250}.
MOD_RES 15 15 N6-acetyllysine. {ECO:0000250}.
MOD_RES 19 19 N6-acetyllysine; alternate.
{ECO:0000250}.
MOD_RES 19 19 N6-methylated lysine; alternate.
{ECO:0000250}.
MOD_RES 24 24 N6-acetyllysine; alternate.
{ECO:0000250}.
MOD_RES 24 24 N6-methylated lysine; alternate.
{ECO:0000250}.
MOD_RES 28 28 N6-methylated lysine.
{ECO:0000269|Ref.1}.
MOD_RES 29 29 Phosphoserine. {ECO:0000250}.
MOD_RES 37 37 N6-methylated lysine. {ECO:0000250}.
VARIANT 54 54 R -> K.
VARIANT 97 97 A -> S.
VARIANT 108 108 T -> S.
VARIANT 125 125 I -> V.
SEQUENCE 136 AA; 15296 MW; 68FB110D0E95DF26 CRC64;
MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RFRPGTVALR EIRRYQKSTE
LLIRKLPFQR LVREIAQDFK TDLRFQSSAV AALQEAAEAY LVGLFEDTNL CAIHAKRVTI
MPKDIQLARR IRGERA


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