UniProt functional annotation for P59226



	UniProt functional annotation for P59226

UniProt code: P59226.

Organism: Arabidopsis thaliana (Mouse-ear cress).

Taxonomy: Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.

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. The H3K9meK27me dimethylated N-terminal tail of histone H3 can directly interact with the chromodomains of CMT3 and/or LHP1. Interacts with ORTH2. Interacts (via N-terminus) with ATXR5 and ATXR6 (via PHD domain). {ECO:0000269|PubMed:11898023, ECO:0000269|PubMed:15457214, ECO:0000269|PubMed:17242155, ECO:0000269|PubMed:20631708}.

Subcellular location: Nucleus {ECO:0000269|PubMed:17439305, ECO:0000269|PubMed:25086063}. Chromosome {ECO:0000269|PubMed:17439305, ECO:0000269|PubMed:25086063}. Note=Localized at chromocenters. {ECO:0000269|PubMed:25086063}.

Tissue specificity: Expressed in inflorescences, buds and seedlings. {ECO:0000269|PubMed:16262706}.

Developmental stage: Expressed during the S phase. {ECO:0000269|PubMed:15010610}.

Ptm: Can be acetylated to form H3K9ac, H3K14ac, H3K18ac and H3K23ac. H3K9ac could compete with H3K9me and prevent gene silencing. H3K9acK14ac molecules are 30-fold less abundant than H3K9ac or H3K14ac. Very low level of H3K9meK14ac. H3K14 is specifically acetylated by HAG1 and deacetylated by HDA6. H3K9ac is deacetylated by HDT1. H3K9ac is restricted to euchromatin. H3K18ac, but not H3K9ac, is cell-cycle dependent and linked to replication. Reduced H4R3me2s increases H3K14ac in the FLC chromatin and activates or maintains its transcription. Vernalization decreases H3K9/14ac in the promoter region of FLC. {ECO:0000269|PubMed:12581305, ECO:0000269|PubMed:15598823, ECO:0000269|PubMed:16648464, ECO:0000269|PubMed:17174094, ECO:0000269|PubMed:17363895}.

Ptm: Mono-, di- or trimethylated to form mainly H3K4me1/2/3, H3K9me1/2/3, H3K27me1/2/3 and H3K36me1/2/3. Very low monomethylation at H3K18me1 or H3K23me1. 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. H3K27me3 is largely restricted to the transcribed regions of single genes and not associated with low-nucleosome density regions. SUVR1 to SUVR5, ASHH1 to ASHH3, ASHR1 to ASHR3, and ATXR5 and ATXR6 methylate H3, with ASHH2 methylating specifically H3K4 and H3K36 and ATXR5 and ATXR6 monomethylating specifically H3K27me1. The Su(var)3-9 homolog proteins (SUVH1 to SUVH10) are H3K9-specific methyltransferases. Among them, KRYPTONITE (SUVH4) is only involved in di- or trimethylation. Regarding H3K9, the major forms are H3K9me1 (20%) and H3K9me2 (10%), while H3K9me3 is rare (0.2%). H3K9me is controlled by DNA methylation and is not required for the formation of constitutive heterochromatin, but double methylation H3K9meK27me is required for the recruitment of CMT3 to methylate heterochromatin and silence euchromatic loci. Very low level of H3K9meK14ac. 60% of H3K27 is found under the form of H3K27me1, 16% of H3K27me2 and 5% of H3K27me3. When associated with H3K27me, H3K36 can only be mono- or di-methylated. H327me2K36me1 or H3K27me1K36me2 are both found in 3% of the proteins. When not associated with H3K27me, H3K36 is only trimethylated. H3K36me3 is found in 3% of the proteins. H2BK143ub1 is probably prerequisite for H3K4me. Elevated H3K4me3 and H3K36me2 formed by ASHH2 are required for high FLC expression. Vernalization increases H3K9me2 and H3K27me2/3 and decreases H3K4me2 at the FLC locus, resulting in the epigenetic silencing of this floral repressor. {ECO:0000269|PubMed:12456661, ECO:0000269|PubMed:12581305, ECO:0000269|PubMed:14712277, ECO:0000269|PubMed:15014946, ECO:0000269|PubMed:15598823, ECO:0000269|PubMed:16258034, ECO:0000269|PubMed:16299497, ECO:0000269|PubMed:17174094, ECO:0000269|PubMed:17439305, ECO:0000269|PubMed:19503079, ECO:0000269|PubMed:24626927}.

Ptm: In meta- and anaphase, H3T11ph is found on the entire length of the condensed chromosomes, whereas H3S10ph and H3S28ph are confined to the pericentromeric regions. During the first meiotic division, H3S10ph and H3S28ph are found on the entire length of the chromosome. Both sites may be involved in sister chromatid cohesion. No phosphorylation detected during interphase. AUR1 and AUR2 phosphorylate only H3S10, while AUR3 phosphorylates both H3S10 and H3S28. {ECO:0000269|PubMed:14610360, ECO:0000269|PubMed:15753571}.

Similarity: Belongs to the histone H3 family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Arabidopsis thaliana (Mouse-ear cress).
Taxonomy:		Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.



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. The H3K9meK27me dimethylated N-terminal tail of histone H3 can directly interact with the chromodomains of CMT3 and/or LHP1. Interacts with ORTH2. Interacts (via N-terminus) with ATXR5 and ATXR6 (via PHD domain). {ECO:0000269\|PubMed:11898023, ECO:0000269\|PubMed:15457214, ECO:0000269\|PubMed:17242155, ECO:0000269\|PubMed:20631708}.
Subcellular location:		Nucleus {ECO:0000269\|PubMed:17439305, ECO:0000269\|PubMed:25086063}. Chromosome {ECO:0000269\|PubMed:17439305, ECO:0000269\|PubMed:25086063}. Note=Localized at chromocenters. {ECO:0000269\|PubMed:25086063}.
Tissue specificity:		Expressed in inflorescences, buds and seedlings. {ECO:0000269\|PubMed:16262706}.
Developmental stage:		Expressed during the S phase. {ECO:0000269\|PubMed:15010610}.
Ptm:		Can be acetylated to form H3K9ac, H3K14ac, H3K18ac and H3K23ac. H3K9ac could compete with H3K9me and prevent gene silencing. H3K9acK14ac molecules are 30-fold less abundant than H3K9ac or H3K14ac. Very low level of H3K9meK14ac. H3K14 is specifically acetylated by HAG1 and deacetylated by HDA6. H3K9ac is deacetylated by HDT1. H3K9ac is restricted to euchromatin. H3K18ac, but not H3K9ac, is cell-cycle dependent and linked to replication. Reduced H4R3me2s increases H3K14ac in the FLC chromatin and activates or maintains its transcription. Vernalization decreases H3K9/14ac in the promoter region of FLC. {ECO:0000269\|PubMed:12581305, ECO:0000269\|PubMed:15598823, ECO:0000269\|PubMed:16648464, ECO:0000269\|PubMed:17174094, ECO:0000269\|PubMed:17363895}.
Ptm:		Mono-, di- or trimethylated to form mainly H3K4me1/2/3, H3K9me1/2/3, H3K27me1/2/3 and H3K36me1/2/3. Very low monomethylation at H3K18me1 or H3K23me1. 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. H3K27me3 is largely restricted to the transcribed regions of single genes and not associated with low-nucleosome density regions. SUVR1 to SUVR5, ASHH1 to ASHH3, ASHR1 to ASHR3, and ATXR5 and ATXR6 methylate H3, with ASHH2 methylating specifically H3K4 and H3K36 and ATXR5 and ATXR6 monomethylating specifically H3K27me1. The Su(var)3-9 homolog proteins (SUVH1 to SUVH10) are H3K9-specific methyltransferases. Among them, KRYPTONITE (SUVH4) is only involved in di- or trimethylation. Regarding H3K9, the major forms are H3K9me1 (20%) and H3K9me2 (10%), while H3K9me3 is rare (0.2%). H3K9me is controlled by DNA methylation and is not required for the formation of constitutive heterochromatin, but double methylation H3K9meK27me is required for the recruitment of CMT3 to methylate heterochromatin and silence euchromatic loci. Very low level of H3K9meK14ac. 60% of H3K27 is found under the form of H3K27me1, 16% of H3K27me2 and 5% of H3K27me3. When associated with H3K27me, H3K36 can only be mono- or di-methylated. H327me2K36me1 or H3K27me1K36me2 are both found in 3% of the proteins. When not associated with H3K27me, H3K36 is only trimethylated. H3K36me3 is found in 3% of the proteins. H2BK143ub1 is probably prerequisite for H3K4me. Elevated H3K4me3 and H3K36me2 formed by ASHH2 are required for high FLC expression. Vernalization increases H3K9me2 and H3K27me2/3 and decreases H3K4me2 at the FLC locus, resulting in the epigenetic silencing of this floral repressor. {ECO:0000269\|PubMed:12456661, ECO:0000269\|PubMed:12581305, ECO:0000269\|PubMed:14712277, ECO:0000269\|PubMed:15014946, ECO:0000269\|PubMed:15598823, ECO:0000269\|PubMed:16258034, ECO:0000269\|PubMed:16299497, ECO:0000269\|PubMed:17174094, ECO:0000269\|PubMed:17439305, ECO:0000269\|PubMed:19503079, ECO:0000269\|PubMed:24626927}.
Ptm:		In meta- and anaphase, H3T11ph is found on the entire length of the condensed chromosomes, whereas H3S10ph and H3S28ph are confined to the pericentromeric regions. During the first meiotic division, H3S10ph and H3S28ph are found on the entire length of the chromosome. Both sites may be involved in sister chromatid cohesion. No phosphorylation detected during interphase. AUR1 and AUR2 phosphorylate only H3S10, while AUR3 phosphorylates both H3S10 and H3S28. {ECO:0000269\|PubMed:14610360, ECO:0000269\|PubMed:15753571}.
Similarity:		Belongs to the histone H3 family. {ECO:0000305}.