P61836 (H3_ZYGBA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone H3

Gene names

Name:

HHT1

Organism

Zygosaccharomyces bailii

Taxonomic identifier

4954 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Zygosaccharomyces

Protein attributes

Sequence length	136 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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 structure	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 By similarity. Chromosome By similarity.
Post-translational modification	Phosphorylated to form H3S10ph. H3S10ph promotes subsequent H3K14ac formation and is required for transcriptional activation through TBP recruitment to the promoters By similarity. Mono-, di- and trimethylated by the COMPASS complex to form H3K4me1/2/3. H3K4me activates gene expression by regulating transcription elongation and plays a role in telomere length maintenance. H3K4me enrichment correlates with transcription levels, and occurs in a 5' to 3' gradient with H3K4me3 enrichment at the 5'-end of genes, shifting to H3K4me2 and then H3K4me1. Methylated by SET2 to form H3K36me. H3K36me represses gene expression. Methylated by DOT1 to form H3K79me. H3K79me is required for association of SIR proteins with telomeric regions and for telomeric silencing. The COMPASS-mediated formation of H3K4me2/3 and the DOT1-mediated formation of H3K79me require H2BK123ub1 By similarity. Acetylation of histone H3 leads to transcriptional activation. H3K14ac formation by GCN5 is promoted by H3S10ph. H3K14ac can also be formed by ESA1. H3K56ac formation occurs predominantly in newly synthesized H3 molecules during G1, S and G2/M of the cell cycle and may be involved in DNA repair By similarity.
Sequence similarities	Belongs to the histone H3 family.
Caution	To ensure consistency between histone entries, we follow the 'Brno' nomenclature for histone modifications, with positions refering 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: H3K4me1/2/3 = mono-, di- and trimethylated Lys-5; H3K9ac = acetylated Lys-10; H3K9me1 = monomethylated Lys-10; H3S10ph = phosphorylated Ser-11; H3K14ac = acetylated Lys-15; H3K14me2 = dimethylated Lys-15; H3K18ac = acetylated Lys-19; H3K18me1 = monomethylated Lys-19; H3K23ac = acetylated Lys-24; H3K23me1 = monomethylated Lys-24; H3K27ac = acetylated Lys-28; H3K27me1/2/3 = mono-, di- and trimethylated Lys-28; H3K36ac = acetylated Lys-37; H3K36me1/2/3 = mono-, di- and trimethylated Lys-37; H3K56ac = acetylated Lys-57; H3K64ac = acetylated Lys-65; H3K79me1/2/3 = mono-, di- and trimethylated Lys-80.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Chromosome Nucleosome core Nucleus
Ligand	DNA-binding
PTM	Acetylation Methylation Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW nucleosome assembly Inferred from electronic annotation. Source: InterPro
Cellular component	nucleosome Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 136	135	Histone H3		PRO_0000221371
Amino acid modifications
	Modified residue	5	1	N6,N6,N6-trimethyllysine; alternate By similarity
	Modified residue	5	1	N6,N6-dimethyllysine; alternate By similarity
	Modified residue	5	1	N6-methyllysine; alternate By similarity
	Modified residue	10	1	N6-acetyllysine; alternate By similarity
	Modified residue	10	1	N6-methyllysine; alternate By similarity
	Modified residue	11	1	Phosphoserine By similarity
	Modified residue	15	1	N6,N6-dimethyllysine; alternate By similarity
	Modified residue	15	1	N6-acetyllysine; alternate By similarity
	Modified residue	19	1	N6-acetyllysine; alternate By similarity
	Modified residue	19	1	N6-methyllysine; alternate By similarity
	Modified residue	24	1	N6-acetyllysine; alternate By similarity
	Modified residue	24	1	N6-methyllysine; alternate By similarity
	Modified residue	28	1	N6,N6,N6-trimethyllysine; alternate By similarity
	Modified residue	28	1	N6,N6-dimethyllysine; alternate By similarity
	Modified residue	28	1	N6-acetyllysine; alternate By similarity
	Modified residue	28	1	N6-methyllysine; alternate By similarity
	Modified residue	37	1	N6,N6,N6-trimethyllysine; alternate By similarity
	Modified residue	37	1	N6,N6-dimethyllysine; alternate By similarity
	Modified residue	37	1	N6-acetyllysine; alternate By similarity
	Modified residue	37	1	N6-methyllysine; alternate By similarity
	Modified residue	57	1	N6-acetyllysine By similarity
	Modified residue	65	1	N6-acetyllysine By similarity
	Modified residue	80	1	N6,N6,N6-trimethyllysine; alternate By similarity
	Modified residue	80	1	N6,N6-dimethyllysine; alternate By similarity
	Modified residue	80	1	N6-methyllysine; alternate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P61836 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: A6115FEB480AC67A	FASTA	136	15,356
	10 20 30 40 50 60 MARTKQTARK STGGKAPRKQ LASKAARKSA PSTGGVKKPH RYKPGTVALR EIRRFQKSTE 70 80 90 100 110 120 LLIRKLPFQR LVREIAQDFK TDLRFQSSAI GALQESVEAY LVSLFEDTNL AAIHAKRVTI 130 QKKDIKLARR LRGERS

References

[1]	"Targeted gene deletion in Zygosaccharomyces bailii." Mollapour M., Piper P.W. Yeast 18:173-186(2001) [PubMed: 11169759] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF296170 Genomic DNA. Translation: AAG30425.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2FUU	NMR	-	B	2-16	[»]

ProteinModelPortal

P61836.

SMR

P61836. Positions 2-136.

ModBase

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Protocols and materials databases

StructuralBiologyKnowledgebase

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Family and domain databases

InterPro

IPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR000164. Histone_H3.
[Graphical view]

Gene3D

G3DSA:1.10.20.10. Histone-fold. 1 hit.

PANTHER

PTHR11426. Histone_H3. 1 hit.

Pfam

PF00125. Histone. 1 hit.
[Graphical view]

PRINTS

PR00622. HISTONEH3.

SMART

SM00428. H3. 1 hit.
[Graphical view]

SUPFAM

SSF47113. Histone-fold. 1 hit.

PROSITE

PS00322. HISTONE_H3_1. 1 hit.
PS00959. HISTONE_H3_2. 1 hit.
[Graphical view]

ProtoNet

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Entry information

Entry name

H3_ZYGBA

Accession

Primary (citable) accession number: P61836

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2004
Last sequence update:	January 23, 2007
Last modified:	November 2, 2010
This is version 44 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program