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Protein

Histone H3.1/H3.2

Gene

hht1

more
Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

GO - Biological processi

  • cellular response to DNA damage stimulus Source: PomBase
  • chromatin assembly or disassembly Source: PomBase
  • nucleosome assembly Source: PomBase
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H3.1/H3.2
Gene namesi
Name:hht1
ORF Names:SPAC1834.04
AND
Name:hht2
ORF Names:pi060, SPBC8D2.04
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componentsi: Chromosome I, Chromosome II

Organism-specific databases

PomBaseiSPAC1834.04. hht1.
SPBC8D2.04. hht2.

Subcellular locationi

GO - Cellular componenti

  • mating-type region heterochromatin Source: PomBase
  • nuclear nucleosome Source: PomBase
  • nuclear pericentric heterochromatin Source: PomBase
  • nuclear subtelomeric heterochromatin Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 136135Histone H3.1/H3.2PRO_0000221366Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei5 – 51N6,N6,N6-trimethyllysine; alternateBy similarity
Modified residuei5 – 51N6,N6-dimethyllysine; alternateBy similarity
Modified residuei5 – 51N6-methyllysine; alternateBy similarity
Modified residuei10 – 101N6-acetyllysine; alternateBy similarity
Modified residuei10 – 101N6-methyllysine; alternate1 Publication
Modified residuei11 – 111PhosphoserineBy similarity
Modified residuei15 – 151N6,N6-dimethyllysine; alternateBy similarity
Modified residuei15 – 151N6-acetyllysine; alternateBy similarity
Modified residuei19 – 191N6-acetyllysine; alternateBy similarity
Modified residuei19 – 191N6-methyllysine; alternateBy similarity
Modified residuei24 – 241N6-acetyllysine; alternateBy similarity
Modified residuei24 – 241N6-methyllysine; alternateBy similarity
Modified residuei28 – 281N6,N6,N6-trimethyllysine; alternateBy similarity
Modified residuei28 – 281N6,N6-dimethyllysine; alternateBy similarity
Modified residuei28 – 281N6-acetyllysine; alternateBy similarity
Modified residuei28 – 281N6-methyllysine; alternateBy similarity
Modified residuei37 – 371N6,N6,N6-trimethyllysine; alternateBy similarity
Modified residuei37 – 371N6,N6-dimethyllysine; alternate1 Publication
Modified residuei37 – 371N6-acetyllysine; alternateBy similarity
Modified residuei37 – 371N6-methyllysine; alternateBy similarity
Modified residuei57 – 571N6-acetyllysineBy similarity
Modified residuei65 – 651N6-acetyllysineBy similarity
Modified residuei80 – 801N6,N6,N6-trimethyllysine; alternateBy similarity
Modified residuei80 – 801N6,N6-dimethyllysine; alternateBy similarity
Modified residuei80 – 801N6-methyllysine; alternateBy similarity

Post-translational modificationi

Phosphorylated by ark1 to form H3S10ph in a cell cycle-dependent manner during mitosis and meiosis. H3S10ph is also formed by ssp2, promotes subsequent H3K14ac formation by gcn5, and is required for transcriptional activation through TBP recruitment to the promoters. Dephosphorylation is performed by sds21.
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 (By similarity). Methylated by clr4 to form H3K9me1. H3K9me1 represents a specific tag for epigenetic transcriptional repression by recruiting swi6/HP1 to methylated histones. Targeting to histone probably involves clr3 and rik1. Essential for silencing of centromeres and directional switching of the mating type. 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).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).By similarity

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

BioGridi276354. 29 interactions.
277734. 39 interactions.
278928. 38 interactions.
IntActiP09988. 1 interaction.
MINTiMINT-195397.

Structurei

Secondary structure

1
136
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 93Combined sources
Beta strandi128 – 1314Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DZEX-ray1.80X123-132[»]
3G7LX-ray2.20P2-17[»]
ProteinModelPortaliP09988.
SMRiP09988. Positions 2-136.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09988.

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H3 family.Curated

Phylogenomic databases

HOGENOMiHOG000155290.
InParanoidiP09988.
KOiK11253.
OMAiTEFANEM.
OrthoDBiEOG092C5B6S.
PhylomeDBiP09988.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007125. Histone_H2A/H2B/H3.
IPR000164. Histone_H3/CENP-A.
[Graphical view]
PANTHERiPTHR11426. PTHR11426. 1 hit.
PfamiPF00125. Histone. 1 hit.
[Graphical view]
PRINTSiPR00622. HISTONEH3.
SMARTiSM00428. H3. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS00322. HISTONE_H3_1. 1 hit.
PS00959. HISTONE_H3_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P09988-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARTKQTARK STGGKAPRKQ LASKAARKAA PATGGVKKPH RYRPGTVALR
60 70 80 90 100
EIRRYQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSSAI GALQEAVEAY
110 120 130
LVSLFEDTNL CAIHGKRVTI QPKDMQLARR LRGERS
Length:136
Mass (Da):15,357
Last modified:January 23, 2007 - v2
Checksum:i346976EDD06C2284
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05222 Genomic DNA. Translation: CAA28851.1.
X05223 Genomic DNA. Translation: CAA28852.1.
AB004538 Genomic DNA. Translation: BAA21441.1.
CU329670 Genomic DNA. Translation: CAB75772.1.
CU329671 Genomic DNA. Translation: CAA17819.1.
PIRiE27399. HSZP3.
RefSeqiNP_594683.1. NM_001020112.2.
NP_595567.1. NM_001021462.2.
NP_596467.1. NM_001022386.2.

Genome annotation databases

EnsemblFungiiSPAC1834.04.1; SPAC1834.04.1:pep; SPAC1834.04.
SPBC1105.11c.1; SPBC1105.11c.1:pep; SPBC1105.11c.
SPBC8D2.04.1; SPBC8D2.04.1:pep; SPBC8D2.04.
GeneIDi2539804.
2541220.
2542467.
KEGGispo:SPAC1834.04.
spo:SPBC1105.11c.
spo:SPBC8D2.04.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05222 Genomic DNA. Translation: CAA28851.1.
X05223 Genomic DNA. Translation: CAA28852.1.
AB004538 Genomic DNA. Translation: BAA21441.1.
CU329670 Genomic DNA. Translation: CAB75772.1.
CU329671 Genomic DNA. Translation: CAA17819.1.
PIRiE27399. HSZP3.
RefSeqiNP_594683.1. NM_001020112.2.
NP_595567.1. NM_001021462.2.
NP_596467.1. NM_001022386.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DZEX-ray1.80X123-132[»]
3G7LX-ray2.20P2-17[»]
ProteinModelPortaliP09988.
SMRiP09988. Positions 2-136.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276354. 29 interactions.
277734. 39 interactions.
278928. 38 interactions.
IntActiP09988. 1 interaction.
MINTiMINT-195397.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC1834.04.1; SPAC1834.04.1:pep; SPAC1834.04.
SPBC1105.11c.1; SPBC1105.11c.1:pep; SPBC1105.11c.
SPBC8D2.04.1; SPBC8D2.04.1:pep; SPBC8D2.04.
GeneIDi2539804.
2541220.
2542467.
KEGGispo:SPAC1834.04.
spo:SPBC1105.11c.
spo:SPBC8D2.04.

Organism-specific databases

PomBaseiSPAC1834.04. hht1.
SPBC8D2.04. hht2.

Phylogenomic databases

HOGENOMiHOG000155290.
InParanoidiP09988.
KOiK11253.
OMAiTEFANEM.
OrthoDBiEOG092C5B6S.
PhylomeDBiP09988.

Miscellaneous databases

EvolutionaryTraceiP09988.
PROiP09988.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007125. Histone_H2A/H2B/H3.
IPR000164. Histone_H3/CENP-A.
[Graphical view]
PANTHERiPTHR11426. PTHR11426. 1 hit.
PfamiPF00125. Histone. 1 hit.
[Graphical view]
PRINTSiPR00622. HISTONEH3.
SMARTiSM00428. H3. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS00322. HISTONE_H3_1. 1 hit.
PS00959. HISTONE_H3_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiH31_SCHPO
AccessioniPrimary (citable) accession number: P09988
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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: 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.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.