UniProtKB - P09988 (H31_SCHPO)
(max 400 entries)x
Your basket is currently empty. i
Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)
Protein
Histone H3.1/H3.2
Gene
hht1
moreOrganism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
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
- DNA binding Source: PomBase
- nucleosomal DNA binding Source: GO_Central
- protein heterodimerization activity Source: InterPro
GO - Biological processi
- cellular response to DNA damage stimulus Source: PomBase
- nucleosome assembly Source: GO_Central
- regulation of extent of heterochromatin assembly Source: PomBase
Keywordsi
Molecular function | DNA-binding |
Enzyme and pathway databases
Reactomei | R-SPO-2559580. Oxidative Stress Induced Senescence. R-SPO-427359. SIRT1 negatively regulates rRNA expression. R-SPO-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks. |
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 |
Organismi | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
Taxonomic identifieri | 284812 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › |
Proteomesi |
|
Organism-specific databases
PomBasei | SPAC1834.04. hht1. SPBC8D2.04. hht2. |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedBy similarity | |||
ChainiPRO_0000221366 | 2 – 136 | Histone H3.1/H3.2Add BLAST | 135 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 5 | N6,N6,N6-trimethyllysine; alternateBy similarity | 1 | |
Modified residuei | 5 | N6,N6-dimethyllysine; alternateBy similarity | 1 | |
Modified residuei | 5 | N6-methyllysine; alternateBy similarity | 1 | |
Modified residuei | 10 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 10 | N6-methyllysine; alternate1 Publication | 1 | |
Modified residuei | 11 | PhosphoserineBy similarity | 1 | |
Modified residuei | 15 | N6,N6-dimethyllysine; alternateBy similarity | 1 | |
Modified residuei | 15 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 19 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 19 | N6-methyllysine; alternateBy similarity | 1 | |
Modified residuei | 24 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 24 | N6-methyllysine; alternateBy similarity | 1 | |
Modified residuei | 28 | N6,N6,N6-trimethyllysine; alternateBy similarity | 1 | |
Modified residuei | 28 | N6,N6-dimethyllysine; alternateBy similarity | 1 | |
Modified residuei | 28 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 28 | N6-methyllysine; alternateBy similarity | 1 | |
Modified residuei | 37 | N6,N6,N6-trimethyllysine; alternateBy similarity | 1 | |
Modified residuei | 37 | N6,N6-dimethyllysine; alternate1 Publication | 1 | |
Modified residuei | 37 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 37 | N6-methyllysine; alternateBy similarity | 1 | |
Modified residuei | 57 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 65 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 80 | N6,N6,N6-trimethyllysine; alternateBy similarity | 1 | |
Modified residuei | 80 | N6,N6-dimethyllysine; alternateBy similarity | 1 | |
Modified residuei | 80 | N6-methyllysine; alternateBy similarity | 1 |
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, PhosphoproteinProteomic databases
MaxQBi | P09988. |
PaxDbi | P09988. |
PRIDEi | P09988. |
PTM databases
iPTMneti | P09988. |
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.
GO - Molecular functioni
- protein heterodimerization activity Source: InterPro
Protein-protein interaction databases
BioGridi | 276354. 34 interactors. 277734. 40 interactors. 278928. 42 interactors. |
IntActi | P09988. 3 interactors. |
MINTi | P09988. |
STRINGi | 4896.SPBC8D2.04.1. |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsFeature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Beta strandi | 7 – 9 | Combined sources | 3 | |
Beta strandi | 128 – 131 | Combined sources | 4 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2DZE | X-ray | 1.80 | X | 123-132 | [»] | |
3G7L | X-ray | 2.20 | P | 2-17 | [»] | |
ProteinModelPortali | P09988. | |||||
SMRi | P09988. | |||||
ModBasei | Search... | |||||
MobiDBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P09988. |
Family & Domainsi
Sequence similaritiesi
Belongs to the histone H3 family.Curated
Phylogenomic databases
HOGENOMi | HOG000155290. |
InParanoidi | P09988. |
KOi | K11253. |
OMAi | KRIEPEY. |
OrthoDBi | EOG092C5B6S. |
PhylomeDBi | P09988. |
Family and domain databases
Gene3Di | 1.10.20.10. 1 hit. |
InterProi | View protein in InterPro IPR009072. Histone-fold. IPR007125. Histone_H2A/H2B/H3. IPR000164. Histone_H3/CENP-A. |
PANTHERi | PTHR11426. PTHR11426. 1 hit. |
Pfami | View protein in Pfam PF00125. Histone. 1 hit. |
PRINTSi | PR00622. HISTONEH3. |
SMARTi | View protein in SMART SM00428. H3. 1 hit. |
SUPFAMi | SSF47113. SSF47113. 1 hit. |
PROSITEi | View protein in PROSITE PS00322. HISTONE_H3_1. 1 hit. PS00959. HISTONE_H3_2. 1 hit. |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P09988-1 [UniParc]FASTAAdd to basket
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
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. |
PIRi | E27399. HSZP3. |
RefSeqi | NP_594683.1. NM_001020112.2. NP_595567.1. NM_001021462.2. NP_596467.1. NM_001022386.2. |
Genome annotation databases
Similar proteinsi
Entry informationi
Entry namei | H31_SCHPO | |
Accessioni | P09988Primary (citable) accession number: P09988 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 1, 1989 |
Last sequence update: | January 23, 2007 | |
Last modified: | March 28, 2018 | |
This is version 162 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal 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