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Protein

Histone H3

Gene

hht1

Organism
Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181) (Aspergillus fischerianus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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

Complete GO annotation...

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H3
Gene namesi
Name:hht1
ORF Names:NFIA_011720
OrganismiNeosartorya fischeri (strain ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181) (Aspergillus fischerianus)
Taxonomic identifieri331117 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeNeosartorya
ProteomesiUP000006702 Componenti: Unassembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:NFIA_011720.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 136135Histone H3PRO_0000297749Add
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; alternateBy similarity
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; alternateBy similarity
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 to form H3S10ph. H3S10ph promotes subsequent H3K14ac formation and is required for transcriptional activation through TBP recruitment to the promoters (By similarity).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).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

Proteomic databases

PRIDEiA1D240.

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.

Structurei

3D structure databases

ProteinModelPortaliA1D240.
SMRiA1D240. Positions 2-136.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H3 family.Curated

Phylogenomic databases

eggNOGiCOG2036.
HOGENOMiHOG000155290.
KOiK11253.
OMAiCHASMAR.
OrthoDBiEOG7T4MZ6.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007125. Histone_core_D.
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.

A1D240-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARTKQTARK STGGKAPRKQ LASKAARKAA PSTGGVKKPH RYKPGTVALR
60 70 80 90 100
EIRRYQKSTE LLIRKLPFQR LVREIAQDFK SDLRFQSSAI GALQESVEAY
110 120 130
LVSLFEDTNL CAIHAKRVTI QSKDIQLARR LRGERS
Length:136
Mass (Da):15,333
Last modified:January 23, 2007 - v1
Checksum:i811AE1772F1DD20C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS027688 Genomic DNA. Translation: EAW22483.1.
RefSeqiXP_001264380.1. XM_001264379.1.

Genome annotation databases

EnsemblFungiiCADNFIAT00001902; CADNFIAP00001863; CADNFIAG00001902.
GeneIDi4591035.
KEGGinfi:NFIA_011720.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS027688 Genomic DNA. Translation: EAW22483.1.
RefSeqiXP_001264380.1. XM_001264379.1.

3D structure databases

ProteinModelPortaliA1D240.
SMRiA1D240. Positions 2-136.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiA1D240.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADNFIAT00001902; CADNFIAP00001863; CADNFIAG00001902.
GeneIDi4591035.
KEGGinfi:NFIA_011720.

Organism-specific databases

EuPathDBiFungiDB:NFIA_011720.

Phylogenomic databases

eggNOGiCOG2036.
HOGENOMiHOG000155290.
KOiK11253.
OMAiCHASMAR.
OrthoDBiEOG7T4MZ6.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007125. Histone_core_D.
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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181.

Entry informationi

Entry nameiH3_NEOFI
AccessioniPrimary (citable) accession number: A1D240
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 49 of the entry and version 1 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

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.