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A1D240 (H3_NEOFI) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length136 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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 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.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
   Cellular componentChromosome
Nucleosome core
Nucleus
   LigandDNA-binding
   PTMAcetylation
Methylation
Phosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processDNA repair

Inferred from electronic annotation. Source: UniProtKB-KW

nucleosome assembly

Inferred from electronic annotation. Source: InterPro

   Cellular_componentnucleosome

Inferred from electronic annotation. Source: UniProtKB-KW

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 136135Histone H3
PRO_0000297749

Amino acid modifications

Modified residue51N6,N6,N6-trimethyllysine; alternate By similarity
Modified residue51N6,N6-dimethyllysine; alternate By similarity
Modified residue51N6-methyllysine; alternate By similarity
Modified residue101N6-acetyllysine; alternate By similarity
Modified residue101N6-methyllysine; alternate By similarity
Modified residue111Phosphoserine By similarity
Modified residue151N6,N6-dimethyllysine; alternate By similarity
Modified residue151N6-acetyllysine; alternate By similarity
Modified residue191N6-acetyllysine; alternate By similarity
Modified residue191N6-methyllysine; alternate By similarity
Modified residue241N6-acetyllysine; alternate By similarity
Modified residue241N6-methyllysine; alternate By similarity
Modified residue281N6,N6,N6-trimethyllysine; alternate By similarity
Modified residue281N6,N6-dimethyllysine; alternate By similarity
Modified residue281N6-acetyllysine; alternate By similarity
Modified residue281N6-methyllysine; alternate By similarity
Modified residue371N6,N6,N6-trimethyllysine; alternate By similarity
Modified residue371N6,N6-dimethyllysine; alternate By similarity
Modified residue371N6-acetyllysine; alternate By similarity
Modified residue371N6-methyllysine; alternate By similarity
Modified residue571N6-acetyllysine By similarity
Modified residue651N6-acetyllysine By similarity
Modified residue801N6,N6,N6-trimethyllysine; alternate By similarity
Modified residue801N6,N6-dimethyllysine; alternate By similarity
Modified residue801N6-methyllysine; alternate By similarity

Sequences

Sequence LengthMass (Da)Tools
A1D240 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 811AE1772F1DD20C

FASTA13615,333
        10         20         30         40         50         60 
MARTKQTARK STGGKAPRKQ LASKAARKAA PSTGGVKKPH RYKPGTVALR EIRRYQKSTE 

        70         80         90        100        110        120 
LLIRKLPFQR LVREIAQDFK SDLRFQSSAI GALQESVEAY LVSLFEDTNL CAIHAKRVTI 

       130 
QSKDIQLARR LRGERS 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS027688 Genomic DNA. Translation: EAW22483.1.
RefSeqXP_001264380.1. XM_001264379.1.

3D structure databases

ProteinModelPortalA1D240.
SMRA1D240. Positions 2-136.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING36630.CADNFIAP00001863.

Proteomic databases

PRIDEA1D240.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADNFIAT00001902; CADNFIAP00001863; CADNFIAG00001902.
GeneID4591035.
KEGGnfi:NFIA_011720.

Phylogenomic databases

eggNOGCOG2036.
HOGENOMHOG000155290.
KOK11253.
OMARRINGVC.
OrthoDBEOG7T4MZ6.

Family and domain databases

Gene3D1.10.20.10. 1 hit.
InterProIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR000164. Histone_H3.
[Graphical view]
PANTHERPTHR11426. PTHR11426. 1 hit.
PfamPF00125. Histone. 1 hit.
[Graphical view]
PRINTSPR00622. HISTONEH3.
SMARTSM00428. H3. 1 hit.
[Graphical view]
SUPFAMSSF47113. SSF47113. 1 hit.
PROSITEPS00322. HISTONE_H3_1. 1 hit.
PS00959. HISTONE_H3_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameH3_NEOFI
AccessionPrimary (citable) accession number: A1D240
Entry history
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: January 23, 2007
Last modified: November 13, 2013
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families