A1D240 (H3_NEOFI) Reviewed, UniProtKB/Swiss-Prot
Last modified April 3, 2013. Version 38. History...
Names and origin
|Protein names||Recommended name:|
|Organism||Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181) (Aspergillus fischerianus) [Complete proteome]|
|Taxonomic identifier||331117 [NCBI]|
|Taxonomic lineage||Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Neosartorya ›|
|Sequence length||136 AA.|
|Sequence processing||The displayed sequence is further processed into a mature form.|
|Protein existence||Inferred from homology|
General annotation (Comments)
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.
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.
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.
Belongs to the histone H3 family.
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.
|Biological process||DNA damage|
|Technical term||Complete proteome|
|Gene Ontology (GO)|
Inferred from electronic annotation. Source: UniProtKB-KWnucleosome assembly
Inferred from electronic annotation. Source: InterPro
Inferred from electronic annotation. Source: UniProtKB-KWnucleus
Inferred from electronic annotation. Source: UniProtKB-SubCell
Inferred from electronic annotation. Source: UniProtKB-KW
|Complete GO annotation...|
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Initiator methionine||1||1||Removed By similarity|
|Chain||2 – 136||135||Histone H3||PRO_0000297749|
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|
|||"Genomic islands in the pathogenic filamentous fungus Aspergillus fumigatus."|
Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M. Nierman W.C.
PLoS Genet. 4:E1000046-E1000046(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181.
|DS027688 Genomic DNA. Translation: EAW22483.1.|
|RefSeq||XP_001264380.1. XM_001264379.1. |
3D structure databases
|SMR||A1D240. Positions 2-136. |
Protein-protein interaction databases
Protocols and materials databases
Genome annotation databases
|EnsemblFungi||CADNFIAT00001902; CADNFIAP00001863; CADNFIAG00001902. |
Family and domain databases
|Gene3D||220.127.116.11. 1 hit. |
|InterPro||IPR009072. Histone-fold. |
|PANTHER||PTHR11426. PTHR11426. 1 hit. |
|Pfam||PF00125. Histone. 1 hit. |
|PRINTS||PR00622. HISTONEH3. |
|SMART||SM00428. H3. 1 hit. |
|SUPFAM||SSF47113. Histone-fold. 1 hit. |
|PROSITE||PS00322. HISTONE_H3_1. 1 hit. |
PS00959. HISTONE_H3_2. 1 hit.
|Accession||Primary (citable) accession number: A1D240|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Fungal Protein Annotation Program|
Index of protein domains and families