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P07041 (H3_NEUCR) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone H3
Gene names
Name:hh3
ORF Names:B7K22.030, NCU01635
OrganismNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) [Reference proteome]
Taxonomic identifier367110 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora

Protein attributes

Sequence length136 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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. Trimethylated by methyltransferase dim-5 to form H3K9me3. H3K9me3, but not H3K9me2, marks chromatin regions for cytosine methylation. Methylated by set-2 to form H3K36me. H3K36me represses gene expression. Methylated by dot-1 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 dot-1-mediated formation of H3K79me require H2BK123ub1 By similarity. Ref.5

Acetylation of histone H3 leads to transcriptional activation. H3K14ac formation by gcn-5 is promoted by H3S10ph. H3K14ac can also be formed by esa-1. 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; H3K9me3 = trimethylated 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
   Cellular componentChromosome
Nucleosome core
Nucleus
   LigandDNA-binding
   PTMAcetylation
Methylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processnucleosome 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

protein binding

Inferred from physical interaction PubMed 12887903. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

dim-5Q8X2252EBI-1270655,EBI-1268994

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 136135Histone H3
PRO_0000221364

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,N6,N6-trimethyllysine; alternate Ref.5
Modified residue101N6-acetyllysine; alternate By similarity
Modified residue111Phosphoserine By similarity
Modified residue151N6,N6-dimethyllysine; alternate By similarity
Modified residue151N6-acetyllysine; alternate By similarity
Modified residue151N6-methyllysine; 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

Experimental info

Sequence conflict921A → L in CAA25761. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P07041 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 9AF51E808E698349

FASTA13615,392
        10         20         30         40         50         60 
MARTKQTARK STGGKAPRKQ LASKAARKSA PSTGGVKKPH RYKPGTVALR EIRRYQKSTE 

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

       130 
QSKDIQLARR LRGERN 

« Hide

References

« Hide 'large scale' references
[1]"The genes coding for histone H3 and H4 in Neurospora crassa are unique and contain intervening sequences."
Woudt L.P., Pastink A., Kempers-Veenstra A.E., Jansen A.E.M., Mager W.H., Planta R.J.
Nucleic Acids Res. 11:5347-5360(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Identification and characterization of the genes encoding the core histones and histone variants of Neurospora crassa."
Hays S.M., Swanson J., Selker E.U.
Genetics 160:961-973(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"What's in the genome of a filamentous fungus? Analysis of the Neurospora genome sequence."
Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.
Nucleic Acids Res. 31:1944-1954(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
[4]"The genome sequence of the filamentous fungus Neurospora crassa."
Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D. expand/collapse author list , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
Nature 422:859-868(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
[5]"Trimethylated lysine 9 of histone H3 is a mark for DNA methylation in Neurospora crassa."
Tamaru H., Zhang X., McMillen D., Singh P.B., Nakayama J., Grewal S.I., Allis C.D., Cheng X., Selker E.U.
Nat. Genet. 34:75-79(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT LYS-10.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X01612 Genomic DNA. Translation: CAA25761.1.
AY062173 Genomic DNA. Translation: AAL38973.1.
AL670543 Genomic DNA. Translation: CAD21510.1.
CM002237 Genomic DNA. Translation: EAA26767.1.
PIRS07350.
RefSeqXP_956003.1. XM_950910.2.
UniGeneNcr.23461.

3D structure databases

ProteinModelPortalP07041.
SMRP07041. Positions 2-135.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-39601N.
IntActP07041. 1 interaction.
STRING5141.NCU01635.1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiEFNCRT00000001782; EFNCRP00000001782; EFNCRG00000001780.
GeneID3872150.
KEGGncr:NCU01635.

Phylogenomic databases

eggNOGCOG2036.
HOGENOMHOG000155290.
KOK11253.
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_NEUCR
AccessionPrimary (citable) accession number: P07041
Secondary accession number(s): Q7RV46, Q8WZD9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 127 of the entry and version 3 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