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A2QRR5

- H3_ASPNC

UniProt

A2QRR5 - H3_ASPNC

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Protein

Histone H3

Gene
hht1, An08g06960
Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Status
Reviewed - 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

  1. DNA binding Source: UniProtKB-KW

GO - Biological processi

  1. nucleosome assembly Source: InterPro
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H3
Gene namesi
Name:hht1
ORF Names:An08g06960
OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
Taxonomic identifieri425011 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006706: Chromosome 8R

Subcellular locationi

Nucleus By similarity. Chromosome By similarity

GO - Cellular componenti

  1. nucleosome Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 136135Histone H3PRO_0000297743Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei5 – 51N6,N6,N6-trimethyllysine; alternate By similarity
Modified residuei5 – 51N6,N6-dimethyllysine; alternate By similarity
Modified residuei5 – 51N6-methyllysine; alternate By similarity
Modified residuei10 – 101N6-acetyllysine; alternate By similarity
Modified residuei10 – 101N6-methyllysine; alternate By similarity
Modified residuei11 – 111Phosphoserine By similarity
Modified residuei15 – 151N6,N6-dimethyllysine; alternate By similarity
Modified residuei15 – 151N6-acetyllysine; alternate By similarity
Modified residuei19 – 191N6-acetyllysine; alternate By similarity
Modified residuei19 – 191N6-methyllysine; alternate By similarity
Modified residuei24 – 241N6-acetyllysine; alternate By similarity
Modified residuei24 – 241N6-methyllysine; alternate By similarity
Modified residuei28 – 281N6,N6,N6-trimethyllysine; alternate By similarity
Modified residuei28 – 281N6,N6-dimethyllysine; alternate By similarity
Modified residuei28 – 281N6-acetyllysine; alternate By similarity
Modified residuei28 – 281N6-methyllysine; alternate By similarity
Modified residuei37 – 371N6,N6,N6-trimethyllysine; alternate By similarity
Modified residuei37 – 371N6,N6-dimethyllysine; alternate By similarity
Modified residuei37 – 371N6-acetyllysine; alternate By similarity
Modified residuei37 – 371N6-methyllysine; alternate By similarity
Modified residuei57 – 571N6-acetyllysine By similarity
Modified residuei65 – 651N6-acetyllysine By similarity
Modified residuei80 – 801N6,N6,N6-trimethyllysine; alternate By similarity
Modified residuei80 – 801N6,N6-dimethyllysine; alternate By similarity
Modified residuei80 – 801N6-methyllysine; alternate By 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.
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.

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

PRIDEiA2QRR5.

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.

Protein-protein interaction databases

STRINGi5061.CADANGAP00006889.

Structurei

3D structure databases

ProteinModelPortaliA2QRR5.
SMRiA2QRR5. Positions 2-136.

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H3 family.

Phylogenomic databases

eggNOGiCOG2036.
HOGENOMiHOG000155290.
KOiK11253.
OrthoDBiEOG7T4MZ6.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR000164. Histone_H3.
[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.

A2QRR5-1 [UniParc]FASTAAdd to Basket

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MARTKQTARK STGGKAPRKQ LASKAARKAA PSTGGVKKPH RYKPGTVALR    50
EIRRYQKSTE LLIRKLPFQR LVREIAQDFK SDLRFQSSAI GALQESVEAY 100
LVSLFEDTNL CAIHAKRVTI QSKDIQLARR LRGERS 136
Length:136
Mass (Da):15,333
Last modified:March 6, 2007 - v1
Checksum:i811AE1772F1DD20C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM270170 Genomic DNA. Translation: CAK45666.1.
RefSeqiXP_001392811.1. XM_001392774.2.

Genome annotation databases

EnsemblFungiiCADANGAT00007018; CADANGAP00006889; CADANGAG00007018.
GeneIDi4983013.
KEGGiang:ANI_1_976074.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM270170 Genomic DNA. Translation: CAK45666.1 .
RefSeqi XP_001392811.1. XM_001392774.2.

3D structure databases

ProteinModelPortali A2QRR5.
SMRi A2QRR5. Positions 2-136.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5061.CADANGAP00006889.

Proteomic databases

PRIDEi A2QRR5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADANGAT00007018 ; CADANGAP00006889 ; CADANGAG00007018 .
GeneIDi 4983013.
KEGGi ang:ANI_1_976074.

Phylogenomic databases

eggNOGi COG2036.
HOGENOMi HOG000155290.
KOi K11253.
OrthoDBi EOG7T4MZ6.

Family and domain databases

Gene3Di 1.10.20.10. 1 hit.
InterProi IPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR000164. Histone_H3.
[Graphical view ]
PANTHERi PTHR11426. PTHR11426. 1 hit.
Pfami PF00125. Histone. 1 hit.
[Graphical view ]
PRINTSi PR00622. HISTONEH3.
SMARTi SM00428. H3. 1 hit.
[Graphical view ]
SUPFAMi SSF47113. SSF47113. 1 hit.
PROSITEi PS00322. HISTONE_H3_1. 1 hit.
PS00959. HISTONE_H3_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88."
    Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M.
    , Coutinho P.M., Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.
    Nat. Biotechnol. 25:221-231(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CBS 513.88 / FGSC A1513.

Entry informationi

Entry nameiH3_ASPNC
AccessioniPrimary (citable) accession number: A2QRR5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: March 6, 2007
Last modified: July 9, 2014
This is version 46 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.

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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