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A2QRR5

- H3_ASPNC

UniProt

A2QRR5 - H3_ASPNC

Protein

Histone H3

Gene

hht1

Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
  1. 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

    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

    Keywords - Cellular componenti

    Chromosome, Nucleosome core, Nucleus

    PTM / Processingi

    Molecule processing

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

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histone H3 family.Curated

    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

    « Hide

    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: October 1, 2014
    This is version 47 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, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3