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O74268

- H2A_BOTFB

UniProt

O74268 - H2A_BOTFB

Protein

Histone H2A

Gene

hta1

Organism
Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
  1. Functioni

    Core component of nucleosome which plays a central role in DNA double strand break (DSB) repair. 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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei121 – 1211Not ubiquitinatedCurated

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. DNA repair Source: UniProtKB-KW
    2. nucleosome assembly Source: InterPro

    Keywords - Biological processi

    DNA damage, DNA repair

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone H2A
    Gene namesi
    Name:hta1
    ORF Names:BC1G_11316
    OrganismiBotryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea)
    Taxonomic identifieri332648 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaLeotiomycetesHelotialesSclerotiniaceaeBotrytis

    Subcellular locationi

    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 H2APRO_0000055209Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei5 – 51N6-acetyllysineBy similarity
    Modified residuei10 – 101N6-acetyllysineBy similarity
    Modified residuei107 – 1071N5-methylglutamineBy similarity
    Modified residuei133 – 1331PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated to form H2AS128ph (gamma-H2A) in response to DNA double-strand breaks (DSBs) generated by exogenous genotoxic agents and by stalled replication forks. Phosphorylation is dependent on the DNA damage checkpoint kinases MEC1/ATR and TEL1/ATM, spreads on either side of a detected DSB site and may mark the surrounding chromatin for recruitment of proteins required for DNA damage signaling and repair. Gamma-H2A is removed from the DNA prior to the strand invasion-primer extension step of the repair process and subsequently dephosphorylated. Dephosphorylation is necessary for efficient recovery from the DNA damage checkpoint By similarity.By similarity
    Acetylated by ESA1 to form H2AK4ac and H2AK7ac.By similarity

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Proteomic databases

    PRIDEiO74268.

    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.

    Structurei

    3D structure databases

    ProteinModelPortaliO74268.
    SMRiO74268. Positions 18-125.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi133 – 1342[ST]-Q motif

    Domaini

    The [ST]-Q motif constitutes a recognition sequence for kinases from the PI3/PI4-kinase family.

    Sequence similaritiesi

    Belongs to the histone H2A family.Curated

    Phylogenomic databases

    eggNOGiCOG5262.
    KOiK11251.
    OMAiTKNAQSR.

    Family and domain databases

    Gene3Di1.10.20.10. 1 hit.
    InterProiIPR009072. Histone-fold.
    IPR007125. Histone_core_D.
    IPR002119. Histone_H2A.
    [Graphical view]
    PfamiPF00125. Histone. 1 hit.
    [Graphical view]
    PRINTSiPR00620. HISTONEH2A.
    SMARTiSM00414. H2A. 1 hit.
    [Graphical view]
    SUPFAMiSSF47113. SSF47113. 1 hit.
    PROSITEiPS00046. HISTONE_H2A. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O74268-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTGGKSAGGK AGTTKNAQSR SSKAGLAFPV GRVHRLLRKG NYAQRVGAGA    50
    PVYLAAVLEY LAAEILELAG NAARDNKKTR IIPRHLQLAI RNDEELNKLL 100
    GHVTIAQGGV LPNIHQNLLP KKTAKTAGGK PASQEL 136
    Length:136
    Mass (Da):14,322
    Last modified:November 13, 2007 - v4
    Checksum:i72F4D1D9584C66BC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti21 – 222SS → FHP in CAA07351. 1 PublicationCurated
    Sequence conflicti117 – 1171N → S in CAA07351. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ006959 Genomic DNA. Translation: CAA07351.1.
    CH476918 Genomic DNA. Translation: EDN31831.1.
    RefSeqiXP_001550543.1. XM_001550493.1.

    Genome annotation databases

    GeneIDi5431036.
    KEGGibfu:BC1G_11316.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ006959 Genomic DNA. Translation: CAA07351.1 .
    CH476918 Genomic DNA. Translation: EDN31831.1 .
    RefSeqi XP_001550543.1. XM_001550493.1.

    3D structure databases

    ProteinModelPortali O74268.
    SMRi O74268. Positions 18-125.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi O74268.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 5431036.
    KEGGi bfu:BC1G_11316.

    Phylogenomic databases

    eggNOGi COG5262.
    KOi K11251.
    OMAi TKNAQSR.

    Family and domain databases

    Gene3Di 1.10.20.10. 1 hit.
    InterProi IPR009072. Histone-fold.
    IPR007125. Histone_core_D.
    IPR002119. Histone_H2A.
    [Graphical view ]
    Pfami PF00125. Histone. 1 hit.
    [Graphical view ]
    PRINTSi PR00620. HISTONEH2A.
    SMARTi SM00414. H2A. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47113. SSF47113. 1 hit.
    PROSITEi PS00046. HISTONE_H2A. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Quidde T., Tudzynski P.
      Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia sclerotiorum and Botrytis cinerea."
      Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A., Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E., Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M., Quevillon E.
      , Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P., Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I., Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P., Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C., Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C., Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E., Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N., Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E., Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O., Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.
      PLoS Genet. 7:E1002230-E1002230(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: B05.10.

    Entry informationi

    Entry nameiH2A_BOTFB
    AccessioniPrimary (citable) accession number: O74268
    Secondary accession number(s): A6SDP9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 31, 2004
    Last sequence update: November 13, 2007
    Last modified: October 1, 2014
    This is version 84 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    In contrast to vertebrates and insects, its C-terminus is not monoubiquitinated.Curated

    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: H2AK4ac = acetylated Lys-5; H2AK7ac = acetylated Lys-10; H2AS128ph = phosphorylated Ser-133.Curated

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3