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Q74ZL4

- H2A1_ASHGO

UniProt

Q74ZL4 - H2A1_ASHGO

Protein

Histone H2A.1

Gene

HTA1

Organism
Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 69 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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
    Sitei119 – 1191Not 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.1
    Gene namesi
    Name:HTA1
    Ordered Locus Names:AGR184W
    OrganismiAshbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii)
    Taxonomic identifieri284811 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeEremothecium
    ProteomesiUP000000591: Chromosome VII

    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 – 131130Histone H2A.1PRO_0000055205Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei4 – 41N6-acetyllysineBy similarity
    Modified residuei7 – 71N6-acetyllysineBy similarity
    Modified residuei105 – 1051N5-methylglutamineBy similarity
    Cross-linki126 – 126Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
    Modified residuei128 – 1281PhosphoserineBy 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 by PPH3, a component of the histone H2A phosphatase complex (HTP-C). Dephosphorylation is necessary for efficient recovery from the DNA damage checkpoint By similarity.By similarity
    Sumoylation on Lys-126 may lead to transcriptional repression.By similarity
    Acetylated by ESA1 to form H2AK4ac and H2AK7ac.By similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiQ74ZL4.

    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

    STRINGi33169.AGOS_AGR184W.

    Structurei

    3D structure databases

    ProteinModelPortaliQ74ZL4.
    SMRiQ74ZL4. Positions 16-125.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi128 – 1292[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

    HOGENOMiHOG000234652.
    KOiK11251.
    OrthoDBiEOG7GN30N.

    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.

    Q74ZL4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGKGGKAGS AAKASQSRSA KAGLTFPVGR VHRLLRKGNY AQRIGSGAPV    50
    YMTAVLEYLA AEILELAGNA ARDNKKTRII PRHLQLAIRN DDELNKLLGN 100
    VTIAQGGVLP NIHANLLPKK SAKATKASQE L 131
    Length:131
    Mass (Da):13,865
    Last modified:January 23, 2007 - v3
    Checksum:i7849DC54E66539AA
    GO

    Sequence cautioni

    The sequence AAS54674.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016820 Genomic DNA. Translation: AAS54674.1. Different initiation.
    RefSeqiNP_986850.1. NM_211912.1.

    Genome annotation databases

    GeneIDi4623152.
    KEGGiago:AGOS_AGR184W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016820 Genomic DNA. Translation: AAS54674.1 . Different initiation.
    RefSeqi NP_986850.1. NM_211912.1.

    3D structure databases

    ProteinModelPortali Q74ZL4.
    SMRi Q74ZL4. Positions 16-125.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 33169.AGOS_AGR184W.

    Proteomic databases

    PRIDEi Q74ZL4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 4623152.
    KEGGi ago:AGOS_AGR184W.

    Phylogenomic databases

    HOGENOMi HOG000234652.
    KOi K11251.
    OrthoDBi EOG7GN30N.

    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. "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome."
      Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P.
      Science 304:304-307(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.
    2. "Genomes of Ashbya fungi isolated from insects reveal four mating-type loci, numerous translocations, lack of transposons, and distinct gene duplications."
      Dietrich F.S., Voegeli S., Kuo S., Philippsen P.
      G3 (Bethesda) 3:1225-1239(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENOME REANNOTATION.
      Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.

    Entry informationi

    Entry nameiH2A1_ASHGO
    AccessioniPrimary (citable) accession number: Q74ZL4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 31, 2004
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 69 of the entry and version 3 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-4; H2AK7ac = acetylated Lys-7; H2AS128ph = phosphorylated Ser-128.Curated

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3