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Q59VP2

- H2A2_CANAL

UniProt

Q59VP2 - H2A2_CANAL

Protein

Histone H2A.2

Gene

HTA2

Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Status
Reviewed - Annotation score: 3 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.

    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.2
    Gene namesi
    Name:HTA2
    ORF Names:CaO19.1051, CaO19.8653
    OrganismiCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
    Taxonomic identifieri237561 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida
    ProteomesiUP000000559: Unassembled WGS sequence

    Organism-specific databases

    CGDiCAL0001183. HTA2.

    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 – 131130Histone H2A.2PRO_0000228726Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei5 – 51N6-acetyllysineBy similarity
    Modified residuei7 – 71N6-acetyllysineBy similarity
    Modified residuei105 – 1051N5-methylglutamineBy 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. 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

    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

    STRINGi5476.CAL0001183.

    Structurei

    3D structure databases

    ProteinModelPortaliQ59VP2.
    SMRiQ59VP2. Positions 13-120.
    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

    eggNOGiCOG5262.
    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.

    Q59VP2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGGKGKAGS SEKASTSRSA KAGLTFPVGR VHRLLRKGNY AQRIGSGAPV    50
    YLTSVLEYLA AEILELAGNA ARDNKKSRII PRHLQLAIRN DEELNKLLGD 100
    VTIAQGGVLP NIHQSLLPAK KAKAGAASQE L 131
    Length:131
    Mass (Da):13,824
    Last modified:January 23, 2007 - v3
    Checksum:iCBB27515958B3108
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AACQ01000121 Genomic DNA. Translation: EAK94551.1.
    AACQ01000120 Genomic DNA. Translation: EAK94597.1.
    RefSeqiXP_713655.1. XM_708562.1.
    XP_713700.1. XM_708607.1.

    Genome annotation databases

    GeneIDi3644634.
    3644715.
    KEGGical:CaO19.1051.
    cal:CaO19.8653.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AACQ01000121 Genomic DNA. Translation: EAK94551.1 .
    AACQ01000120 Genomic DNA. Translation: EAK94597.1 .
    RefSeqi XP_713655.1. XM_708562.1.
    XP_713700.1. XM_708607.1.

    3D structure databases

    ProteinModelPortali Q59VP2.
    SMRi Q59VP2. Positions 13-120.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5476.CAL0001183.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 3644634.
    3644715.
    KEGGi cal:CaO19.1051.
    cal:CaO19.8653.

    Organism-specific databases

    CGDi CAL0001183. HTA2.

    Phylogenomic databases

    eggNOGi COG5262.
    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: SC5314 / ATCC MYA-2876.

    Entry informationi

    Entry nameiH2A2_CANAL
    AccessioniPrimary (citable) accession number: Q59VP2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 21, 2006
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 58 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-5; H2AK7ac = acetylated Lys-7; H2AS128ph = phosphorylated Ser-128.Curated

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Candida albicans
      Candida albicans: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3