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P04909

- H2A1_SCHPO

UniProt

P04909 - H2A1_SCHPO

Protein

Histone H2A-alpha

Gene

hta1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  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.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei120 – 1201Not ubiquitinatedCurated

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. protein binding Source: IntAct

    GO - Biological processi

    1. DNA damage induced protein phosphorylation Source: PomBase
    2. DNA repair Source: UniProtKB-KW
    3. nucleosome assembly Source: InterPro
    4. protein localization to kinetochore Source: PomBase
    5. signal transduction in response to DNA damage Source: PomBase

    Keywords - Biological processi

    DNA damage, DNA repair

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone H2A-alpha
    Alternative name(s):
    H2A.1
    Gene namesi
    Name:hta1
    ORF Names:SPCC622.08c
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485: Chromosome III

    Organism-specific databases

    PomBaseiSPCC622.08c.

    Subcellular locationi

    GO - Cellular componenti

    1. mating-type region heterochromatin Source: PomBase
    2. nuclear pericentric heterochromatin Source: PomBase
    3. nuclear rDNA heterochromatin Source: PomBase
    4. nuclear telomeric heterochromatin Source: PomBase
    5. nucleosome Source: UniProtKB-KW

    Keywords - Cellular componenti

    Chromosome, Nucleosome core, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi129 – 1291S → A: Causes hypersensitivity to DNA-damage-inducing agents and impairs recruitment of crb2 to DSB sites. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 132131Histone H2A-alphaPRO_0000055324Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei5 – 51N6-acetyllysineBy similarity
    Modified residuei9 – 91N6-acetyllysineBy similarity
    Modified residuei106 – 1061N5-methylglutamine1 Publication
    Modified residuei129 – 1291Phosphoserine1 Publication

    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 rad3/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 required for recruiting crb2, a modulator of DNA damage checkpoint signaling, to DSB sites. 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.1 Publication
    Acetylated by esa1 to form H2AK4ac and H2AK7ac.By similarity

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiP04909.

    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.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    brc1Q103374EBI-7764873,EBI-7764855

    Protein-protein interaction databases

    BioGridi276062. 63 interactions.
    IntActiP04909. 1 interaction.
    MINTiMINT-4783472.
    STRINGi4896.SPCC622.08c-1.

    Structurei

    3D structure databases

    ProteinModelPortaliP04909.
    SMRiP04909. Positions 14-120.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi129 – 1302[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.
    OMAiMKAGLQF.
    OrthoDBiEOG7GN30N.
    PhylomeDBiP04909.

    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.

    P04909-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGGKSGGKA AVAKSAQSRS AKAGLAFPVG RVHRLLRKGN YAQRVGAGAP    50
    VYLAAVLEYL AAEILELAGN AARDNKKTRI IPRHLQLAIR NDEELNKLLG 100
    HVTIAQGGVV PNINAHLLPK TSGRTGKPSQ EL 132
    Length:132
    Mass (Da):13,878
    Last modified:January 23, 2007 - v3
    Checksum:iD1F5C136916AC273
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti124 – 1241R → G in AAA35311. (PubMed:3018512)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M11494 Genomic DNA. Translation: AAA35311.1.
    X05220 Genomic DNA. Translation: CAA28848.1.
    CU329672 Genomic DNA. Translation: CAA21864.1.
    PIRiB27399. HSZPA2.
    RefSeqiNP_588180.1. NM_001023170.2.

    Genome annotation databases

    EnsemblFungiiSPCC622.08c.1; SPCC622.08c.1:pep; SPCC622.08c.
    GeneIDi2539499.
    KEGGispo:SPCC622.08c.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M11494 Genomic DNA. Translation: AAA35311.1 .
    X05220 Genomic DNA. Translation: CAA28848.1 .
    CU329672 Genomic DNA. Translation: CAA21864.1 .
    PIRi B27399. HSZPA2.
    RefSeqi NP_588180.1. NM_001023170.2.

    3D structure databases

    ProteinModelPortali P04909.
    SMRi P04909. Positions 14-120.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 276062. 63 interactions.
    IntActi P04909. 1 interaction.
    MINTi MINT-4783472.
    STRINGi 4896.SPCC622.08c-1.

    Proteomic databases

    MaxQBi P04909.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii SPCC622.08c.1 ; SPCC622.08c.1:pep ; SPCC622.08c .
    GeneIDi 2539499.
    KEGGi spo:SPCC622.08c.

    Organism-specific databases

    PomBasei SPCC622.08c.

    Phylogenomic databases

    HOGENOMi HOG000234652.
    KOi K11251.
    OMAi MKAGLQF.
    OrthoDBi EOG7GN30N.
    PhylomeDBi P04909.

    Miscellaneous databases

    NextBioi 20800661.
    PROi P04909.

    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. "Organization, primary structure, and evolution of histone H2A and H2B genes of the fission yeast Schizosaccharomyces pombe."
      Choe J., Schuster T., Grunstein M.
      Mol. Cell. Biol. 5:3261-3269(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Histone gene organization of fission yeast: a common upstream sequence."
      Matsumoto S., Yanagida M.
      EMBO J. 4:3531-3538(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The genome sequence of Schizosaccharomyces pombe."
      Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
      , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
      Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 972 / ATCC 24843.
    4. "Histone H2A phosphorylation controls Crb2 recruitment at DNA breaks, maintains checkpoint arrest, and influences DNA repair in fission yeast."
      Nakamura T.M., Du L.-L., Redon C., Russell P.
      Mol. Cell. Biol. 24:6215-6230(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF SER-129, PHOSPHORYLATION AT SER-129.
    5. "Glutamine methylation in histone H2A is an RNA-polymerase-I-dedicated modification."
      Tessarz P., Santos-Rosa H., Robson S.C., Sylvestersen K.B., Nelson C.J., Nielsen M.L., Kouzarides T.
      Nature 505:564-568(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT GLN-106.

    Entry informationi

    Entry nameiH2A1_SCHPO
    AccessioniPrimary (citable) accession number: P04909
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 117 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-9; H2AS128ph = phosphorylated Ser-129.Curated

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Schizosaccharomyces pombe
      Schizosaccharomyces pombe: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3