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Q8IUE6

- H2A2B_HUMAN

UniProt

Q8IUE6 - H2A2B_HUMAN

Protein

Histone H2A type 2-B

Gene

HIST2H2AB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  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

    Enzyme and pathway databases

    ReactomeiREACT_172610. HATs acetylate histones.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone H2A type 2-B
    Gene namesi
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:20508. HIST2H2AB.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. nucleosome Source: UniProtKB-KW
    3. nucleus Source: UniProt

    Keywords - Cellular componenti

    Chromosome, Nucleosome core, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2 – 21S → A: Blocks the inhibition of transcription by RPS6KA5/MSK1. 1 Publication

    Organism-specific databases

    PharmGKBiPA134884141.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 130129Histone H2A type 2-BPRO_0000227505Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei2 – 21Phosphoserine; by RPS6KA51 Publication
    Modified residuei4 – 41Citrulline; alternate1 Publication
    Modified residuei4 – 41Symmetric dimethylarginine; by PRMT5; alternateBy similarity
    Modified residuei6 – 61N6-acetyllysineBy similarity
    Cross-linki14 – 14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
    Cross-linki16 – 16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
    Modified residuei105 – 1051N5-methylglutamine1 Publication
    Cross-linki120 – 120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)3 Publications
    Modified residuei121 – 1211Phosphothreonine; by VPRBP2 Publications

    Post-translational modificationi

    Monoubiquitination of Lys-120 (H2AK119Ub) by RING1 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is involved in the initiation of both imprinted and random X inactivation. Ubiquitinated H2A is enriched in inactive X chromosome chromatin. Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3 (H3K27me). H2AK119Ub by RNF2/RING2 can also be induced by ultraviolet and may be involved in DNA repair. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the recruitment of repair proteins to sites of DNA damage. Ubiquitination at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage is initiated by RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-linked ubiquitin are then conjugated to monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin chains in vitro. H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events.10 Publications
    Phosphorylation on Ser-2 (H2AS1ph) is enhanced during mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1. Phosphorylation at Thr-121 (H2AT120ph) by VPRBP is present in the regulatory region of many tumor suppresor genes and down-regulates their transcription.4 Publications
    Deiminated on Arg-4 in granulocytes upon calcium entry.
    Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex (PubMed:24352239).1 Publication
    Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage.By similarity

    Keywords - PTMi

    Acetylation, Citrullination, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ8IUE6.
    PaxDbiQ8IUE6.
    PeptideAtlasiQ8IUE6.
    PRIDEiQ8IUE6.

    PTM databases

    PhosphoSiteiQ8IUE6.

    Expressioni

    Gene expression databases

    BgeeiQ8IUE6.
    CleanExiHS_HIST2H2AB.
    GenevestigatoriQ8IUE6.

    Organism-specific databases

    HPAiHPA041189.

    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

    BioGridi130469. 15 interactions.
    IntActiQ8IUE6. 3 interactions.
    MINTiMINT-2809410.
    STRINGi9606.ENSP00000332790.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8IUE6.
    SMRiQ8IUE6. Positions 14-119.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histone H2A family.Curated

    Phylogenomic databases

    eggNOGiCOG5262.
    HOGENOMiHOG000234652.
    HOVERGENiHBG009342.
    InParanoidiQ8IUE6.
    KOiK11251.
    OMAiKAGQKGD.
    OrthoDBiEOG7M0NTR.
    PhylomeDBiQ8IUE6.
    TreeFamiTF300137.

    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.

    Q8IUE6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGRGKQGGK ARAKAKSRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV    50
    YLAAVLEYLT AEILELAGNA ARDNKKTRII PRHLQLAVRN DEELNKLLGG 100
    VTIAQGGVLP NIQAVLLPKK TESHKPGKNK 130
    Length:130
    Mass (Da):13,995
    Last modified:January 23, 2007 - v3
    Checksum:i87932FEA853F5E93
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti53 – 531A → T in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035802

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY131972 Genomic DNA. Translation: AAN59958.1.
    AL591493 Genomic DNA. Translation: CAI12570.1.
    CCDSiCCDS938.1.
    RefSeqiNP_778235.1. NM_175065.2.
    UniGeneiHs.664173.

    Genome annotation databases

    EnsembliENST00000331128; ENSP00000332790; ENSG00000184270.
    GeneIDi317772.
    KEGGihsa:317772.
    UCSCiuc001ete.3. human.

    Polymorphism databases

    DMDMi74750623.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY131972 Genomic DNA. Translation: AAN59958.1 .
    AL591493 Genomic DNA. Translation: CAI12570.1 .
    CCDSi CCDS938.1.
    RefSeqi NP_778235.1. NM_175065.2.
    UniGenei Hs.664173.

    3D structure databases

    ProteinModelPortali Q8IUE6.
    SMRi Q8IUE6. Positions 14-119.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 130469. 15 interactions.
    IntActi Q8IUE6. 3 interactions.
    MINTi MINT-2809410.
    STRINGi 9606.ENSP00000332790.

    PTM databases

    PhosphoSitei Q8IUE6.

    Polymorphism databases

    DMDMi 74750623.

    Proteomic databases

    MaxQBi Q8IUE6.
    PaxDbi Q8IUE6.
    PeptideAtlasi Q8IUE6.
    PRIDEi Q8IUE6.

    Protocols and materials databases

    DNASUi 317772.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000331128 ; ENSP00000332790 ; ENSG00000184270 .
    GeneIDi 317772.
    KEGGi hsa:317772.
    UCSCi uc001ete.3. human.

    Organism-specific databases

    CTDi 317772.
    GeneCardsi GC01M149861.
    HGNCi HGNC:20508. HIST2H2AB.
    HPAi HPA041189.
    MIMi 615014. gene.
    neXtProti NX_Q8IUE6.
    PharmGKBi PA134884141.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5262.
    HOGENOMi HOG000234652.
    HOVERGENi HBG009342.
    InParanoidi Q8IUE6.
    KOi K11251.
    OMAi KAGQKGD.
    OrthoDBi EOG7M0NTR.
    PhylomeDBi Q8IUE6.
    TreeFami TF300137.

    Enzyme and pathway databases

    Reactomei REACT_172610. HATs acetylate histones.

    Miscellaneous databases

    GeneWikii HIST2H2AB.
    GenomeRNAii 317772.
    NextBioi 96429.
    PROi Q8IUE6.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8IUE6.
    CleanExi HS_HIST2H2AB.
    Genevestigatori Q8IUE6.

    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 human and mouse replication-dependent histone genes."
      Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.
      Genomics 80:487-498(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "Nucleosomal histone kinase-1 phosphorylates H2A Thr 119 during mitosis in the early Drosophila embryo."
      Aihara H., Nakagawa T., Yasui K., Ohta T., Hirose S., Dhomae N., Takio K., Kaneko M., Takeshima Y., Muramatsu M., Ito T.
      Genes Dev. 18:877-888(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-121.
    4. "Phosphorylation of histone H2A inhibits transcription on chromatin templates."
      Zhang Y., Griffin K., Mondal N., Parvin J.D.
      J. Biol. Chem. 279:21866-21872(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-2, MUTAGENESIS OF SER-2.
    5. "Role of histone H2A ubiquitination in Polycomb silencing."
      Wang H., Wang L., Erdjument-Bromage H., Vidal M., Tempst P., Jones R.S., Zhang Y.
      Nature 431:873-878(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION AT LYS-120.
    6. "Deimination of histone H2A and H4 at arginine 3 in HL-60 granulocytes."
      Hagiwara T., Hidaka Y., Yamada M.
      Biochemistry 44:5827-5834(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT SER-2, CITRULLINATION AT ARG-4, IDENTIFICATION BY MASS SPECTROMETRY.
    7. "Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing."
      Cao R., Tsukada Y., Zhang Y.
      Mol. Cell 20:845-854(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION AT LYS-120.
    8. Cited for: UBIQUITINATION AT LYS-120.
    9. "RNF8 ubiquitylates histones at DNA double-strand breaks and promotes assembly of repair proteins."
      Mailand N., Bekker-Jensen S., Faustrup H., Melander F., Bartek J., Lukas C., Lukas J.
      Cell 131:887-900(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION.
    10. "RNF8 transduces the DNA-damage signal via histone ubiquitylation and checkpoint protein assembly."
      Huen M.S.Y., Grant R., Manke I., Minn K., Yu X., Yaffe M.B., Chen J.
      Cell 131:901-914(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION.
    11. Cited for: UBIQUITINATION.
    12. "RNF168 binds and amplifies ubiquitin conjugates on damaged chromosomes to allow accumulation of repair proteins."
      Doil C., Mailand N., Bekker-Jensen S., Menard P., Larsen D.H., Pepperkok R., Ellenberg J., Panier S., Durocher D., Bartek J., Lukas J., Lukas C.
      Cell 136:435-446(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "RNF168 ubiquitinates K13-15 on H2A/H2AX to drive DNA Damage signaling."
      Mattiroli F., Vissers J.H., van Dijk W.J., Ikpa P., Citterio E., Vermeulen W., Marteijn J.A., Sixma T.K.
      Cell 150:1182-1195(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION AT LYS-14 AND LYS-16 BY RNF168.
    15. "A novel ubiquitin mark at the N-terminal tail of histone H2As targeted by RNF168 ubiquitin ligase."
      Gatti M., Pinato S., Maspero E., Soffientini P., Polo S., Penengo L.
      Cell Cycle 11:2538-2544(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION AT LYS-14 AND LYS-16 BY RNF168.
    16. "VprBP has intrinsic kinase activity targeting histone H2A and represses gene transcription."
      Kim K., Kim J.M., Kim J.S., Choi J., Lee Y.S., Neamati N., Song J.S., Heo K., An W.
      Mol. Cell 52:459-467(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-121.
    17. "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-105.
    18. Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-53.

    Entry informationi

    Entry nameiH2A2B_HUMAN
    AccessioniPrimary (citable) accession number: Q8IUE6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 7, 2006
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 105 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3