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P04908

- H2A1B_HUMAN

UniProt

P04908 - H2A1B_HUMAN

Protein

Histone H2A type 1-B/E

Gene

HIST1H2AB

more
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

    GO - Biological processi

    1. nucleosome assembly Source: InterPro

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_169168. Senescence-Associated Secretory Phenotype (SASP).
    REACT_169185. DNA Damage/Telomere Stress Induced Senescence.
    REACT_169436. Oxidative Stress Induced Senescence.
    REACT_172610. HATs acetylate histones.
    REACT_172744. Condensation of Prophase Chromosomes.
    REACT_200753. formation of the beta-catenin:TCF transactivating complex.
    REACT_200808. PRC2 methylates histones and DNA.
    REACT_200827. SIRT1 negatively regulates rRNA Expression.
    REACT_200856. NoRC negatively regulates rRNA expression.
    REACT_2204. RNA Polymerase I Chain Elongation.
    REACT_22186. Deposition of new CENPA-containing nucleosomes at the centromere.
    REACT_2232. RNA Polymerase I Promoter Opening.
    REACT_27271. Meiotic recombination.
    REACT_75792. Meiotic synapsis.
    REACT_75925. Amyloids.
    REACT_7963. Packaging Of Telomere Ends.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone H2A type 1-B/E
    Alternative name(s):
    Histone H2A.2
    Histone H2A/a
    Histone H2A/m
    Gene namesi
    Name:HIST1H2AB
    Synonyms:H2AFM
    AND
    Name:HIST1H2AE
    Synonyms:H2AFA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:4734. HIST1H2AB.
    HGNC:4724. HIST1H2AE.

    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

    PharmGKBiPA29111.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 130129Histone H2A type 1-B/EPRO_0000055237Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine3 Publications
    Modified residuei2 – 21Phosphoserine; by RPS6KA52 Publications
    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 residuei37 – 371N6-crotonyllysine1 Publication
    Modified residuei105 – 1051N5-methylglutamine1 Publication
    Modified residuei119 – 1191N6-crotonyllysine1 Publication
    Modified residuei120 – 1201N6-crotonyllysine; alternate1 Publication
    Cross-linki120 – 120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate3 Publications
    Modified residuei121 – 1211Phosphothreonine; by VPRBP2 Publications
    Modified residuei126 – 1261N6-crotonyllysine1 Publication

    Post-translational modificationi

    Deiminated on Arg-4 in granulocytes upon calcium entry.
    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.6 Publications
    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
    Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes.1 Publication

    Keywords - PTMi

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

    Proteomic databases

    MaxQBiP04908.
    PaxDbiP04908.
    PRIDEiP04908.

    PTM databases

    PhosphoSiteiP04908.

    Expressioni

    Gene expression databases

    ArrayExpressiP04908.
    BgeeiP04908.
    CleanExiHS_HIST1H2AB.
    HS_HIST1H2AE.
    GenevestigatoriP04908.

    Organism-specific databases

    HPAiCAB011483.
    CAB012242.

    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

    BioGridi109266. 16 interactions.
    113931. 30 interactions.
    DIPiDIP-44197N.
    IntActiP04908. 26 interactions.
    MINTiMINT-1139478.
    STRINGi9606.ENSP00000259791.

    Structurei

    Secondary structure

    1
    130
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi18 – 225
    Helixi28 – 369
    Turni37 – 393
    Beta strandi42 – 443
    Helixi47 – 7327
    Beta strandi77 – 793
    Helixi81 – 899
    Helixi92 – 976
    Turni98 – 1003
    Beta strandi101 – 1033
    Helixi114 – 1163

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CV5X-ray2.50C/G1-130[»]
    3A6NX-ray2.70C/G1-130[»]
    3AFAX-ray2.50C/G1-130[»]
    3AN2X-ray3.60C/G1-130[»]
    3AV1X-ray2.50C/G1-130[»]
    3AV2X-ray2.80C/G1-130[»]
    3AYWX-ray2.90C/G1-130[»]
    3AZEX-ray3.00C/G1-130[»]
    3AZFX-ray2.70C/G1-130[»]
    3AZGX-ray2.40C/G1-130[»]
    3AZHX-ray3.49C/G1-130[»]
    3AZIX-ray2.70C/G1-130[»]
    3AZJX-ray2.89C/G1-130[»]
    3AZKX-ray3.20C/G1-130[»]
    3AZLX-ray2.70C/G1-130[»]
    3AZMX-ray2.89C/G1-130[»]
    3AZNX-ray3.00C/G1-130[»]
    3W96X-ray3.00C/G11-130[»]
    3W97X-ray3.20C/G1-130[»]
    3W98X-ray3.42C/G1-130[»]
    3W99X-ray3.00C/G1-130[»]
    3WKJX-ray2.80C/G1-130[»]
    ProteinModelPortaliP04908.
    SMRiP04908. Positions 12-119.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP04908.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histone H2A family.Curated

    Phylogenomic databases

    eggNOGiCOG5262.
    HOGENOMiHOG000234652.
    HOVERGENiHBG009342.
    InParanoidiP04908.
    KOiK11251.
    OMAiTKNAQSR.
    OrthoDBiEOG7M0NTR.
    PhylomeDBiP04908.
    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.

    P04908-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGRGKQGGK ARAKAKTRSS RAGLQFPVGR VHRLLRKGNY SERVGAGAPV    50
    YLAAVLEYLT AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGR 100
    VTIAQGGVLP NIQAVLLPKK TESHHKAKGK 130
    Length:130
    Mass (Da):14,135
    Last modified:January 23, 2007 - v2
    Checksum:i9CFE6184B2CC89F5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti38 – 392GN → AH in CAA24951. (PubMed:6647026)Curated

    Mass spectrometryi

    Molecular mass is 14037.9 Da from positions 2 - 130. Determined by ESI. Monoisotopic with N-acetylserine.1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X00089 Genomic DNA. Translation: CAA24951.1.
    M60752 Genomic DNA. Translation: AAA63191.1.
    Z83741 Genomic DNA. Translation: CAB06036.1.
    AY131983 Genomic DNA. Translation: AAN59964.1.
    AY131986 Genomic DNA. Translation: AAN59967.1.
    AL031777 Genomic DNA. Translation: CAB39192.1.
    BC093836 mRNA. Translation: AAH93836.1.
    BC093862 mRNA. Translation: AAH93862.1.
    CCDSiCCDS4574.1.
    CCDS4595.1.
    PIRiB26318. HSHUA5.
    G40335.
    RefSeqiNP_003504.2. NM_003513.2.
    NP_066390.1. NM_021052.2.
    UniGeneiHs.121017.
    Hs.248174.

    Genome annotation databases

    EnsembliENST00000303910; ENSP00000303373; ENSG00000277075.
    GeneIDi3012.
    8335.
    KEGGihsa:3012.
    hsa:8335.
    UCSCiuc003nft.1. human.

    Polymorphism databases

    DMDMi124028530.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X00089 Genomic DNA. Translation: CAA24951.1 .
    M60752 Genomic DNA. Translation: AAA63191.1 .
    Z83741 Genomic DNA. Translation: CAB06036.1 .
    AY131983 Genomic DNA. Translation: AAN59964.1 .
    AY131986 Genomic DNA. Translation: AAN59967.1 .
    AL031777 Genomic DNA. Translation: CAB39192.1 .
    BC093836 mRNA. Translation: AAH93836.1 .
    BC093862 mRNA. Translation: AAH93862.1 .
    CCDSi CCDS4574.1.
    CCDS4595.1.
    PIRi B26318. HSHUA5.
    G40335.
    RefSeqi NP_003504.2. NM_003513.2.
    NP_066390.1. NM_021052.2.
    UniGenei Hs.121017.
    Hs.248174.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CV5 X-ray 2.50 C/G 1-130 [» ]
    3A6N X-ray 2.70 C/G 1-130 [» ]
    3AFA X-ray 2.50 C/G 1-130 [» ]
    3AN2 X-ray 3.60 C/G 1-130 [» ]
    3AV1 X-ray 2.50 C/G 1-130 [» ]
    3AV2 X-ray 2.80 C/G 1-130 [» ]
    3AYW X-ray 2.90 C/G 1-130 [» ]
    3AZE X-ray 3.00 C/G 1-130 [» ]
    3AZF X-ray 2.70 C/G 1-130 [» ]
    3AZG X-ray 2.40 C/G 1-130 [» ]
    3AZH X-ray 3.49 C/G 1-130 [» ]
    3AZI X-ray 2.70 C/G 1-130 [» ]
    3AZJ X-ray 2.89 C/G 1-130 [» ]
    3AZK X-ray 3.20 C/G 1-130 [» ]
    3AZL X-ray 2.70 C/G 1-130 [» ]
    3AZM X-ray 2.89 C/G 1-130 [» ]
    3AZN X-ray 3.00 C/G 1-130 [» ]
    3W96 X-ray 3.00 C/G 11-130 [» ]
    3W97 X-ray 3.20 C/G 1-130 [» ]
    3W98 X-ray 3.42 C/G 1-130 [» ]
    3W99 X-ray 3.00 C/G 1-130 [» ]
    3WKJ X-ray 2.80 C/G 1-130 [» ]
    ProteinModelPortali P04908.
    SMRi P04908. Positions 12-119.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109266. 16 interactions.
    113931. 30 interactions.
    DIPi DIP-44197N.
    IntActi P04908. 26 interactions.
    MINTi MINT-1139478.
    STRINGi 9606.ENSP00000259791.

    PTM databases

    PhosphoSitei P04908.

    Polymorphism databases

    DMDMi 124028530.

    Proteomic databases

    MaxQBi P04908.
    PaxDbi P04908.
    PRIDEi P04908.

    Protocols and materials databases

    DNASUi 3012.
    8335.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000303910 ; ENSP00000303373 ; ENSG00000277075 .
    GeneIDi 3012.
    8335.
    KEGGi hsa:3012.
    hsa:8335.
    UCSCi uc003nft.1. human.

    Organism-specific databases

    CTDi 3012.
    8335.
    GeneCardsi GC06M026033.
    GC06P026255.
    HGNCi HGNC:4734. HIST1H2AB.
    HGNC:4724. HIST1H2AE.
    HPAi CAB011483.
    CAB012242.
    MIMi 602786. gene.
    602795. gene.
    neXtProti NX_P04908.
    PharmGKBi PA29111.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5262.
    HOGENOMi HOG000234652.
    HOVERGENi HBG009342.
    InParanoidi P04908.
    KOi K11251.
    OMAi TKNAQSR.
    OrthoDBi EOG7M0NTR.
    PhylomeDBi P04908.
    TreeFami TF300137.

    Enzyme and pathway databases

    Reactomei REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
    REACT_169185. DNA Damage/Telomere Stress Induced Senescence.
    REACT_169436. Oxidative Stress Induced Senescence.
    REACT_172610. HATs acetylate histones.
    REACT_172744. Condensation of Prophase Chromosomes.
    REACT_200753. formation of the beta-catenin:TCF transactivating complex.
    REACT_200808. PRC2 methylates histones and DNA.
    REACT_200827. SIRT1 negatively regulates rRNA Expression.
    REACT_200856. NoRC negatively regulates rRNA expression.
    REACT_2204. RNA Polymerase I Chain Elongation.
    REACT_22186. Deposition of new CENPA-containing nucleosomes at the centromere.
    REACT_2232. RNA Polymerase I Promoter Opening.
    REACT_27271. Meiotic recombination.
    REACT_75792. Meiotic synapsis.
    REACT_75925. Amyloids.
    REACT_7963. Packaging Of Telomere Ends.

    Miscellaneous databases

    EvolutionaryTracei P04908.
    GeneWikii HIST1H2AB.
    HIST1H2AE.
    NextBioi 11940.
    PROi P04908.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P04908.
    Bgeei P04908.
    CleanExi HS_HIST1H2AB.
    HS_HIST1H2AE.
    Genevestigatori P04908.

    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 primary structure and expression of four cloned human histone genes."
      Zhong R., Roeder R.G., Heintz N.
      Nucleic Acids Res. 11:7409-7425(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H2AB).
    2. "Isolation and characterization of two human H1 histone genes within clusters of core histone genes."
      Albig W., Kardalinou E., Drabent B., Zimmer A., Doenecke D.
      Genomics 10:940-948(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H2AE).
    3. "The human histone gene cluster at the D6S105 locus."
      Albig W., Doenecke D.
      Hum. Genet. 101:284-294(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H2AE).
    4. "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] (HIST1H2AB AND HIST1H2AE).
    5. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (HIST1H2AE).
      Tissue: Liver.
    7. "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.
    8. "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.
    9. "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.
    10. "Global regulation of post-translational modifications on core histones."
      Galasinski S.C., Louie D.F., Gloor K.K., Resing K.A., Ahn N.G.
      J. Biol. Chem. 277:2579-2588(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT SER-2, ACETYLATION AT SER-2.
    11. "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.
    12. "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.
    13. Cited for: UBIQUITINATION AT LYS-120.
    14. "Precise characterization of human histones in the H2A gene family by top down mass spectrometry."
      Boyne M.T. II, Pesavento J.J., Mizzen C.A., Kelleher N.L.
      J. Proteome Res. 5:248-253(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: MASS SPECTROMETRY, ACETYLATION AT SER-2.
    15. "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.
    16. "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.
    17. Cited for: UBIQUITINATION.
    18. "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.
    19. "Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification."
      Tan M., Luo H., Lee S., Jin F., Yang J.S., Montellier E., Buchou T., Cheng Z., Rousseaux S., Rajagopal N., Lu Z., Ye Z., Zhu Q., Wysocka J., Ye Y., Khochbin S., Ren B., Zhao Y.
      Cell 146:1016-1028(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: CROTONYLATION AT LYS-37; LYS-119; LYS-120 AND LYS-126.
    20. "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.
    21. "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.
    22. "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.
    23. "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.

    Entry informationi

    Entry nameiH2A1B_HUMAN
    AccessioniPrimary (citable) accession number: P04908
    Secondary accession number(s): P28001, Q76P63
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 152 of the entry and version 2 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3