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B4DR52

- B4DR52_HUMAN

UniProt

B4DR52 - B4DR52_HUMAN

Protein

Histone H2B

Gene
N/A
Organism
Homo sapiens (Human)
Status
Unreviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
  1. Functioni

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. nucleosome assembly Source: InterPro

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone H2BUniRule annotation
    OrganismiHomo sapiens (Human)Imported
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

    Subcellular locationi

    Nucleus UniRule annotation
    Nucleus SAAS annotation. Chromosome SAAS annotation

    GO - Cellular componenti

    1. nucleosome Source: UniProtKB-KW
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Chromosome, Nucleosome coreUniRule annotationSAAS annotation, NucleusUniRule annotationSAAS annotation

    PTM / Processingi

    Keywords - PTMi

    Isopeptide bondSAAS annotation

    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.UniRule annotation

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histone H2B family.UniRule annotation

    Phylogenomic databases

    HOGENOMiHOG000231213.
    HOVERGENiHBG007774.
    OMAiILQGMTA.
    OrthoDBiEOG72VH8J.

    Family and domain databases

    Gene3Di1.10.20.10. 1 hit.
    InterProiIPR009072. Histone-fold.
    IPR007125. Histone_core_D.
    IPR000558. Histone_H2B.
    [Graphical view]
    PANTHERiPTHR23428. PTHR23428. 1 hit.
    PfamiPF00125. Histone. 1 hit.
    [Graphical view]
    PRINTSiPR00621. HISTONEH2B.
    SMARTiSM00427. H2B. 1 hit.
    [Graphical view]
    SUPFAMiSSF47113. SSF47113. 1 hit.
    PROSITEiPS00357. HISTONE_H2B. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    B4DR52-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPDPAKSAPA PKKGSKKAVT KVQKKDGKKR KRSRKESYSV YVYKVLKQVH    50
    PDTGISSKAM GIMNSFVNDI FERIAGEASR LAHYNKRSTI TSREIQTAVR 100
    LLLPGELAKH AVSEGTKAVT KYTSSNPRNL SPTKPGGSED RQPPPSQLSA 150
    IPPFCLVLRA GIAGQV 166
    Length:166
    Mass (Da):18,041
    Last modified:September 23, 2008 - v1
    Checksum:iAEBDFA360570C0DC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK299108 mRNA. Translation: BAG61164.1.
    UniGeneiHs.632451.

    Genome annotation databases

    UCSCiuc010pbk.2. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK299108 mRNA. Translation: BAG61164.1 .
    UniGenei Hs.632451.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    UCSCi uc010pbk.2. human.

    Phylogenomic databases

    HOGENOMi HOG000231213.
    HOVERGENi HBG007774.
    OMAi ILQGMTA.
    OrthoDBi EOG72VH8J.

    Miscellaneous databases

    ChiTaRSi HIST2H2BF. human.
    NextBioi 35474298.

    Family and domain databases

    Gene3Di 1.10.20.10. 1 hit.
    InterProi IPR009072. Histone-fold.
    IPR007125. Histone_core_D.
    IPR000558. Histone_H2B.
    [Graphical view ]
    PANTHERi PTHR23428. PTHR23428. 1 hit.
    Pfami PF00125. Histone. 1 hit.
    [Graphical view ]
    PRINTSi PR00621. HISTONEH2B.
    SMARTi SM00427. H2B. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47113. SSF47113. 1 hit.
    PROSITEi PS00357. HISTONE_H2B. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of histones H2A and H2B variants and their post-translational modifications by mass spectrometry."
      Bonenfant D., Coulot M., Towbin H., Schindler P., van Oostrum J.
      Mol. Cell. Proteomics 5:541-552(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    2. "NEDO human cDNA sequencing project focused on splicing variants."
      Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A., Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y., Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T.
      , Sugano S., Nomura N., Isogai T.
      Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE.
    3. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiB4DR52_HUMAN
    AccessioniPrimary (citable) accession number: B4DR52
    Entry historyi
    Integrated into UniProtKB/TrEMBL: September 23, 2008
    Last sequence update: September 23, 2008
    Last modified: October 1, 2014
    This is version 56 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)
    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.