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Q6ZWY9

- H2B1C_MOUSE

UniProt

Q6ZWY9 - H2B1C_MOUSE

Protein

Histone H2B type 1-C/E/G

Gene

Hist1h2bc

more
Organism
Mus musculus (Mouse)
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_198626. Meiotic synapsis.
    REACT_200667. NoRC negatively regulates rRNA expression.
    REACT_214440. NoRC negatively regulates rRNA expression.
    REACT_226917. HATs acetylate histones.
    REACT_27235. Meiotic Recombination.
    REACT_75800. Meiotic Synapsis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone H2B type 1-C/E/G
    Gene namesi
    Name:Hist1h2bc
    AND
    Name:Hist1h2be
    AND
    Name:Hist1h2bg
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 13

    Organism-specific databases

    MGIiMGI:1915274. Hist1h2bc.
    MGI:2448380. Hist1h2be.
    MGI:2448386. Hist1h2bg.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleoplasm Source: Reactome
    2. nucleosome Source: UniProtKB-KW

    Keywords - Cellular componenti

    Chromosome, Nucleosome core, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 126125Histone H2B type 1-C/E/GPRO_0000244831Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylprolineBy similarity
    Modified residuei6 – 61N6-acetyllysine; alternateBy similarity
    Modified residuei6 – 61N6-crotonyllysine; alternate1 Publication
    Modified residuei12 – 121N6-acetyllysine; alternateBy similarity
    Modified residuei12 – 121N6-crotonyllysine; alternate1 Publication
    Modified residuei13 – 131N6-acetyllysine; alternateBy similarity
    Modified residuei13 – 131N6-crotonyllysine; alternate1 Publication
    Modified residuei15 – 151Phosphoserine; by STK4/MST12 Publications
    Modified residuei16 – 161N6-acetyllysine; alternateBy similarity
    Modified residuei16 – 161N6-crotonyllysine; alternate1 Publication
    Modified residuei17 – 171N6-acetyllysine; alternateBy similarity
    Modified residuei17 – 171N6-crotonyllysine; alternate1 Publication
    Modified residuei21 – 211N6-acetyllysine; alternateBy similarity
    Modified residuei21 – 211N6-crotonyllysine; alternate1 Publication
    Modified residuei24 – 241N6-acetyllysine; alternateBy similarity
    Modified residuei24 – 241N6-crotonyllysine; alternate1 Publication
    Modified residuei35 – 351N6-crotonyllysine; alternate1 Publication
    Cross-linki35 – 35Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
    Modified residuei37 – 371Phosphoserine; by AMPK1 Publication
    Modified residuei47 – 471N6-methyllysineBy similarity
    Modified residuei58 – 581N6,N6-dimethyllysineBy similarity
    Modified residuei80 – 801Dimethylated arginineBy similarity
    Modified residuei86 – 861N6,N6,N6-trimethyllysine; alternateBy similarity
    Modified residuei86 – 861N6-acetyllysine; alternateBy similarity
    Modified residuei87 – 871Omega-N-methylarginineBy similarity
    Modified residuei93 – 931Omega-N-methylarginineBy similarity
    Modified residuei109 – 1091N6-methyllysineBy similarity
    Glycosylationi113 – 1131O-linked (GlcNAc)By similarity
    Modified residuei116 – 1161PhosphothreonineBy similarity
    Modified residuei117 – 1171N6-methylated lysineBy similarity
    Cross-linki121 – 121Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

    Post-translational modificationi

    Monoubiquitination at Lys-35 (H2BK34Ub) by the MSL1/MSL2 dimer is required for histone H3 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) methylation and transcription activation at specific gene loci, such as HOXA9 and MEIS1 loci. Similarly, monoubiquitination at Lys-121 (H2BK120Ub) by the RNF20/40 complex gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation. It also functions cooperatively with the FACT dimer to stimulate elongation by RNA polymerase II. H2BK120Ub also acts as a regulator of mRNA splicing: deubiquitination by USP49 is required for efficient cotranscriptional splicing of a large set of exons By similarity.By similarity
    Phosphorylated on Ser-15 (H2BS14ph) by STK4/MST1 during apoptosis; which facilitates apoptotic chromatin condensation. Also phosphorylated on Ser-15 in response to DNA double strand breaks (DSBs), and in correlation with somatic hypermutation and immunoglobulin class-switch recombination. Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response to stress promotes transcription.3 Publications
    GlcNAcylation at Ser-113 promotes monoubiquitination of Lys-121. It fluctuates in response to extracellular glucose, and associates with transcribed genes By similarity.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, Glycoprotein, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ6ZWY9.
    PRIDEiQ6ZWY9.

    PTM databases

    PhosphoSiteiQ6ZWY9.

    Expressioni

    Gene expression databases

    BgeeiQ6ZWY9.
    CleanExiMM_HIST1H2BC.
    MM_HIST1H2BE.
    GenevestigatoriQ6ZWY9.

    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

    BioGridi212605. 9 interactions.
    235098. 8 interactions.
    235100. 8 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6ZWY9.
    SMRiQ6ZWY9. Positions 5-126.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histone H2B family.Curated

    Phylogenomic databases

    eggNOGiNOG289161.
    GeneTreeiENSGT00690000101835.
    HOGENOMiHOG000231213.
    HOVERGENiHBG007774.
    InParanoidiQ6ZWY9.
    KOiK11252.
    OMAiILQGMTA.
    OrthoDBiEOG72VH8J.
    PhylomeDBiQ6ZWY9.
    TreeFamiTF300212.

    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q6ZWY9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPEPAKSAPA PKKGSKKAVT KAQKKDGKKR KRSRKESYSV YVYKVLKQVH    50
    PDTGISSKAM GIMNSFVNDI FERIAGEASR LAHYNKRSTI TSREIQTAVR 100
    LLLPGELAKH AVSEGTKAVT KYTSSK 126
    Length:126
    Mass (Da):13,906
    Last modified:January 23, 2007 - v3
    Checksum:iFAE1479F44BE703D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY158934 Genomic DNA. Translation: AAO06244.1.
    AY158936 Genomic DNA. Translation: AAO06246.1.
    AY158937 Genomic DNA. Translation: AAO06247.1.
    AK005407 mRNA. Translation: BAB24007.1.
    AK011516 mRNA. Translation: BAB27670.1.
    AK030546 mRNA. Translation: BAC27014.1.
    AK049948 mRNA. Translation: BAC34000.1.
    AL592149 Genomic DNA. Translation: CAI24894.1.
    BC019673 mRNA. Translation: AAH19673.1.
    BC060304 mRNA. Translation: AAH60304.1.
    BC069889 mRNA. Translation: AAH69889.1.
    CCDSiCCDS26349.1.
    CCDS26354.1.
    CCDS26357.1.
    RefSeqiNP_001171124.1. NM_001177653.1.
    NP_001277309.1. NM_001290380.1.
    NP_001277459.1. NM_001290530.1.
    NP_075911.2. NM_023422.3.
    NP_835501.1. NM_178194.4.
    NP_835503.1. NM_178196.4.
    UniGeneiMm.261673.
    Mm.261676.
    Mm.440391.

    Genome annotation databases

    EnsembliENSMUST00000018246; ENSMUSP00000018246; ENSMUSG00000018102.
    ENSMUST00000051091; ENSMUSP00000061247; ENSMUSG00000047246.
    ENSMUST00000079251; ENSMUSP00000078239; ENSMUSG00000058385.
    ENSMUST00000091704; ENSMUSP00000089296; ENSMUSG00000047246.
    GeneIDi319179.
    319181.
    68024.
    KEGGimmu:319179.
    mmu:319181.
    mmu:68024.
    UCSCiuc007pue.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY158934 Genomic DNA. Translation: AAO06244.1 .
    AY158936 Genomic DNA. Translation: AAO06246.1 .
    AY158937 Genomic DNA. Translation: AAO06247.1 .
    AK005407 mRNA. Translation: BAB24007.1 .
    AK011516 mRNA. Translation: BAB27670.1 .
    AK030546 mRNA. Translation: BAC27014.1 .
    AK049948 mRNA. Translation: BAC34000.1 .
    AL592149 Genomic DNA. Translation: CAI24894.1 .
    BC019673 mRNA. Translation: AAH19673.1 .
    BC060304 mRNA. Translation: AAH60304.1 .
    BC069889 mRNA. Translation: AAH69889.1 .
    CCDSi CCDS26349.1.
    CCDS26354.1.
    CCDS26357.1.
    RefSeqi NP_001171124.1. NM_001177653.1.
    NP_001277309.1. NM_001290380.1.
    NP_001277459.1. NM_001290530.1.
    NP_075911.2. NM_023422.3.
    NP_835501.1. NM_178194.4.
    NP_835503.1. NM_178196.4.
    UniGenei Mm.261673.
    Mm.261676.
    Mm.440391.

    3D structure databases

    ProteinModelPortali Q6ZWY9.
    SMRi Q6ZWY9. Positions 5-126.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 212605. 9 interactions.
    235098. 8 interactions.
    235100. 8 interactions.

    PTM databases

    PhosphoSitei Q6ZWY9.

    Proteomic databases

    PaxDbi Q6ZWY9.
    PRIDEi Q6ZWY9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000018246 ; ENSMUSP00000018246 ; ENSMUSG00000018102 .
    ENSMUST00000051091 ; ENSMUSP00000061247 ; ENSMUSG00000047246 .
    ENSMUST00000079251 ; ENSMUSP00000078239 ; ENSMUSG00000058385 .
    ENSMUST00000091704 ; ENSMUSP00000089296 ; ENSMUSG00000047246 .
    GeneIDi 319179.
    319181.
    68024.
    KEGGi mmu:319179.
    mmu:319181.
    mmu:68024.
    UCSCi uc007pue.2. mouse.

    Organism-specific databases

    CTDi 8339.
    8344.
    8347.
    MGIi MGI:1915274. Hist1h2bc.
    MGI:2448380. Hist1h2be.
    MGI:2448386. Hist1h2bg.

    Phylogenomic databases

    eggNOGi NOG289161.
    GeneTreei ENSGT00690000101835.
    HOGENOMi HOG000231213.
    HOVERGENi HBG007774.
    InParanoidi Q6ZWY9.
    KOi K11252.
    OMAi ILQGMTA.
    OrthoDBi EOG72VH8J.
    PhylomeDBi Q6ZWY9.
    TreeFami TF300212.

    Enzyme and pathway databases

    Reactomei REACT_198626. Meiotic synapsis.
    REACT_200667. NoRC negatively regulates rRNA expression.
    REACT_214440. NoRC negatively regulates rRNA expression.
    REACT_226917. HATs acetylate histones.
    REACT_27235. Meiotic Recombination.
    REACT_75800. Meiotic Synapsis.

    Miscellaneous databases

    NextBioi 326230.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q6ZWY9.
    CleanExi MM_HIST1H2BC.
    MM_HIST1H2BE.
    Genevestigatori Q6ZWY9.

    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. "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] (HIST1H2BC; HIST1H2BE AND HIST1H2BG)).
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Hippocampus, Pituitary and Placenta.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. "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].
      Strain: Czech II and FVB/N.
      Tissue: Colon and Mammary tumor.
    5. "Phosphorylation of histone H2B at DNA double-strand breaks."
      Fernandez-Capetillo O., Allis C.D., Nussenzweig A.
      J. Exp. Med. 199:1671-1677(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-15.
    6. "Histone modifications associated with somatic hypermutation."
      Odegard V.H., Kim S.T., Anderson S.M., Shlomchik M.J., Schatz D.G.
      Immunity 23:101-110(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-15.
    7. "Signaling kinase AMPK activates stress-promoted transcription via histone H2B phosphorylation."
      Bungard D., Fuerth B.J., Zeng P.Y., Faubert B., Maas N.L., Viollet B., Carling D., Thompson C.B., Jones R.G., Berger S.L.
      Science 329:1201-1205(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-37.
    8. "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-6; LYS-12; LYS-13; LYS-16; LYS-17; LYS-21; LYS-24 AND LYS-35.

    Entry informationi

    Entry nameiH2B1C_MOUSE
    AccessioniPrimary (citable) accession number: Q6ZWY9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 11, 2006
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 107 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3