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P62807

- H2B1C_HUMAN

UniProt

P62807 - H2B1C_HUMAN

Protein

Histone H2B type 1-C/E/F/G/I

Gene

HIST1H2BC

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.
    Has broad antibacterial activity. May contribute to the formation of the functional antimicrobial barrier of the colonic epithelium, and to the bactericidal activity of amniotic fluid.

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB

    GO - Biological processi

    1. antibacterial humoral response Source: UniProt
    2. chromatin organization Source: Reactome
    3. defense response to Gram-positive bacterium Source: UniProt
    4. innate immune response in mucosa Source: UniProt
    5. nucleosome assembly Source: UniProtKB

    Keywords - Molecular functioni

    Antibiotic, Antimicrobial

    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 H2B type 1-C/E/F/G/I
    Alternative name(s):
    Histone H2B.1 A
    Histone H2B.a
    Short name:
    H2B/a
    Histone H2B.g
    Short name:
    H2B/g
    Histone H2B.h
    Short name:
    H2B/h
    Histone H2B.k
    Short name:
    H2B/k
    Histone H2B.l
    Short name:
    H2B/l
    Gene namesi
    Name:HIST1H2BC
    Synonyms:H2BFL
    AND
    Name:HIST1H2BE
    Synonyms:H2BFH
    AND
    Name:HIST1H2BF
    Synonyms:H2BFG
    AND
    Name:HIST1H2BG
    Synonyms:H2BFA
    AND
    Name:HIST1H2BI
    Synonyms:H2BFK
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:4757. HIST1H2BC.
    HGNC:4753. HIST1H2BE.
    HGNC:4752. HIST1H2BF.
    HGNC:4746. HIST1H2BG.
    HGNC:4756. HIST1H2BI.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: UniProt
    2. extracellular vesicular exosome Source: UniProt
    3. nucleoplasm Source: Reactome
    4. nucleosome Source: UniProtKB
    5. nucleus Source: UniProt

    Keywords - Cellular componenti

    Chromosome, Nucleosome core, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29132.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed5 Publications
    Chaini2 – 126125Histone H2B type 1-C/E/F/G/IPRO_0000071826Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylprolineBy similarity
    Modified residuei6 – 61N6-acetyllysine; alternate2 Publications
    Modified residuei6 – 61N6-crotonyllysine; alternate1 Publication
    Modified residuei12 – 121N6-acetyllysine; alternate1 Publication
    Modified residuei12 – 121N6-crotonyllysine; alternate1 Publication
    Modified residuei13 – 131N6-acetyllysine; alternate2 Publications
    Modified residuei13 – 131N6-crotonyllysine; alternate1 Publication
    Modified residuei15 – 151Phosphoserine; by STK4/MST11 Publication
    Modified residuei16 – 161N6-acetyllysine; alternate2 Publications
    Modified residuei16 – 161N6-crotonyllysine; alternate1 Publication
    Modified residuei17 – 171N6-acetyllysine; alternate1 Publication
    Modified residuei17 – 171N6-crotonyllysine; alternate1 Publication
    Modified residuei21 – 211N6-acetyllysine; alternate2 Publications
    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); alternate2 Publications
    Modified residuei37 – 371Phosphoserine; by AMPKBy similarity
    Modified residuei47 – 471N6-methyllysine1 Publication
    Modified residuei58 – 581N6,N6-dimethyllysine1 Publication
    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-methyllysine1 Publication
    Glycosylationi113 – 1131O-linked (GlcNAc)1 Publication
    Modified residuei116 – 1161PhosphothreonineBy similarity
    Modified residuei117 – 1171N6-methylated lysineBy similarity
    Cross-linki121 – 121Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)5 Publications

    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.1 Publication
    Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response to stress promotes transcription 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.By similarity1 Publication
    GlcNAcylation at Ser-113 promotes monoubiquitination of Lys-121. It fluctuates in response to extracellular glucose, and associates with transcribed genes.
    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

    MaxQBiP62807.
    PaxDbiP62807.
    PRIDEiP62807.

    PTM databases

    PhosphoSiteiP62807.

    Expressioni

    Gene expression databases

    ArrayExpressiP62807.
    BgeeiP62807.
    CleanExiHS_HIST1H2BC.
    HS_HIST1H2BE.
    HS_HIST1H2BF.
    HS_HIST1H2BG.
    HS_HIST1H2BI.
    GenevestigatoriP62807.

    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

    BioGridi109270. 14 interactions.
    113935. 9 interactions.
    113939. 3 interactions.
    113940. 8 interactions.
    113942. 5 interactions.
    113943. 17 interactions.
    DIPiDIP-32890N.
    IntActiP62807. 19 interactions.
    MINTiMINT-276222.
    STRINGi9606.ENSP00000321744.

    Structurei

    3D structure databases

    ProteinModelPortaliP62807.
    SMRiP62807. Positions 5-126.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histone H2B family.Curated

    Phylogenomic databases

    eggNOGiNOG289161.
    HOGENOMiHOG000231213.
    HOVERGENiHBG007774.
    InParanoidiP62807.
    KOiK11252.
    OMAiNETYSIY.
    OrthoDBiEOG72VH8J.
    PhylomeDBiP62807.
    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.

    P62807-1 [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:March 2, 2010 - v4
    Checksum:iFAE1479F44BE703D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti5 – 51A → S in CAB02545. (PubMed:9119399)Curated
    Sequence conflicti33 – 331S → T in CAB02545. (PubMed:9119399)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti27 – 271G → S.1 Publication
    Corresponds to variant rs7766641 [ dbSNP | Ensembl ].
    VAR_055887

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M60750 Genomic DNA. Translation: AAA63189.1.
    Z80782 Genomic DNA. Translation: CAB02544.1.
    Z80779 Genomic DNA. Translation: CAB02541.1.
    Z80780 Genomic DNA. Translation: CAB02542.1.
    Z80783 Genomic DNA. Translation: CAB02545.1.
    AF531286 Genomic DNA. Translation: AAN06686.1.
    AF531288 Genomic DNA. Translation: AAN06688.1.
    AF531289 Genomic DNA. Translation: AAN06689.1.
    AF531290 Genomic DNA. Translation: AAN06690.1.
    AF531292 Genomic DNA. Translation: AAN06692.1.
    AL031777 Genomic DNA. Translation: CAC03411.1.
    AL031777 Genomic DNA. Translation: CAC03417.1.
    AL031777 Genomic DNA. Translation: CAC03420.1.
    AL353759 Genomic DNA. Translation: CAC04130.1.
    BC001131 mRNA. No translation available.
    BC009612 mRNA. No translation available.
    BC096120 mRNA. Translation: AAH96120.1.
    BC096122 mRNA. Translation: AAH96122.1.
    BC096123 mRNA. Translation: AAH96123.1.
    BC101653 mRNA. Translation: AAI01654.1.
    BC101655 mRNA. Translation: AAI01656.1.
    BC101748 mRNA. Translation: AAI01749.1.
    BC101750 mRNA. Translation: AAI01751.1.
    BC106899 mRNA. Translation: AAI06900.1.
    CCDSiCCDS4584.1.
    CCDS4588.1.
    CCDS4592.1.
    CCDS4594.1.
    CCDS4603.1.
    PIRiE40335. HSHUB2.
    S65409.
    RefSeqiNP_003509.1. NM_003518.3.
    NP_003513.1. NM_003522.3.
    NP_003514.2. NM_003523.2.
    NP_003516.1. NM_003525.2.
    NP_003517.2. NM_003526.2.
    NP_066407.1. NM_021063.3.
    UniGeneiHs.182137.
    Hs.534369.
    Hs.553506.
    Hs.591797.
    Hs.591809.
    Hs.658713.
    Hs.726509.

    Genome annotation databases

    EnsembliENST00000314332; ENSP00000321744; ENSG00000180596.
    ENST00000356530; ENSP00000348924; ENSG00000277224.
    ENST00000396984; ENSP00000380180; ENSG00000180596.
    GeneIDi3017.
    8339.
    8343.
    8344.
    8346.
    8347.
    KEGGihsa:3017.
    hsa:8339.
    hsa:8343.
    hsa:8344.
    hsa:8346.
    hsa:8347.
    UCSCiuc003ngk.4. human.

    Polymorphism databases

    DMDMi290457686.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M60750 Genomic DNA. Translation: AAA63189.1 .
    Z80782 Genomic DNA. Translation: CAB02544.1 .
    Z80779 Genomic DNA. Translation: CAB02541.1 .
    Z80780 Genomic DNA. Translation: CAB02542.1 .
    Z80783 Genomic DNA. Translation: CAB02545.1 .
    AF531286 Genomic DNA. Translation: AAN06686.1 .
    AF531288 Genomic DNA. Translation: AAN06688.1 .
    AF531289 Genomic DNA. Translation: AAN06689.1 .
    AF531290 Genomic DNA. Translation: AAN06690.1 .
    AF531292 Genomic DNA. Translation: AAN06692.1 .
    AL031777 Genomic DNA. Translation: CAC03411.1 .
    AL031777 Genomic DNA. Translation: CAC03417.1 .
    AL031777 Genomic DNA. Translation: CAC03420.1 .
    AL353759 Genomic DNA. Translation: CAC04130.1 .
    BC001131 mRNA. No translation available.
    BC009612 mRNA. No translation available.
    BC096120 mRNA. Translation: AAH96120.1 .
    BC096122 mRNA. Translation: AAH96122.1 .
    BC096123 mRNA. Translation: AAH96123.1 .
    BC101653 mRNA. Translation: AAI01654.1 .
    BC101655 mRNA. Translation: AAI01656.1 .
    BC101748 mRNA. Translation: AAI01749.1 .
    BC101750 mRNA. Translation: AAI01751.1 .
    BC106899 mRNA. Translation: AAI06900.1 .
    CCDSi CCDS4584.1.
    CCDS4588.1.
    CCDS4592.1.
    CCDS4594.1.
    CCDS4603.1.
    PIRi E40335. HSHUB2.
    S65409.
    RefSeqi NP_003509.1. NM_003518.3.
    NP_003513.1. NM_003522.3.
    NP_003514.2. NM_003523.2.
    NP_003516.1. NM_003525.2.
    NP_003517.2. NM_003526.2.
    NP_066407.1. NM_021063.3.
    UniGenei Hs.182137.
    Hs.534369.
    Hs.553506.
    Hs.591797.
    Hs.591809.
    Hs.658713.
    Hs.726509.

    3D structure databases

    ProteinModelPortali P62807.
    SMRi P62807. Positions 5-126.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109270. 14 interactions.
    113935. 9 interactions.
    113939. 3 interactions.
    113940. 8 interactions.
    113942. 5 interactions.
    113943. 17 interactions.
    DIPi DIP-32890N.
    IntActi P62807. 19 interactions.
    MINTi MINT-276222.
    STRINGi 9606.ENSP00000321744.

    PTM databases

    PhosphoSitei P62807.

    Polymorphism databases

    DMDMi 290457686.

    Proteomic databases

    MaxQBi P62807.
    PaxDbi P62807.
    PRIDEi P62807.

    Protocols and materials databases

    DNASUi 8339.
    8344.
    8347.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000314332 ; ENSP00000321744 ; ENSG00000180596 .
    ENST00000356530 ; ENSP00000348924 ; ENSG00000277224 .
    ENST00000396984 ; ENSP00000380180 ; ENSG00000180596 .
    GeneIDi 3017.
    8339.
    8343.
    8344.
    8346.
    8347.
    KEGGi hsa:3017.
    hsa:8339.
    hsa:8343.
    hsa:8344.
    hsa:8346.
    hsa:8347.
    UCSCi uc003ngk.4. human.

    Organism-specific databases

    CTDi 3017.
    8339.
    8343.
    8344.
    8346.
    8347.
    GeneCardsi GC06M026115.
    GC06M026216.
    GC06P026183.
    GC06P026199.
    GC06P026273.
    HGNCi HGNC:4757. HIST1H2BC.
    HGNC:4753. HIST1H2BE.
    HGNC:4752. HIST1H2BF.
    HGNC:4746. HIST1H2BG.
    HGNC:4756. HIST1H2BI.
    MIMi 602798. gene.
    602804. gene.
    602805. gene.
    602807. gene.
    602847. gene.
    neXtProti NX_P62807.
    PharmGKBi PA29132.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG289161.
    HOGENOMi HOG000231213.
    HOVERGENi HBG007774.
    InParanoidi P62807.
    KOi K11252.
    OMAi NETYSIY.
    OrthoDBi EOG72VH8J.
    PhylomeDBi P62807.
    TreeFami TF300212.

    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

    ChiTaRSi HIST1H2BC. human.
    GeneWikii HIST1H2BE.
    HIST1H2BF.
    HIST1H2BG.
    HIST1H2BI.
    Histone_H2B_type_1-C.
    NextBioi 11956.
    PROi P62807.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P62807.
    Bgeei P62807.
    CleanExi HS_HIST1H2BC.
    HS_HIST1H2BE.
    HS_HIST1H2BF.
    HS_HIST1H2BG.
    HS_HIST1H2BI.
    Genevestigatori P62807.

    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. "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] (HIST1H2BG).
    2. "Human histone gene organization: nonregular arrangement within a large cluster."
      Albig W., Kioschis P., Poustka A., Meergans K., Doenecke D.
      Genomics 40:314-322(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H2BC; HIST1H2BE; HIST1H2BF AND HIST1H2BI), VARIANT SER-27.
    3. "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; HIST1H2BF; HIST1H2BG AND HIST1H2BI).
    4. "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] (HIST1H2BC; HIST1H2BE; HIST1H2BF; HIST1H2BG AND HIST1H2BI).
    5. "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].
      Tissue: Lung and Ovary.
    6. "Human spleen histone H2B. Isolation and amino acid sequence."
      Ohe Y., Hayashi H., Iwai K.
      J. Biochem. 85:615-624(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-126.
      Tissue: Spleen.
    7. "Endotoxin-neutralizing antimicrobial proteins of the human placenta."
      Kim H.S., Cho J.H., Park H.W., Yoon H., Kim M.S., Kim S.C.
      J. Immunol. 168:2356-2364(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-21, FUNCTION.
    8. "Biochemical and antibacterial analysis of human wound and blister fluid."
      Frohm M., Gunne H., Bergman A.-C., Agerberth B., Bergman T., Boman A., Liden S., Joernvall H., Boman H.G.
      Eur. J. Biochem. 237:86-92(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-13.
    9. "Antimicrobial peptides in the first line defence of human colon mucosa."
      Tollin M., Bergman P., Svenberg T., Joernvall H., Gudmundsson G.H., Agerberth B.
      Peptides 24:523-530(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-13, FUNCTION.
    10. "Antimicrobial polypeptides of the human colonic epithelium."
      Howell S.J., Wilk D., Yadav S.P., Bevins C.L.
      Peptides 24:1763-1770(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-13, FUNCTION.
    11. "Quantitative proteomic analysis of post-translational modifications of human histones."
      Beck H.C., Nielsen E.C., Matthiesen R., Jensen L.H., Sehested M., Finn P., Grauslund M., Hansen A.M., Jensen O.N.
      Mol. Cell. Proteomics 5:1314-1325(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 7-24, ACETYLATION AT LYS-6; LYS-12; LYS-13; LYS-16; LYS-17 AND LYS-21, METHYLATION AT LYS-47; LYS-58 AND LYS-109, UBIQUITINATION AT LYS-121, IDENTIFICATION BY MASS SPECTROMETRY.
    12. "Apoptotic phosphorylation of histone H2B is mediated by mammalian sterile twenty kinase."
      Cheung W.L., Ajiro K., Samejima K., Kloc M., Cheung P., Mizzen C.A., Beeser A., Etkin L.D., Chernoff J., Earnshaw W.C., Allis C.D.
      Cell 113:507-517(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-15.
    13. "Monoubiquitination of human histone H2B: the factors involved and their roles in HOX gene regulation."
      Zhu B., Zheng Y., Pham A.-D., Mandal S.S., Erdjument-Bromage H., Tempst P., Reinberg D.
      Mol. Cell 20:601-611(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION AT LYS-121.
    14. "Inhibition of core histones acetylation by carcinogenic nickel(II)."
      Golebiowski F., Kasprzak K.S.
      Mol. Cell. Biochem. 279:133-139(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-6; LYS-13; LYS-16 AND LYS-21.
    15. "Histone H2B monoubiquitination functions cooperatively with FACT to regulate elongation by RNA polymerase II."
      Pavri R., Zhu B., Li G., Trojer P., Mandal S., Shilatifard A., Reinberg D.
      Cell 125:703-717(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION AT LYS-121.
    16. "Gene-specific characterization of human histone H2B by electron capture dissociation."
      Siuti N., Roth M.J., Mizzen C.A., Kelleher N.L., Pesavento J.J.
      J. Proteome Res. 5:233-239(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
    17. "The RING finger protein MSL2 in the MOF complex is an E3 ubiquitin ligase for H2B K34 and is involved in crosstalk with H3 K4 and K79 methylation."
      Wu L., Zee B.M., Wang Y., Garcia B.A., Dou Y.
      Mol. Cell 43:132-144(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION AT LYS-35.
    18. Cited for: GLYCOSYLATION AT SER-113, UBIQUITINATION AT LYS-121.
    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-6; LYS-12; LYS-13; LYS-16; LYS-17; LYS-21; LYS-24 AND LYS-35.
    20. "USP49 deubiquitinates histone H2B and regulates cotranscriptional pre-mRNA splicing."
      Zhang Z., Jones A., Joo H.Y., Zhou D., Cao Y., Chen S., Erdjument-Bromage H., Renfrow M., He H., Tempst P., Townes T.M., Giles K.E., Ma L., Wang H.
      Genes Dev. 27:1581-1595(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, DEUBIQUITINATION BY USP49.

    Entry informationi

    Entry nameiH2B1C_HUMAN
    AccessioniPrimary (citable) accession number: P62807
    Secondary accession number(s): P02278
    , Q3B872, Q4VB69, Q93078, Q93080
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: March 2, 2010
    Last modified: October 1, 2014
    This is version 121 of the entry and version 4 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: 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