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Q16778

- H2B2E_HUMAN

UniProt

Q16778 - H2B2E_HUMAN

Protein

Histone H2B type 2-E

Gene

HIST2H2BE

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 2-E
    Alternative name(s):
    Histone H2B-GL105
    Histone H2B.q
    Short name:
    H2B/q
    Gene namesi
    Name:HIST2H2BE
    Synonyms:H2BFQ
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:4760. HIST2H2BE.

    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

    PharmGKBiPA29135.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 126125Histone H2B type 2-EPRO_0000071835Add
    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)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)4 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 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

    MaxQBiQ16778.
    PaxDbiQ16778.
    PRIDEiQ16778.

    PTM databases

    PhosphoSiteiQ16778.

    Expressioni

    Gene expression databases

    BgeeiQ16778.
    CleanExiHS_HIST2H2BE.
    GenevestigatoriQ16778.

    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

    BioGridi113945. 107 interactions.
    DIPiDIP-39324N.
    IntActiQ16778. 12 interactions.
    MINTiMINT-1461208.
    STRINGi9606.ENSP00000358151.

    Structurei

    Secondary structure

    1
    126
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi39 – 4911
    Helixi57 – 8226
    Helixi92 – 10211
    Helixi105 – 12319

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4NFTX-ray2.61A/B/C/D34-126[»]
    ProteinModelPortaliQ16778.
    SMRiQ16778. Positions 5-126.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histone H2B family.Curated

    Phylogenomic databases

    eggNOGiNOG315146.
    HOGENOMiHOG000231213.
    HOVERGENiHBG007774.
    InParanoidiQ16778.
    KOiK11252.
    OMAiNESENHF.
    OrthoDBiEOG72VH8J.
    PhylomeDBiQ16778.
    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.

    Q16778-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPEPAKSAPA PKKGSKKAVT KAQKKDGKKR KRSRKESYSI YVYKVLKQVH    50
    PDTGISSKAM GIMNSFVNDI FERIAGEASR LAHYNKRSTI TSREIQTAVR 100
    LLLPGELAKH AVSEGTKAVT KYTSSK 126
    Length:126
    Mass (Da):13,920
    Last modified:January 23, 2007 - v3
    Checksum:i0410A881ABBE6647
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti5 – 51A → S in AAH98112. (PubMed:15489334)Curated
    Sequence conflicti5 – 51A → S in AAH98289. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X57985 Genomic DNA. Translation: CAA41051.1.
    AY131979 Genomic DNA. Translation: AAN59961.1.
    CR541895 mRNA. Translation: CAG46693.1.
    AK289725 mRNA. Translation: BAF82414.1.
    AL591493 Genomic DNA. Translation: CAI12568.1.
    CH471121 Genomic DNA. Translation: EAW53605.1.
    BC005827 mRNA. Translation: AAH05827.1.
    BC069193 mRNA. Translation: AAH69193.1.
    BC096121 mRNA. Translation: AAH96121.1.
    BC098112 mRNA. Translation: AAH98112.1.
    BC098289 mRNA. Translation: AAH98289.1.
    BC107084 mRNA. Translation: AAI07085.1.
    BC107085 mRNA. Translation: AAI07086.1.
    M60756 mRNA. Translation: AAA63192.1.
    CCDSiCCDS936.1.
    PIRiI37467.
    S65409.
    RefSeqiNP_003519.1. NM_003528.2.
    UniGeneiHs.2178.

    Genome annotation databases

    EnsembliENST00000369155; ENSP00000358151; ENSG00000184678.
    GeneIDi8349.
    KEGGihsa:8349.
    UCSCiuc001etc.3. human.

    Polymorphism databases

    DMDMi7387736.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X57985 Genomic DNA. Translation: CAA41051.1 .
    AY131979 Genomic DNA. Translation: AAN59961.1 .
    CR541895 mRNA. Translation: CAG46693.1 .
    AK289725 mRNA. Translation: BAF82414.1 .
    AL591493 Genomic DNA. Translation: CAI12568.1 .
    CH471121 Genomic DNA. Translation: EAW53605.1 .
    BC005827 mRNA. Translation: AAH05827.1 .
    BC069193 mRNA. Translation: AAH69193.1 .
    BC096121 mRNA. Translation: AAH96121.1 .
    BC098112 mRNA. Translation: AAH98112.1 .
    BC098289 mRNA. Translation: AAH98289.1 .
    BC107084 mRNA. Translation: AAI07085.1 .
    BC107085 mRNA. Translation: AAI07086.1 .
    M60756 mRNA. Translation: AAA63192.1 .
    CCDSi CCDS936.1.
    PIRi I37467.
    S65409.
    RefSeqi NP_003519.1. NM_003528.2.
    UniGenei Hs.2178.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4NFT X-ray 2.61 A/B/C/D 34-126 [» ]
    ProteinModelPortali Q16778.
    SMRi Q16778. Positions 5-126.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113945. 107 interactions.
    DIPi DIP-39324N.
    IntActi Q16778. 12 interactions.
    MINTi MINT-1461208.
    STRINGi 9606.ENSP00000358151.

    PTM databases

    PhosphoSitei Q16778.

    Polymorphism databases

    DMDMi 7387736.

    Proteomic databases

    MaxQBi Q16778.
    PaxDbi Q16778.
    PRIDEi Q16778.

    Protocols and materials databases

    DNASUi 8349.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000369155 ; ENSP00000358151 ; ENSG00000184678 .
    GeneIDi 8349.
    KEGGi hsa:8349.
    UCSCi uc001etc.3. human.

    Organism-specific databases

    CTDi 8349.
    GeneCardsi GC01M149856.
    H-InvDB HIX0029389.
    HGNCi HGNC:4760. HIST2H2BE.
    MIMi 601831. gene.
    neXtProti NX_Q16778.
    PharmGKBi PA29135.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG315146.
    HOGENOMi HOG000231213.
    HOVERGENi HBG007774.
    InParanoidi Q16778.
    KOi K11252.
    OMAi NESENHF.
    OrthoDBi EOG72VH8J.
    PhylomeDBi Q16778.
    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 HIST2H2BE. human.
    GeneWikii HIST2H2BE.
    GenomeRNAii 8349.
    NextBioi 31268.
    PROi Q16778.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q16778.
    CleanExi HS_HIST2H2BE.
    Genevestigatori Q16778.

    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. "A human histone H2B.1 variant gene, located on chromosome 1, utilizes alternative 3' end processing."
      Collart D., Romain P.L., Huebner K., Pockwinse S., Pilapil S., Cannizzaro L.A., Lian J.B., Croce C.M., Stein J.L., Stein G.S.
      J. Cell. Biochem. 50:374-385(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Lymphocyte.
    2. "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].
    3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    5. "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].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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.
    8. "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.
    9. "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.
    10. "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.
    11. "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.
    12. "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.
    13. "Isolation and characterization of a cDNA from a human histone H2B gene which is reciprocally expressed in relation to replication-dependent H2B histone genes during HL60 cell differentiation."
      Collart D., Ramsey-Ewing A., Bortell R., Lian J., Stein J., Stein G.
      Biochemistry 30:1610-1617(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 26-126.
      Tissue: Liver.
    14. "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.
    15. "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.
    16. "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.
    17. "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.
    18. "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.
    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. "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.
    21. "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 nameiH2B2E_HUMAN
    AccessioniPrimary (citable) accession number: Q16778
    Secondary accession number(s): A3KMC7
    , A8K110, Q4KMY1, Q5QNX0, Q9UE88
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 142 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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