Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q5QNW6

- H2B2F_HUMAN

UniProt

Q5QNW6 - H2B2F_HUMAN

Protein

Histone H2B type 2-F

Gene

HIST2H2BF

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-KW

    GO - Biological processi

    1. chromatin organization Source: Reactome
    2. nucleosome assembly Source: InterPro

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_172610. HATs acetylate histones.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone H2B type 2-F
    Gene namesi
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:24700. HIST2H2BF.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Chromosome, Nucleosome core, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA145148722.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 126125Histone H2B type 2-FPRO_0000244826Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylprolineBy similarity
    Modified residuei6 – 61N6-acetyllysine; alternate1 Publication
    Modified residuei6 – 61N6-crotonyllysine; alternate1 Publication
    Modified residuei12 – 121N6-acetyllysine; alternateBy similarity
    Modified residuei12 – 121N6-crotonyllysine; alternate1 Publication
    Modified residuei13 – 131N6-acetyllysine; alternate1 Publication
    Modified residuei13 – 131N6-crotonyllysine; alternate1 Publication
    Modified residuei15 – 151Phosphoserine; by STK4/MST11 Publication
    Modified residuei16 – 161N6-acetyllysine; alternate1 Publication
    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-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)3 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.
    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

    PaxDbiQ5QNW6.
    PRIDEiQ5QNW6.

    PTM databases

    PhosphoSiteiQ5QNW6.

    Expressioni

    Gene expression databases

    BgeeiQ5QNW6.
    CleanExiHS_HIST2H2BF.
    GenevestigatoriQ5QNW6.

    Organism-specific databases

    HPAiCAB007814.

    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

    BioGridi136811. 8 interactions.
    IntActiQ5QNW6. 7 interactions.
    MINTiMINT-3296686.
    STRINGi9606.ENSP00000358164.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5QNW6.
    SMRiQ5QNW6. Positions 5-126.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histone H2B family.Curated

    Phylogenomic databases

    eggNOGiNOG289161.
    HOGENOMiHOG000231213.
    HOVERGENiHBG007774.
    InParanoidiQ5QNW6.
    KOiK11252.
    PhylomeDBiQ5QNW6.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q5QNW6-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MPDPAKSAPA PKKGSKKAVT KVQKKDGKKR KRSRKESYSV 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:iE951DF3D7E97C106
    GO
    Isoform 2 (identifier: Q5QNW6-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         126-126: K → KLIGPILWK

    Note: No experimental confirmation available.

    Show »
    Length:134
    Mass (Da):14,841
    Checksum:i6F656197FE8FD5E2
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei126 – 1261K → KLIGPILWK in isoform 2. 1 PublicationVSP_043431

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK289664 mRNA. Translation: BAF82353.1.
    AK296916 mRNA. Translation: BAG59471.1.
    AL591493 Genomic DNA. Translation: CAI12558.1.
    BC110793 mRNA. Translation: AAI10794.1.
    CCDSiCCDS30846.1. [Q5QNW6-1]
    CCDS53359.1. [Q5QNW6-2]
    RefSeqiNP_001019770.1. NM_001024599.4. [Q5QNW6-1]
    NP_001154806.1. NM_001161334.1. [Q5QNW6-2]
    XP_006711400.1. XM_006711337.1. [Q5QNW6-1]
    UniGeneiHs.632451.

    Genome annotation databases

    EnsembliENST00000369167; ENSP00000358164; ENSG00000203814. [Q5QNW6-1]
    ENST00000545683; ENSP00000445831; ENSG00000203814. [Q5QNW6-2]
    GeneIDi440689.
    KEGGihsa:440689.
    UCSCiuc001esr.4. human. [Q5QNW6-1]
    uc010pbj.2. human. [Q5QNW6-2]

    Polymorphism databases

    DMDMi74743113.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK289664 mRNA. Translation: BAF82353.1 .
    AK296916 mRNA. Translation: BAG59471.1 .
    AL591493 Genomic DNA. Translation: CAI12558.1 .
    BC110793 mRNA. Translation: AAI10794.1 .
    CCDSi CCDS30846.1. [Q5QNW6-1 ]
    CCDS53359.1. [Q5QNW6-2 ]
    RefSeqi NP_001019770.1. NM_001024599.4. [Q5QNW6-1 ]
    NP_001154806.1. NM_001161334.1. [Q5QNW6-2 ]
    XP_006711400.1. XM_006711337.1. [Q5QNW6-1 ]
    UniGenei Hs.632451.

    3D structure databases

    ProteinModelPortali Q5QNW6.
    SMRi Q5QNW6. Positions 5-126.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 136811. 8 interactions.
    IntActi Q5QNW6. 7 interactions.
    MINTi MINT-3296686.
    STRINGi 9606.ENSP00000358164.

    PTM databases

    PhosphoSitei Q5QNW6.

    Polymorphism databases

    DMDMi 74743113.

    Proteomic databases

    PaxDbi Q5QNW6.
    PRIDEi Q5QNW6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000369167 ; ENSP00000358164 ; ENSG00000203814 . [Q5QNW6-1 ]
    ENST00000545683 ; ENSP00000445831 ; ENSG00000203814 . [Q5QNW6-2 ]
    GeneIDi 440689.
    KEGGi hsa:440689.
    UCSCi uc001esr.4. human. [Q5QNW6-1 ]
    uc010pbj.2. human. [Q5QNW6-2 ]

    Organism-specific databases

    CTDi 440689.
    GeneCardsi GC01M149767.
    HGNCi HGNC:24700. HIST2H2BF.
    HPAi CAB007814.
    neXtProti NX_Q5QNW6.
    PharmGKBi PA145148722.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG289161.
    HOGENOMi HOG000231213.
    HOVERGENi HBG007774.
    InParanoidi Q5QNW6.
    KOi K11252.
    PhylomeDBi Q5QNW6.
    TreeFami TF300212.

    Enzyme and pathway databases

    Reactomei REACT_172610. HATs acetylate histones.

    Miscellaneous databases

    ChiTaRSi HIST2H2BF. human.
    GeneWikii HIST2H2BF.
    GenomeRNAii 440689.
    NextBioi 109448.
    PROi Q5QNW6.

    Gene expression databases

    Bgeei Q5QNW6.
    CleanExi HS_HIST2H2BF.
    Genevestigatori Q5QNW6.

    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. "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] (ISOFORMS 1 AND 2).
      Tissue: Amygdala and Tongue.
    2. "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].
    3. "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] (ISOFORM 1).
      Tissue: Pancreas.
    4. "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.
    5. "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.
    6. "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.
    7. "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.
    8. "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].
    9. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-17 AND LYS-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "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.
    11. "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.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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 nameiH2B2F_HUMAN
    AccessioniPrimary (citable) accession number: Q5QNW6
    Secondary accession number(s): A8K0U9, B4DLA9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 11, 2006
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 94 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3