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Q96A08

- H2B1A_HUMAN

UniProt

Q96A08 - H2B1A_HUMAN

Protein

Histone H2B type 1-A

Gene

HIST1H2BA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Variant histone specifically required to direct the transformation of dissociating nucleosomes to protamine in male germ cells. Entirely replaces classical histone H2B prior nucleosome to protamine transition and probably acts as a nucleosome dissociating factor that creates a more dynamic chromatin, facilitating the large-scale exchange of histones. Also expressed maternally and is present in the female pronucleus, suggesting a similar role in protamine replacement by nucleosomes at fertilization By similarity. Also found in fat cells, its function and the presence of post-translational modifications specific to such cells are still unclear. 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.By similarity1 Publication

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. cellular response to acid chemical Source: Ensembl
    2. chromatin organization Source: Reactome
    3. inflammatory response Source: Ensembl
    4. mononuclear cell migration Source: Ensembl
    5. nucleosome assembly Source: UniProtKB
    6. nucleosome disassembly Source: UniProtKB
    7. plasminogen activation Source: Ensembl
    8. positive regulation of binding Source: Ensembl
    9. spermatogenesis, exchange of chromosomal proteins Source: UniProtKB

    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-A
    Alternative name(s):
    Histone H2B, testis
    Short name:
    TSH2B.1
    Testis-specific histone H2B
    Gene namesi
    Name:HIST1H2BA
    Synonyms:TSH2B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:18730. HIST1H2BA.

    Subcellular locationi

    GO - Cellular componenti

    1. extrinsic component of plasma membrane Source: Ensembl
    2. nucleoplasm Source: Reactome
    3. nucleosome Source: UniProtKB
    4. nucleus Source: UniProt

    Keywords - Cellular componenti

    Chromosome, Nucleosome core, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134937673.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 127126Histone H2B type 1-APRO_0000071842Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylprolineBy similarity
    Modified residuei7 – 71N6-acetyllysine; alternate1 Publication
    Modified residuei7 – 71N6-crotonyllysine; alternate1 Publication
    Modified residuei13 – 131N6-acetyllysine; alternateBy similarity
    Modified residuei13 – 131N6-crotonyllysine; alternate1 Publication
    Modified residuei14 – 141N6-acetyllysine; alternate1 Publication
    Modified residuei14 – 141N6-crotonyllysine; alternate1 Publication
    Modified residuei17 – 171N6-acetyllysine; alternate1 Publication
    Modified residuei17 – 171N6-crotonyllysine; alternate1 Publication
    Modified residuei18 – 181N6-acetyllysine; alternateBy similarity
    Modified residuei18 – 181N6-crotonyllysine; alternate1 Publication
    Modified residuei22 – 221N6-acetyllysine; alternate1 Publication
    Modified residuei22 – 221N6-crotonyllysine; alternate1 Publication
    Modified residuei25 – 251N6-acetyllysine; alternateBy similarity
    Modified residuei25 – 251N6-crotonyllysine; alternate1 Publication
    Modified residuei36 – 361N6-crotonyllysine; alternate1 Publication
    Cross-linki36 – 36Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
    Modified residuei38 – 381PhosphoserineBy similarity
    Modified residuei48 – 481N6-methyllysineBy similarity
    Modified residuei59 – 591N6,N6-dimethyllysineBy similarity
    Modified residuei81 – 811Dimethylated arginine1 Publication
    Modified residuei86 – 861Phosphoserine1 Publication
    Modified residuei87 – 871N6,N6,N6-trimethyllysine; alternate1 Publication
    Modified residuei87 – 871N6-acetyllysine; alternate1 Publication
    Modified residuei88 – 881Omega-N-methylarginine1 Publication
    Modified residuei94 – 941Omega-N-methylarginine1 Publication
    Modified residuei110 – 1101N6-methyllysineBy similarity
    Modified residuei117 – 1171PhosphothreonineBy similarity
    Modified residuei118 – 1181N6-methylated lysineBy similarity
    Cross-linki122 – 122Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications

    Post-translational modificationi

    Monoubiquitination at Lys-36 (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-122 (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
    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
    Acetylated during spermatogenesis. Acetylated form is most abundant in spermatogonia compared to spermatocytes and round spermatids By similarity.By similarity
    Phosphorylated at Thr-117 in spermatogonia, spermatocytes and round spermatids.By similarity
    Methylated at Lys-118 in spermatogonia, spermatocytes and round spermatids.By similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ96A08.
    PaxDbiQ96A08.
    PRIDEiQ96A08.

    PTM databases

    PhosphoSiteiQ96A08.

    Expressioni

    Tissue specificityi

    Mainly expressed in testis, and the corresponding protein is also present in mature sperm (at protein level). Also found in some fat cells.2 Publications

    Gene expression databases

    BgeeiQ96A08.
    CleanExiHS_HIST1H2BA.
    GenevestigatoriQ96A08.

    Organism-specific databases

    HPAiCAB011603.

    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

    BioGridi129111. 17 interactions.
    IntActiQ96A08. 4 interactions.
    MINTiMINT-2813617.
    STRINGi9606.ENSP00000274764.

    Structurei

    Secondary structure

    1
    127
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi40 – 5011
    Helixi58 – 8528
    Beta strandi89 – 913
    Helixi93 – 10311
    Helixi108 – 12417

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3WKJX-ray2.80D/H1-127[»]
    ProteinModelPortaliQ96A08.
    SMRiQ96A08. Positions 6-127.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histone H2B family.Curated

    Phylogenomic databases

    eggNOGiNOG291964.
    HOGENOMiHOG000231213.
    HOVERGENiHBG007774.
    InParanoidiQ96A08.
    KOiK11252.
    OMAiERVSCEA.
    OrthoDBiEOG72VH8J.
    PhylomeDBiQ96A08.
    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.

    Q96A08-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPEVSSKGAT ISKKGFKKAV VKTQKKEGKK RKRTRKESYS IYIYKVLKQV    50
    HPDTGISSKA MSIMNSFVTD IFERIASEAS RLAHYSKRST ISSREIQTAV 100
    RLLLPGELAK HAVSEGTKAV TKYTSSK 127
    Length:127
    Mass (Da):14,167
    Last modified:January 23, 2007 - v3
    Checksum:i3EE4124DA9B3C3E8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21P → A in AAH66243. (PubMed:15489334)Curated
    Sequence conflicti22 – 221K → E in AAH66241. (PubMed:15489334)Curated
    Sequence conflicti80 – 801S → P in AAH66240. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF397301 Genomic DNA. Translation: AAK84040.1.
    AF531284 Genomic DNA. Translation: AAN06684.1.
    AK312055 mRNA. Translation: BAG34991.1.
    AL512384 Genomic DNA. Translation: CAC44615.1.
    CH471087 Genomic DNA. Translation: EAW55490.1.
    BC066238 mRNA. Translation: AAH66238.1.
    BC066239 mRNA. Translation: AAH66239.1.
    BC066240 mRNA. Translation: AAH66240.1.
    BC066241 mRNA. Translation: AAH66241.1.
    BC066242 mRNA. Translation: AAH66242.1.
    BC066243 mRNA. Translation: AAH66243.1.
    CCDSiCCDS4563.1.
    RefSeqiNP_733759.1. NM_170610.2.
    UniGeneiHs.591786.

    Genome annotation databases

    EnsembliENST00000274764; ENSP00000274764; ENSG00000146047.
    GeneIDi255626.
    KEGGihsa:255626.
    UCSCiuc003nfd.3. human.

    Polymorphism databases

    DMDMi51316070.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF397301 Genomic DNA. Translation: AAK84040.1 .
    AF531284 Genomic DNA. Translation: AAN06684.1 .
    AK312055 mRNA. Translation: BAG34991.1 .
    AL512384 Genomic DNA. Translation: CAC44615.1 .
    CH471087 Genomic DNA. Translation: EAW55490.1 .
    BC066238 mRNA. Translation: AAH66238.1 .
    BC066239 mRNA. Translation: AAH66239.1 .
    BC066240 mRNA. Translation: AAH66240.1 .
    BC066241 mRNA. Translation: AAH66241.1 .
    BC066242 mRNA. Translation: AAH66242.1 .
    BC066243 mRNA. Translation: AAH66243.1 .
    CCDSi CCDS4563.1.
    RefSeqi NP_733759.1. NM_170610.2.
    UniGenei Hs.591786.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3WKJ X-ray 2.80 D/H 1-127 [» ]
    ProteinModelPortali Q96A08.
    SMRi Q96A08. Positions 6-127.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 129111. 17 interactions.
    IntActi Q96A08. 4 interactions.
    MINTi MINT-2813617.
    STRINGi 9606.ENSP00000274764.

    PTM databases

    PhosphoSitei Q96A08.

    Polymorphism databases

    DMDMi 51316070.

    Proteomic databases

    MaxQBi Q96A08.
    PaxDbi Q96A08.
    PRIDEi Q96A08.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000274764 ; ENSP00000274764 ; ENSG00000146047 .
    GeneIDi 255626.
    KEGGi hsa:255626.
    UCSCi uc003nfd.3. human.

    Organism-specific databases

    CTDi 255626.
    GeneCardsi GC06P025727.
    HGNCi HGNC:18730. HIST1H2BA.
    HPAi CAB011603.
    MIMi 609904. gene.
    neXtProti NX_Q96A08.
    PharmGKBi PA134937673.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG291964.
    HOGENOMi HOG000231213.
    HOVERGENi HBG007774.
    InParanoidi Q96A08.
    KOi K11252.
    OMAi ERVSCEA.
    OrthoDBi EOG72VH8J.
    PhylomeDBi Q96A08.
    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

    GeneWikii HIST1H2BA.
    GenomeRNAii 255626.
    NextBioi 92610.
    PROi Q96A08.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q96A08.
    CleanExi HS_HIST1H2BA.
    Genevestigatori Q96A08.

    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. "Human testis/sperm-specific histone H2B (hTSH2B). Molecular cloning and characterization."
      Zalensky A.O., Siino J.S., Gineitis A.A., Zalenskaya I.A., Tomilin N.V., Yau P., Bradbury E.M.
      J. Biol. Chem. 277:43474-43480(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
    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. "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: Testis.
    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].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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].
    7. "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-122.
    8. "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-7; LYS-14; LYS-17 AND LYS-22.
    9. "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-122.
    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-7; LYS-13; LYS-14; LYS-17; LYS-18; LYS-22; LYS-25 AND LYS-36.
    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-36.
    12. "Histone variants and their post-translational modifications in primary human fat cells."
      Jufvas A., Stralfors P., Vener A.V.
      PLoS ONE 6:E15960-E15960(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-87, METHYLATION AT ARG-81; LYS-87; ARG-88 AND ARG-94, PHOSPHORYLATION AT SER-86, FUNCTION, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiH2B1A_HUMAN
    AccessioniPrimary (citable) accession number: Q96A08
    Secondary accession number(s): B2R544
    , Q6NZ98, Q6NZA0, Q6NZA1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 103 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, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: 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