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P02294

- H2B2_YEAST

UniProt

P02294 - H2B2_YEAST

Protein

Histone H2B.2

Gene

HTB2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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.7 Publications

    GO - Molecular functioni

    1. DNA binding Source: SGD
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. chromatin assembly or disassembly Source: SGD
    2. nucleosome assembly Source: InterPro

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-28908-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone H2B.2
    Gene namesi
    Name:HTB2
    Synonyms:H2B2
    Ordered Locus Names:YBL002W
    ORF Names:YBL0104
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome II

    Organism-specific databases

    SGDiS000000098. HTB2.

    Subcellular locationi

    GO - Cellular componenti

    1. nuclear nucleosome Source: SGD
    2. replication fork protection complex Source: SGD

    Keywords - Cellular componenti

    Chromosome, Nucleosome core, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi7 – 82KK → AA: Reduces sumoylation. 1 Publication
    Mutagenesisi11 – 111S → A: Desensitizes cells to H(2)O(2) treatment. 2 Publications
    Mutagenesisi11 – 111S → E: Induces apoptotic-like features including chromatin condensation. 2 Publications
    Mutagenesisi17 – 182KK → AA: Reduces sumoylation. 1 Publication
    Mutagenesisi124 – 1241K → R: Impairs ubiquitin conjugation, DNA double-strand breaks formation during meiosis and histone H3-K79 methylation. 4 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedCurated
    Chaini2 – 131130Histone H2B.2PRO_0000071939Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei7 – 71N6-acetyllysine; alternate2 Publications
    Cross-linki7 – 7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
    Modified residuei8 – 81N6-acetyllysine; alternate2 Publications
    Cross-linki8 – 8Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
    Modified residuei11 – 111Phosphoserine2 Publications
    Modified residuei12 – 121N6-acetyllysine3 Publications
    Modified residuei17 – 171N6-acetyllysine; alternate4 Publications
    Cross-linki17 – 17Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateCurated
    Cross-linki18 – 18Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)Curated
    Cross-linki124 – 124Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)5 Publications

    Post-translational modificationi

    Monoubiquitinated by the RAD6/UBC2-BRE1 complex to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for H3K4me and H3K79me formation. H2BK123ub1 also modulates the formation of double-strand breaks during meiosis and is a prerequisite for DNA-damage checkpoint activation. Deubiquitination is performed by UBP8 in presence of SGF11.
    Phosphorylated by STE20 to form H2BS10ph during progression through meiotic prophase. May be correlated with chromosome condensation. H2BS10ph is also formed after H2O2 treatment, and is a step leading to apoptosis.2 Publications
    Acetylated by GCN5, a component of the SAGA complex, to form H2BK11ac and H2BK16ac. H2BK16ac can also be formed by ESA1, a component of the NuA4 histone acetyltransferase (HAT) complex. Acetylation of N-terminal lysines and particularly formation of H2BK11acK16ac has a positive effect on transcription.4 Publications
    Sumoylation to form H2BK6su or H2BK7su, and probably also H2BK16su or H2BK17su, occurs preferentially near the telomeres and represses gene transcription.2 Publications

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP02294.
    PaxDbiP02294.
    PRIDEiP02294.

    Expressioni

    Gene expression databases

    GenevestigatoriP02294.

    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. Interacts with NAP1.2 Publications

    Protein-protein interaction databases

    BioGridi32700. 202 interactions.
    DIPiDIP-3897N.
    IntActiP02294. 80 interactions.
    MINTiMINT-482371.
    STRINGi4932.YBL002W.

    Structurei

    Secondary structure

    1
    131
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi42 – 498
    Turni50 – 523
    Helixi60 – 8728
    Beta strandi91 – 933
    Helixi95 – 10511
    Helixi109 – 12820

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ID3X-ray3.10D/H2-131[»]
    2FSBmodel-D/H1-131[»]
    4JJNX-ray3.09D/H2-131[»]
    ProteinModelPortaliP02294.
    SMRiP02294. Positions 10-128.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02294.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histone H2B family.Curated

    Phylogenomic databases

    eggNOGiNOG289161.
    GeneTreeiENSGT00730000110319.
    HOGENOMiHOG000231213.
    KOiK11252.
    OMAiANSEGMK.
    OrthoDBiEOG7WHHPK.

    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.

    P02294-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSAAEKKPA SKAPAEKKPA AKKTSTSVDG KKRSKVRKET YSSYIYKVLK    50
    QTHPDTGISQ KSMSILNSFV NDIFERIATE ASKLAAYNKK STISAREIQT 100
    AVRLILPGEL AKHAVSEGTR AVTKYSSSTQ A 131
    Length:131
    Mass (Da):14,237
    Last modified:January 23, 2007 - v2
    Checksum:i3DCC26FF124D71E8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V01308 Genomic DNA. Translation: CAA24615.1.
    Z26494 Genomic DNA. Translation: CAA81268.1.
    Z35763 Genomic DNA. Translation: CAA84817.1.
    AY693063 Genomic DNA. Translation: AAT93082.1.
    BK006936 Genomic DNA. Translation: DAA07120.1.
    PIRiS44558. HSBYB2.
    RefSeqiNP_009553.1. NM_001178242.1.

    Genome annotation databases

    EnsemblFungiiYBL002W; YBL002W; YBL002W.
    GeneIDi852284.
    KEGGisce:YBL002W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V01308 Genomic DNA. Translation: CAA24615.1 .
    Z26494 Genomic DNA. Translation: CAA81268.1 .
    Z35763 Genomic DNA. Translation: CAA84817.1 .
    AY693063 Genomic DNA. Translation: AAT93082.1 .
    BK006936 Genomic DNA. Translation: DAA07120.1 .
    PIRi S44558. HSBYB2.
    RefSeqi NP_009553.1. NM_001178242.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ID3 X-ray 3.10 D/H 2-131 [» ]
    2FSB model - D/H 1-131 [» ]
    4JJN X-ray 3.09 D/H 2-131 [» ]
    ProteinModelPortali P02294.
    SMRi P02294. Positions 10-128.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32700. 202 interactions.
    DIPi DIP-3897N.
    IntActi P02294. 80 interactions.
    MINTi MINT-482371.
    STRINGi 4932.YBL002W.

    Proteomic databases

    MaxQBi P02294.
    PaxDbi P02294.
    PRIDEi P02294.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YBL002W ; YBL002W ; YBL002W .
    GeneIDi 852284.
    KEGGi sce:YBL002W.

    Organism-specific databases

    SGDi S000000098. HTB2.

    Phylogenomic databases

    eggNOGi NOG289161.
    GeneTreei ENSGT00730000110319.
    HOGENOMi HOG000231213.
    KOi K11252.
    OMAi ANSEGMK.
    OrthoDBi EOG7WHHPK.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-28908-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P02294.
    NextBioi 970916.

    Gene expression databases

    Genevestigatori P02294.

    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. "Histone H2B genes of yeast encode two different proteins."
      Wallis J.W., Hereford L., Grunstein M.
      Cell 22:799-805(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Sequence around the centromere of Saccharomyces cerevisiae chromosome II: similarity of CEN2 to CEN4."
      Wolfe K.H., Lohan A.J.E.
      Yeast 10:S41-S46(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. "Complete DNA sequence of yeast chromosome II."
      Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
      , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
      EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    6. "The histones of yeast. The isolation and partial structure of the core histones."
      Brandt W.F., Patterson K., von Holt C.
      Eur. J. Biochem. 110:67-76(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 64-89, PROBABLE CLEAVAGE OF INITIATOR METHIONINE.
    7. "Steady-state levels of histone acetylation in Saccharomyces cerevisiae."
      Waterborg J.H.
      J. Biol. Chem. 275:13007-13011(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION.
    8. "Highly specific antibodies determine histone acetylation site usage in yeast heterochromatin and euchromatin."
      Suka N., Suka Y., Carmen A.A., Wu J., Grunstein M.
      Mol. Cell 8:473-479(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-12 AND LYS-17.
    9. Cited for: FUNCTION, MUTAGENESIS OF LYS-124.
    10. "Transcriptional activation via sequential histone H2B ubiquitylation and deubiquitylation, mediated by SAGA-associated Ubp8."
      Henry K.W., Wyce A., Lo W.-S., Duggan L.J., Emre N.C.T., Kao C.-F., Pillus L., Shilatifard A., Osley M.A., Berger S.L.
      Genes Dev. 17:2648-2663(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, DEUBIQUITINATION BY UBP8.
    11. "A conserved RING finger protein required for histone H2B monoubiquitination and cell size control."
      Hwang W.W., Venkatasubrahmanyam S., Ianculescu A.G., Tong A., Boone C., Madhani H.D.
      Mol. Cell 11:261-266(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION AT LYS-124.
    12. "Bre1, an E3 ubiquitin ligase required for recruitment and substrate selection of Rad6 at a promoter."
      Wood A., Krogan N.J., Dover J., Schneider J., Heidt J., Boateng M.A., Dean K., Golshani A., Zhang Y., Greenblatt J.F., Johnston M., Shilatifard A.
      Mol. Cell 11:267-274(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION AT LYS-124.
    13. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    14. "A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery."
      Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.
      Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-124.
    15. "Mapping global histone acetylation patterns to gene expression."
      Kurdistani S.K., Tavazoie S., Grunstein M.
      Cell 117:721-733(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-12 AND LYS-17.
    16. "Rad6 plays a role in transcriptional activation through ubiquitylation of histone H2B."
      Kao C.-F., Hillyer C., Tsukuda T., Henry K.W., Berger S.L., Osley M.A.
      Genes Dev. 18:184-195(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION BY UBC2, FUNCTION.
    17. "Carbohydrates induce mono-ubiquitination of H2B in yeast."
      Dong L., Xu C.W.
      J. Biol. Chem. 279:1577-1580(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION AT LYS-124, MUTAGENESIS OF LYS-124.
    18. "Global analyses of sumoylated proteins in Saccharomyces cerevisiae. Induction of protein sumoylation by cellular stresses."
      Zhou W., Ryan J.J., Zhou H.
      J. Biol. Chem. 279:32262-32268(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION [LARGE SCALE ANALYSIS].
    19. "Rad6-Bre1-mediated histone H2B ubiquitylation modulates the formation of double-strand breaks during meiosis."
      Yamashita K., Shinohara M., Shinohara A.
      Proc. Natl. Acad. Sci. U.S.A. 101:11380-11385(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, UBIQUITINATION AT LYS-124 BY THE UBC2-BRE1 COMPLEX, MUTAGENESIS OF LYS-124.
    20. "Sterile 20 kinase phosphorylates histone H2B at serine 10 during hydrogen peroxide-induced apoptosis in S. cerevisiae."
      Ahn S.-H., Cheung W.L., Hsu J.-Y., Diaz R.L., Smith M.M., Allis C.D.
      Cell 120:25-36(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-11, MUTAGENESIS OF SER-11, FUNCTION.
    21. "H2B (Ser10) phosphorylation is induced during apoptosis and meiosis in S. cerevisiae."
      Ahn S.-H., Henderson K.A., Keeney S., Allis C.D.
      Cell Cycle 4:780-783(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-11, FUNCTION.
    22. "Histone H2B ubiquitylation is associated with elongating RNA polymerase II."
      Xiao T., Kao C.-F., Krogan N.J., Sun Z.-W., Greenblatt J.F., Osley M.A., Strahl B.D.
      Mol. Cell. Biol. 25:637-651(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION BY THE UBC2-BRE1 COMPLEX, FUNCTION.
    23. "H2B ubiquitin protease Ubp8 and Sgf11 constitute a discrete functional module within the Saccharomyces cerevisiae SAGA complex."
      Ingvarsdottir K., Krogan N.J., Emre N.C.T., Wyce A., Thompson N.J., Emili A., Hughes T.R., Greenblatt J.F., Berger S.L.
      Mol. Cell. Biol. 25:1162-1172(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEUBIQUITINATION BY THE UBP8-SGF11 COMPLEX.
    24. "The deubiquitylation activity of Ubp8 is dependent upon Sgf11 and its association with the SAGA complex."
      Lee K.K., Florens L., Swanson S.K., Washburn M.P., Workman J.L.
      Mol. Cell. Biol. 25:1173-1182(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEUBIQUITINATION BY THE UBP8-SGF11 COMPLEX.
    25. "Histone sumoylation is a negative regulator in Saccharomyces cerevisiae and shows dynamic interplay with positive-acting histone modifications."
      Nathan D., Ingvarsdottir K., Sterner D.E., Bylebyl G.R., Dokmanovic M., Dorsey J.A., Whelan K.A., Krsmanovic M., Lane W.S., Meluh P.B., Johnson E.S., Berger S.L.
      Genes Dev. 20:966-976(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-7; LYS-8; LYS-17 AND LYS-18, ACETYLATION AT LYS-7; LYS-8 AND LYS-17, MUTAGENESIS OF 7-LYS-LYS-8 AND 17-LYS-LYS-18, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY.
    26. "Phosphorylation by casein kinase 2 regulates Nap1 localization and function."
      Calvert M.E.K., Keck K.M., Ptak C., Shabanowitz J., Hunt D.F., Pemberton L.F.
      Mol. Cell. Biol. 28:1313-1325(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NAP1, IDENTIFICATION BY MASS SPECTROMETRY.
    27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions."
      White C.L., Suto R.K., Luger K.
      EMBO J. 20:5207-5218(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF NUCLEOSOME CORE COMPLEX, SUBUNIT.
    29. Cited for: 3D-STRUCTURE MODELING.

    Entry informationi

    Entry nameiH2B2_YEAST
    AccessioniPrimary (citable) accession number: P02294
    Secondary accession number(s): D6VQ00
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 149 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 443000 molecules/cell in log phase SD medium.1 Publication

    Caution

    To ensure consistency between histone entries, we follow the 'Brno' nomenclature for histone modifications, with positions referring to those used in the literature for the 'closest' model organism. Due to slight variations in histone sequences between organisms and to the presence of initiator methionine in UniProtKB/Swiss-Prot sequences, the actual positions of modified amino acids in the sequence generally differ. In this entry the following conventions are used: H2BK6ac = acetylated Lys-7; H2BK6su = sumoylated Lys-7; H2BK7ac = acetylated Lys-8; H2BK7su = sumoylated Lys-8; H2BS10ph = phosphorylated Ser-11; H2BK11ac = acetylated Lys-12; H2BK16ac = acetylated Lys-17; H2BK16su = sumoylated Lys-17; H2BK17su = sumoylated Lys-18; H2BK123ub1 = monoubiquitinated Lys-124.Curated

    Keywords - Technical termi

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

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome II
      Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

    External Data

    Dasty 3