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P02294

- H2B2_YEAST

UniProt

P02294 - H2B2_YEAST

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Protein
Histone H2B.2
Gene
HTB2, H2B2, YBL002W, YBL0104
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

GO - Biological processi

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

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
Complete GO annotation...

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 – 11Removed Inferred
Chaini2 – 131130Histone H2B.2
PRO_0000071939Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei7 – 71N6-acetyllysine; alternate1 Publication
Cross-linki7 – 7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate1 Publication
Modified residuei8 – 81N6-acetyllysine; alternate1 Publication
Cross-linki8 – 8Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate1 Publication
Modified residuei11 – 111Phosphoserine2 Publications
Modified residuei12 – 121N6-acetyllysine2 Publications
Modified residuei17 – 171N6-acetyllysine; alternate3 Publications
Cross-linki17 – 17Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate Inferred
Cross-linki18 – 18Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Inferred
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.1 Publication

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

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.

Miscellaneous databases

EvolutionaryTraceiP02294.

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H2B family.

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...

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

« Hide 'large scale' publications
  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: June 11, 2014
This is version 148 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.

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.

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

Similar proteinsi