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P02293

- H2B1_YEAST

UniProt

P02293 - H2B1_YEAST

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Protein

Histone H2B.1

Gene

HTB1

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.9 Publications

GO - Molecular functioni

  1. DNA binding Source: SGD

GO - Biological processi

  1. chromatin assembly or disassembly Source: SGD
  2. negative regulation of transcription from RNA polymerase II promoter Source: SGD
  3. postreplication repair Source: SGD
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29804-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H2B.1
Alternative name(s):
Suppressor of Ty protein 12
Gene namesi
Name:HTB1
Synonyms:H2B1, SPT12
Ordered Locus Names:YDR224C
ORF Names:YD9934.09C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

SGDiS000002632. HTB1.

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. 1 Publication
Mutagenesisi11 – 111S → E: Induces apoptotic-like features including chromatin condensation. 1 Publication
Mutagenesisi17 – 182KK → AA: Reduces sumoylation. 1 Publication
Mutagenesisi48 – 481V → F: Confers UV-radiation sensitivity; when associated with F-87 and S-88. 1 Publication
Mutagenesisi87 – 871Y → F: Confers UV-radiation sensitivity; when associated with F-48 and S-88. 1 Publication
Mutagenesisi88 – 881N → S: Confers UV-radiation sensitivity; when associated with F-48 and F-87. 1 Publication
Mutagenesisi124 – 1241K → R: Impairs ubiquitin conjugation, DNA double-strand brakes formation during meiosis and histone H3-K79 methylation. 5 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedCurated
Chaini2 – 131130Histone H2B.1PRO_0000071938Add
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); alternate
Modified residuei8 – 81N6-acetyllysine; alternate1 Publication
Cross-linki8 – 8Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
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); 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)6 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

PRIDEiP02293.

Expressioni

Gene expression databases

GenevestigatoriP02293.

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
STH1P325973EBI-8088,EBI-18410
SWR1Q054712EBI-8088,EBI-22102

Protein-protein interaction databases

BioGridi32276. 381 interactions.
DIPiDIP-416N.
IntActiP02293. 224 interactions.
MINTiMINT-564492.
STRINGi4932.YDR224C.

Structurei

Secondary structure

1
131
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi42 – 5211Combined sources
Beta strandi57 – 593Combined sources
Helixi60 – 8728Combined sources
Beta strandi91 – 933Combined sources
Helixi95 – 10511Combined sources
Helixi108 – 12720Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JSSNMR-A37-131[»]
4KUDX-ray3.20D/H1-131[»]
4M6BX-ray1.78A/D37-131[»]
ProteinModelPortaliP02293.
SMRiP02293. Positions 10-128.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02293.

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H2B family.Curated

Phylogenomic databases

GeneTreeiENSGT00730000110319.
HOGENOMiHOG000231213.
InParanoidiP02293.
KOiK11252.
OMAiMSAKAEK.
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.

P02293-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSAKAEKKPA SKAPAEKKPA AKKTSTSTDG KKRSKARKET YSSYIYKVLK
60 70 80 90 100
QTHPDTGISQ KSMSILNSFV NDIFERIATE ASKLAAYNKK STISAREIQT
110 120 130
AVRLILPGEL AKHAVSEGTR AVTKYSSSTQ A
Length:131
Mass (Da):14,252
Last modified:January 23, 2007 - v2
Checksum:i9F5E9CFB341DB399
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01327 Genomic DNA. Translation: AAA88719.1.
U13239 Genomic DNA. Translation: AAC33141.1.
Z48612 Genomic DNA. Translation: CAA88504.1.
AY557724 Genomic DNA. Translation: AAS56050.1.
M37743 mRNA. Translation: AAA34694.2.
BK006938 Genomic DNA. Translation: DAA12066.1.
PIRiA02621. HSBY22.
RefSeqiNP_010510.3. NM_001180532.3.

Genome annotation databases

EnsemblFungiiYDR224C; YDR224C; YDR224C.
GeneIDi851810.
KEGGisce:YDR224C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01327 Genomic DNA. Translation: AAA88719.1 .
U13239 Genomic DNA. Translation: AAC33141.1 .
Z48612 Genomic DNA. Translation: CAA88504.1 .
AY557724 Genomic DNA. Translation: AAS56050.1 .
M37743 mRNA. Translation: AAA34694.2 .
BK006938 Genomic DNA. Translation: DAA12066.1 .
PIRi A02621. HSBY22.
RefSeqi NP_010510.3. NM_001180532.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2JSS NMR - A 37-131 [» ]
4KUD X-ray 3.20 D/H 1-131 [» ]
4M6B X-ray 1.78 A/D 37-131 [» ]
ProteinModelPortali P02293.
SMRi P02293. Positions 10-128.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32276. 381 interactions.
DIPi DIP-416N.
IntActi P02293. 224 interactions.
MINTi MINT-564492.
STRINGi 4932.YDR224C.

Proteomic databases

PRIDEi P02293.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YDR224C ; YDR224C ; YDR224C .
GeneIDi 851810.
KEGGi sce:YDR224C.

Organism-specific databases

SGDi S000002632. HTB1.

Phylogenomic databases

GeneTreei ENSGT00730000110319.
HOGENOMi HOG000231213.
InParanoidi P02293.
KOi K11252.
OMAi MSAKAEK.
OrthoDBi EOG7WHHPK.

Enzyme and pathway databases

BioCyci YEAST:G3O-29804-MONOMER.

Miscellaneous databases

EvolutionaryTracei P02293.
NextBioi 969662.

Gene expression databases

Genevestigatori P02293.

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. "Insertion site specificity of the transposon Tn3."
    Davies C.J., Hutchison C.A. III
    Nucleic Acids Res. 23:507-514(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [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. "Coding and noncoding sequences at the 3' end of yeast histone H2B mRNA confer cell cycle regulation."
    Xu H., Johnson L., Grunstein M.
    Mol. Cell. Biol. 10:2687-2694(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 115-131.
  8. "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.
  9. "Rad6-dependent ubiquitination of histone H2B in yeast."
    Robzyk K., Recht J., Osley M.A.
    Science 287:501-504(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION AT LYS-124, MUTAGENESIS OF LYS-124.
  10. "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.
  11. "A role for histone H2B during repair of UV-induced DNA damage in Saccharomyces cerevisiae."
    Martini E.M.D., Keeney S., Osley M.A.
    Genetics 160:1375-1387(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF VAL-48; TYR-87 AND ASN-88.
  12. Cited for: FUNCTION, MUTAGENESIS OF LYS-124.
  13. "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.
  14. "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.
  15. "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.
  16. "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.
  17. "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.
  18. "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.
  19. "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].
  20. "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.
  21. "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.
  22. "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.
  23. "The DNA damage checkpoint response requires histone H2B ubiquitination by Rad6-Bre1 and H3 methylation by Dot1."
    Giannattasio M., Lazzaro F., Plevani P., Muzi-Falconi M.
    J. Biol. Chem. 280:9879-9886(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF LYS-124.
  24. "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.
  25. "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.
  26. "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.
  27. "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.
  28. "A tandem affinity tag for two-step purification under fully denaturing conditions: application in ubiquitin profiling and protein complex identification combined with in vivocross-linking."
    Tagwerker C., Flick K., Cui M., Guerrero C., Dou Y., Auer B., Baldi P., Huang L., Kaiser P.
    Mol. Cell. Proteomics 5:737-748(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION AT LYS-124.
  29. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  30. "NMR structure of chaperone Chz1 complexed with histones H2A.Z-H2B."
    Zhou Z., Feng H., Hansen D.F., Kato H., Luk E., Freedberg D.I., Kay L.E., Wu C., Bai Y.
    Nat. Struct. Mol. Biol. 15:868-869(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 37-131.

Entry informationi

Entry nameiH2B1_YEAST
AccessioniPrimary (citable) accession number: P02293
Secondary accession number(s): D6VSK6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 150 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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 IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3