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P61830 (H3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone H3
Gene names
Name:HHT1
Ordered Locus Names:YBR010W
ORF Names:YBR0201
AND
Name:HHT2
Synonyms:SIN2
Ordered Locus Names:YNL031C
ORF Names:N2749
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length136 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Component of the UAF (upstream activation factor) complex which interacts with the upstream element of the RNA polymerase I promoter and forms a stable preinitiation complex. Together with SPT15/TBP, UAF seems to stimulate basal transcription to a fully activated level.

Subunit structure

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. Histone H3 is a component of the UAF (upstream activation factor) complex, which consists of UAF30, RRN5, RRN9, RRN10, and histones H3 and H4. Ref.11

Subcellular location

Nucleus. Chromosome.

Post-translational modification

Phosphorylated by IPL1 to form H3S10ph in a cell cycle-dependent manner during mitosis and meiosis. H3S10ph is also formed by SNF1, promotes subsequent H3K14ac formation by GCN5, and is required for transcriptional activation through TBP recruitment to the promoters. Dephosphorylation is performed by GLC7. Ref.14 Ref.16 Ref.32

Mono-, di- and trimethylated by the COMPASS complex to form H3K4me1/2/3. H3K4me activates gene expression by regulating transcription elongation and plays a role in telomere length maintenance. H3K4me enrichment correlates with transcription levels, and occurs in a 5' to 3' gradient with H3K4me3 enrichment at the 5'-end of genes, shifting to H3K4me2 and then H3K4me1. Methylated by SET2 to form H3K36me. H3K36me represses gene expression. Methylated by DOT1 to form H3K79me. H3K79me is required for association of SIR proteins with telomeric regions and for telomeric silencing. The COMPASS-mediated formation of H3K4me2/3 and the DOT1-mediated formation of H3K79me require H2BK123ub1. Ref.17 Ref.18 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.30 Ref.31 Ref.33 Ref.35 Ref.36 Ref.37 Ref.38 Ref.40 Ref.41

Acetylation of histone H3 leads to transcriptional activation. H3K14ac formation by GCN5, a component of the SAGA complex, is promoted by H3S10ph. Further acetylated by GCN5 to form H3K9ac, H3K18ac, H3K23ac, H3K27ac and H3K36ac. H3K14ac can also be formed by ESA1, a component of the NuA4 histone acetyltransferase (HAT) complex. H3K56ac formation occurs predominantly in newly synthesized H3 molecules during G1, S and G2/M of the cell cycle and may be involved in DNA repair. Ref.9 Ref.10 Ref.12 Ref.13 Ref.15 Ref.16 Ref.19 Ref.32 Ref.34 Ref.39 Ref.40 Ref.41 Ref.42

Miscellaneous

Present with 213000 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the histone H3 family.

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: H3K4me1/2/3 = mono-, di- and trimethylated Lys-5; H3K9ac = acetylated Lys-10; H3K9me1 = monomethylated Lys-10; H3S10ph = phosphorylated Ser-11; H3K14ac = acetylated Lys-15; H3K14me2 = dimethylated Lys-15; H3K18ac = acetylated Lys-19; H3K18me1 = monomethylated Lys-19; H3K23ac = acetylated Lys-24; H3K23me1 = monomethylated Lys-24; H3K27ac = acetylated Lys-28; H3K27me1/2/3 = mono-, di- and trimethylated Lys-28; H3K36ac = acetylated Lys-37; H3K36me1/2/3 = mono-, di- and trimethylated Lys-37; H3K56ac = acetylated Lys-57; H3K64ac = acetylated Lys-65; H3K79me1/2/3 = mono-, di- and trimethylated Lys-80.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6 Ref.8
Chain2 – 136135Histone H3
PRO_0000221370

Amino acid modifications

Modified residue51N6,N6,N6-trimethyllysine; alternate Ref.17 Ref.18 Ref.23 Ref.24 Ref.25 Ref.31 Ref.35 Ref.36 Ref.37 Ref.40 Ref.41
Modified residue51N6,N6-dimethyllysine; alternate Ref.17 Ref.18 Ref.23 Ref.24 Ref.25 Ref.31 Ref.35 Ref.36 Ref.37 Ref.40 Ref.41
Modified residue51N6-methyllysine; alternate Ref.17 Ref.18 Ref.23 Ref.24 Ref.25 Ref.31 Ref.35 Ref.36 Ref.37 Ref.40 Ref.41
Modified residue101N6-acetyllysine; alternate Ref.12 Ref.19 Ref.40 Ref.41
Modified residue101N6-methyllysine; alternate Ref.41
Modified residue111Phosphoserine Ref.14 Ref.16 Ref.32
Modified residue151N6,N6-dimethyllysine; alternate Ref.41
Modified residue151N6-acetyllysine; alternate Ref.12 Ref.13 Ref.16 Ref.19 Ref.32 Ref.40 Ref.41
Modified residue191N6-acetyllysine; alternate Ref.12 Ref.19 Ref.40 Ref.41
Modified residue191N6-methyllysine; alternate Ref.41
Modified residue241N6-acetyllysine; alternate Ref.19 Ref.41
Modified residue241N6-methyllysine; alternate Ref.41
Modified residue281N6,N6,N6-trimethyllysine; alternate Ref.41
Modified residue281N6,N6-dimethyllysine; alternate Ref.41
Modified residue281N6-acetyllysine; alternate Ref.19 Ref.41
Modified residue281N6-methyllysine; alternate Ref.41
Modified residue371N6,N6,N6-trimethyllysine; alternate Ref.22 Ref.23 Ref.26 Ref.27 Ref.28 Ref.38 Ref.41
Modified residue371N6,N6-dimethyllysine; alternate Ref.22 Ref.23 Ref.26 Ref.27 Ref.28 Ref.38 Ref.41
Modified residue371N6-acetyllysine; alternate Ref.9 Ref.41
Modified residue371N6-methyllysine; alternate Ref.22 Ref.23 Ref.26 Ref.27 Ref.28 Ref.38 Ref.41
Modified residue571N6-acetyllysine Ref.10 Ref.34 Ref.39 Ref.41 Ref.42
Modified residue651N6-acetyllysine Ref.41
Modified residue801N6,N6,N6-trimethyllysine; alternate Ref.20 Ref.21 Ref.23 Ref.30 Ref.33 Ref.41
Modified residue801N6,N6-dimethyllysine; alternate Ref.20 Ref.21 Ref.23 Ref.30 Ref.33 Ref.41
Modified residue801N6-methyllysine; alternate Ref.20 Ref.21 Ref.23 Ref.30 Ref.33 Ref.41

Experimental info

Mutagenesis111S → A: Impairs histone H3 phosphorylation and reduces transcription of some GCN5 regulated genes. Ref.14 Ref.16
Mutagenesis531R → A, K or Q: Lethal. Ref.10
Mutagenesis571K → A, Q or R: Increases sensitivity to genotoxic agents inducing DNA breaks during replication. Ref.10 Ref.34 Ref.39
Mutagenesis801K → A, P or Q: Compromises telomeric silencing. Ref.10 Ref.20
Mutagenesis1191T → A or E: Lethal. Ref.10
Sequence conflict1241D → E AA sequence Ref.6

Secondary structure

............... 136
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P61830 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: A6115FEB480AC67A

FASTA13615,356
        10         20         30         40         50         60 
MARTKQTARK STGGKAPRKQ LASKAARKSA PSTGGVKKPH RYKPGTVALR EIRRFQKSTE 

        70         80         90        100        110        120 
LLIRKLPFQR LVREIAQDFK TDLRFQSSAI GALQESVEAY LVSLFEDTNL AAIHAKRVTI 

       130 
QKKDIKLARR LRGERS 

« Hide

References

« Hide 'large scale' references
[1]"DNA sequences of yeast H3 and H4 histone genes from two non-allelic gene sets encode identical H3 and H4 proteins."
Smith M.M., Andresson O.S.
J. Mol. Biol. 169:663-690(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"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. expand/collapse author list , 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] (HHT1).
Strain: ATCC 204508 / S288c.
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. expand/collapse author list , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HHT2).
Strain: ATCC 204508 / S288c.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION (HHT1 AND HHT2).
Strain: ATCC 204508 / S288c.
[5]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HHT1 AND HHT2).
Strain: ATCC 204508 / S288c.
[6]"The primary structure of yeast histone H3."
Brandt W.F., von Holt C.
Eur. J. Biochem. 121:501-510(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-136.
[7]"Population genetic variation in gene expression is associated with phenotypic variation in Saccharomyces cerevisiae."
Fay J.C., McCullough H.L., Sniegowski P.D., Eisen M.B.
Genome Biol. 5:R26.1-R26.14(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-134.
Strain: ATCC 204508 / S288c, M13, M14, M22, M32, M34, M5, M8 and YPS163.
[8]"The occurrence of histone H3 and H4 in yeast."
Brandt W.F., von Holt C.
FEBS Lett. 65:386-390(1976) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-16.
[9]"Identification of histone H3 lysine 36 acetylation as a highly conserved histone modification."
Morris S.A., Rao B., Garcia B.A., Hake S.B., Diaz R.L., Shabanowitz J., Hunt D.F., Allis C.D., Lieb J.D., Strahl B.D.
J. Biol. Chem. 282:7632-7640(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 28-41, ACETYLATION AT LYS-37.
[10]"Insights into the role of histone H3 and histone H4 core modifiable residues in Saccharomyces cerevisiae."
Hyland E.M., Cosgrove M.S., Molina H., Wang D., Pandey A., Cottee R.J., Boeke J.D.
Mol. Cell. Biol. 25:10060-10070(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 55-64, ACETYLATION AT LYS-57, MUTAGENESIS OF ARG-53; LYS-57; LYS-80 AND THR-119.
[11]"Histones H3 and H4 are components of upstream activation factor required for the high-level transcription of yeast rDNA by RNA polymerase I."
Keener J., Dodd J.A., Lalo D., Nomura M.
Proc. Natl. Acad. Sci. U.S.A. 94:13458-13462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE UAF COMPLEX.
[12]"Essential and redundant functions of histone acetylation revealed by mutation of target lysines and loss of the Gcn5p acetyltransferase."
Zhang W., Bone J.R., Edmondson D.G., Turner B.M., Roth S.Y.
EMBO J. 17:3155-3167(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-10; LYS-15 AND LYS-19.
[13]"Esa1p is an essential histone acetyltransferase required for cell cycle progression."
Clarke A.S., Lowell J.E., Jacobson S.J., Pillus L.
Mol. Cell. Biol. 19:2515-2526(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-15.
[14]"Mitotic phosphorylation of histone H3 is governed by Ipl1/aurora kinase and Glc7/PP1 phosphatase in budding yeast and nematodes."
Hsu J.-Y., Sun Z.-W., Li X., Reuben M., Tatchell K., Bishop D.K., Grushcow J.M., Brame C.J., Caldwell J.A., Hunt D.F., Lin R., Smith M.M., Allis C.D.
Cell 102:279-291(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-11 BY IPL1, DEPHOSPHORYLATION BY GLC7, MUTAGENESIS OF SER-11.
[15]"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.
[16]"Phosphorylation of serine 10 in histone H3 is functionally linked in vitro and in vivo to Gcn5-mediated acetylation at lysine 14."
Lo W.-S., Trievel R.C., Rojas J.R., Duggan L., Hsu J.-Y., Allis C.D., Marmorstein R., Berger S.L.
Mol. Cell 5:917-926(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-11, ACETYLATION AT LYS-15, MUTAGENESIS OF SER-11.
[17]"The Saccharomyces cerevisiae Set1 complex includes an Ash2 homologue and methylates histone 3 lysine 4."
Roguev A., Schaft D., Shevchenko A., Pijnappel W.W.M.P., Wilm M., Aasland R., Stewart A.F.
EMBO J. 20:7137-7148(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT LYS-5.
[18]"Histone H3 lysine 4 methylation is mediated by Set1 and required for cell growth and rDNA silencing in Saccharomyces cerevisiae."
Briggs S.D., Bryk M., Strahl B.D., Cheung W.L., Davie J.K., Dent S.Y.R., Winston F., Allis C.D.
Genes Dev. 15:3286-3295(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT LYS-5.
[19]"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-10; LYS-15; LYS-19; LYS-24 AND LYS-28.
[20]"Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein association."
Ng H.H., Feng Q., Wang H., Erdjument-Bromage H., Tempst P., Zhang Y., Struhl K.
Genes Dev. 16:1518-1527(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT LYS-80, MUTAGENESIS OF LYS-80.
[21]"Disruptor of telomeric silencing-1 is a chromatin-specific histone H3 methyltransferase."
Lacoste N., Utley R.T., Hunter J.M., Poirier G.G., Cote J.
J. Biol. Chem. 277:30421-30424(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT LYS-80.
[22]"Set2 is a nucleosomal histone H3-selective methyltransferase that mediates transcriptional repression."
Strahl B.D., Grant P.A., Briggs S.D., Sun Z.-W., Bone J.R., Caldwell J.A., Mollah S., Cook R.G., Shabanowitz J., Hunt D.F., Allis C.D.
Mol. Cell. Biol. 22:1298-1306(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT LYS-37.
[23]"Gene silencing: trans-histone regulatory pathway in chromatin."
Briggs S.D., Xiao T., Sun Z.-W., Caldwell J.A., Shabanowitz J., Hunt D.F., Allis C.D., Strahl B.D.
Nature 418:498-498(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT LYS-5; LYS-37 AND LYS-80.
[24]"Active genes are tri-methylated at K4 of histone H3."
Santos-Rosa H., Schneider R., Bannister A.J., Sherriff J., Bernstein B.E., Emre N.C.T., Schreiber S.L., Mellor J., Kouzarides T.
Nature 419:407-411(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT LYS-5.
[25]"A trithorax-group complex purified from Saccharomyces cerevisiae is required for methylation of histone H3."
Nagy P.L., Griesenbeck J., Kornberg R.D., Cleary M.L.
Proc. Natl. Acad. Sci. U.S.A. 99:90-94(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT LYS-5.
[26]"Phosphorylation of RNA polymerase II CTD regulates H3 methylation in yeast."
Xiao T., Hall H., Kizer K.O., Shibata Y., Hall M.C., Borchers C.H., Strahl B.D.
Genes Dev. 17:654-663(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT LYS-37.
[27]"Methylation of histone H3 by Set2 in Saccharomyces cerevisiae is linked to transcriptional elongation by RNA polymerase II."
Krogan N.J., Kim M., Tong A., Golshani A., Cagney G., Canadien V., Richards D.P., Beattie B.K., Emili A., Boone C., Shilatifard A., Buratowski S., Greenblatt J.
Mol. Cell. Biol. 23:4207-4218(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT LYS-37.
[28]"Set2-catalyzed methylation of histone H3 represses basal expression of GAL4 in Saccharomyces cerevisiae."
Landry J., Sutton A., Hesman T., Min J., Xu R.-M., Johnston M., Sternglanz R.
Mol. Cell. Biol. 23:5972-5978(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT LYS-37.
[29]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[30]"Lysine-79 of histone H3 is hypomethylated at silenced loci in yeast and mammalian cells: a potential mechanism for position-effect variegation."
Ng H.H., Ciccone D.N., Morshead K.B., Oettinger M.A., Struhl K.
Proc. Natl. Acad. Sci. U.S.A. 100:1820-1825(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT LYS-80.
[31]"Saccharomyces cerevisiae Set1p is a methyltransferase specific for lysine 4 of histone H3 and is required for efficient gene expression."
Boa S., Coert C., Patterton H.-G.
Yeast 20:827-835(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT LYS-5, IDENTIFICATION BY MASS SPECTROMETRY.
[32]"Histone H3 phosphorylation can promote TBP recruitment through distinct promoter-specific mechanisms."
Lo W.-S., Gamache E.R., Henry K.W., Yang D., Pillus L., Berger S.L.
EMBO J. 24:997-1008(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-11, ACETYLATION AT LYS-15.
[33]"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: METHYLATION AT LYS-80.
[34]"Characterization of lysine 56 of histone H3 as an acetylation site in Saccharomyces cerevisiae."
Ozdemir A., Spicuglia S., Lasonder E., Vermeulen M., Campsteijn C., Stunnenberg H.G., Logie C.
J. Biol. Chem. 280:25949-25952(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-57, MUTAGENESIS OF LYS-57.
[35]"Histone H3 lysine 4 mono-methylation does not require ubiquitination of histone H2B."
Dehe P.-M., Pamblanco M., Luciano P., Lebrun R., Moinier D., Sendra R., Verreault A., Tordera V., Geli V.
J. Mol. Biol. 353:477-484(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT LYS-5.
[36]"Dynamic lysine methylation on histone H3 defines the regulatory phase of gene transcription."
Morillon A., Karabetsou N., Nair A., Mellor J.
Mol. Cell 18:723-734(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT LYS-5.
[37]"Molecular regulation of histone H3 trimethylation by COMPASS and the regulation of gene expression."
Schneider J., Wood A., Lee J.-S., Schuster R., Dueker J., Maguire C., Swanson S.K., Florens L., Washburn M.P., Shilatifard A.
Mol. Cell 19:849-856(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT LYS-5.
[38]"A novel domain in Set2 mediates RNA polymerase II interaction and couples histone H3 K36 methylation with transcript elongation."
Kizer K.O., Phatnani H.P., Shibata Y., Hall H., Greenleaf A.L., Strahl B.D.
Mol. Cell. Biol. 25:3305-3316(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT LYS-37.
[39]"A role for cell-cycle-regulated histone H3 lysine 56 acetylation in the DNA damage response."
Masumoto H., Hawke D., Kobayashi R., Verreault A.
Nature 436:294-298(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-57, MUTAGENESIS OF LYS-57, IDENTIFICATION BY MASS SPECTROMETRY.
[40]"Single-nucleosome mapping of histone modifications in S. cerevisiae."
Liu C.L., Kaplan T., Kim M., Buratowski S., Schreiber S.L., Friedman N., Rando O.J.
PLoS Biol. 3:1-17(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT LYS-5, ACETYLATION AT LYS-10; LYS-15 AND LYS-19.
[41]"Organismal differences in post-translational modifications in histones H3 and H4."
Garcia B.A., Hake S.B., Diaz R.L., Kauer M., Morris S.A., Recht J., Shabanowitz J., Mishra N., Strahl B.D., Allis C.D., Hunt D.F.
J. Biol. Chem. 282:7641-7655(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-10; LYS-15; LYS-19; LYS-24; LYS-28; LYS-37; LYS-57 AND LYS-65, METHYLATION AT LYS-5; LYS-10; LYS-15; LYS-19; LYS-24; LYS-28; LYS-37 AND LYS-80, IDENTIFICATION BY MASS SPECTROMETRY.
[42]"Histone H3-K56 acetylation is catalyzed by histone chaperone-dependent complexes."
Tsubota T., Berndsen C.E., Erkmann J.A., Smith C.L., Yang L., Freitas M.A., Denu J.M., Kaufman P.D.
Mol. Cell 25:703-712(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-57, IDENTIFICATION BY MASS SPECTROMETRY.
[43]"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 H3 IN NUCLEOSOME COMPLEX.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X00724 Genomic DNA. Translation: CAA25310.1.
X00725 Genomic DNA. Translation: CAA25312.1.
Z35879 Genomic DNA. Translation: CAA84948.1.
Z71306 Genomic DNA. Translation: CAA95893.1.
Z71307 Genomic DNA. Translation: CAA95894.1.
AY558343 Genomic DNA. Translation: AAS56669.1.
AY692987 Genomic DNA. Translation: AAT93006.1.
AY554000 Genomic DNA. Translation: AAS64341.1.
AY554001 Genomic DNA. Translation: AAS64342.1.
AY554002 Genomic DNA. Translation: AAS64343.1.
AY554003 Genomic DNA. Translation: AAS64344.1.
AY554004 Genomic DNA. Translation: AAS64345.1.
AY554005 Genomic DNA. Translation: AAS64346.1.
AY554006 Genomic DNA. Translation: AAS64347.1.
AY554007 Genomic DNA. Translation: AAS64348.1.
AY554008 Genomic DNA. Translation: AAS64349.1.
BK006936 Genomic DNA. Translation: DAA07131.1.
BK006947 Genomic DNA. Translation: DAA10514.1.
PIRHSBY3. S45265.
RefSeqNP_009564.1. NM_001178358.1.
NP_014367.1. NM_001182870.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ID3X-ray3.10A/E2-136[»]
1M1DX-ray2.20B/D2-21[»]
1QSNX-ray2.20B10-20[»]
2H2GX-ray1.63B114-124[»]
2IDCX-ray2.20A122-134[»]
2JMJNMR-P2-10[»]
2RNWNMR-B2-16[»]
2RNXNMR-B32-43[»]
2RSNNMR-B2-18[»]
3MP1X-ray2.60P2-6[»]
3MP6X-ray1.48P2-5[»]
3Q33X-ray2.80D2-15[»]
4JJNX-ray3.09A/E2-136[»]
4KUDX-ray3.20A/E1-136[»]
ProteinModelPortalP61830.
SMRP61830. Positions 2-136.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32711. 719 interactions.
35796. 647 interactions.
DIPDIP-417N.
IntActP61830. 144 interactions.
MINTMINT-702778.

Proteomic databases

PaxDbP61830.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYBR010W; YBR010W; YBR010W.
YNL031C; YNL031C; YNL031C.
GeneID852295.
855700.
KEGGsce:YBR010W.
sce:YNL031C.

Organism-specific databases

SGDS000000214. HHT1.
S000004976. HHT2.

Phylogenomic databases

eggNOGCOG2036.
GeneTreeENSGT00750000117538.
KOK11253.
OMALARRIRX.
OrthoDBEOG7T4MZ6.

Enzyme and pathway databases

BioCycYEAST:G3O-28997-MONOMER.
YEAST:G3O-33068-MONOMER.

Gene expression databases

GenevestigatorP61830.

Family and domain databases

Gene3D1.10.20.10. 1 hit.
InterProIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR000164. Histone_H3.
[Graphical view]
PANTHERPTHR11426. PTHR11426. 1 hit.
PfamPF00125. Histone. 1 hit.
[Graphical view]
PRINTSPR00622. HISTONEH3.
SMARTSM00428. H3. 1 hit.
[Graphical view]
SUPFAMSSF47113. SSF47113. 1 hit.
PROSITEPS00322. HISTONE_H3_1. 1 hit.
PS00959. HISTONE_H3_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP61830.
NextBio970949.

Entry information

Entry nameH3_YEAST
AccessionPrimary (citable) accession number: P61830
Secondary accession number(s): D6VQ11 expand/collapse secondary AC list , E9PAG1, P02303, P13996, Q6B1U3, Q6Q7G9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome II

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

Yeast chromosome XIV

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

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references