Reviewed, UniProtKB/Swiss-Prot P61830 (H3_YEAST)

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	136 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
Subcellular location	Nucleus.
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.13 Ref.15 Ref.31 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.16 Ref.17 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.29 Ref.30 Ref.32 Ref.34 Ref.35 Ref.36 Ref.37 Ref.39 Ref.40 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.
Miscellaneous	Present with 213000 molecules/cell in log phase SD medium. Ref.28
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 refering 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.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Chromosomal protein Nucleosome core Nucleus
Ligand	DNA-binding
PTM	Acetylation Methylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of transposition, RNA-mediated Inferred from mutant phenotype. Source: SGD nucleosome assembly Inferred from electronic annotation. Source: InterPro
Cellular component	nuclear nucleosome Traceable author statement. Source: SGD replication fork protection complex Inferred from direct assay. Source: SGD
Molecular function	DNA binding Traceable author statement. Source: SGD identical protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-8098,EBI-8098
ASF1	P32447	1	EBI-8098,EBI-3003
BDF1	P35817	1	EBI-8098,EBI-3493
FPR4	Q06205	2	EBI-8098,EBI-6956
HHF1	P02309	1	EBI-8098,EBI-8113
HHO1	P53551	1	EBI-8098,EBI-8064
HIF1	Q12373	1	EBI-8098,EBI-31911
HOS2	P53096	2	EBI-8098,EBI-8475
MCM10	P32354	1	EBI-8098,EBI-5965
RPB9	P27999	1	EBI-8098,EBI-15798
SET1	P38827	1	EBI-8098,EBI-16977
SET2	P46995	1	EBI-8098,EBI-16985
SET3	P36124	1	EBI-8098,EBI-16993
STH1	P32597	2	EBI-8098,EBI-18410

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.5 Ref.7

Chain

2 – 136

135

Histone H3

PRO_0000221370

Amino acid modifications

Modified residue

5

1

N6,N6,N6-trimethyllysine; alternate Ref.16 Ref.17 Ref.22 Ref.23 Ref.24 Ref.30 Ref.34 Ref.35 Ref.36 Ref.39 Ref.40

Modified residue

5

1

N6,N6-dimethyllysine; alternate Ref.16 Ref.17 Ref.22 Ref.23 Ref.24 Ref.30 Ref.34 Ref.35 Ref.36 Ref.39 Ref.40

Modified residue

5

1

N6-methyllysine; alternate Ref.16 Ref.17 Ref.22 Ref.23 Ref.24 Ref.30 Ref.34 Ref.35 Ref.36 Ref.39 Ref.40

Modified residue

10

1

N6-acetyllysine; alternate Ref.39 Ref.40 Ref.11 Ref.18

Modified residue

10

1

N6-methyllysine; alternate Ref.40

Modified residue

11

1

Phosphoserine Ref.13 Ref.15 Ref.31

Modified residue

15

1

N6,N6-dimethyllysine; alternate Ref.40

Modified residue

15

1

N6-acetyllysine; alternate Ref.15 Ref.31 Ref.39 Ref.40 Ref.11 Ref.18 Ref.12

Modified residue

19

1

N6-acetyllysine; alternate Ref.39 Ref.40 Ref.11 Ref.18

Modified residue

19

1

N6-methyllysine; alternate Ref.40

Modified residue

24

1

N6-acetyllysine; alternate Ref.40 Ref.18

Modified residue

24

1

N6-methyllysine; alternate Ref.40

Modified residue

28

1

N6,N6,N6-trimethyllysine; alternate Ref.40

Modified residue

28

1

N6,N6-dimethyllysine; alternate Ref.40

Modified residue

28

1

N6-acetyllysine; alternate Ref.40 Ref.18

Modified residue

28

1

N6-methyllysine; alternate Ref.40

Modified residue

37

1

N6,N6,N6-trimethyllysine; alternate Ref.21 Ref.22 Ref.25 Ref.26 Ref.27 Ref.37 Ref.40

Modified residue

37

1

N6,N6-dimethyllysine; alternate Ref.21 Ref.22 Ref.25 Ref.26 Ref.27 Ref.37 Ref.40

Modified residue

37

1

N6-acetyllysine; alternate Ref.40 Ref.8

Modified residue

37

1

N6-methyllysine; alternate Ref.21 Ref.22 Ref.25 Ref.26 Ref.27 Ref.37 Ref.40

Modified residue

57

1

N6-acetyllysine Ref.40 Ref.9 Ref.33 Ref.38 Ref.41

Modified residue

65

1

N6-acetyllysine Ref.40

Modified residue

80

1

N6,N6,N6-trimethyllysine; alternate Ref.19 Ref.20 Ref.22 Ref.29 Ref.32 Ref.40

Modified residue

80

1

N6,N6-dimethyllysine; alternate Ref.19 Ref.20 Ref.22 Ref.29 Ref.32 Ref.40

Modified residue

80

1

N6-methyllysine; alternate Ref.19 Ref.20 Ref.22 Ref.29 Ref.32 Ref.40

Experimental info

Mutagenesis

11

1

S → A: Impairs histone H3 phosphorylation and reduces transcription of some GCN5 regulated genes. Ref.13 Ref.15

Mutagenesis

53

1

R → A, K or Q: Lethal. Ref.9

Mutagenesis

57

1

K → A, Q or R: Increases sensitivity to genotoxic agents inducing DNA breaks during replication. Ref.9 Ref.33 Ref.38

Mutagenesis

80

1

K → A, P or Q: Compromises telomeric silencing. Ref.19 Ref.9

Mutagenesis

119

1

T → A or E: Lethal. Ref.9

Sequence conflict

124

1

D → E AA sequence Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

136

Helix Strand Turn

Details...

Helix

46 – 57

12

Helix

65 – 77

13

Helix

87 – 114

28

Beta strand

118 – 120

3

Helix

122 – 130

9

Sequences

	Sequence		Length	Mass (Da)
	P61830-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: A6115FEB480AC67A	FASTA	136	15,356
	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

References

	« Hide 'large scale' referencesShow '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: 6355483] [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. , 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: 7813418] [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. , 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: 9169873] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HHT2). Strain: ATCC 204508 / S288c.
[4]	"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. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HHT1 AND HHT2). Strain: ATCC 204508 / S288c.
[5]	"The primary structure of yeast histone H3." Brandt W.F., von Holt C. Eur. J. Biochem. 121:501-510(1982) [PubMed: 7035169] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-136.
[6]	"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: 15059259] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-134. Strain: ATCC 204508 / S288c, M13, M14, M22, M32, M34, M5, M8 and YPS163.
[7]	"The occurrence of histone H3 and H4 in yeast." Brandt W.F., von Holt C. FEBS Lett. 65:386-390(1976) [PubMed: 782914] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-16.
[8]	"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: 17189264] [Abstract] Cited for: PROTEIN SEQUENCE OF 28-41, ACETYLATION AT LYS-37.
[9]	"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: 16260619] [Abstract] Cited for: PROTEIN SEQUENCE OF 55-64, ACETYLATION AT LYS-57, MUTAGENESIS OF ARG-53; LYS-57; LYS-80 AND THR-119.
[10]	"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: 9391047] [Abstract] Cited for: IDENTIFICATION IN THE UAF COMPLEX.
[11]	"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: 9606197] [Abstract] Cited for: ACETYLATION AT LYS-10; LYS-15 AND LYS-19.
[12]	"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: 10082517] [Abstract] Cited for: ACETYLATION AT LYS-15.
[13]	"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: 10975519] [Abstract] Cited for: PHOSPHORYLATION AT SER-11 BY IPL1, DEPHOSPHORYLATION BY GLC7, MUTAGENESIS OF SER-11.
[14]	"Steady-state levels of histone acetylation in Saccharomyces cerevisiae." Waterborg J.H. J. Biol. Chem. 275:13007-13011(2000) [PubMed: 10777603] [Abstract] Cited for: ACETYLATION.
[15]	"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: 10911986] [Abstract] Cited for: PHOSPHORYLATION AT SER-11, ACETYLATION AT LYS-15, MUTAGENESIS OF SER-11.
[16]	"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: 11742990] [Abstract] Cited for: METHYLATION AT LYS-5.
[17]	"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: 11751634] [Abstract] Cited for: METHYLATION AT LYS-5.
[18]	"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: 11545749] [Abstract] Cited for: ACETYLATION AT LYS-10; LYS-15; LYS-19; LYS-24 AND LYS-28.
[19]	"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: 12080090] [Abstract] Cited for: METHYLATION AT LYS-80, MUTAGENESIS OF LYS-80.
[20]	"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: 12097318] [Abstract] Cited for: METHYLATION AT LYS-80.
[21]	"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: 11839797] [Abstract] Cited for: METHYLATION AT LYS-37.
[22]	"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: 12152067] [Abstract] Cited for: METHYLATION AT LYS-5; LYS-37 AND LYS-80.
[23]	"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: 12353038] [Abstract] Cited for: METHYLATION AT LYS-5.
[24]	"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: 11752412] [Abstract] Cited for: METHYLATION AT LYS-5.
[25]	"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: 12629047] [Abstract] Cited for: METHYLATION AT LYS-37.
[26]	"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: 12773564] [Abstract] Cited for: METHYLATION AT LYS-37.
[27]	"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: 12917322] [Abstract] Cited for: METHYLATION AT LYS-37.
[28]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[29]	"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: 12574507] [Abstract] Cited for: METHYLATION AT LYS-80.
[30]	"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: 12845608] [Abstract] Cited for: MASS SPECTROMETRY, METHYLATION AT LYS-5.
[31]	"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: 15719021] [Abstract] Cited for: PHOSPHORYLATION AT SER-11, ACETYLATION AT LYS-15.
[32]	"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: 15632126] [Abstract] Cited for: METHYLATION AT LYS-80.
[33]	"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: 15888442] [Abstract] Cited for: ACETYLATION AT LYS-57, MUTAGENESIS OF LYS-57.
[34]	"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: 16185711] [Abstract] Cited for: METHYLATION AT LYS-5.
[35]	"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: 15949446] [Abstract] Cited for: METHYLATION AT LYS-5.
[36]	"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: 16168379] [Abstract] Cited for: METHYLATION AT LYS-5.
[37]	"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: 15798214] [Abstract] Cited for: METHYLATION AT LYS-37.
[38]	"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: 16015338] [Abstract] Cited for: MASS SPECTROMETRY, ACETYLATION AT LYS-57, MUTAGENESIS OF LYS-57.
[39]	"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: 16122352] [Abstract] Cited for: METHYLATION AT LYS-5, ACETYLATION AT LYS-10; LYS-15 AND LYS-19.
[40]	"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: 17194708] [Abstract] Cited for: MASS SPECTROMETRY, 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.
[41]	"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: 17320445] [Abstract] Cited for: MASS SPECTROMETRY, ACETYLATION AT LYS-57.
[42]	"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: 11566884] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF H3 IN NUCLEOSOME COMPLEX.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X00724 Genomic DNA. Translation: CAA25310.1.
X00725 Genomic DNA. Translation: CAA25312.1.
Z35879 Genomic DNA. Translation: CAA84948.1.
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.

PIR

HSBY3. S45265.

RefSeq

NP_009564.1.
NP_014367.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ID3	X-ray	3.10	A/E	2-136	[»]
1M1D	X-ray	2.20	B/D	2-21	[»]
1QSN	X-ray	2.20	B	10-20	[»]
2H2G	X-ray	1.63	B	114-124	[»]
2IDC	X-ray	2.20	A	122-134	[»]
2JMJ	NMR	-	P	2-10	[»]
2RNW	NMR	-	B	2-16	[»]
2RNX	NMR	-	B	32-43	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-417N.

IntAct

P61830. 41 interactions.

STRING

P61830.

Proteomic databases

PRIDE

P61830.

Genome annotation databases

Ensembl

YBR010W; YBR010W; YBR010W; Saccharomyces cerevisiae. [Genome view]
YNL031C; YNL031C; YNL031C; Saccharomyces cerevisiae. [Genome view]

GeneID

852295.
855700.

KEGG

sce:YBR010W.
sce:YNL031C.

Organism-specific databases

CYGD

YBR010w.
YNL031c.

SGD

S000000214. HHT1.
S000004976. HHT2.

Phylogenomic databases

HOGENOM

HBG715487.

OMA

FAMARTK.

OrthoDB

EOG9641V0.

Gene expression databases

ArrayExpress

P61830.

Genevestigator

P61830.

GermOnline

YBR010W. Saccharomyces cerevisiae.
YNL031C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR000164. Histone_H3.
[Graphical view]

Gene3D

G3DSA:1.10.20.10. Histone-fold. 1 hit.

PANTHER

PTHR11426. Histone_H3. 1 hit.

Pfam

PF00125. Histone. 1 hit.
[Graphical view]

PRINTS

PR00622. HISTONEH3.

SMART

SM00428. H3. 1 hit.
[Graphical view]

PROSITE

PS00322. HISTONE_H3_1. 1 hit.
PS00959. HISTONE_H3_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

970949.

Entry information

Entry name

H3_YEAST

Accession

Primary (citable) accession number: P61830
Secondary accession number(s): P02303 , P13996, Q6B1U3, Q6Q7G9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	December 15, 2009
This is version 73 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)