P32561 (RPD3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone deacetylase RPD3
EC=3.5.1.98

Alternative name(s):
Transcriptional regulatory protein RPD3

Gene names

Name:	RPD3
Synonyms:	MOF6, REC3, SDI2, SDS6
Ordered Locus Names:	YNL330C
ORF Names:	N0305

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	433 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalytic component of the RPD3 histone deacetylase (HDAC) complexes RPD3C(L) and RPD3C(S) responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation plays an important role in transcriptional regulation, cell cycle progression, DNA damage response, osmotic stress response and developmental events. Is involved in rDNA and telomere silencing and in double strand breaks repair. Required for both full transcription repression and activation of many genes including cell type-specific genes (STE6, TY2 and HO), cell differentiation-specific genes (SPO13), genes that respond to external signals (PHO5) and TRK2. The RPD3 complexes regulate also chromosomal replication timing. Ref.1 Ref.7 Ref.8 Ref.11 Ref.12 Ref.14 Ref.15 Ref.16 Ref.18 Ref.19 Ref.22 Ref.23 Ref.25 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.34
Catalytic activity	Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.
Subunit structure	Component of the RPD3C(L) complex composed of at least ASH1, CTI6, DEP1, PHO23, RPD3, RXT2, RXT3, SAP30, SDS3, SIN3, UME1 and UME6. Component of the RPD3C(S) complex composed of at least EAF3, RCO1, RPD3, SIN3, and UME1. Interacts with cyclophilins CPR1, CPR6 and CPR7, with the kinase HOG1, and with ESS1, CYC8 and HAC1. Ref.8 Ref.9 Ref.10 Ref.17 Ref.20 Ref.24 Ref.28 Ref.31 Ref.33 Ref.34
Subcellular location	Cytoplasm. Nucleus Ref.26.
Domain	The ESA1-RPD3 (ER) motif is common to ESA1 and RPD3 and is required for ESA1 histone acetyl-transferase (HAT) activity and RPD3 histone deacetylase (HDAC) activity. Ref.21
Miscellaneous	Present with 3850 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the histone deacetylase family. HD type 1 subfamily.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Molecular function	Chromatin regulator Hydrolase Repressor
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	histone H3 deacetylation Inferred from mutant phenotype Ref.8. Source: SGD histone H4 deacetylation Inferred from mutant phenotype Ref.8Ref.13. Source: SGD negative regulation of chromatin silencing at rDNA Inferred from mutant phenotype PubMed 10082585Ref.15PubMed 10512855. Source: SGD negative regulation of chromatin silencing at silent mating-type cassette Inferred from mutant phenotype Ref.15PubMed 10512855PubMed 19372273. Source: SGD negative regulation of chromatin silencing at telomere Inferred from direct assay PubMed 20133733. Source: SGD negative regulation of reciprocal meiotic recombination Inferred from mutant phenotype PubMed 18515193. Source: SGD negative regulation of transcription during meiosis Inferred from mutant phenotype PubMed 17158929. Source: SGD negative regulation of transcription from RNA polymerase I promoter Inferred from mutant phenotype PubMed 14609951PubMed 19270272. Source: SGD negative regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype Ref.28Ref.33PubMed 17121596. Source: SGD positive regulation of macroautophagy Inferred from mutant phenotype PubMed 22539722. Source: SGD positive regulation of transcription from RNA polymerase II promoter in response to heat stress Inferred from mutant phenotype PubMed 20398213. Source: SGD protein localization to nucleolar rDNA repeats Inferred from mutant phenotype PubMed 17203076. Source: SGD regulation of DNA-dependent DNA replication initiation Inferred from mutant phenotype PubMed 12453428Ref.29PubMed 19417103. Source: SGD regulation of transcription by chromatin organization Inferred from mutant phenotype PubMed 11867538Ref.12. Source: SGD regulation of transcription involved in G1/S phase of mitotic cell cycle Inferred from genetic interaction PubMed 19823668. Source: SGD regulation of transcription involved in G2/M-phase of mitotic cell cycle Inferred from genetic interaction PubMed 17908798. Source: SGD regulation of transcription involved in S phase of mitotic cell cycle Inferred from mutant phenotype PubMed 18408055. Source: SGD replicative cell aging Inferred from mutant phenotype PubMed 10512855. Source: SGD transcription elongation from RNA polymerase II promoter Inferred from genetic interaction PubMed 19948887. Source: SGD
Cellular_component	Rpd3L complex Inferred from direct assay PubMed 16286007Ref.34Ref.33PubMed 19040720. Source: SGD Rpd3L-Expanded complex Inferred from direct assay PubMed 19040720. Source: SGD Rpd3S complex Inferred from direct assay PubMed 16286007Ref.34. Source: SGD Snt2C complex Inferred from direct assay PubMed 19040720. Source: SGD cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	NAD-dependent histone deacetylase activity (H3-K14 specific) Inferred from electronic annotation. Source: EC NAD-dependent histone deacetylase activity (H3-K18 specific) Inferred from electronic annotation. Source: EC NAD-dependent histone deacetylase activity (H3-K9 specific) Inferred from electronic annotation. Source: EC NAD-dependent histone deacetylase activity (H4-K16 specific) Inferred from electronic annotation. Source: EC histone deacetylase activity Inferred from direct assay Ref.21. Source: SGD transcription coactivator activity Inferred from mutant phenotype Ref.31. Source: SGD transcription corepressor activity Inferred from mutant phenotype PubMed 9150136. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CPR6	P53691	2	EBI-15864,EBI-5429
CPR7	P47103	2	EBI-15864,EBI-5436
CYC8	P14922	6	EBI-15864,EBI-18215
HOT1	Q03213	3	EBI-15864,EBI-27376
RXT2	P38255	6	EBI-15864,EBI-21537
SIN3	P22579	11	EBI-15864,EBI-17160
TUP1	P16649	2	EBI-15864,EBI-19654

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 433	433	Histone deacetylase RPD3		PRO_0000114724
Regions
	Region	19 – 331	313	Histone deacetylase
	Motif	320 – 340	21	ESA1-RPD3 motif
Sites
	Active site	151	1	Probable
Amino acid modifications
	Modified residue	6	1	Phosphothreonine Ref.37
	Modified residue	388	1	Phosphoserine Ref.37
	Modified residue	394	1	Phosphothreonine Ref.35 Ref.36 Ref.37
	Modified residue	408	1	Phosphoserine Ref.36 Ref.37
Experimental info
	Mutagenesis	150	1	H → A: Impairs histone deacetylase activity and transcription repression. Ref.11
	Mutagenesis	151	1	H → A: Impairs histone deacetylase activity and transcription repression. Ref.11
	Mutagenesis	188	1	H → A: Impairs histone deacetylase activity and transcription repression. Ref.11
	Mutagenesis	322	1	W → A: Reduces strongly HDAC activity. Ref.21
	Mutagenesis	325	1	E → A: Reduces strongly HDAC activity. Ref.21
	Mutagenesis	327	1	G → A: Reduces strongly HDAC activity. Ref.21
	Mutagenesis	328	1	L → A: Reduces strongly HDAC activity. Ref.21
	Mutagenesis	329	1	L → A: Reduces strongly HDAC activity. Ref.21
	Mutagenesis	332	1	V → A: Reduces strongly HDAC activity. Ref.21
	Mutagenesis	334	1	L → A: Reduces strongly HDAC activity. Ref.21
	Mutagenesis	335	1	D → A: Reduces strongly HDAC activity. Ref.21
	Mutagenesis	338	1	L → A: Reduces strongly HDAC activity. Ref.21
	Mutagenesis	339	1	P → A: Reduces strongly HDAC activity. Ref.21

Sequences

	Sequence		Length	Mass (Da)
	P32561 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: 34FFD72A7E7425DB	FASTA	433	48,904
	10 20 30 40 50 60 MVYEATPFDP ITVKPSDKRR VAYFYDADVG NYAYGAGHPM KPHRIRMAHS LIMNYGLYKK 70 80 90 100 110 120 MEIYRAKPAT KQEMCQFHTD EYIDFLSRVT PDNLEMFKRE SVKFNVGDDC PVFDGLYEYC 130 140 150 160 170 180 SISGGGSMEG AARLNRGKCD VAVNYAGGLH HAKKSEASGF CYLNDIVLGI IELLRYHPRV 190 200 210 220 230 240 LYIDIDVHHG DGVEEAFYTT DRVMTCSFHK YGEFFPGTGE LRDIGVGAGK NYAVNVPLRD 250 260 270 280 290 300 GIDDATYRSV FEPVIKKIME WYQPSAVVLQ CGGDSLSGDR LGCFNLSMEG HANCVNYVKS 310 320 330 340 350 360 FGIPMMVVGG GGYTMRNVAR TWCFETGLLN NVVLDKDLPY NEYYEYYGPD YKLSVRPSNM 370 380 390 400 410 420 FNVNTPEYLD KVMTNIFANL ENTKYAPSVQ LNHTPRDAED LGDVEEDSAE AKDTKGGSQY 430 ARDLHVEHDN EFY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"RPD3 encodes a second factor required to achieve maximum positive and negative transcriptional states in Saccharomyces cerevisiae." Vidal M., Gaber R.F. Mol. Cell. Biol. 11:6317-6327(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[2]	"An 8.2 kb DNA segment from chromosome XIV carries the RPD3 and PAS8 genes as well as the Saccharomyces cerevisiae homologue of the thiamine-repressed nmt1 gene and a chromosome III-duplicated gene for a putative aryl-alcohol dehydrogenase." van Dyck L., Pascual-Ahuir A., Purnelle B., Goffeau A. Yeast 11:987-991(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. 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. , 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]. Strain: ATCC 204508 / S288c.
[6]	"Sequencing analysis of a 15.4 kb fragment of yeast chromosome XIV identifies the RPD3, PAS8 and KRE1 loci, five new open reading frames." Maftahi M., Nicaud J.-M., Levesque H., Gaillardin C. Yeast 11:567-572(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-201. Strain: S288c / FY1676.
[7]	"Evidence that the transcriptional regulators SIN3 and RPD3, and a novel gene (SDS3) with similar functions, are involved in transcriptional silencing in S. cerevisiae." Vannier D., Balderes D., Shore D. Genetics 144:1343-1353(1996) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION. Strain: ATCC 200060 / W303.
[8]	"HDA1 and RPD3 are members of distinct yeast histone deacetylase complexes that regulate silencing and transcription." Rundlett S.E., Carmen A.A., Kobayashi R., Bavykin S., Turner B.M., Grunstein M. Proc. Natl. Acad. Sci. U.S.A. 93:14503-14508(1996) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN A HISTONE DEACETYLASE COMPLEX.
[9]	"Identification of two CyP-40-like cyclophilins in Saccharomyces cerevisiae, one of which is required for normal growth." Duina A.A., Marsh J.A., Gaber R.F. Yeast 12:943-952(1996) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CPR6 AND CPR7.
[10]	"A large protein complex containing the yeast Sin3p and Rpd3p transcriptional regulators." Kasten M.M., Dorland S., Stillman D.J. Mol. Cell. Biol. 17:4852-4858(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE RPD3 COMPLEX.
[11]	"Histone deacetylase activity of Rpd3 is important for transcriptional repression in vivo." Kadosh D., Struhl K. Genes Dev. 12:797-805(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF HIS-150; HIS-151 AND HIS-188.
[12]	"Targeted recruitment of the Sin3-Rpd3 histone deacetylase complex generates a highly localized domain of repressed chromatin in vivo." Kadosh D., Struhl K. Mol. Cell. Biol. 18:5121-5127(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE RPD3 COMPLEX.
[13]	"Transcriptional repression by UME6 involves deacetylation of lysine 5 of histone H4 by RPD3." Rundlett S.E., Carmen A.A., Suka N., Turner B.M., Grunstein M. Nature 392:831-835(1998) [PubMed] [Europe PMC] [Abstract] Cited for: DEACETYLATION OF HISTONE H4.
[14]	"RPD3 (REC3) mutations affect mitotic recombination in Saccharomyces cerevisiae." Dora E.G., Rudin N., Martell J.R., Esposito M.S., Ramirez R.M. Curr. Genet. 35:68-76(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[15]	"A general requirement for the Sin3-Rpd3 histone deacetylase complex in regulating silencing in Saccharomyces cerevisiae." Sun Z.-W., Hampsey M. Genetics 152:921-932(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE RPD3 COMPLEX.
[16]	"GCN5-dependent histone H3 acetylation and RPD3-dependent histone H4 deacetylation have distinct, opposing effects on IME2 transcription, during meiosis and during vegetative growth, in budding yeast." Burgess S.M., Ajimura M., Kleckner N. Proc. Natl. Acad. Sci. U.S.A. 96:6835-6840(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[17]	"Cyclophilin A and Ess1 interact with and regulate silencing by the Sin3-Rpd3 histone deacetylase." Arevalo-Rodriguez M., Cardenas M.E., Wu X., Hanes S.D., Heitman J. EMBO J. 19:3739-3749(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CPR1 AND ESS1.
[18]	"Ssn6-Tup1 interacts with class I histone deacetylases required for repression." Watson A.D., Edmondson D.G., Bone J.R., Mukai Y., Yu Y., Du W., Stillman D.J., Roth S.Y. Genes Dev. 14:2737-2744(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[19]	"Combinatorial regulation of phospholipid biosynthetic gene expression by the UME6, SIN3 and RPD3 genes." Elkhaimi M., Kaadige M.R., Kamath D., Jackson J.C., Biliran H. Jr., Lopes J.M. Nucleic Acids Res. 28:3160-3167(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[20]	"RPD3 is required for the inactivation of yeast ribosomal DNA genes in stationary phase." Sandmeier J.J., French S., Osheim Y., Cheung W.L., Gallo C.M., Beyer A.L., Smith J.S. EMBO J. 21:4959-4968(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CYC8.
[21]	"A conserved motif common to the histone acetyltransferase Esa1 and the histone deacetylase Rpd3." Adachi N., Kimura A., Horikoshi M. J. Biol. Chem. 277:35688-35695(2002) [PubMed] [Europe PMC] [Abstract] Cited for: DOMAIN, MUTAGENESIS OF TRP-322; GLU-325; GLY-327; LEU-328; LEU-329; VAL-332; LEU-334; ASP-335; LEU-338 AND PRO-339.
[22]	"Targeted recruitment of Rpd3 histone deacetylase represses transcription by inhibiting recruitment of Swi/Snf, SAGA, and TATA binding protein." Deckert J., Struhl K. Mol. Cell. Biol. 22:6458-6470(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[23]	"Genome-wide binding map of the histone deacetylase Rpd3 in yeast." Kurdistani S.K., Robyr D., Tavazoie S., Grunstein M. Nat. Genet. 31:248-254(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DNA-BINDING.
[24]	"Opposite role of yeast ING family members in p53-dependent transcriptional activation." Nourani A., Howe L., Pray-Grant M.G., Workman J.L., Grant P.A., Cote J. J. Biol. Chem. 278:19171-19175(2003) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE RPD3 COMPLEX, MASS SPECTROMETRY.
[25]	"Loss of Sin3/Rpd3 histone deacetylase restores the DNA damage response in checkpoint-deficient strains of Saccharomyces cerevisiae." Scott K.L., Plon S.E. Mol. Cell. Biol. 23:4522-4531(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE RPD3 COMPLEX.
[26]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[27]	"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].
[28]	"The unfolded protein response represses differentiation through the RPD3-SIN3 histone deacetylase." Schroeder M., Clark R., Liu C.Y., Kaufman R.J. EMBO J. 23:2281-2292(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HAC1, FUNCTION OF THE RPD3 COMPLEX.
[29]	"The Rpd3-Sin3 histone deacetylase regulates replication timing and enables intra-S origin control in Saccharomyces cerevisiae." Aparicio J.G., Viggiani C.J., Gibson D.G., Aparicio O.M. Mol. Cell. Biol. 24:4769-4780(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[30]	"Genome-wide analysis of the relationship between transcriptional regulation by Rpd3p and the histone H3 and H4 amino termini in budding yeast." Sabet N., Volo S., Yu C., Madigan J.P., Morse R.H. Mol. Cell. Biol. 24:8823-8833(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[31]	"The MAPK Hog1 recruits Rpd3 histone deacetylase to activate osmoresponsive genes." De Nadal E., Zapater M., Alepuz P.M., Sumoy L., Mas G., Posas F. Nature 427:370-374(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HOG1, FUNCTION OF THE RPD3 COMPLEX.
[32]	"Saccharomyces cerevisiae Sin3p facilitates DNA double-strand break repair." Jazayeri A., McAinsh A.D., Jackson S.P. Proc. Natl. Acad. Sci. U.S.A. 101:1644-1649(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE RPD3 COMPLEX.
[33]	"Stable incorporation of sequence specific repressors Ash1 and Ume6 into the Rpd3L complex." Carrozza M.J., Florens L., Swanson S.K., Shia W.-J., Anderson S., Yates J., Washburn M.P., Workman J.L. Biochim. Biophys. Acta 1731:77-87(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE RPD3C(L) COMPLEX, MASS SPECTROMETRY.
[34]	"Cotranscriptional set2 methylation of histone H3 lysine 36 recruits a repressive Rpd3 complex." Keogh M.-C., Kurdistani S.K., Morris S.A., Ahn S.H., Podolny V., Collins S.R., Schuldiner M., Chin K., Punna T., Thompson N.J., Boone C., Emili A., Weissman J.S., Hughes T.R., Strahl B.D., Grunstein M., Greenblatt J.F., Buratowski S., Krogan N.J. Cell 123:593-605(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE RPD3C(L) AND RPD3C(S) COMPLEXES, MASS SPECTROMETRY, FUNCTION OF THE RPD3C(S) COMPLEX.
[35]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-394, MASS SPECTROMETRY. Strain: ADR376.
[36]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-394 AND SER-408, MASS SPECTROMETRY.
[37]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-6; SER-388; THR-394 AND SER-408, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	S66438 Genomic DNA. Translation: AAB20328.1. X83226 Genomic DNA. Translation: CAA58228.1. Z46259 Genomic DNA. Translation: CAA86368.1. Z71605 Genomic DNA. Translation: CAA96262.1. Z71606 Genomic DNA. Translation: CAA96263.1. AY692813 Genomic DNA. Translation: AAT92832.1. BK006947 Genomic DNA. Translation: DAA10233.1.
PIR	S22284.
RefSeq	NP_014069.1. NM_001183168.1.
3D structure databases
ProteinModelPortal	P32561.
SMR	P32561. Positions 18-380.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-681N.
IntAct	P32561. 57 interactions.
MINT	MINT-614075.
STRING	4932.YNL330C.
Proteomic databases
PaxDb	P32561.
PeptideAtlas	P32561.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YNL330C; YNL330C; YNL330C.
GeneID	855386.
KEGG	sce:YNL330C.
Organism-specific databases
CYGD	YNL330c.
SGD	S000005274. RPD3.
Phylogenomic databases
eggNOG	COG0123.
GeneTree	ENSGT00530000062889.
HOGENOM	HOG000225180.
KO	K06067.
OMA	IPEDAPH.
OrthoDB	EOG4RV60J.
Gene expression databases
Genevestigator	P32561.
GermOnline	YNL330C. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	3.40.800.20. 1 hit.
InterPro	IPR000286. His_deacetylse. IPR003084. His_deacetylse_1. IPR023801. His_deacetylse_dom. [Graphical view]
PANTHER	PTHR10625. PTHR10625. 1 hit.
Pfam	PF00850. Hist_deacetyl. 1 hit. [Graphical view]
PIRSF	PIRSF037913. His_deacetylse_1. 1 hit.
PRINTS	PR01270. HDASUPER. PR01271. HISDACETLASE.
ProtoNet	Search...
Other
NextBio	979187.

Entry information

Entry name

RPD3_YEAST

Accession

Primary (citable) accession number: P32561
Secondary accession number(s): D6W0L7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	May 1, 2013
This is version 135 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program