Reviewed, UniProtKB/Swiss-Prot P32561 (RPD3_YEAST)

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 (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	433 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.6 Ref.7 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.21 Ref.22 Ref.24 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.33
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.27 Ref.30 Ref.8 Ref.16 Ref.19
Subcellular location	Cytoplasm. Nucleus. Ref.25
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.20
Miscellaneous	Present with 3850 molecules/cell in log phase SD medium. Ref.26
Sequence similarities	Belongs to the histone deacetylase family. 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
Gene Ontology (GO)
Biological process	chromatin silencing at rDNA Ref.14 Inferred from mutant phenotype. Source: SGD chromatin silencing at silent mating-type cassette Ref.14 Inferred from mutant phenotype. Source: SGD chromatin silencing at telomere Ref.14 Inferred from mutant phenotype. Source: SGD double-strand break repair via nonhomologous end joining Ref.31 Inferred from mutant phenotype. Source: SGD establishment or maintenance of chromatin architecture during transcription Inferred from mutant phenotype. Source: SGD histone deacetylation Ref.11 Inferred from mutant phenotype. Source: SGD loss of chromatin silencing during replicative cell aging Inferred from mutant phenotype. Source: SGD mitotic recombination Ref.13 Inferred from mutant phenotype. Source: SGD negative regulation of transcription by transcription factor localization Inferred from genetic interaction. Source: SGD negative regulation of transcription from RNA polymerase II promoter Ref.1 Inferred from mutant phenotype. Source: SGD negative regulation of transposition, RNA-mediated Inferred from mutant phenotype. Source: SGD positive regulation of specific transcription from RNA polymerase II promoter Inferred from mutant phenotype. Source: SGD transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	Rpd3/Clr6 histone deacetylase complex I/I' Inferred from direct assay. Source: SGD Rpd3/Clr6 histone deacetylase complex II' Inferred from direct assay. Source: SGD Rpd3L-Expanded complex Inferred from direct assay. Source: SGD Snt2C complex Inferred from direct assay. Source: SGD cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	histone deacetylase activity Ref.7 Inferred from direct assay. Source: SGD transcription coactivator activity Ref.30 Inferred from mutant phenotype. Source: SGD transcription corepressor activity Inferred from mutant phenotype. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CPR1	P14832	1	EBI-15864,EBI-5463
CPR6	P53691	1	EBI-15864,EBI-5429
CPR7	P47103	1	EBI-15864,EBI-5436
CYC8	P14922	4	EBI-15864,EBI-18215
ESS1	P22696	1	EBI-15864,EBI-6679
HOT1	Q03213	3	EBI-15864,EBI-27376
RXT2	P38255	1	EBI-15864,EBI-21537
SIN3	P22579	1	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.36
	Modified residue	388	1	Phosphoserine Ref.36
	Modified residue	394	1	Phosphothreonine Ref.36 Ref.34 Ref.35
	Modified residue	408	1	Phosphoserine Ref.36 Ref.35
Experimental info
	Mutagenesis	150	1	H → A: Impairs histone deacetylase activity and transcription repression. Ref.10
	Mutagenesis	151	1	H → A: Impairs histone deacetylase activity and transcription repression. Ref.10
	Mutagenesis	188	1	H → A: Impairs histone deacetylase activity and transcription repression. Ref.10
	Mutagenesis	322	1	W → A: Reduces strongly HDAC activity. Ref.20
	Mutagenesis	325	1	E → A: Reduces strongly HDAC activity. Ref.20
	Mutagenesis	327	1	G → A: Reduces strongly HDAC activity. Ref.20
	Mutagenesis	328	1	L → A: Reduces strongly HDAC activity. Ref.20
	Mutagenesis	329	1	L → A: Reduces strongly HDAC activity. Ref.20
	Mutagenesis	332	1	V → A: Reduces strongly HDAC activity. Ref.20
	Mutagenesis	334	1	L → A: Reduces strongly HDAC activity. Ref.20
	Mutagenesis	335	1	D → A: Reduces strongly HDAC activity. Ref.20
	Mutagenesis	338	1	L → A: Reduces strongly HDAC activity. Ref.20
	Mutagenesis	339	1	P → A: Reduces strongly HDAC activity. Ref.20

Sequences

	Sequence		Length	Mass (Da)
	P32561-1 [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: 1944291] [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: 8533474] [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: 9169873] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[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]. Strain: ATCC 204508 / S288c.
[5]	"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: 7645347] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-201. Strain: S288c / FY1676.
[6]	"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: 8978024] [Abstract] Cited for: FUNCTION. Strain: ATCC 200060 / W303.
[7]	"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: 8962081] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN A HISTONE DEACETYLASE COMPLEX.
[8]	"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: 8873448] [Abstract] Cited for: INTERACTION WITH CPR6 AND CPR7.
[9]	"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: 9234741] [Abstract] Cited for: IDENTIFICATION IN THE RPD3 COMPLEX.
[10]	"Histone deacetylase activity of Rpd3 is important for transcriptional repression in vivo." Kadosh D., Struhl K. Genes Dev. 12:797-805(1998) [PubMed: 9512514] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF HIS-150; HIS-151 AND HIS-188.
[11]	"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: 9710596] [Abstract] Cited for: FUNCTION OF THE RPD3 COMPLEX.
[12]	"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: 9572144] [Abstract] Cited for: DEACETYLATION OF HISTONE H4.
[13]	"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: 10079324] [Abstract] Cited for: FUNCTION.
[14]	"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: 10388812] [Abstract] Cited for: FUNCTION OF THE RPD3 COMPLEX.
[15]	"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: 10359799] [Abstract] Cited for: FUNCTION.
[16]	"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: 10899127] [Abstract] Cited for: INTERACTION WITH CPR1 AND ESS1.
[17]	"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: 11069890] [Abstract] Cited for: FUNCTION.
[18]	"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: 10931932] [Abstract] Cited for: FUNCTION.
[19]	"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: 12234935] [Abstract] Cited for: INTERACTION WITH CYC8.
[20]	"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: 12110674] [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.
[21]	"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: 12192044] [Abstract] Cited for: FUNCTION.
[22]	"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: 12089521] [Abstract] Cited for: FUNCTION, DNA-BINDING.
[23]	"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: 12672825] [Abstract] Cited for: IDENTIFICATION IN THE RPD3 COMPLEX, MASS SPECTROMETRY.
[24]	"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: 12808094] [Abstract] Cited for: FUNCTION OF THE RPD3 COMPLEX.
[25]	"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: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[26]	"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].
[27]	"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: 15141165] [Abstract] Cited for: INTERACTION WITH HAC1, FUNCTION OF THE RPD3 COMPLEX.
[28]	"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: 15143171] [Abstract] Cited for: FUNCTION.
[29]	"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: 15456858] [Abstract] Cited for: FUNCTION.
[30]	"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: 14737171] [Abstract] Cited for: INTERACTION WITH HOG1, FUNCTION OF THE RPD3 COMPLEX.
[31]	"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: 14711989] [Abstract] Cited for: FUNCTION OF THE RPD3 COMPLEX.
[32]	"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: 16314178] [Abstract] Cited for: IDENTIFICATION IN THE RPD3C(L) COMPLEX, MASS SPECTROMETRY.
[33]	"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: 16286008] [Abstract] Cited for: IDENTIFICATION IN THE RPD3C(L) AND RPD3C(S) COMPLEXES, MASS SPECTROMETRY, FUNCTION OF THE RPD3C(S) COMPLEX.
[34]	"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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-394, MASS SPECTROMETRY.
[35]	"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: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-394 AND SER-408, MASS SPECTROMETRY.
[36]	"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: 18407956] [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
EMBLGenBankDDBJ	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.
PIR	S22284.
RefSeq	NP_014069.1.
3D structure databases
HSSP	HSSP built from PDB template 1C3P based on UniProtKB O67135.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:681N.
IntAct	P32561. 52 interactions.
Proteomic databases
PeptideAtlas	P32561.
PRIDE	P32561.
Genome annotation databases
Ensembl	YNL330C. Saccharomyces cerevisiae. [Contig view]
GeneID	855386.
GenomeReviews	Gene locus YNL330C in contig Y13139_GR.
KEGG	sce:YNL330C.
NMPDR	fig|4932.3.peg.5131.
Organism-specific databases
CYGD	YNL330c.
SGD	S000005274. RPD3.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P32561.
OMA	P32561. QHGCDTH.
Gene expression databases
GermOnline	YNL330C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000286. His_deacetylse. IPR003084. His_deacetylse_1. [Graphical view]
Gene3D	G3DSA:3.40.800.20. His_deacetylse. 1 hit.
PANTHER	PTHR10625. His_deacetylse. 1 hit. PTHR10625:SF28. His_deacetylse_1. 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 Resources
NextBio	979187.

Entry information

Entry name

RPD3_YEAST

Accession

Primary (citable) accession number: P32561

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	June 16, 2009
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)