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P32561 (RPD3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 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
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length433 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Molecular functionChromatin regulator
Hydrolase
Repressor
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processhistone 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

Inferred from mutant phenotype PubMed 15254041PubMed 17210643PubMed 17296735PubMed 17706600. 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 transition of mitotic cell cycle

Inferred from genetic interaction PubMed 19823668. Source: SGD

regulation of transcription involved in G2/M transition of mitotic cell cycle

Inferred from genetic interaction PubMed 17908798. 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

transfer RNA gene-mediated silencing

Inferred from mutant phenotype PubMed 23707796. Source: SGD

   Cellular_componentRpd3L complex

Inferred from direct assay PubMed 16286007Ref.34Ref.33. Source: SGD

Rpd3S complex

Inferred from direct assay PubMed 16286007Ref.34. Source: SGD

Sin3-type complex

Inferred from direct assay Ref.10. Source: SGD

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

histone deacetylase complex

Inferred from direct assay Ref.8. Source: SGD

   Molecular_functionNAD-dependent histone deacetylase activity (H3-K14 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

NAD-dependent histone deacetylase activity (H3-K18 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

NAD-dependent histone deacetylase activity (H3-K9 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

NAD-dependent histone deacetylase activity (H4-K16 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

histone deacetylase activity

Inferred from direct assay Ref.21. Source: SGD

protein binding

Inferred from physical interaction Ref.18PubMed 11805826PubMed 14525981Ref.31PubMed 16275642PubMed 16429126PubMed 17101441PubMed 21179020Ref.9. Source: IntAct

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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 433433Histone deacetylase RPD3
PRO_0000114724

Regions

Region19 – 331313Histone deacetylase
Motif320 – 34021ESA1-RPD3 motif

Sites

Active site1511 Probable

Amino acid modifications

Modified residue3941Phosphothreonine Ref.35 Ref.36
Modified residue4081Phosphoserine Ref.36 Ref.37

Experimental info

Mutagenesis1501H → A: Impairs histone deacetylase activity and transcription repression. Ref.11
Mutagenesis1511H → A: Impairs histone deacetylase activity and transcription repression. Ref.11
Mutagenesis1881H → A: Impairs histone deacetylase activity and transcription repression. Ref.11
Mutagenesis3221W → A: Reduces strongly HDAC activity. Ref.21
Mutagenesis3251E → A: Reduces strongly HDAC activity. Ref.21
Mutagenesis3271G → A: Reduces strongly HDAC activity. Ref.21
Mutagenesis3281L → A: Reduces strongly HDAC activity. Ref.21
Mutagenesis3291L → A: Reduces strongly HDAC activity. Ref.21
Mutagenesis3321V → A: Reduces strongly HDAC activity. Ref.21
Mutagenesis3341L → A: Reduces strongly HDAC activity. Ref.21
Mutagenesis3351D → A: Reduces strongly HDAC activity. Ref.21
Mutagenesis3381L → A: Reduces strongly HDAC activity. Ref.21
Mutagenesis3391P → A: Reduces strongly HDAC activity. Ref.21

Sequences

Sequence LengthMass (Da)Tools
P32561 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 34FFD72A7E7425DB

FASTA43348,904
        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 

« Hide

References

« Hide '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. 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].
Strain: ATCC 204508 / S288c.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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. 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].
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, IDENTIFICATION BY 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, IDENTIFICATION BY 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, IDENTIFICATION BY 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-394 AND SER-408, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[37]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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.
PIRS22284.
RefSeqNP_014069.1. NM_001183168.1.

3D structure databases

ProteinModelPortalP32561.
SMRP32561. Positions 18-380.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35511. 724 interactions.
DIPDIP-681N.
IntActP32561. 57 interactions.
MINTMINT-614075.
STRING4932.YNL330C.

Proteomic databases

MaxQBP32561.
PaxDbP32561.
PeptideAtlasP32561.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYNL330C; YNL330C; YNL330C.
GeneID855386.
KEGGsce:YNL330C.

Organism-specific databases

CYGDYNL330c.
SGDS000005274. RPD3.

Phylogenomic databases

eggNOGCOG0123.
GeneTreeENSGT00530000062889.
HOGENOMHOG000225180.
KOK06067.
OMAYEYCSIS.
OrthoDBEOG78M0B2.

Enzyme and pathway databases

BioCycYEAST:G3O-33314-MONOMER.

Gene expression databases

GenevestigatorP32561.

Family and domain databases

Gene3D3.40.800.20. 1 hit.
InterProIPR000286. His_deacetylse.
IPR003084. His_deacetylse_1.
IPR023801. His_deacetylse_dom.
[Graphical view]
PANTHERPTHR10625. PTHR10625. 1 hit.
PfamPF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PIRSFPIRSF037913. His_deacetylse_1. 1 hit.
PRINTSPR01270. HDASUPER.
PR01271. HISDACETLASE.
ProtoNetSearch...

Other

NextBio979187.

Entry information

Entry nameRPD3_YEAST
AccessionPrimary (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: July 9, 2014
This is version 147 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

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