[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION. PubMed=1944291 [NCBI, ExPASy, EBI, Israel, Japan] Vidal M., Gaber R.F.; "RPD3 encodes a second factor required to achieve maximum positive and negative transcriptional states in Saccharomyces cerevisiae."; Mol. Cell. Biol. 11:6317-6327(1991).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 96604 / S288c / FY1679; DOI=10.1002/yea.320111010; PubMed=8533474 [NCBI, ExPASy, EBI, Israel, Japan] van Dyck L., Pascual-Ahuir A., Purnelle B., Goffeau A.; "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."; Yeast 11:987-991(1995).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 96604 / S288c / FY1679; PubMed=9169873 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."; Nature 387:93-98(1997).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 204508 / S288c; DOI=10.1101/gr.6037607; PubMed=17322287 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."; Genome Res. 17:536-543(2007).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-201. STRAIN=S288c / FY1676; PubMed=7645347 [NCBI, ExPASy, EBI, Israel, Japan] Maftahi M., Nicaud J.-M., Levesque H., Gaillardin C.; "Sequencing analysis of a 15.4 kb fragment of yeast chromosome XIV identifies the RPD3, PAS8 and KRE1 loci, five new open reading frames."; Yeast 11:567-572(1995).
[6]	FUNCTION. STRAIN=ATCC 200060 / W303; PubMed=8978024 [NCBI, ExPASy, EBI, Israel, Japan] Vannier D., Balderes D., Shore D.; "Evidence that the transcriptional regulators SIN3 and RPD3, and a novel gene (SDS3) with similar functions, are involved in transcriptional silencing in S. cerevisiae."; Genetics 144:1343-1353(1996).
[7]	FUNCTION, AND IDENTIFICATION IN A HISTONE DEACETYLASE COMPLEX. DOI=10.1073/pnas.93.25.14503; PubMed=8962081 [NCBI, ExPASy, EBI, Israel, Japan] Rundlett S.E., Carmen A.A., Kobayashi R., Bavykin S., Turner B.M., Grunstein M.; "HDA1 and RPD3 are members of distinct yeast histone deacetylase complexes that regulate silencing and transcription."; Proc. Natl. Acad. Sci. U.S.A. 93:14503-14508(1996).
[8]	INTERACTION WITH CPR6 AND CPR7. DOI=10.1002/(SICI)1097-0061(199608)12:10<943::AID-YEA997>3.0.CO;2-3; PubMed=8873448 [NCBI, ExPASy, EBI, Israel, Japan] Duina A.A., Marsh J.A., Gaber R.F.; "Identification of two CyP-40-like cyclophilins in Saccharomyces cerevisiae, one of which is required for normal growth."; Yeast 12:943-952(1996).
[9]	IDENTIFICATION IN THE RPD3 COMPLEX. PubMed=9234741 [NCBI, ExPASy, EBI, Israel, Japan] Kasten M.M., Dorland S., Stillman D.J.; "A large protein complex containing the yeast Sin3p and Rpd3p transcriptional regulators."; Mol. Cell. Biol. 17:4852-4858(1997).
[10]	FUNCTION, AND MUTAGENESIS OF HIS-150; HIS-151 AND HIS-188. PubMed=9512514 [NCBI, ExPASy, EBI, Israel, Japan] Kadosh D., Struhl K.; "Histone deacetylase activity of Rpd3 is important for transcriptional repression in vivo."; Genes Dev. 12:797-805(1998).
[11]	FUNCTION OF THE RPD3 COMPLEX. PubMed=9710596 [NCBI, ExPASy, EBI, Israel, Japan] Kadosh D., Struhl K.; "Targeted recruitment of the Sin3-Rpd3 histone deacetylase complex generates a highly localized domain of repressed chromatin in vivo."; Mol. Cell. Biol. 18:5121-5127(1998).
[12]	DEACETYLATION OF HISTONE H4. DOI=10.1038/33952; PubMed=9572144 [NCBI, ExPASy, EBI, Israel, Japan] Rundlett S.E., Carmen A.A., Suka N., Turner B.M., Grunstein M.; "Transcriptional repression by UME6 involves deacetylation of lysine 5 of histone H4 by RPD3."; Nature 392:831-835(1998).
[13]	FUNCTION. DOI=10.1007/s002940050434; PubMed=10079324 [NCBI, ExPASy, EBI, Israel, Japan] Dora E.G., Rudin N., Martell J.R., Esposito M.S., Ramirez R.M.; "RPD3 (REC3) mutations affect mitotic recombination in Saccharomyces cerevisiae."; Curr. Genet. 35:68-76(1999).
[14]	FUNCTION OF THE RPD3 COMPLEX. PubMed=10388812 [NCBI, ExPASy, EBI, Israel, Japan] Sun Z.-W., Hampsey M.; "A general requirement for the Sin3-Rpd3 histone deacetylase complex in regulating silencing in Saccharomyces cerevisiae."; Genetics 152:921-932(1999).
[15]	FUNCTION. DOI=10.1073/pnas.96.12.6835; PubMed=10359799 [NCBI, ExPASy, EBI, Israel, Japan] Burgess S.M., Ajimura M., Kleckner N.; "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."; Proc. Natl. Acad. Sci. U.S.A. 96:6835-6840(1999).
[16]	INTERACTION WITH CPR1 AND ESS1. DOI=10.1093/emboj/19.14.3739; PubMed=10899127 [NCBI, ExPASy, EBI, Israel, Japan] Arevalo-Rodriguez M., Cardenas M.E., Wu X., Hanes S.D., Heitman J.; "Cyclophilin A and Ess1 interact with and regulate silencing by the Sin3-Rpd3 histone deacetylase."; EMBO J. 19:3739-3749(2000).
[17]	FUNCTION. DOI=10.1101/gad.829100; PubMed=11069890 [NCBI, ExPASy, EBI, Israel, Japan] Watson A.D., Edmondson D.G., Bone J.R., Mukai Y., Yu Y., Du W., Stillman D.J., Roth S.Y.; "Ssn6-Tup1 interacts with class I histone deacetylases required for repression."; Genes Dev. 14:2737-2744(2000).
[18]	FUNCTION. DOI=10.1093/nar/28.16.3160; PubMed=10931932 [NCBI, ExPASy, EBI, Israel, Japan] Elkhaimi M., Kaadige M.R., Kamath D., Jackson J.C., Biliran H. Jr., Lopes J.M.; "Combinatorial regulation of phospholipid biosynthetic gene expression by the UME6, SIN3 and RPD3 genes."; Nucleic Acids Res. 28:3160-3167(2000).
[19]	INTERACTION WITH CYC8. DOI=10.1093/emboj/cdf498; PubMed=12234935 [NCBI, ExPASy, EBI, Israel, Japan] Sandmeier J.J., French S., Osheim Y., Cheung W.L., Gallo C.M., Beyer A.L., Smith J.S.; "RPD3 is required for the inactivation of yeast ribosomal DNA genes in stationary phase."; EMBO J. 21:4959-4968(2002).
[20]	DOMAIN, AND MUTAGENESIS OF TRP-322; GLU-325; GLY-327; LEU-328; LEU-329; VAL-332; LEU-334; ASP-335; LEU-338 AND PRO-339. DOI=10.1074/jbc.M204640200; PubMed=12110674 [NCBI, ExPASy, EBI, Israel, Japan] Adachi N., Kimura A., Horikoshi M.; "A conserved motif common to the histone acetyltransferase Esa1 and the histone deacetylase Rpd3."; J. Biol. Chem. 277:35688-35695(2002).
[21]	FUNCTION. DOI=10.1128/MCB.22.18.6458-6470.2002; PubMed=12192044 [NCBI, ExPASy, EBI, Israel, Japan] Deckert J., Struhl K.; "Targeted recruitment of Rpd3 histone deacetylase represses transcription by inhibiting recruitment of Swi/Snf, SAGA, and TATA binding protein."; Mol. Cell. Biol. 22:6458-6470(2002).
[22]	FUNCTION, AND DNA-BINDING. DOI=10.1038/ng907; PubMed=12089521 [NCBI, ExPASy, EBI, Israel, Japan] Kurdistani S.K., Robyr D., Tavazoie S., Grunstein M.; "Genome-wide binding map of the histone deacetylase Rpd3 in yeast."; Nat. Genet. 31:248-254(2002).
[23]	IDENTIFICATION IN THE RPD3 COMPLEX, AND MASS SPECTROMETRY. DOI=10.1074/jbc.C300036200; PubMed=12672825 [NCBI, ExPASy, EBI, Israel, Japan] Nourani A., Howe L., Pray-Grant M.G., Workman J.L., Grant P.A., Cote J.; "Opposite role of yeast ING family members in p53-dependent transcriptional activation."; J. Biol. Chem. 278:19171-19175(2003).
[24]	FUNCTION OF THE RPD3 COMPLEX. DOI=10.1128/MCB.23.13.4522-4531.2003; PubMed=12808094 [NCBI, ExPASy, EBI, Israel, Japan] Scott K.L., Plon S.E.; "Loss of Sin3/Rpd3 histone deacetylase restores the DNA damage response in checkpoint-deficient strains of Saccharomyces cerevisiae."; Mol. Cell. Biol. 23:4522-4531(2003).
[25]	SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. DOI=10.1038/nature02026; PubMed=14562095 [NCBI, ExPASy, EBI, Israel, Japan] Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.; "Global analysis of protein localization in budding yeast."; Nature 425:686-691(2003).
[26]	LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan] Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.; "Global analysis of protein expression in yeast."; Nature 425:737-741(2003).
[27]	INTERACTION WITH HAC1, AND FUNCTION OF THE RPD3 COMPLEX. DOI=10.1038/sj.emboj.7600233; PubMed=15141165 [NCBI, ExPASy, EBI, Israel, Japan] Schroeder M., Clark R., Liu C.Y., Kaufman R.J.; "The unfolded protein response represses differentiation through the RPD3-SIN3 histone deacetylase."; EMBO J. 23:2281-2292(2004).
[28]	FUNCTION. DOI=10.1128/MCB.24.11.4769-4780.2004; PubMed=15143171 [NCBI, ExPASy, EBI, Israel, Japan] Aparicio J.G., Viggiani C.J., Gibson D.G., Aparicio O.M.; "The Rpd3-Sin3 histone deacetylase regulates replication timing and enables intra-S origin control in Saccharomyces cerevisiae."; Mol. Cell. Biol. 24:4769-4780(2004).
[29]	FUNCTION. DOI=10.1128/MCB.24.20.8823-8833.2004; PubMed=15456858 [NCBI, ExPASy, EBI, Israel, Japan] Sabet N., Volo S., Yu C., Madigan J.P., Morse R.H.; "Genome-wide analysis of the relationship between transcriptional regulation by Rpd3p and the histone H3 and H4 amino termini in budding yeast."; Mol. Cell. Biol. 24:8823-8833(2004).
[30]	INTERACTION WITH HOG1, AND FUNCTION OF THE RPD3 COMPLEX. DOI=10.1038/nature02258; PubMed=14737171 [NCBI, ExPASy, EBI, Israel, Japan] De Nadal E., Zapater M., Alepuz P.M., Sumoy L., Mas G., Posas F.; "The MAPK Hog1 recruits Rpd3 histone deacetylase to activate osmoresponsive genes."; Nature 427:370-374(2004).
[31]	FUNCTION OF THE RPD3 COMPLEX. DOI=10.1073/pnas.0304797101; PubMed=14711989 [NCBI, ExPASy, EBI, Israel, Japan] Jazayeri A., McAinsh A.D., Jackson S.P.; "Saccharomyces cerevisiae Sin3p facilitates DNA double-strand break repair."; Proc. Natl. Acad. Sci. U.S.A. 101:1644-1649(2004).
[32]	IDENTIFICATION IN THE RPD3C(L) COMPLEX, AND MASS SPECTROMETRY. DOI=10.1016/j.bbaexp.2005.09.005; PubMed=16314178 [NCBI, ExPASy, EBI, Israel, Japan] Carrozza M.J., Florens L., Swanson S.K., Shia W.-J., Anderson S., Yates J., Washburn M.P., Workman J.L.; "Stable incorporation of sequence specific repressors Ash1 and Ume6 into the Rpd3L complex."; Biochim. Biophys. Acta 1731:77-87(2005).
[33]	IDENTIFICATION IN THE RPD3C(L) AND RPD3C(S) COMPLEXES, MASS SPECTROMETRY, AND FUNCTION OF THE RPD3C(S) COMPLEX. DOI=10.1016/j.cell.2005.10.025; PubMed=16286008 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Cotranscriptional set2 methylation of histone H3 lysine 36 recruits a repressive Rpd3 complex."; Cell 123:593-605(2005).
[34]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-394, AND MASS SPECTROMETRY. DOI=10.1021/pr060559j; PubMed=17330950 [NCBI, ExPASy, EBI, Israel, Japan] Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.; "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."; J. Proteome Res. 6:1190-1197(2007).
[35]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-394 AND SER-408, AND MASS SPECTROMETRY. DOI=10.1073/pnas.0701622104; PubMed=17563356 [NCBI, ExPASy, EBI, Israel, Japan] Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; "Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases."; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
[36]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-6; SER-388; THR-394 AND SER-408, AND MASS SPECTROMETRY. DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan] Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; "A multidimensional chromatography technology for in-depth phosphoproteome analysis."; Mol. Cell. Proteomics 7:1389-1396(2008).

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.
CATALYTIC ACTIVITY: Hydrolysis of an N⁶-acetyl-lysine residue of a histone to yield a deacetylated histone.
SUBUNIT: 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.
INTERACTION:
P53691:CPR6; NbExp=1; IntAct=EBI-15864, EBI-5429;
P47103:CPR7; NbExp=1; IntAct=EBI-15864, EBI-5436;
P14922:CYC8; NbExp=4; IntAct=EBI-15864, EBI-18215;
Q03213:HOT1; NbExp=3; IntAct=EBI-15864, EBI-27376;
P38255:RXT2; NbExp=1; IntAct=EBI-15864, EBI-21537;
P22579:SIN3; NbExp=1; IntAct=EBI-15864, EBI-17160;
P16649:TUP1; NbExp=2; IntAct=EBI-15864, EBI-19654;
SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
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.
MISCELLANEOUS: Present with 3850 molecules/cell in log phase SD medium.
SIMILARITY: Belongs to the histone deacetylase family. Type 1 subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

S66438; AAB20328.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X83226; CAA58228.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z46259; CAA86368.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z71605; CAA96262.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z71606; CAA96263.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY692813; AAT92832.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S22284; S22284.

RefSeq

NP_014069.1; -.

3D structure databases

HSSP

O67135; 1C3P. [HSSP ENTRY / PDB]

ModBase

P32561.

Protein-protein interaction databases

DIP

DIP:681N; -.

IntAct

P32561; -.

Organism-specific databases

YNL330c; -.

S000005274; RPD3.

Gene expression databases

GermOnline

YNL330C; Saccharomyces cerevisiae.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0000508;	Cellular component: Rpd3L complex (inferred from direct assay from SGD).
GO:0000509;	Cellular component: Rpd3S complex (inferred from direct assay from SGD).
GO:0004407;	Molecular function: histone deacetylase activity (inferred from electronic annotation from InterPro).
GO:0003713;	Molecular function: transcription coactivator activity (inferred from mutant phenotype from SGD).
GO:0003714;	Molecular function: transcription corepressor activity (inferred from mutant phenotype from SGD).
GO:0000183;	Biological process: chromatin silencing at rDNA (inferred from mutant phenotype from SGD).
GO:0030466;	Biological process: chromatin silencing at silent mating-type cassette (inferred from mutant phenotype from SGD).
GO:0006348;	Biological process: chromatin silencing at telomere (inferred from mutant phenotype from SGD).
GO:0006303;	Biological process: double-strand break repair via nonhomologous end joining (inferred from mutant phenotype from SGD).
GO:0016575;	Biological process: histone deacetylation (inferred from electronic annotation from InterPro).
GO:0001308;	Biological process: loss of chromatin silencing during replicative cell aging (inferred from mutant phenotype from SGD).
GO:0006312;	Biological process: mitotic recombination (inferred from mutant phenotype from SGD).
GO:0000122;	Biological process: negative regulation of transcription from RNA polymerase II promoter (inferred from mutant phenotype from SGD).
GO:0010526;	Biological process: negative regulation of transposition, RNA-mediated (inferred from mutant phenotype from SGD).
GO:0045944;	Biological process: positive regulation of transcription from RNA polymerase II promoter (inferred from mutant phenotype from SGD).
QuickGo view.

Family and domain databases

InterPro

IPR000286; His_deacetylse.
IPR003084; His_deacetylse_1.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.800.20; His_deacetylse; 1.

PANTHER

PTHR10625; His_deacetylse; 1.
PTHR10625:SF28; His_deacetylse_1; 1.

Pfam

PF00850; Hist_deacetyl; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF037913; His_deacetylse_1; 1.

PRINTS

PR01270; HDASUPER.
PR01271; HISDACETLASE.

Proteomic databases

P32561; -.

Genome annotation databases

Ensembl

YNL330C; Saccharomyces cerevisiae. [Contig view]

855386; -.

Y13139_GR; YNL330C.

sce:YNL330C; -.

fig|4932.3.peg.5131; -.

Phylogenomic databases

HOGENOM

P32561; -.

Other

LinkHub

P32561; -.

NextBio

979187; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Chromatin regulator; Complete proteome; Cytoplasm; Hydrolase; Nucleus; Phosphoprotein; Repressor; Transcription; Transcription regulation.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 433`	`433`	`Histone deacetylase RPD3.`	`PRO_0000114724`
`REGION`	`19 331`	`313`	`Histone deacetylase.`
`MOTIF`	`320 340`	`21`	`ESA1-RPD3 motif.`
`ACT_SITE`	`151 151`		`Probable.`
`MOD_RES`	`6 6`		`Phosphothreonine.`
`MOD_RES`	`388 388`		`Phosphoserine.`
`MOD_RES`	`394 394`		`Phosphothreonine.`
`MOD_RES`	`408 408`		`Phosphoserine.`
`MUTAGEN`	`150 150`		`H->A: Impairs histone deacetylase activity and transcription repression.`
`MUTAGEN`	`151 151`		`H->A: Impairs histone deacetylase activity and transcription repression.`
`MUTAGEN`	`188 188`		`H->A: Impairs histone deacetylase activity and transcription repression.`
`MUTAGEN`	`322 322`		`W->A: Reduces strongly HDAC activity.`
`MUTAGEN`	`325 325`		`E->A: Reduces strongly HDAC activity.`
`MUTAGEN`	`327 327`		`G->A: Reduces strongly HDAC activity.`
`MUTAGEN`	`328 328`		`L->A: Reduces strongly HDAC activity.`
`MUTAGEN`	`329 329`		`L->A: Reduces strongly HDAC activity.`
`MUTAGEN`	`332 332`		`V->A: Reduces strongly HDAC activity.`
`MUTAGEN`	`334 334`		`L->A: Reduces strongly HDAC activity.`
`MUTAGEN`	`335 335`		`D->A: Reduces strongly HDAC activity.`
`MUTAGEN`	`338 338`		`L->A: Reduces strongly HDAC activity.`
`MUTAGEN`	`339 339`		`P->A: Reduces strongly HDAC activity.`

Sequence information

Length: 433 AA [This is the length of the unprocessed precursor]

Molecular weight: 48904 Da [This is the MW of the unprocessed precursor]

CRC64: 34FFD72A7E7425DB [This is a checksum on the sequence]

        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

P32561 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools