P22579 (SIN3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transcriptional regulatory protein SIN3

Gene names

Name:	SIN3
Synonyms:	CPE1, GAM2, RPD1, SDI1, SDS16, UME4
Ordered Locus Names:	YOL004W

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	1536 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalytic component of the RPD3 histone deacetylase 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 gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. SIN3 has also a RPD3 independent function required for normal longevity. Ref.1 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.18 Ref.20 Ref.21 Ref.22 Ref.23 Ref.25 Ref.26
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 ESS1 and STB1. Ref.8 Ref.9 Ref.13 Ref.15 Ref.17 Ref.24 Ref.25
Subcellular location	Nucleus.
Miscellaneous	Present with 1660 molecules/cell in log phase SD medium.
Sequence similarities	Contains 3 PAH (paired amphipathic helix) domains.

Ontologies

Keywords
Biological process	Cell cycle Cell division Transcription Transcription regulation
Cellular component	Nucleus
Domain	Repeat
Molecular function	Activator Chromatin regulator Repressor
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW double-strand break repair via nonhomologous end joining Inferred from mutant phenotype Ref.23. Source: SGD histone deacetylation Inferred from mutant phenotype PubMed 16286007Ref.10. Source: SGD negative regulation of chromatin silencing at rDNA Inferred from mutant phenotype PubMed 10082585Ref.12. Source: SGD negative regulation of chromatin silencing at silent mating-type cassette Inferred from mutant phenotype Ref.12. Source: SGD negative regulation of chromatin silencing at telomere Inferred from mutant phenotype Ref.12PubMed 19372273. 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 19270272. Source: SGD negative regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype PubMed 11095743PubMed 2690066. Source: SGD positive regulation of transcription from RNA polymerase II promoter in response to heat stress Inferred from mutant phenotype PubMed 20398213. Source: SGD regulation of DNA-dependent DNA replication initiation Inferred from mutant phenotype Ref.21. Source: SGD regulation of transcription involved in G2/M-phase of mitotic cell cycle Inferred from genetic interaction PubMed 17908798. Source: SGD transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Rpd3L complex Inferred from direct assay PubMed 16286007Ref.25Ref.24PubMed 19040720. Source: SGD Rpd3L-Expanded complex Inferred from direct assay PubMed 19040720. Source: SGD Rpd3S complex Inferred from direct assay PubMed 16286007Ref.25. Source: SGD
Molecular_function	transcription coactivator activity Inferred from mutant phenotype Ref.22. Source: SGD transcription corepressor activity Inferred from mutant phenotype PubMed 9150136. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		3	EBI-17160,EBI-17160
OPI1	P21957	5	EBI-17160,EBI-12555
RPD3	P32561	11	EBI-17160,EBI-15864

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1536	1536	Transcriptional regulatory protein SIN3		PRO_0000121544
Regions
	Domain	217 – 287	71	PAH 1
	Domain	404 – 474	71	PAH 2
	Domain	656 – 727	72	PAH 3
	Compositional bias	480 – 519	40	Gln-rich
Amino acid modifications
	Modified residue	137	1	Phosphoserine Ref.29
	Modified residue	294	1	Phosphoserine Ref.29
	Modified residue	303	1	Phosphothreonine Ref.16 Ref.29
	Modified residue	304	1	Phosphothreonine Ref.27 Ref.29
	Modified residue	308	1	Phosphothreonine Ref.29
	Modified residue	316	1	Phosphoserine Ref.16 Ref.29
	Modified residue	318	1	Phosphoserine Ref.29
	Modified residue	1046	1	Phosphoserine Ref.29
	Modified residue	1483	1	Phosphoserine Ref.28 Ref.29
Experimental info
	Sequence conflict	510	1	Q → QAQ Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P22579 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 0834726312B13878	FASTA	1,536	174,839
	10 20 30 40 50 60 MSQVWHNSNS QSNDVATSND ATGSNERNEK EPSLQGNKPG FVQQQQRITL PSLSALSTKE 70 80 90 100 110 120 EDRRDSNGQQ ALTSHAAHIL GYPPPHSNAM PSIATDSALK QPHEYHPRPK SSSSSPSINA 130 140 150 160 170 180 SLMNAGPAPL PTVGAASFSL SRFDNPLPIK APVHTEEPKS YNGLQEEEKA TQRPQDCKEV 190 200 210 220 230 240 PAGVQPADAP DPSSNHADAN DDNNNNENSH DEDADYRPLN VKDALSYLEQ VKFQFSSRPD 250 260 270 280 290 300 IYNLFLDIMK DFKSQAIDTP GVIERVSTLF RGYPILIQGF NTFLPQGYRI ECSSNPDDPI 310 320 330 340 350 360 RVTTPMGTTT VNNNISPSGR GTTDAQELGS FPESDGNGVQ QPSNVPMVPS SVYQSEQNQD 370 380 390 400 410 420 QQQSLPLLAT SSGLPSIQQP EMPAHRQIPQ SQSLVPQEDA KKNVDVEFSQ AISYVNKIKT 430 440 450 460 470 480 RFADQPDIYK HFLEILQTYQ REQKPINEVY AQVTHLFQNA PDLLEDFKKF LPDSSASANQ 490 500 510 520 530 540 QVQHAQQHAQ QQHEAQMHAQ AQAQAQAQAQ VEQQKQQQQF LYPASGYYGH PSNRGIPQQN 550 560 570 580 590 600 LPPIGSFSPP TNGSTVHEAY QDQQHMQPPH FMPLPSIVQH GPNMVHQGIA NENPPLSDLR 610 620 630 640 650 660 TSLTEQYAPS SIQHQQQHPQ SISPIANTQY GDIPVRPEID LDPSIVPVVP EPTEPIENNI 670 680 690 700 710 720 SLNEEVTFFE KAKRYIGNKH LYTEFLKILN LYSQDILDLD DLVEKVDFYL GSNKELFTWF 730 740 750 760 770 780 KNFVGYQEKT KCIENIVHEK HRLDLDLCEA FGPSYKRLPK SDTFMPCSGR DDMCWEVLND 790 800 810 820 830 840 EWVGHPVWAS EDSGFIAHRK NQYEETLFKI EEERHEYDFY IESNLRTIQC LETIVNKIEN 850 860 870 880 890 900 MTENEKANFK LPPGLGHTSM TIYKKVIRKV YDKERGFEII DALHEHPAVT APVVLKRLKQ 910 920 930 940 950 960 KDEEWRRAQR EWNKVWRELE QKVFFKSLDH LGLTFKQADK KLLTTKQLIS EISSIKVDQT 970 980 990 1000 1010 1020 NKKIHWLTPK PKSQLDFDFP DKNIFYDILC LADTFITHTT AYSNPDKERL KDLLKYFISL 1030 1040 1050 1060 1070 1080 FFSISFEKIE ESLYSHKQNV SESSGSDDGS SIASRKRPYQ QEMSLLDILH RSRYQKLKRS 1090 1100 1110 1120 1130 1140 NDEDGKVPQL SEPPEEEPNT IEEEELIDEE AKNPWLTGNL VEEANSQGII QNRSIFNLFA 1150 1160 1170 1180 1190 1200 NTNIYIFFRH WTTIYERLLE IKQMNERVTK EINTRSTVTF AKDLDLLSSQ LSEMGLDFVG 1210 1220 1230 1240 1250 1260 EDAYKQVLRL SRRLINGDLE HQWFEESLRQ AYNNKAFKLY TIDKVTQSLV KHAHTLMTDA 1270 1280 1290 1300 1310 1320 KTAEIMALFV KDRNASTTSA KDQIIYRLQV RSHMSNTENM FRIEFDKRTL HVSIQYIALD 1330 1340 1350 1360 1370 1380 DLTLKEPKAD EDKWKYYVTS YALPHPTEGI PHEKLKIPFL ERLIEFGQDI DGTEVDEEFS 1390 1400 1410 1420 1430 1440 PEGISVSTLK IKIQPITYQL HIENGSYDVF TRKATNKYPT IANDNTQKGM VSQKKELISK 1450 1460 1470 1480 1490 1500 FLDCAVGLRN NLDEAQKLSM QKKWENLKDS IAKTSAGNQG IESETEKGKI TKQEQSDNLD 1510 1520 1530 SSTASVLPAS ITTVPQDDNI ETTGNTESSD KGAKIQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Saccharomyces cerevisiae SIN3 gene, a negative regulator of HO, contains four paired amphipathic helix motifs." Wang H., Clark I., Nicholson P.R., Herskowitz I., Stillman D.J. Mol. Cell. Biol. 10:5927-5936(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION. Strain: S288c / GRF88.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV." Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K. Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"RPD1 (SIN3/UME4) is required for maximal activation and repression of diverse yeast genes." Vidal M., Strich R., Easton Esposito R., Gaber R.F. Mol. Cell. Biol. 11:6306-6316(1991) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[5]	"The Saccharomyces cerevisiae GAM2/SIN3 protein plays a role in both activation and repression of transcription." Yoshimoto H., Ohmae M., Yamashita I. Mol. Gen. Genet. 233:327-330(1992) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[6]	"Transcriptional repression in Saccharomyces cerevisiae by a SIN3-LexA fusion protein." Wang H., Stillman D.J. Mol. Cell. Biol. 13:1805-1814(1993) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[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.
[8]	"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: FUNCTION, IDENTIFICATION IN THE RPD3 COMPLEX.
[9]	"Identification of the Saccharomyces cerevisiae genes STB1-STB5 encoding Sin3p binding proteins." Kasten M.M., Stillman D.J. Mol. Gen. Genet. 256:376-386(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH STB1.
[10]	"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.
[11]	"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: FUNCTION.
[12]	"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.
[13]	"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 ESS1.
[14]	"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.
[15]	"Identification of the Sin3-binding site in Ume6 defines a two-step process for conversion of Ume6 from a transcriptional repressor to an activator in yeast." Washburn B.K., Easton Esposito R. Mol. Cell. Biol. 21:2057-2069(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH UME6.
[16]	"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae." Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M. Nat. Biotechnol. 20:301-305(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-303 AND SER-316, MASS SPECTROMETRY. Strain: 2124.
[17]	"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.
[18]	"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.
[19]	"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].
[20]	"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: FUNCTION OF THE RPD3 COMPLEX.
[21]	"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.
[22]	"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: FUNCTION OF THE RPD3 COMPLEX.
[23]	"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.
[24]	"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.
[25]	"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.
[26]	"Genes determining yeast replicative life span in a long-lived genetic background." Kaeberlein M., Kirkland K.T., Fields S., Kennedy B.K. Mech. Ageing Dev. 126:491-504(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[27]	"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-304, MASS SPECTROMETRY. Strain: ADR376.
[28]	"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 SER-1483, MASS SPECTROMETRY.
[29]	"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 SER-137; SER-294; THR-303; THR-304; THR-308; SER-316; SER-318; SER-1046 AND SER-1483, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M36822 Genomic DNA. Translation: AAA34839.1. Z74746 Genomic DNA. Translation: CAA99003.1. BK006948 Genomic DNA. Translation: DAA10779.1.
PIR	RGBYS3. S66686.
RefSeq	NP_014639.1. NM_001183258.1.
3D structure databases
ProteinModelPortal	P22579.
SMR	P22579. Positions 219-287, 401-474, 665-728.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-597N.
IntAct	P22579. 84 interactions.
MINT	MINT-422975.
STRING	4932.YOL004W.
Proteomic databases
PaxDb	P22579.
PeptideAtlas	P22579.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YOL004W; YOL004W; YOL004W.
GeneID	854158.
KEGG	sce:YOL004W.
Organism-specific databases
CYGD	YOL004w.
SGD	S000005364. SIN3.
Phylogenomic databases
eggNOG	COG5602.
GeneTree	ENSGT00390000007239.
HOGENOM	HOG000248545.
KO	K11644.
OMA	NDEWASH.
OrthoDB	EOG4X3M8D.
Enzyme and pathway databases
BioCyc	YEAST:G3O-33421-MONOMER.
Gene expression databases
Genevestigator	P22579.
GermOnline	YOL004W. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	1.20.1160.11. 3 hits.
InterPro	IPR013194. HDAC_interact. IPR003822. PAH. [Graphical view]
Pfam	PF02671. PAH. 3 hits. PF08295. Sin3_corepress. 1 hit. [Graphical view]
SMART	SM00761. HDAC_interact. 1 hit. [Graphical view]
SUPFAM	SSF47762. PAH. 3 hits.
PROSITE	PS51477. PAH. 3 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	975926.

Entry information

Entry name

SIN3_YEAST

Accession

Primary (citable) accession number: P22579
Secondary accession number(s): D6W263, Q08049

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	November 1, 1997
Last modified:	May 29, 2013
This is version 129 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program