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P22579 (SIN3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 139. 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:
Transcriptional regulatory protein SIN3
Gene names
Name:SIN3
Synonyms:CPE1, GAM2, RPD1, SDI1, SDS16, UME4
Ordered Locus Names:YOL004W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1536 AA.
Sequence statusComplete.
Protein existenceEvidence 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.17 Ref.19 Ref.20 Ref.21 Ref.22 Ref.24 Ref.25

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.16 Ref.23 Ref.24

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 processCell cycle
Cell division
Transcription
Transcription regulation
   Cellular componentNucleus
   DomainRepeat
   Molecular functionActivator
Chromatin regulator
Repressor
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdouble-strand break repair via nonhomologous end joining

Inferred from mutant phenotype Ref.22. 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

Inferred from mutant phenotype PubMed 11095743Ref.21. 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.20. Source: SGD

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

Inferred from genetic interaction PubMed 17908798. Source: SGD

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transfer RNA gene-mediated silencing

Inferred from mutant phenotype PubMed 23707796. Source: SGD

   Cellular_componentRpd3L complex

Inferred from direct assay PubMed 16286007Ref.24Ref.23. Source: SGD

Rpd3S complex

Inferred from direct assay PubMed 16286007Ref.24. Source: SGD

Sin3-type complex

Inferred from direct assay Ref.8. Source: SGD

   Molecular_functionidentical protein binding

Inferred from physical interaction PubMed 11454208PubMed 11805826PubMed 21179020. Source: IntAct

protein binding

Inferred from physical interaction PubMed 11454208PubMed 11805826PubMed 16275642PubMed 16429126PubMed 17101441PubMed 21179020. Source: IntAct

transcription coactivator activity

Inferred from mutant phenotype Ref.21. Source: SGD

transcription corepressor activity

Inferred from mutant phenotype PubMed 9150136. Source: SGD

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 15361536Transcriptional regulatory protein SIN3
PRO_0000121544

Regions

Domain217 – 28771PAH 1
Domain404 – 47471PAH 2
Domain656 – 72772PAH 3
Compositional bias480 – 51940Gln-rich

Amino acid modifications

Modified residue1371Phosphoserine Ref.27
Modified residue3031Phosphothreonine Ref.28
Modified residue3041Phosphothreonine Ref.26 Ref.28
Modified residue3161Phosphoserine Ref.28
Modified residue10461Phosphoserine Ref.28

Experimental info

Sequence conflict5101Q → QAQ Ref.1

Sequences

Sequence LengthMass (Da)Tools
P22579 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 0834726312B13878

FASTA1,536174,839
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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 204508 / S288c.
[3]"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.
[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]"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.
[17]"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.
[18]"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].
[19]"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.
[20]"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.
[21]"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.
[22]"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.
[23]"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.
[24]"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.
[25]"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.
[26]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[27]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"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 THR-303; THR-304; SER-316 AND SER-1046, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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.
PIRRGBYS3. S66686.
RefSeqNP_014639.1. NM_001183258.1.

3D structure databases

ProteinModelPortalP22579.
SMRP22579. Positions 219-287.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34400. 533 interactions.
DIPDIP-597N.
IntActP22579. 84 interactions.
MINTMINT-422975.
STRING4932.YOL004W.

Proteomic databases

MaxQBP22579.
PaxDbP22579.
PeptideAtlasP22579.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYOL004W; YOL004W; YOL004W.
GeneID854158.
KEGGsce:YOL004W.

Organism-specific databases

CYGDYOL004w.
SGDS000005364. SIN3.

Phylogenomic databases

eggNOGCOG5602.
GeneTreeENSGT00390000007239.
HOGENOMHOG000248545.
KOK11644.
OMAREQKPIQ.
OrthoDBEOG7T4MTQ.

Enzyme and pathway databases

BioCycYEAST:G3O-33421-MONOMER.

Gene expression databases

GenevestigatorP22579.

Family and domain databases

Gene3D1.20.1160.11. 3 hits.
InterProIPR013194. HDAC_interact.
IPR003822. PAH.
[Graphical view]
PfamPF02671. PAH. 3 hits.
PF08295. Sin3_corepress. 1 hit.
[Graphical view]
SMARTSM00761. HDAC_interact. 1 hit.
[Graphical view]
SUPFAMSSF47762. SSF47762. 3 hits.
PROSITEPS51477. PAH. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio975926.
PROP22579.

Entry information

Entry nameSIN3_YEAST
AccessionPrimary (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: June 11, 2014
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XV

Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families