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P06701 (SIR3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Regulatory protein SIR3
Alternative name(s):
Silent information regulator 3
Gene names
Name:SIR3
Synonyms:CMT1, MAR2, STE8
Ordered Locus Names:YLR442C
ORF Names:L9753.10
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length978 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The proteins SIR1 through SIR4 are required for transcriptional repression of the silent mating type loci, HML and HMR. The proteins SIR2 through SIR4 repress mulitple loci by modulating chromatin structure. Involves the compaction of chromatin fiber into a more condensed form.

Subunit structure

Homodimer and interacts with SIR4 and RAP1 C-terminus. Interacts with MCM10. Ref.9

Subcellular location

Nucleus.

Post-translational modification

N-terminal acetylation by NatA is important for transcriptional silencing activity. Ref.8

Miscellaneous

Present with 1400 molecules/cell in log phase SD medium.

Sequence similarities

Contains 1 BAH domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   LigandDNA-binding
   Molecular functionRepressor
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from electronic annotation. Source: InterPro

chromatin silencing at silent mating-type cassette

Inferred from mutant phenotype PubMed 16581798. Source: SGD

heterochromatin assembly

Inferred from mutant phenotype PubMed 16908543. Source: SGD

negative regulation of chromatin silencing involved in replicative cell aging

Inferred from direct assay PubMed 9150138. Source: SGD

nuclear-transcribed mRNA catabolic process, non-stop decay

Inferred from mutant phenotype PubMed 17660569. Source: SGD

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentchromatin silencing complex

Inferred from direct assay PubMed 9122169. Source: SGD

chromosome, telomeric region

Inferred from direct assay PubMed 16956377. Source: SGD

nuclear chromosome, telomeric region

Inferred from direct assay PubMed 9710643. Source: SGD

nuclear heterochromatin

Inferred from direct assay PubMed 20176978. Source: SGD

nuclear telomeric heterochromatin

Inferred from direct assay PubMed 9214640. Source: SGD

nucleolus

Inferred from direct assay PubMed 9150138. Source: SGD

origin recognition complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionchromatin binding

Inferred from direct assay PubMed 18195043. Source: SGD

double-stranded DNA binding

Inferred from direct assay PubMed 19099415. Source: SGD

identical protein binding

Inferred from physical interaction PubMed 16717101PubMed 21179020PubMed 23299941. Source: IntAct

nucleosomal histone binding

Inferred from direct assay PubMed 18158898. Source: SGD

nucleosome binding

Inferred from direct assay PubMed 19217406. Source: SGD

protein binding

Inferred from physical interaction PubMed 11689698PubMed 16717101. Source: IntAct

protein homodimerization activity

Inferred from physical interaction PubMed 16908543. Source: SGD

single-stranded DNA binding

Inferred from direct assay PubMed 19099415. Source: SGD

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 978977Regulatory protein SIR3
PRO_0000097768

Regions

Domain48 – 188141BAH

Amino acid modifications

Modified residue21N-acetylalanine Ref.8

Experimental info

Mutagenesis21A → G: No acetylation, reduced silencing activity. Ref.8
Mutagenesis21A → Q: No acetylation, No silencing activity. Ref.8
Mutagenesis21A → S: No effect. Ref.8
Mutagenesis21A → T: Reduced silencing activity. Ref.8
Sequence conflict741I → T in AAT93176. Ref.4
Sequence conflict3311P → S in CAA25668. Ref.1
Sequence conflict3351T → P in CAA25668. Ref.1
Sequence conflict4051S → G in CAA25668. Ref.1
Sequence conflict4211K → Q in CAA25668. Ref.1
Sequence conflict429 – 4302NE → KK in CAA25668. Ref.1
Sequence conflict4971L → V in CAA25668. Ref.1
Sequence conflict5871Q → R in CAA25668. Ref.1
Sequence conflict5971I → V in CAA25668. Ref.1
Sequence conflict6691E → D in CAA25668. Ref.1
Sequence conflict7041R → G in CAA25668. Ref.1
Sequence conflict7121S → T in CAA25668. Ref.1
Sequence conflict7261D → N in CAA25668. Ref.1
Sequence conflict8281L → F Ref.1
Sequence conflict8301V → L Ref.1
Sequence conflict9251Q → K in CAA25668. Ref.1

Secondary structure

............................................................................................................................... 978
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P06701 [UniParc].

Last modified January 23, 2007. Version 6.
Checksum: CA2503D7645397AC

FASTA978111,360
        10         20         30         40         50         60 
MAKTLKDLDG WQVIITDDQG RVIDDNNRRR SRKRGGENVF LKRISDGLSF GKGESVIFND 

        70         80         90        100        110        120 
NVTETYSVYL IHEIRLNTLN NVVEIWVFSY LRWFELKPKL YYEQFRPDLI KEDHPLEFYK 

       130        140        150        160        170        180 
DKFFNEVNKS ELYLTAELSE IWLKDFIAVG QILPESQWND SSIDKIEDRD FLVRYACEPT 

       190        200        210        220        230        240 
AEKFVPIDIF QIIRRVKEME PKQSDEYLKR VSVPVSGQKT NRQVMHKMGV ERSSKRLAKK 

       250        260        270        280        290        300 
PSMKKIKIEP SADDDVNNGN IPSQRGTSTT HGSISPQEES VSPNISSASP SALTSPTDSS 

       310        320        330        340        350        360 
KILQKRSISK ELIVSEEIPI NSSEQESDYE PNNETSVLSS KPGSKPEKTS TELVDGRENF 

       370        380        390        400        410        420 
VYANNPEVSD DGGLEEETDE VSSESSDEAI IPVNKRRGAH GSELSSKIRK IHIQETQEFS 

       430        440        450        460        470        480 
KNYTTETDNE MNGNGKPGIP RGNTKIHSMN ENPTPEKGNA KMIDFATLSK LKKKYQIILD 

       490        500        510        520        530        540 
RFAPDNQVTD SSQLNKLTDE QSSLDVAGLE DKFRKACSSS GRETILSNFN ADINLEESIR 

       550        560        570        580        590        600 
ESLQKRELLK SQVEDFTRIF LPIYDSLMSS QNKLFYITNA DDSTKFQLVN DVMDELITSS 

       610        620        630        640        650        660 
ARKELPIFDY IHIDALELAG MDALYEKIWF AISKENLCGD ISLEALNFYI TNVPKAKKRK 

       670        680        690        700        710        720 
TLILIQNPEN LLSEKILQYF EKWISSKNSK LSIICVGGHN VTIREQINIM PSLKAHFTEI 

       730        740        750        760        770        780 
KLNKVDKNEL QQMIITRLKS LLKPFHVKVN DKKEMTIYNN IREGQNQKIP DNVIVINHKI 

       790        800        810        820        830        840 
NNKITQLIAK NVANVSGSTE KAFKICEAAV EISKKDFVRK GGLQKGKLVV SQEMVPRYFS 

       850        860        870        880        890        900 
EAINGFKDET ISKKIIGMSL LMRTFLYTLA QETEGTNRHT LALETVLIKM VKMLRDNPGY 

       910        920        930        940        950        960 
KASKEIKKVI CGAWEPAITI EKLKQFSWIS VVNDLVGEKL VVVVLEEPSA SIMVELKLPL 

       970 
EINYAFSMDE EFKNMDCI 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of two genes required for the position-effect control of yeast mating-type genes."
Shore D., Squire M., Nasmyth K.A.
EMBO J. 3:2817-2823(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. expand/collapse author list , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
Nature 387:87-90(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]"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.
[5]"Activation of an MAP kinase cascade leads to Sir3p hyperphosphorylation and strengthens transcriptional silencing."
Stone E.M., Pillus L.
J. Cell Biol. 135:571-583(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[6]"The molecular biology of the SIR proteins."
Gasser S.M., Cockell M.M.
Gene 279:1-16(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[7]"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].
[8]"Importance of the sir3 N terminus and its acetylation for yeast transcriptional silencing."
Wang X., Connelly J.J., Wang C.L., Sternglanz R.
Genetics 168:547-551(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ALA-2, ACETYLATION AT ALA-2.
[9]"Dual roles for Mcm10 in DNA replication initiation and silencing at the mating-type loci."
Douglas N.L., Dozier S.K., Donato J.J.
Mol. Biol. Rep. 32:197-204(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MCM10.
[10]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Structure of the Sir3 protein bromo adjacent homology (BAH) domain from S. cerevisiae at 1.95 A resolution."
Hou Z., Danzer J.R., Fox C.A., Keck J.L.
Protein Sci. 15:1182-1186(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 2-229.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X01420 Genomic DNA. Translation: CAA25668.1.
U21094 Genomic DNA. Translation: AAB67522.1.
AY693157 Genomic DNA. Translation: AAT93176.1.
BK006945 Genomic DNA. Translation: DAA09743.1.
PIRRGBYI3. S59410.
RefSeqNP_013547.3. NM_001182330.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2FL7X-ray1.85A1-229[»]
2FVUX-ray2.00A/B1-219[»]
3OWTX-ray2.00C456-481[»]
3TE6X-ray2.80A/B530-845[»]
3TU4X-ray3.00K/L1-213[»]
3ZCOX-ray2.70A840-978[»]
4JJNX-ray3.09K/L2-382[»]
4KUDX-ray3.20K/L2-219[»]
4KUIX-ray1.85A2-219[»]
4KULX-ray2.62A2-219[»]
4LD9X-ray3.31K/L2-229[»]
DisProtDP00533.
ProteinModelPortalP06701.
SMRP06701. Positions 2-215, 530-844, 849-975.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31701. 96 interactions.
DIPDIP-595N.
IntActP06701. 22 interactions.
MINTMINT-673027.
STRING4932.YLR442C.

Proteomic databases

MaxQBP06701.
PaxDbP06701.
PeptideAtlasP06701.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYLR442C; YLR442C; YLR442C.
GeneID851163.
KEGGsce:YLR442C.

Organism-specific databases

SGDS000004434. SIR3.

Phylogenomic databases

eggNOGCOG1474.
GeneTreeENSGT00750000118511.
KOK11122.
OMAYLIHEIR.
OrthoDBEOG7ZWD9N.

Enzyme and pathway databases

BioCycYEAST:G3O-32498-MONOMER.

Gene expression databases

GenevestigatorP06701.

Family and domain databases

InterProIPR001025. BAH_dom.
[Graphical view]
PfamPF01426. BAH. 1 hit.
[Graphical view]
SMARTSM00439. BAH. 1 hit.
[Graphical view]
PROSITEPS51038. BAH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP06701.
NextBio967960.

Entry information

Entry nameSIR3_YEAST
AccessionPrimary (citable) accession number: P06701
Secondary accession number(s): D6VZ77, E9P924
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 132 of the entry and version 6 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XII

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references