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P21691 (SIR1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Regulatory protein SIR1
Alternative name(s):
Heterochromatin protein SIR1
Silent information regulator 1
Gene names
Name:SIR1
Ordered Locus Names:YKR101W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length654 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the establishment, but not the maintenance, of heterochromatic silencing at the cryptic mating-type loci HMR and HML. Is recruited by interacting with the ORC1 subunit of the origin recognition complex (ORC), which binds to HML-I or HMR-E silencers, DNA elements that direct the formation of silent chromatin at the mating-type loci. Establishes transcriptional silencing by recruiting the three other SIR proteins, SIR2, SIR3, and SIR4, that function directly in silenced chromatin and establish repression. Also found in centromeric chromatin. Binds to and helps retain CAC1, a subunit of chromatin assembly factor I (CAF-I) at centromeric loci independent on the other SIR proteins. Ref.4 Ref.5 Ref.9

Subunit structure

Interacts (via OIR domain) with ORC1 (via BAH domain). Interacts with SIR4. Interacts with CAC1. Ref.5 Ref.8 Ref.10 Ref.11

Subcellular location

Nucleus. Chromosomecentromere. Note: Associated primarily with the HMR-E silencer at the HMR locus. Ref.7 Ref.8 Ref.9 Ref.10

Sequence caution

The sequence AAA35046.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAA82181.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 654654Regulatory protein SIR1
PRO_0000097767

Regions

Region322 – 654333Sufficient for interaction with SIR4
Region449 – 587139ORC interacting region (OIR)

Experimental info

Mutagenesis462 – 4643EEE → AAA: No effect. Ref.11
Mutagenesis4661V → G: Abolishes interaction with ORC1. Ref.11
Mutagenesis4691R → G: Abolishes interaction with ORC1. Ref.11
Mutagenesis4701F → S: Abolishes interaction with ORC1 and SIR4. Ref.11
Mutagenesis4771L → P: Abolishes interaction with ORC1 and SIR4. Ref.11
Mutagenesis4791D → N: Abolishes interaction with ORC1. Ref.11
Mutagenesis4801L → P: Abolishes interaction with ORC1. Ref.11
Mutagenesis482 – 4832EE → AA: No effect.
Mutagenesis489 – 4902KD → AA: No effect.
Mutagenesis498 – 4992KD → AA: No effect.
Mutagenesis5131W → R: Abolishes interaction with ORC1 and SIR4. Ref.11
Mutagenesis517 – 5182KK → AA: No effect.
Mutagenesis5341C → A: No effect. Ref.11
Mutagenesis538 – 5403KKK → AAA: Abolishes interaction with SIR4. Ref.11
Mutagenesis5691C → A: No effect.
Mutagenesis5711C → R: Abolishes interaction with ORC1 and SIR4. Ref.11
Mutagenesis5721V → G: No effect. Ref.11
Mutagenesis5731P → S: No effect. Ref.11
Mutagenesis577 – 5782DD → AA: Abolishes interaction with SIR4.
Mutagenesis5841L → P or Q: Abolishes interaction with ORC1 and SIR4. Ref.11
Mutagenesis586 – 5872DD → AA: Abolishes interaction with SIR4.

Secondary structure

........................... 654
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P21691 [UniParc].

Last modified July 28, 2009. Version 2.
Checksum: 00FEABD1BD35BC81

FASTA65476,933
        10         20         30         40         50         60 
MLQINSRLAV IDGWLVDTVK RKPINFRSPE VRLLLPNDDD YKKLSQQNLV DWTRLKKDSN 

        70         80         90        100        110        120 
SVLVGVKSME LFKHIKLVLR EFFLLEDGRI ILKRIRSKLR YKVVKKLTCK CCRLYLPKWG 

       130        140        150        160        170        180 
TVYIHPMLKD KEKPLAGVCE FSLDVNPDRE YPLIEINVSH QYIIIEGFLL YLNERRLYRW 

       190        200        210        220        230        240 
NDNNLRSQVG LTKWAHLRKT YNPVSLDILY SLNSNFYFVK DDLLFQLLGK RVFVKFCKVM 

       250        260        270        280        290        300 
ENGKCGKAPL WYRVKRTTTA KATHIAYAIS NSTAPDSFKS KNNDYRFIVR EKPIVENTIS 

       310        320        330        340        350        360 
NLDYSDIKKQ QFTEAEVVKR KISADISQIE NVHTQFNSQK EKNNIRVNKV SSEVLDQISK 

       370        380        390        400        410        420 
FPVSRVTLLL MSAGQDKNYI ELVEELARRL EKICIEKTTQ SLEEIRDTFQ ANPEMQASFD 

       430        440        450        460        470        480 
KEYYQSIEEY KITLELIKED LLITLIKQME NMWAAEKKFS TEEEYVSPRF LVADGFLIDL 

       490        500        510        520        530        540 
AEEKPINPKD PRLLTLLKDH QRAMIDQMNL VKWNDFKKYQ DPIPLKAKTL FKFCKQIKKK 

       550        560        570        580        590        600 
FLRGADFKLH TLPTEANLKY EPERMTVLCS CVPILLDDQT VQYLYDDSII PEFEATSSYA 

       610        620        630        640        650 
TKQSKCGRKM SLQMEPDLLF QEAIRRMRHL TAYDVLRRNY IAAFEELYMG NCND 

« Hide

References

« Hide 'large scale' references
[1]"The SIR1 gene of Saccharomyces cerevisiae and its role as an extragenic suppressor of several mating-defective mutants."
Stone E.M., Swanson M.J., Romeo A.M., Hicks J.B., Sternglanz R.
Mol. Cell. Biol. 11:2253-2262(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete DNA sequence of yeast chromosome XI."
Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C. expand/collapse author list , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
Nature 369:371-378(1994) [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]"Targeting of SIR1 protein establishes transcriptional silencing at HM loci and telomeres in yeast."
Chien C.T., Buck S., Sternglanz R., Shore D.
Cell 75:531-541(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"Role of interactions between the origin recognition complex and SIR1 in transcriptional silencing."
Triolo T., Sternglanz R.
Nature 381:251-253(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ORC1.
[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]"The Sir1 protein's association with a silenced chromosome domain."
Gardner K.A., Fox C.A.
Genes Dev. 15:147-157(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[8]"Structure and function of the BAH-containing domain of Orc1p in epigenetic silencing."
Zhang Z., Hayashi M.K., Merkel O., Stillman B., Xu R.-M.
EMBO J. 21:4600-4611(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ORC1.
[9]"Ordered nucleation and spreading of silenced chromatin in Saccharomyces cerevisiae."
Rusche L.N., Kirchmaier A.L., Rine J.
Mol. Biol. Cell 13:2207-2222(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[10]"The budding yeast silencing protein Sir1 is a functional component of centromeric chromatin."
Sharp J.A., Krawitz D.C., Gardner K.A., Fox C.A., Kaufman P.D.
Genes Dev. 17:2356-2361(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CAC1.
[11]"The origin recognition complex and Sir4 protein recruit Sir1p to yeast silent chromatin through independent interactions requiring a common Sir1p domain."
Bose M.E., McConnell K.H., Gardner-Aukema K.A., Mueller U., Weinreich M., Keck J.L., Fox C.A.
Mol. Cell. Biol. 24:774-786(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ORC1 AND SIR4, MUTAGENESIS OF 462-GLU--GLU-464; VAL-466; ARG-469; PHE-470; LEU-477; ASP-479; LEU-480; 482-GLU-GLU-483; 489-LYS-ASP-490; 498-LYS-ASP-499; TRP-513; 517-LYS-LYS-518; CYS-534; 538-LYS--LYS-540; CYS-571; VAL-572; PRO-573; 577-ASP-ASP-578; LEU-584 AND 586-ASP-ASP-587.
[12]"Elaboration, diversification and regulation of the sir1 family of silencing proteins in Saccharomyces."
Gallagher J.E.G., Babiarz J.E., Teytelman L., Wolfe K.H., Rine J.
Genetics 181:1477-1491(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF INITIATION SITE.
[13]"Structural basis of the Sir1-origin recognition complex interaction in transcriptional silencing."
Hou Z., Bernstein D.A., Fox C.A., Keck J.L.
Proc. Natl. Acad. Sci. U.S.A. 102:8489-8494(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 449-587 OF MUTANT ALA-569 IN COMPLEX WITH ORC1.
[14]"Structural basis for origin recognition complex 1 protein-silence information regulator 1 protein interaction in epigenetic silencing."
Hsu H.-C., Stillman B., Xu R.-M.
Proc. Natl. Acad. Sci. U.S.A. 102:8519-8524(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 456-588 IN COMPLEX WITH ORC1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M38524 Genomic DNA. Translation: AAA35046.1. Different initiation.
Z28326 Genomic DNA. Translation: CAA82181.1. Different initiation.
BK006944 Genomic DNA. Translation: DAA09252.1.
PIRS14173.
RefSeqNP_013027.4. NM_001179891.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z1AX-ray2.50A/B449-587[»]
1ZBXX-ray2.50B456-588[»]
1ZHIX-ray2.70B456-587[»]
ProteinModelPortalP21691.
SMRP21691. Positions 463-587.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34232. 70 interactions.
DIPDIP-2453N.
IntActP21691. 3 interactions.
MINTMINT-518571.
STRING4932.YKR101W.

Proteomic databases

MaxQBP21691.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYKR101W; YKR101W; YKR101W.
GeneID853976.
KEGGsce:YKR101W.

Organism-specific databases

CYGDYKR101w.
SGDS000001809. SIR1.

Phylogenomic databases

eggNOGNOG281951.
KOK11120.
OMAVENTISN.
OrthoDBEOG7Z0K50.

Enzyme and pathway databases

BioCycYEAST:G3O-32063-MONOMER.

Gene expression databases

GenevestigatorP21691.

Family and domain databases

InterProIPR021646. Regulatory_Sir1.
[Graphical view]
PfamPF11603. Sir1. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP21691.
NextBio975431.

Entry information

Entry nameSIR1_YEAST
AccessionPrimary (citable) accession number: P21691
Secondary accession number(s): D6VXG2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: July 28, 2009
Last modified: June 11, 2014
This is version 108 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 XI

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

Yeast

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references