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P21691

- SIR1_YEAST

UniProt

P21691 - SIR1_YEAST

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Protein

Regulatory protein SIR1

Gene

SIR1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.3 Publications

GO - Molecular functioni

  1. chromatin binding Source: SGD
  2. sequence-specific DNA binding Source: SGD

GO - Biological processi

  1. chromatin silencing at silent mating-type cassette Source: SGD
  2. establishment of chromatin silencing Source: SGD
  3. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciYEAST:G3O-32063-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Regulatory protein SIR1
Alternative name(s):
Heterochromatin protein SIR1
Silent information regulator 1
Gene namesi
Name:SIR1
Ordered Locus Names:YKR101W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XI

Organism-specific databases

CYGDiYKR101w.
SGDiS000001809. SIR1.

Subcellular locationi

Nucleus. Chromosomecentromere
Note: Associated primarily with the HMR-E silencer at the HMR locus.

GO - Cellular componenti

  1. chromatin silencing complex Source: SGD
  2. chromosome, centromeric region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi462 – 4643EEE → AAA: No effect. 1 Publication
Mutagenesisi466 – 4661V → G: Abolishes interaction with ORC1. 1 Publication
Mutagenesisi469 – 4691R → G: Abolishes interaction with ORC1. 1 Publication
Mutagenesisi470 – 4701F → S: Abolishes interaction with ORC1 and SIR4. 1 Publication
Mutagenesisi477 – 4771L → P: Abolishes interaction with ORC1 and SIR4. 1 Publication
Mutagenesisi479 – 4791D → N: Abolishes interaction with ORC1. 1 Publication
Mutagenesisi480 – 4801L → P: Abolishes interaction with ORC1. 1 Publication
Mutagenesisi482 – 4832EE → AA: No effect. 1 Publication
Mutagenesisi489 – 4902KD → AA: No effect. 1 Publication
Mutagenesisi498 – 4992KD → AA: No effect. 1 Publication
Mutagenesisi513 – 5131W → R: Abolishes interaction with ORC1 and SIR4. 1 Publication
Mutagenesisi517 – 5182KK → AA: No effect. 1 Publication
Mutagenesisi534 – 5341C → A: No effect. 1 Publication
Mutagenesisi538 – 5403KKK → AAA: Abolishes interaction with SIR4. 1 Publication
Mutagenesisi569 – 5691C → A: No effect.
Mutagenesisi571 – 5711C → R: Abolishes interaction with ORC1 and SIR4. 1 Publication
Mutagenesisi572 – 5721V → G: No effect. 1 Publication
Mutagenesisi573 – 5731P → S: No effect. 1 Publication
Mutagenesisi577 – 5782DD → AA: Abolishes interaction with SIR4. 1 Publication
Mutagenesisi584 – 5841L → P or Q: Abolishes interaction with ORC1 and SIR4. 1 Publication
Mutagenesisi586 – 5872DD → AA: Abolishes interaction with SIR4. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 654654Regulatory protein SIR1PRO_0000097767Add
BLAST

Proteomic databases

MaxQBiP21691.

Expressioni

Gene expression databases

GenevestigatoriP21691.

Interactioni

Subunit structurei

Interacts (via OIR domain) with ORC1 (via BAH domain). Interacts with SIR4. Interacts with CAC1.6 Publications

Protein-protein interaction databases

BioGridi34232. 72 interactions.
DIPiDIP-2453N.
IntActiP21691. 3 interactions.
MINTiMINT-518571.
STRINGi4932.YKR101W.

Structurei

Secondary structure

1
654
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi464 – 47310
Beta strandi476 – 4794
Turni480 – 4834
Beta strandi484 – 4863
Helixi493 – 4964
Helixi499 – 5068
Helixi513 – 5164
Beta strandi523 – 5253
Helixi530 – 5334
Beta strandi537 – 5437
Beta strandi547 – 5504
Beta strandi566 – 57510
Beta strandi577 – 5793
Beta strandi581 – 5866

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z1AX-ray2.50A/B449-587[»]
1ZBXX-ray2.50B456-588[»]
1ZHIX-ray2.70B456-587[»]
ProteinModelPortaliP21691.
SMRiP21691. Positions 463-587.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21691.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni322 – 654333Sufficient for interaction with SIR4Add
BLAST
Regioni449 – 587139ORC interacting region (OIR)Add
BLAST

Phylogenomic databases

eggNOGiNOG281951.
InParanoidiP21691.
KOiK11120.
OMAiVENTISN.
OrthoDBiEOG7Z0K50.

Family and domain databases

InterProiIPR021646. Regulatory_Sir1.
[Graphical view]
PfamiPF11603. Sir1. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P21691-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLQINSRLAV IDGWLVDTVK RKPINFRSPE VRLLLPNDDD YKKLSQQNLV
60 70 80 90 100
DWTRLKKDSN SVLVGVKSME LFKHIKLVLR EFFLLEDGRI ILKRIRSKLR
110 120 130 140 150
YKVVKKLTCK CCRLYLPKWG TVYIHPMLKD KEKPLAGVCE FSLDVNPDRE
160 170 180 190 200
YPLIEINVSH QYIIIEGFLL YLNERRLYRW NDNNLRSQVG LTKWAHLRKT
210 220 230 240 250
YNPVSLDILY SLNSNFYFVK DDLLFQLLGK RVFVKFCKVM ENGKCGKAPL
260 270 280 290 300
WYRVKRTTTA KATHIAYAIS NSTAPDSFKS KNNDYRFIVR EKPIVENTIS
310 320 330 340 350
NLDYSDIKKQ QFTEAEVVKR KISADISQIE NVHTQFNSQK EKNNIRVNKV
360 370 380 390 400
SSEVLDQISK FPVSRVTLLL MSAGQDKNYI ELVEELARRL EKICIEKTTQ
410 420 430 440 450
SLEEIRDTFQ ANPEMQASFD KEYYQSIEEY KITLELIKED LLITLIKQME
460 470 480 490 500
NMWAAEKKFS TEEEYVSPRF LVADGFLIDL AEEKPINPKD PRLLTLLKDH
510 520 530 540 550
QRAMIDQMNL VKWNDFKKYQ DPIPLKAKTL FKFCKQIKKK FLRGADFKLH
560 570 580 590 600
TLPTEANLKY EPERMTVLCS CVPILLDDQT VQYLYDDSII PEFEATSSYA
610 620 630 640 650
TKQSKCGRKM SLQMEPDLLF QEAIRRMRHL TAYDVLRRNY IAAFEELYMG

NCND
Length:654
Mass (Da):76,933
Last modified:July 28, 2009 - v2
Checksum:i00FEABD1BD35BC81
GO

Sequence cautioni

The sequence AAA35046.1 differs from that shown. Reason: Erroneous initiation.
The sequence CAA82181.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M38524 Genomic DNA. Translation: AAA35046.1. Different initiation.
Z28326 Genomic DNA. Translation: CAA82181.1. Different initiation.
BK006944 Genomic DNA. Translation: DAA09252.1.
PIRiS14173.
RefSeqiNP_013027.4. NM_001179891.3.

Genome annotation databases

EnsemblFungiiYKR101W; YKR101W; YKR101W.
GeneIDi853976.
KEGGisce:YKR101W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M38524 Genomic DNA. Translation: AAA35046.1 . Different initiation.
Z28326 Genomic DNA. Translation: CAA82181.1 . Different initiation.
BK006944 Genomic DNA. Translation: DAA09252.1 .
PIRi S14173.
RefSeqi NP_013027.4. NM_001179891.3.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1Z1A X-ray 2.50 A/B 449-587 [» ]
1ZBX X-ray 2.50 B 456-588 [» ]
1ZHI X-ray 2.70 B 456-587 [» ]
ProteinModelPortali P21691.
SMRi P21691. Positions 463-587.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 34232. 72 interactions.
DIPi DIP-2453N.
IntActi P21691. 3 interactions.
MINTi MINT-518571.
STRINGi 4932.YKR101W.

Proteomic databases

MaxQBi P21691.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YKR101W ; YKR101W ; YKR101W .
GeneIDi 853976.
KEGGi sce:YKR101W.

Organism-specific databases

CYGDi YKR101w.
SGDi S000001809. SIR1.

Phylogenomic databases

eggNOGi NOG281951.
InParanoidi P21691.
KOi K11120.
OMAi VENTISN.
OrthoDBi EOG7Z0K50.

Enzyme and pathway databases

BioCyci YEAST:G3O-32063-MONOMER.

Miscellaneous databases

EvolutionaryTracei P21691.
NextBioi 975431.

Gene expression databases

Genevestigatori P21691.

Family and domain databases

InterProi IPR021646. Regulatory_Sir1.
[Graphical view ]
Pfami PF11603. Sir1. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiSIR1_YEAST
AccessioniPrimary (citable) accession number: P21691
Secondary accession number(s): D6VXG2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: July 28, 2009
Last modified: October 29, 2014
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

External Data

Dasty 3