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P06701

- SIR3_YEAST

UniProt

P06701 - SIR3_YEAST

Protein

Regulatory protein SIR3

Gene

SIR3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 6 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    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.

    GO - Molecular functioni

    1. chromatin binding Source: SGD
    2. double-stranded DNA binding Source: SGD
    3. identical protein binding Source: IntAct
    4. nucleosomal histone binding Source: SGD
    5. nucleosome binding Source: SGD
    6. protein binding Source: IntAct
    7. protein homodimerization activity Source: SGD
    8. single-stranded DNA binding Source: SGD

    GO - Biological processi

    1. chromatin silencing at silent mating-type cassette Source: SGD
    2. heterochromatin assembly Source: SGD
    3. negative regulation of chromatin silencing involved in replicative cell aging Source: SGD
    4. nuclear-transcribed mRNA catabolic process, non-stop decay Source: SGD
    5. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-32498-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Regulatory protein SIR3
    Alternative name(s):
    Silent information regulator 3
    Gene namesi
    Name:SIR3
    Synonyms:CMT1, MAR2, STE8
    Ordered Locus Names:YLR442C
    ORF Names:L9753.10
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XII

    Organism-specific databases

    SGDiS000004434. SIR3.

    Subcellular locationi

    GO - Cellular componenti

    1. chromatin silencing complex Source: SGD
    2. chromosome, telomeric region Source: SGD
    3. nuclear chromosome, telomeric region Source: SGD
    4. nuclear heterochromatin Source: SGD
    5. nuclear telomeric heterochromatin Source: SGD
    6. nucleolus Source: SGD

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2 – 21A → G: No acetylation, reduced silencing activity. 1 Publication
    Mutagenesisi2 – 21A → Q: No acetylation, No silencing activity. 1 Publication
    Mutagenesisi2 – 21A → S: No effect. 1 Publication
    Mutagenesisi2 – 21A → T: Reduced silencing activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 978977Regulatory protein SIR3PRO_0000097768Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication

    Post-translational modificationi

    N-terminal acetylation by NatA is important for transcriptional silencing activity.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP06701.
    PaxDbiP06701.
    PeptideAtlasiP06701.

    Expressioni

    Gene expression databases

    GenevestigatoriP06701.

    Interactioni

    Subunit structurei

    Homodimer and interacts with SIR4 and RAP1 C-terminus. Interacts with MCM10.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself8EBI-17230,EBI-17230
    RAP1P119382EBI-17230,EBI-14821
    SIR4P119786EBI-17230,EBI-17237

    Protein-protein interaction databases

    BioGridi31701. 96 interactions.
    DIPiDIP-595N.
    IntActiP06701. 22 interactions.
    MINTiMINT-673027.
    STRINGi4932.YLR442C.

    Structurei

    Secondary structure

    1
    978
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 43
    Helixi5 – 84
    Beta strandi11 – 166
    Beta strandi18 – 203
    Beta strandi22 – 243
    Beta strandi27 – 304
    Turni31 – 355
    Beta strandi37 – 437
    Turni44 – 463
    Beta strandi49 – 513
    Beta strandi55 – 606
    Turni61 – 644
    Beta strandi65 – 7511
    Beta strandi79 – 824
    Beta strandi84 – 918
    Helixi93 – 953
    Helixi98 – 1058
    Helixi107 – 1115
    Helixi116 – 12611
    Beta strandi131 – 14111
    Helixi143 – 1453
    Beta strandi146 – 1494
    Beta strandi151 – 1533
    Turni155 – 1573
    Beta strandi159 – 1635
    Turni167 – 1693
    Beta strandi170 – 1767
    Turni179 – 1813
    Beta strandi184 – 1863
    Helixi189 – 19810
    Helixi201 – 21111
    Helixi465 – 47511
    Helixi535 – 56834
    Beta strandi574 – 5785
    Helixi583 – 59816
    Turni599 – 6035
    Beta strandi608 – 6147
    Helixi622 – 63211
    Helixi643 – 65210
    Helixi655 – 6573
    Beta strandi660 – 6667
    Beta strandi669 – 6713
    Helixi675 – 68511
    Beta strandi691 – 6966
    Helixi704 – 7085
    Helixi711 – 7144
    Beta strandi717 – 7215
    Helixi727 – 74115
    Beta strandi745 – 7495
    Beta strandi755 – 7573
    Beta strandi773 – 7764
    Helixi782 – 79615
    Helixi799 – 82022
    Beta strandi831 – 8333
    Helixi837 – 8437
    Helixi851 – 8566
    Helixi860 – 87314
    Beta strandi874 – 8763
    Beta strandi880 – 8823
    Helixi883 – 89614
    Helixi901 – 91010
    Helixi920 – 9234
    Helixi928 – 93710
    Beta strandi940 – 9456
    Beta strandi947 – 9493
    Beta strandi952 – 9565
    Helixi959 – 96810
    Helixi970 – 9723

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    DisProtiDP00533.
    ProteinModelPortaliP06701.
    SMRiP06701. Positions 2-215, 530-844, 849-975.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06701.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini48 – 188141BAHPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 BAH domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG1474.
    GeneTreeiENSGT00750000118511.
    KOiK11122.
    OMAiYLIHEIR.
    OrthoDBiEOG7ZWD9N.

    Family and domain databases

    InterProiIPR001025. BAH_dom.
    [Graphical view]
    PfamiPF01426. BAH. 1 hit.
    [Graphical view]
    SMARTiSM00439. BAH. 1 hit.
    [Graphical view]
    PROSITEiPS51038. BAH. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P06701-1 [UniParc]FASTAAdd to Basket

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    MAKTLKDLDG WQVIITDDQG RVIDDNNRRR SRKRGGENVF LKRISDGLSF    50
    GKGESVIFND NVTETYSVYL IHEIRLNTLN NVVEIWVFSY LRWFELKPKL 100
    YYEQFRPDLI KEDHPLEFYK DKFFNEVNKS ELYLTAELSE IWLKDFIAVG 150
    QILPESQWND SSIDKIEDRD FLVRYACEPT AEKFVPIDIF QIIRRVKEME 200
    PKQSDEYLKR VSVPVSGQKT NRQVMHKMGV ERSSKRLAKK PSMKKIKIEP 250
    SADDDVNNGN IPSQRGTSTT HGSISPQEES VSPNISSASP SALTSPTDSS 300
    KILQKRSISK ELIVSEEIPI NSSEQESDYE PNNETSVLSS KPGSKPEKTS 350
    TELVDGRENF VYANNPEVSD DGGLEEETDE VSSESSDEAI IPVNKRRGAH 400
    GSELSSKIRK IHIQETQEFS KNYTTETDNE MNGNGKPGIP RGNTKIHSMN 450
    ENPTPEKGNA KMIDFATLSK LKKKYQIILD RFAPDNQVTD SSQLNKLTDE 500
    QSSLDVAGLE DKFRKACSSS GRETILSNFN ADINLEESIR ESLQKRELLK 550
    SQVEDFTRIF LPIYDSLMSS QNKLFYITNA DDSTKFQLVN DVMDELITSS 600
    ARKELPIFDY IHIDALELAG MDALYEKIWF AISKENLCGD ISLEALNFYI 650
    TNVPKAKKRK TLILIQNPEN LLSEKILQYF EKWISSKNSK LSIICVGGHN 700
    VTIREQINIM PSLKAHFTEI KLNKVDKNEL QQMIITRLKS LLKPFHVKVN 750
    DKKEMTIYNN IREGQNQKIP DNVIVINHKI NNKITQLIAK NVANVSGSTE 800
    KAFKICEAAV EISKKDFVRK GGLQKGKLVV SQEMVPRYFS EAINGFKDET 850
    ISKKIIGMSL LMRTFLYTLA QETEGTNRHT LALETVLIKM VKMLRDNPGY 900
    KASKEIKKVI CGAWEPAITI EKLKQFSWIS VVNDLVGEKL VVVVLEEPSA 950
    SIMVELKLPL EINYAFSMDE EFKNMDCI 978
    Length:978
    Mass (Da):111,360
    Last modified:January 23, 2007 - v6
    Checksum:iCA2503D7645397AC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti74 – 741I → T in AAT93176. (PubMed:17322287)Curated
    Sequence conflicti331 – 3311P → S in CAA25668. (PubMed:6098447)Curated
    Sequence conflicti335 – 3351T → P in CAA25668. (PubMed:6098447)Curated
    Sequence conflicti405 – 4051S → G in CAA25668. (PubMed:6098447)Curated
    Sequence conflicti421 – 4211K → Q in CAA25668. (PubMed:6098447)Curated
    Sequence conflicti429 – 4302NE → KK in CAA25668. (PubMed:6098447)Curated
    Sequence conflicti497 – 4971L → V in CAA25668. (PubMed:6098447)Curated
    Sequence conflicti587 – 5871Q → R in CAA25668. (PubMed:6098447)Curated
    Sequence conflicti597 – 5971I → V in CAA25668. (PubMed:6098447)Curated
    Sequence conflicti669 – 6691E → D in CAA25668. (PubMed:6098447)Curated
    Sequence conflicti704 – 7041R → G in CAA25668. (PubMed:6098447)Curated
    Sequence conflicti712 – 7121S → T in CAA25668. (PubMed:6098447)Curated
    Sequence conflicti726 – 7261D → N in CAA25668. (PubMed:6098447)Curated
    Sequence conflicti828 – 8281L → F(PubMed:6098447)Curated
    Sequence conflicti830 – 8301V → L(PubMed:6098447)Curated
    Sequence conflicti925 – 9251Q → K in CAA25668. (PubMed:6098447)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01420 Genomic DNA. Translation: CAA25668.1.
    U21094 Genomic DNA. Translation: AAB67522.1.
    AY693157 Genomic DNA. Translation: AAT93176.1.
    BK006945 Genomic DNA. Translation: DAA09743.1.
    PIRiS59410. RGBYI3.
    RefSeqiNP_013547.3. NM_001182330.3.

    Genome annotation databases

    EnsemblFungiiYLR442C; YLR442C; YLR442C.
    GeneIDi851163.
    KEGGisce:YLR442C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01420 Genomic DNA. Translation: CAA25668.1 .
    U21094 Genomic DNA. Translation: AAB67522.1 .
    AY693157 Genomic DNA. Translation: AAT93176.1 .
    BK006945 Genomic DNA. Translation: DAA09743.1 .
    PIRi S59410. RGBYI3.
    RefSeqi NP_013547.3. NM_001182330.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2FL7 X-ray 1.85 A 1-229 [» ]
    2FVU X-ray 2.00 A/B 1-219 [» ]
    3OWT X-ray 2.00 C 456-481 [» ]
    3TE6 X-ray 2.80 A/B 530-845 [» ]
    3TU4 X-ray 3.00 K/L 1-213 [» ]
    3ZCO X-ray 2.70 A 840-978 [» ]
    4JJN X-ray 3.09 K/L 2-382 [» ]
    4KUD X-ray 3.20 K/L 2-219 [» ]
    4KUI X-ray 1.85 A 2-219 [» ]
    4KUL X-ray 2.62 A 2-219 [» ]
    4LD9 X-ray 3.31 K/L 2-229 [» ]
    DisProti DP00533.
    ProteinModelPortali P06701.
    SMRi P06701. Positions 2-215, 530-844, 849-975.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31701. 96 interactions.
    DIPi DIP-595N.
    IntActi P06701. 22 interactions.
    MINTi MINT-673027.
    STRINGi 4932.YLR442C.

    Proteomic databases

    MaxQBi P06701.
    PaxDbi P06701.
    PeptideAtlasi P06701.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YLR442C ; YLR442C ; YLR442C .
    GeneIDi 851163.
    KEGGi sce:YLR442C.

    Organism-specific databases

    SGDi S000004434. SIR3.

    Phylogenomic databases

    eggNOGi COG1474.
    GeneTreei ENSGT00750000118511.
    KOi K11122.
    OMAi YLIHEIR.
    OrthoDBi EOG7ZWD9N.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-32498-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P06701.
    NextBioi 967960.

    Gene expression databases

    Genevestigatori P06701.

    Family and domain databases

    InterProi IPR001025. BAH_dom.
    [Graphical view ]
    Pfami PF01426. BAH. 1 hit.
    [Graphical view ]
    SMARTi SM00439. BAH. 1 hit.
    [Graphical view ]
    PROSITEi PS51038. BAH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. 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. 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.

    Entry informationi

    Entry nameiSIR3_YEAST
    AccessioniPrimary (citable) accession number: P06701
    Secondary accession number(s): D6VZ77, E9P924
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 134 of the entry and version 6 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 1400 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome XII
      Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

    External Data

    Dasty 3