Regulatory protein SIR3

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

Miscellaneous

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• chromatin binding Source: SGD <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "Long-range communication between the silencers of HMR."
    Valenzuela L., Dhillon N., Dubey R.N., Gartenberg M.R., Kamakaka R.T.
    Mol Cell Biol 28:1924-1935(2008) [PubMed] [Europe PMC] [Abstract]
• double-stranded DNA binding Source: SGDInferred from direct assayⁱ
  • "Role of nucleic acid binding in Sir3p-dependent interactions with chromatin fibers."
    Adkins N.L., McBryant S.J., Johnson C.N., Leidy J.M., Woodcock C.L., Robert C.H., Hansen J.C., Georgel P.T.
    Biochemistry 48:276-288(2009) [PubMed] [Europe PMC] [Abstract]
• identical protein binding Source: IntAct <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • "Domain structure and protein interactions of the silent information regulator Sir3 revealed by screening a nested deletion library of protein fragments."
    King D.A., Hall B.E., Iwamoto M.A., Win K.Z., Chang J.F., Ellenberger T.
    J Biol Chem 281:20107-20119(2006) [PubMed] [Europe PMC] [Abstract]
  • "Defining the budding yeast chromatin-associated interactome."
    Lambert J.P., Fillingham J., Siahbazi M., Greenblatt J., Baetz K., Figeys D.
    Mol Syst Biol 6:448-448(2010) [PubMed] [Europe PMC] [Abstract]
  • "Dimerization of Sir3 via its C-terminal winged helix domain is essential for yeast heterochromatin formation."
    Oppikofer M., Kueng S., Keusch J.J., Hassler M., Ladurner A.G., Gut H., Gasser S.M.
    EMBO J 32:437-449(2013) [PubMed] [Europe PMC] [Abstract]
• nucleosome binding Source: SGDInferred from direct assayⁱ
  • "Reconstitution of yeast silent chromatin: multiple contact sites and O-AADPR binding load SIR complexes onto nucleosomes in vitro."
    Martino F., Kueng S., Robinson P., Tsai-Pflugfelder M., van Leeuwen F., Ziegler M., Cubizolles F., Cockell M.M., Rhodes D., Gasser S.M.
    Mol Cell 33:323-334(2009) [PubMed] [Europe PMC] [Abstract]
  • "Heterochromatin assembly by interrupted Sir3 bridges across neighboring nucleosomes."
    Behrouzi R., Lu C., Currie M.A., Jih G., Iglesias N., Moazed D.
    Elife 5:e17556-e17556(2016) [PubMed] [Europe PMC] [Abstract]
• single-stranded DNA binding Source: SGDInferred from direct assayⁱ
  • "Role of nucleic acid binding in Sir3p-dependent interactions with chromatin fibers."
    Adkins N.L., McBryant S.J., Johnson C.N., Leidy J.M., Woodcock C.L., Robert C.H., Hansen J.C., Georgel P.T.
    Biochemistry 48:276-288(2009) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• double-strand break repair via nonhomologous end joining Source: SGD <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "Components of the Ku-dependent non-homologous end-joining pathway are involved in telomeric length maintenance and telomeric silencing."
    Boulton S.J., Jackson S.P.
    EMBO J 17:1819-1828(1998) [PubMed] [Europe PMC] [Abstract]
• establishment of protein-containing complex localization to telomere Source: SGDInferred from mutant phenotypeⁱ
  • "The Ku subunit of telomerase binds Sir4 to recruit telomerase to lengthen telomeres in S. cerevisiae."
    Hass E.P., Zappulla D.C.
    Elife 4:0-0(2015) [PubMed] [Europe PMC] [Abstract]
• heterochromatin assembly Source: SGDInferred from mutant phenotypeⁱ
  • "Sir3 C-terminal domain involvement in the initiation and spreading of heterochromatin."
    Liaw H., Lustig A.J.
    Mol Cell Biol 26:7616-7631(2006) [PubMed] [Europe PMC] [Abstract]
• nuclear-transcribed mRNA catabolic process, non-stop decay Source: SGDInferred from mutant phenotypeⁱ
  • "A genomic screen in yeast reveals novel aspects of nonstop mRNA metabolism."
    Wilson M.A., Meaux S., van Hoof A.
    Genetics 177:773-784(2007) [PubMed] [Europe PMC] [Abstract]
• silent mating-type cassette heterochromatin assembly Source: SGDInferred from mutant phenotypeⁱ
  • "Structure and function of the Saccharomyces cerevisiae Sir3 BAH domain."
    Connelly J.J., Yuan P., Hsu H.C., Li Z., Xu R.M., Sternglanz R.
    Mol Cell Biol 26:3256-3265(2006) [PubMed] [Europe PMC] [Abstract]
  • "Four genes responsible for a position effect on expression from HML and HMR in Saccharomyces cerevisiae."
    Rine J., Herskowitz I.
    Genetics 116:9-22(1987) [PubMed] [Europe PMC] [Abstract]
• subtelomeric heterochromatin assembly Source: SGDInferred from mutant phenotypeⁱ
  • "Modifiers of position effect are shared between telomeric and silent mating-type loci in S. cerevisiae."
    Aparicio O.M., Billington B.L., Gottschling D.E.
    Cell 66:1279-1287(1991) [PubMed] [Europe PMC] [Abstract]
  • "Reciprocal interactions between mtDNA and lifespan control in budding yeast."
    Garcia E.J., de Jonge J.J., Liao P.C., Stivison E., Sing C.N., Higuchi-Sanabria R., Boldogh I.R., Pon L.A.
    Mol Biol Cell 30:2943-2952(2019) [PubMed] [Europe PMC] [Abstract]
  • "Components of the Ku-dependent non-homologous end-joining pathway are involved in telomeric length maintenance and telomeric silencing."
    Boulton S.J., Jackson S.P.
    EMBO J 17:1819-1828(1998) [PubMed] [Europe PMC] [Abstract]
• telomere tethering at nuclear periphery Source: SGDInferred from mutant phenotypeⁱ
  • "Spatial reorganization of telomeres in long-lived quiescent cells."
    Guidi M., Ruault M., Marbouty M., Loiodice I., Cournac A., Billaudeau C., Hocher A., Mozziconacci J., Koszul R., Taddei A.
    Genome Biol 16:206-206(2015) [PubMed] [Europe PMC] [Abstract]
  • "Quiescent Saccharomyces cerevisiae forms telomere hyperclusters at the nuclear membrane vicinity through a multifaceted mechanism involving Esc1, the Sir complex, and chromatin condensation."
    Laporte D., Courtout F., Tollis S., Sagot I.
    Mol Biol Cell 27:1875-1884(2016) [PubMed] [Europe PMC] [Abstract]

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

• UniProt annotation
• GO - Cellular component

Keywords - Cellular componentⁱ

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

Mutagenesis

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Amino acid modifications

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationⁱ

Keywords - PTMⁱ

Proteomic databases

PTM databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• identical protein binding Source: IntActInferred from physical interactionⁱ
  • "Domain structure and protein interactions of the silent information regulator Sir3 revealed by screening a nested deletion library of protein fragments."
    King D.A., Hall B.E., Iwamoto M.A., Win K.Z., Chang J.F., Ellenberger T.
    J Biol Chem 281:20107-20119(2006) [PubMed] [Europe PMC] [Abstract]
  • "Defining the budding yeast chromatin-associated interactome."
    Lambert J.P., Fillingham J., Siahbazi M., Greenblatt J., Baetz K., Figeys D.
    Mol Syst Biol 6:448-448(2010) [PubMed] [Europe PMC] [Abstract]
  • "Dimerization of Sir3 via its C-terminal winged helix domain is essential for yeast heterochromatin formation."
    Oppikofer M., Kueng S., Keusch J.J., Hassler M., Ladurner A.G., Gut H., Gasser S.M.
    EMBO J 32:437-449(2013) [PubMed] [Europe PMC] [Abstract]

Protein-protein interaction databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Domains and Repeats

Region

Compositional bias

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequenceⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingⁱ: The displayed sequence is further processed into a mature form.

        10         20         30         40         50
MAKTLKDLDG WQVIITDDQG RVIDDNNRRR SRKRGGENVF LKRISDGLSF 
        60         70         80         90        100
GKGESVIFND NVTETYSVYL IHEIRLNTLN NVVEIWVFSY LRWFELKPKL 
       110        120        130        140        150
YYEQFRPDLI KEDHPLEFYK DKFFNEVNKS ELYLTAELSE IWLKDFIAVG 
       160        170        180        190        200
QILPESQWND SSIDKIEDRD FLVRYACEPT AEKFVPIDIF QIIRRVKEME 
       210        220        230        240        250
PKQSDEYLKR VSVPVSGQKT NRQVMHKMGV ERSSKRLAKK PSMKKIKIEP 
       260        270        280        290        300
SADDDVNNGN IPSQRGTSTT HGSISPQEES VSPNISSASP SALTSPTDSS 
       310        320        330        340        350
KILQKRSISK ELIVSEEIPI NSSEQESDYE PNNETSVLSS KPGSKPEKTS 
       360        370        380        390        400
TELVDGRENF VYANNPEVSD DGGLEEETDE VSSESSDEAI IPVNKRRGAH 
       410        420        430        440        450
GSELSSKIRK IHIQETQEFS KNYTTETDNE MNGNGKPGIP RGNTKIHSMN 
       460        470        480        490        500
ENPTPEKGNA KMIDFATLSK LKKKYQIILD RFAPDNQVTD SSQLNKLTDE 
       510        520        530        540        550
QSSLDVAGLE DKFRKACSSS GRETILSNFN ADINLEESIR ESLQKRELLK 
       560        570        580        590        600
SQVEDFTRIF LPIYDSLMSS QNKLFYITNA DDSTKFQLVN DVMDELITSS 
       610        620        630        640        650
ARKELPIFDY IHIDALELAG MDALYEKIWF AISKENLCGD ISLEALNFYI 
       660        670        680        690        700
TNVPKAKKRK TLILIQNPEN LLSEKILQYF EKWISSKNSK LSIICVGGHN 
       710        720        730        740        750
VTIREQINIM PSLKAHFTEI KLNKVDKNEL QQMIITRLKS LLKPFHVKVN 
       760        770        780        790        800
DKKEMTIYNN IREGQNQKIP DNVIVINHKI NNKITQLIAK NVANVSGSTE 
       810        820        830        840        850
KAFKICEAAV EISKKDFVRK GGLQKGKLVV SQEMVPRYFS EAINGFKDET 
       860        870        880        890        900
ISKKIIGMSL LMRTFLYTLA QETEGTNRHT LALETVLIKM VKMLRDNPGY 
       910        920        930        940        950
KASKEIKKVI CGAWEPAITI EKLKQFSWIS VVNDLVGEKL VVVVLEEPSA 
       960        970 
SIMVELKLPL EINYAFSMDE EFKNMDCI                         

Experimental Info

Sequence databases

Genome annotation databases

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 100% Identity
• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ

Documents

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