SIR2/YDL042C Gene Ontology Annotations Help

This page displays GO annotations in different sections according to the annotation method used to add that annotation to SGD.

SIR2 Manually curated*:

Last Reviewed on: 2004-07-25    Molecular Function | Biological Process | Cellular Component

Manually curated Molecular Function
Annotation(s) Evidence Reference(s) Assigned By
NAD-dependent histone deacetylase activity IDA: Inferred from Direct Assay
Assigned on 2007-02-15
Landry J, et al.  (2000) The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases. Proc Natl Acad Sci U S A 97(11):5807-11 SGD
NAD-dependent histone deacetylase activity (H3-K14 specific) ISS: Inferred from Sequence or structural Similarity
with GenBank/EMBL/DDBJ:AF214646
Assigned on 2006-04-21
IDA: Inferred from Direct Assay
Assigned on 2006-04-21
Imai S, et al.  (2000) Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature 403(6771):795-800 SGD
NAD-dependent histone deacetylase activity (H3-K9 specific) ISS: Inferred from Sequence or structural Similarity
with GenBank/EMBL/DDBJ:AF214646
Assigned on 2006-03-14
IDA: Inferred from Direct Assay
Assigned on 2006-03-14
Imai S, et al.  (2000) Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature 403(6771):795-800 SGD
NAD-dependent histone deacetylase activity (H4-K16 specific) ISS: Inferred from Sequence or structural Similarity
with GenBank/EMBL/DDBJ:AF214646
Assigned on 2006-03-14
IDA: Inferred from Direct Assay
Assigned on 2006-03-14
Imai S, et al.  (2000) Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature 403(6771):795-800 SGD
contributes_to nucleosome binding IDA: Inferred from Direct Assay
Assigned on 2009-03-03
Martino F, et al.  (2009) Reconstitution of yeast silent chromatin: multiple contact sites and O-AADPR binding load SIR complexes onto nucleosomes in vitro. Mol Cell 33(3):323-34 SGD

Manually curated Biological Process
Annotation(s) Evidence Reference(s) Assigned By
chromatin assembly or disassembly IDA: Inferred from Direct Assay
Assigned on 2002-11-01
Thrower DA and Bloom K  (2001) Dicentric chromosome stretching during anaphase reveals roles of Sir2/Ku in chromatin compaction in budding yeast. Mol Biol Cell 12(9):2800-12 SGD
chromatin silencing at rDNA IMP: Inferred from Mutant Phenotype
Assigned on 2003-08-14
Gottlieb S and Esposito RE  (1989) A new role for a yeast transcriptional silencer gene, SIR2, in regulation of recombination in ribosomal DNA. Cell 56(5):771-6 SGD
chromatin silencing at silent mating-type cassette IMP: Inferred from Mutant Phenotype
Assigned on 2002-12-02
Armstrong CM, et al.  (2002) Mutations in Saccharomyces cerevisiae gene SIR2 can have differential effects on in vivo silencing phenotypes and in vitro histone deacetylation activity. Mol Biol Cell 13(4):1427-38 SGD
chromatin silencing at telomere IMP: Inferred from Mutant Phenotype
Assigned on 2002-12-02
Armstrong CM, et al.  (2002) Mutations in Saccharomyces cerevisiae gene SIR2 can have differential effects on in vivo silencing phenotypes and in vitro histone deacetylation activity. Mol Biol Cell 13(4):1427-38 SGD
IPI: Inferred from Physical Interaction
Assigned on 2002-12-02
Strahl-Bolsinger S, et al.  (1997) SIR2 and SIR4 interactions differ in core and extended telomeric heterochromatin in yeast. Genes Dev 11(1):83-93 SGD
chronological cell aging IMP: Inferred from Mutant Phenotype
Assigned on 2005-12-19
Fabrizio P, et al.  (2005) Sir2 blocks extreme life-span extension. Cell 123(4):655-67 SGD
double-strand break repair via nonhomologous end joining IDA: Inferred from Direct Assay
Assigned on 2002-11-01
Hegde V and Klein H  (2000) Requirement for the SRS2 DNA helicase gene in non-homologous end joining in yeast. Nucleic Acids Res 28(14):2779-83 SGD
negative regulation of chromatin silencing involved in replicative cell aging TAS: Traceable Author Statement
Assigned on 2003-08-14
Guarente L  (2000) Sir2 links chromatin silencing, metabolism, and aging. Genes Dev 14(9):1021-6 SGD
negative regulation of DNA recombination IGI: Inferred from Genetic Interaction
with SGD:CHL1
Assigned on 2010-03-31
Das SP and Sinha P  (2005) The budding yeast protein Chl1p has a role in transcriptional silencing, rDNA recombination, and aging. Biochem Biophys Res Commun 337(1):167-72 SGD
negative regulation of DNA replication IMP: Inferred from Mutant Phenotype
Assigned on 2004-07-25
Pappas DL Jr, et al.  (2004) The NAD(+)-dependent Sir2p histone deacetylase is a negative regulator of chromosomal DNA replication. Genes Dev 18(7):769-81 SGD
replicative cell aging IMP: Inferred from Mutant Phenotype
Assigned on 2005-03-14
Kaeberlein M, et al.  (2005) Genes determining yeast replicative life span in a long-lived genetic background. Mech Ageing Dev 126(4):491-504 SGD

Manually curated Cellular Component
Annotation(s) Evidence Reference(s) Assigned By
chromatin silencing complex IDA: Inferred from Direct Assay
Assigned on 2004-04-07
Moazed D, et al.  (1997) Silent information regulator protein complexes in Saccharomyces cerevisiae: a SIR2/SIR4 complex and evidence for a regulatory domain in SIR4 that inhibits its interaction with SIR3. Proc Natl Acad Sci U S A 94(6):2186-91 SGD
nuclear heterochromatin IDA: Inferred from Direct Assay
Assigned on 2010-12-02
Lynch PJ and Rusche LN  (2010) An auxiliary silencer and a boundary element maintain high levels of silencing proteins at HMR in Saccharomyces cerevisiae. Genetics 185(1):113-27 SGD
nuclear telomere cap complex IDA: Inferred from Direct Assay
Assigned on 2003-04-03
Bourns BD, et al.  (1998) Sir proteins, Rif proteins, and Cdc13p bind Saccharomyces telomeres in vivo. Mol Cell Biol 18(9):5600-8 SGD
nuclear telomeric heterochromatin IDA: Inferred from Direct Assay
Assigned on 2002-12-02
Strahl-Bolsinger S, et al.  (1997) SIR2 and SIR4 interactions differ in core and extended telomeric heterochromatin in yeast. Genes Dev 11(1):83-93 SGD
nucleolus IDA: Inferred from Direct Assay
Assigned on 2002-12-02
Gotta M, et al.  (1997) Localization of Sir2p: the nucleolus as a compartment for silent information regulators. EMBO J 16(11):3243-55 SGD
RENT complex IDA: Inferred from Direct Assay
Assigned on 2004-09-06
Shou W, et al.  (1999) Exit from mitosis is triggered by Tem1-dependent release of the protein phosphatase Cdc14 from nucleolar RENT complex. Cell 97(2):233-44 SGD

* Manually curated GO annotations reflect our best understanding of the basic molecular function, biological process, and cellular component for this gene product. Manually curated annotations are assigned by SGD curators based on published papers when available, or by curatorial statements if necessary. Curators periodically review all Manually curated GO annotations for accuracy and completeness. The "Last Reviewed on:" date at the top of this section indicates when these annotations were last reviewed.


SIR2 High-throughput**:


There are no High-throughput annotations for SIR2

** GO annotations from High-throughput experiments are made based on a variety of large scale high-throughput experiments, including genome-wide experiments. Many of these annotations are made based on GO annotations (or mappings to GO annotations) assigned by the authors, rather than SGD curators. While SGD curators read these publications and often work closely with authors to incorporate the information, each individual annotation may not necessarily be reviewed by a curator. GO Annotations from high-throughput experiments will be assigned only when this type of data is available, and thus may not be assigned in all three aspects of the Gene Ontologies.


SIR2 Computational***:

Molecular Function | Biological Process | Cellular Component

Computational Molecular Function
Annotation(s) Evidence Reference(s) Assigned By
hydrolase activity IEA: Inferred from Electronic Annotation
with EBI:KW-0378
Last updated 2013-03-02
UniProt-GOA  (2011) Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries. UniProtKB
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides IEA: Inferred from Electronic Annotation
with EBI:IPR007654
Last updated 2013-03-02
DDB, et al.  (2001) Gene Ontology annotation through association of InterPro records with GO terms. InterPro
metal ion binding IEA: Inferred from Electronic Annotation
with EBI:KW-0479
Last updated 2013-03-02
UniProt-GOA  (2011) Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries. UniProtKB
NAD binding IEA: Inferred from Electronic Annotation
with EBI:IPR007654
Last updated 2013-03-02
DDB, et al.  (2001) Gene Ontology annotation through association of InterPro records with GO terms. InterPro
NAD+ binding IEA: Inferred from Electronic Annotation
with EBI:IPR003000
Last updated 2013-03-02
DDB, et al.  (2001) Gene Ontology annotation through association of InterPro records with GO terms. InterPro
NAD-dependent histone deacetylase activity IEA: Inferred from Electronic Annotation
with EBI:IPR007654
Last updated 2013-03-02
DDB, et al.  (2001) Gene Ontology annotation through association of InterPro records with GO terms. InterPro
zinc ion binding IEA: Inferred from Electronic Annotation
with EBI:IPR007654
Last updated 2013-03-02
DDB, et al.  (2001) Gene Ontology annotation through association of InterPro records with GO terms. InterPro

Computational Biological Process
Annotation(s) Evidence Reference(s) Assigned By
chromatin modification IEA: Inferred from Electronic Annotation
with EBI:KW-0156
Last updated 2013-03-02
UniProt-GOA  (2011) Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries. UniProtKB
chromatin silencing IEA: Inferred from Electronic Annotation
with EBI:IPR007654
Last updated 2013-03-02
DDB, et al.  (2001) Gene Ontology annotation through association of InterPro records with GO terms. InterPro
DNA repair IEA: Inferred from Electronic Annotation
with EBI:KW-0234
Last updated 2013-03-02
UniProt-GOA  (2011) Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries. UniProtKB
protein deacetylation IEA: Inferred from Electronic Annotation
with EBI:IPR007654
Last updated 2013-03-02
DDB, et al.  (2001) Gene Ontology annotation through association of InterPro records with GO terms. InterPro
regulation of transcription, DNA-dependent IEA: Inferred from Electronic Annotation
with EBI:IPR007654
Last updated 2013-03-02
DDB, et al.  (2001) Gene Ontology annotation through association of InterPro records with GO terms. InterPro
IEA: Inferred from Electronic Annotation
with EBI:KW-0805
Last updated 2013-03-02
UniProt-GOA  (2011) Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries. UniProtKB
response to DNA damage stimulus IEA: Inferred from Electronic Annotation
with EBI:KW-0227
Last updated 2013-03-02
UniProt-GOA  (2011) Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries. UniProtKB
transcription, DNA-dependent IEA: Inferred from Electronic Annotation
with EBI:KW-0804
Last updated 2013-03-02
UniProt-GOA  (2011) Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries. UniProtKB

Computational Cellular Component
Annotation(s) Evidence Reference(s) Assigned By
nucleolus IEA: Inferred from Electronic Annotation
with EBI:SL-0188
Last updated 2013-03-02
UniProt-GOA  (2011) Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries. UniProtKB
nucleus IEA: Inferred from Electronic Annotation
with EBI:KW-0539
Last updated 2013-03-02
UniProt-GOA  (2011) Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries. UniProtKB

*** Computational GO Annotations are predictions. These annotations are NOT reviewed by a curator. Currently, all computational GO annotations for S. cerevisiae are assigned by an external source (for example, the Gene Ontology Annotation (GOA) project of the European Bioinformatics Institute (EBI)).