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SGD:RTT109
Contents |
| Species (Taxon ID) | Saccharomyces cerevisiae (baker's yeast) (taxon:4932) | |
| Gene Name(s) | RTT109 ( synonyms: YLL002W, KIM2, REM50 ) | |
| Protein Name(s) | Histone acetyltransferase, | |
| External Links | ||
| SGD | S000003925 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | Evidence Code | with/from | Aspect | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0004402 |
histone acetyltransferase activity |
SGD_REF:S000124037 |
IEA: Inferred from Electronic Annotation |
F |
From SGD |
|||
| GO:0005634 |
nucleus |
SGD_REF:S000074185 |
IDA: Inferred from Direct Assay |
C |
From SGD |
|||
| GO:0005634 |
nucleus |
SGD_REF:S000077144 |
IDA: Inferred from Direct Assay |
C |
From SGD |
|||
| GO:0005634 |
nucleus |
SGD_REF:S000148669 |
IEA: Inferred from Electronic Annotation |
UniProtKB-KW:KW-0539 |
C |
From SGD |
||
| GO:0005634 |
nucleus |
SGD_REF:S000148671 |
IEA: Inferred from Electronic Annotation |
UniProtKB-SubCell:SL-0191 |
C |
From SGD |
||
| GO:0006281 |
DNA repair |
SGD_REF:S000148669 |
IEA: Inferred from Electronic Annotation |
UniProtKB-KW:KW-0234 |
P |
From SGD |
||
| GO:0006303 |
double-strand break repair via nonhomologous end joining |
SGD_REF:S000124825 |
IMP: Inferred from Mutant Phenotype |
P |
From SGD |
|||
| GO:0006351 |
transcription, DNA-dependent |
SGD_REF:S000148669 |
IEA: Inferred from Electronic Annotation |
UniProtKB-KW:KW-0804 |
P |
From SGD |
||
| GO:0006355 |
regulation of transcription, DNA-dependent |
SGD_REF:S000148669 |
IEA: Inferred from Electronic Annotation |
UniProtKB-KW:KW-0805 |
P |
From SGD |
||
| GO:0006974 |
response to DNA damage stimulus |
SGD_REF:S000076175 |
IMP: Inferred from Mutant Phenotype |
P |
From SGD |
|||
| GO:0006974 |
response to DNA damage stimulus |
SGD_REF:S000148669 |
IEA: Inferred from Electronic Annotation |
UniProtKB-KW:KW-0227 |
P |
From SGD |
||
| GO:0010484 |
H3 histone acetyltransferase activity |
SGD_REF:S000119240 |
IMP: Inferred from Mutant Phenotype |
F |
From SGD |
|||
| GO:0010484 |
H3 histone acetyltransferase activity |
SGD_REF:S000120595 |
IDA: Inferred from Direct Assay |
F |
From SGD |
|||
| GO:0010484 |
H3 histone acetyltransferase activity |
SGD_REF:S000120595 |
IMP: Inferred from Mutant Phenotype |
F |
From SGD |
|||
| GO:0010484 |
H3 histone acetyltransferase activity |
SGD_REF:S000120673 |
IDA: Inferred from Direct Assay |
F |
From SGD |
|||
| GO:0010484 |
H3 histone acetyltransferase activity |
SGD_REF:S000120673 |
IMP: Inferred from Mutant Phenotype |
F |
From SGD |
|||
| GO:0010484 |
H3 histone acetyltransferase activity |
SGD_REF:S000126328 |
IGI: Inferred from Genetic Interaction |
SGD:S000003484 |
F |
From SGD |
||
| GO:0010484 |
H3 histone acetyltransferase activity |
SGD_REF:S000126328 |
IMP: Inferred from Mutant Phenotype |
F |
From SGD |
|||
| GO:0010526 |
negative regulation of transposition, RNA-mediated |
SGD_REF:S000068874 |
IMP: Inferred from Mutant Phenotype |
P |
From SGD |
|||
| GO:0016573 |
histone acetylation |
SGD_REF:S000119240 |
IMP: Inferred from Mutant Phenotype |
P |
From SGD |
|||
| GO:0016573 |
histone acetylation |
SGD_REF:S000120595 |
IGI: Inferred from Genetic Interaction |
SGD:S000002599 |
P |
From SGD |
||
| GO:0016573 |
histone acetylation |
SGD_REF:S000120595 |
IMP: Inferred from Mutant Phenotype |
P |
From SGD |
|||
| GO:0016573 |
histone acetylation |
SGD_REF:S000120673 |
IDA: Inferred from Direct Assay |
P |
From SGD |
|||
| GO:0016573 |
histone acetylation |
SGD_REF:S000120673 |
IMP: Inferred from Mutant Phenotype |
P |
From SGD |
|||
| GO:0016573 |
histone acetylation |
SGD_REF:S000124037 |
IEA: Inferred from Electronic Annotation |
P |
From SGD |
|||
| GO:0016573 |
histone acetylation |
SGD_REF:S000126328 |
IGI: Inferred from Genetic Interaction |
SGD:S000003484 |
P |
From SGD |
||
| GO:0016573 |
histone acetylation |
SGD_REF:S000126328 |
IMP: Inferred from Mutant Phenotype |
P |
From SGD |
|||
| GO:0016740 |
transferase activity |
SGD_REF:S000148669 |
IEA: Inferred from Electronic Annotation |
UniProtKB-KW:KW-0808 |
F |
From SGD |
||
| GO:0043618 |
regulation of transcription from RNA polymerase II promoter in response to stress |
SGD_REF:S000130988 |
IMP: Inferred from Mutant Phenotype |
P |
From SGD |
| ||
| edit table |
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ Huh WK et al. (2003) Global analysis of protein localization in budding yeast. Nature 425: 686-91 PubMed GONUTS page
- ↑ Sundin BA et al. (2004) Localization of proteins that are coordinately expressed with Cln2 during the cell cycle. Yeast 21: 793-800 PubMed GONUTS page
- ↑ Jessulat M et al. (2008) Interacting proteins Rtt109 and Vps75 affect the efficiency of non-homologous end-joining in Saccharomyces cerevisiae. Arch Biochem Biophys 469: 157-64 PubMed GONUTS page
- ↑ Chang M et al. (2002) A genome-wide screen for methyl methanesulfonate-sensitive mutants reveals genes required for S phase progression in the presence of DNA damage. Proc Natl Acad Sci U S A 99: 16934-9 PubMed GONUTS page
- ↑ 5.0 5.1 Schneider J et al. (2006) Rtt109 is required for proper H3K56 acetylation: a chromatin mark associated with the elongating RNA polymerase II. J Biol Chem 281: 37270-4 PubMed GONUTS page
- ↑ 6.0 6.1 6.2 6.3 Driscoll R et al. (2007) Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine 56. Science 315: 649-52 PubMed GONUTS page
- ↑ 7.0 7.1 7.2 7.3 Han J et al. (2007) Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication. Science 315: 653-5 PubMed GONUTS page
- ↑ 8.0 8.1 8.2 8.3 Fillingham J et al. (2008) Chaperone control of the activity and specificity of the histone H3 acetyltransferase Rtt109. Mol Cell Biol 28: 4342-53 PubMed GONUTS page
- ↑ Scholes DT et al. (2001) Multiple regulators of Ty1 transposition in Saccharomyces cerevisiae have conserved roles in genome maintenance. Genetics 159: 1449-65 PubMed GONUTS page
- ↑ Klopf E et al. (2009) Cooperation between the INO80 complex and histone chaperones determines adaptation of stress gene transcription in the yeast Saccharomyces cerevisiae. Mol Cell Biol 29: 4994-5007 PubMed GONUTS page
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