| Type | Description |
|---|---|
| Definition | Hsm3p |
| Date | Results | Publications |
|---|---|---|
| 2015-03-28 11:11:00 | Combinations of hsm3 and hsm6 mutations with mutations in other genes of the RAD52 epistatic group did not provide a spontaneous mutation rate decrease. | 25711034 |
| 2012-08-04 11:22:00 | The results made it possible to assume that the hsm3 mutation destabilizes the D-loop, which is a key substrate of both Rad5- and Rad52-dependent postreplicative repair pathways. | 22679780 |
| 2012-07-14 11:23:00 | provide structural and biochemical evidence on how Hsm3/S5b may regulate the 19S RP association to the 20S CP proteasome | 22460800 |
| 2012-06-09 10:26:00 | the structural basis of the molecular functions of Hsm3 for the regulatory particle assembly. | 22334676 |
| 2012-06-02 11:07:00 | Hsm3 protein contains at least two domains; the N-terminal part of the domain is responsible for the proteasome assembly, whereas the C-terminal portion of the protein is responsible for mutagenesis. | 22567994 |
| Type | IDs |
|---|---|
| Gene |
UniProtKB-ID:
HSM3_YEAST
UniprotKB:
P38348
UniParc:
UPI00000530B9
EMBL:
Z36141,
BK006936,
AY692825
EnsemblGenome:
YBR272C
KO:
sce:YBR272C
|
| Nucleutide sequences |
EMBL-CDS:
DAA07388.1,
CAA85235.1,
AAT92844.1
Gene_ORFName:
YBR1740
EnsemblGenome_TRS:
YBR272C_mRNA
|
| Protein sequencees |
EnsemblGenome_PRO:
YBR272C
RefSeq:
NP_009831.3
|
| Others |
UniRef100:
UniRef100_P38348
UniRef90:
UniRef90_P38348
UniRef50:
UniRef50_P38348
|
| {{proteinIndex+1}} | mRNA | Protein | UniprotKB | Description | ||||
|---|---|---|---|---|---|---|---|---|
| Refseq |
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| Conserved domain | Region: {{conservedDomain.region == '' || conservedDomain.region == null ? "-": conservedDomain.region}} GFID: {{conservedDomain.gfid == '' || conservedDomain.gfid == null ? "-": conservedDomain.gfid}} Family: {{conservedDomain.family == '' || conservedDomain.family == null ? "-": conservedDomain.family}} CDD: {{conservedDomain.cdd}} - |
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