| Type | Description |
|---|---|
| Definition | Csm2p |
| Date | Results | Publications |
|---|---|---|
| 2019-12-14 10:09:00 | Study provides evidence that DNA-binding components of the budding yeast Shu complex, Csm2-Psy3, bind double-flap DNA substrates containing an abasic site analog, and increase chromatin association when abasic sites accumulate. Importantly, Csm2-Psy3 blocks AP endonuclease cleavage at a double-flap DNA substrate, thus preventing in vitro double-strand break formation. | 31383866 |
| 2018-01-20 10:21:00 | Data indicate that Csm2, Psy3, Shu1 and Shu2 interact with each other in sequence to form a V-shape overall structure in Shu complex. | 29069504 |
| 2013-06-29 12:08:00 | The data suggest a model in which Csm2-Psy3 recruit the Shu complex to homologous recombination substrates, where it interacts with Rad51 through Rad55-Rad57 to stimulate Rad51 filament assembly and stability, promoting error-free repair. | 23460207 |
| 2012-10-13 10:13:00 | analysis of the crystal structure of the Psy3-Csm2 sub-complex | 22749910 |
| Type | IDs |
|---|---|
| Gene |
UniProtKB-ID:
CSM2_YEAST
UniprotKB:
P40465
UniParc:
UPI000013B44B
EMBL:
DQ115392,
Z38059,
BK006942
EnsemblGenome:
YIL132C
KO:
sce:YIL132C
|
| Nucleutide sequences |
EMBL-CDS:
CAA86146.1,
AAZ22495.1,
DAA08421.1
EnsemblGenome_TRS:
YIL132C_mRNA
|
| Protein sequencees |
EnsemblGenome_PRO:
YIL132C
RefSeq:
NP_012134.1
|
| Others |
UniRef100:
UniRef100_P40465
UniRef90:
UniRef90_P40465
UniRef50:
UniRef50_P40465
|
| {{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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