Type | Description |
---|---|
Definition | ribonuclease P/MRP protein subunit POP1 |
Date | Results | Publications |
---|---|---|
2020-08-15 19:03:00 | In pop mutants, TLC1 is more abundant, telomeres are short, and TLC1 accumulates in the cytoplasm. Although Est1/2 binding to TLC1 occurs at normal levels, Est1 (and hence Est3) binding is highly unstable. | 32358529 |
2016-11-12 10:51:00 | Study reports that the Pop1, Pop6, and Pop7 proteins, known components of RNase P and RNase MRP, bind to yeast telomerase RNA and are essential constituents of the telomerase holoenzyme. | 27156450 |
2015-11-21 10:52:00 | Results suggest that Pop1 plays the role of a scaffold for the stabilization of the global architecture of eukaryotic RNase P RNA, substituting for the network of RNA-RNA tertiary interactions that maintain the global RNA structure in bacterial RNase P. | 26135751 |
2010-01-21 00:00:00 | This study shows that the Pop1p subunit plays multiple roles in the assembly and function of of RNases P and MRP, and that the functions can be differentiated through the mutations in conserved residues. | 16618965 |
Type | IDs |
---|---|
Gene |
UniProtKB-ID:
POP1_YEAST
UniprotKB:
P41812
UniParc:
UPI0000131F35
EMBL:
X80358,
BK006947,
Z71497
EnsemblGenome:
YNL221C
KO:
sce:YNL221C
|
Nucleutide sequences |
EMBL-CDS:
CAA96124.1,
CAA56589.1,
DAA10335.1
Gene_ORFName:
N1285
EnsemblGenome_TRS:
YNL221C_mRNA
|
Protein sequencees |
EnsemblGenome_PRO:
YNL221C
RefSeq:
NP_014178.1
|
Others |
UniRef100:
UniRef100_P41812
UniRef90:
UniRef90_P41812
UniRef50:
UniRef50_P41812
|
{{proteinIndex+1}} | mRNA | Protein | UniprotKB | Description | ||||
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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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