Type | Description |
---|---|
Definition | mRNA-decapping complex catalytic subunit Dcp2 |
Date | Results | Publications |
---|---|---|
2019-08-03 12:33:00 | Elements in the C-terminus of Dcp2 inhibit decapping at the catalytic step. | 29618050 |
2018-05-26 10:09:00 | Authors demonstrate that only three of the six domain orientations are present in solution, where Dcp2 adopts an open, a closed, or a catalytically active state, and show how mRNA substrate and the activator proteins Dcp1 and Edc1 influence the dynamic equilibria between these states and how this modulates catalytic activity. | 28533364 |
2017-10-02 01:05:00 | These results determine the dynamics of the open-to-closed transition in Dcp2. | 22323607 |
2017-05-20 12:46:00 | This study reports a 1.6-A-resolution crystal structure of the Schizosaccharomyces pombe Dcp2-Dcp1 heterodimer in an unprecedented conformation that is tied together by an intrinsically disordered peptide from Edc1. | 27183195 |
2017-05-20 10:08:00 | Here is presented a 2.6-A-resolution crystal structure of a heterotrimer of fission yeast Dcp2, its essential activator Dcp1 and the human NMD cofactor PNRC2, in complex with a tight-binding cap analog. | 27694842 |
Type | IDs |
---|---|
Gene |
UniProtKB-ID:
DCP2_SCHPO
UniprotKB:
O13828
UniParc:
UPI000006B3D3
EMBL:
CU329670
EnsemblGenome:
SPAC19A8.12
KO:
spo:SPAC19A8.12
|
Nucleutide sequences |
EMBL-CDS:
CAB11648.1
Gene_ORFName:
SPAC19A8.12
EnsemblGenome_TRS:
SPAC19A8.12.1
|
Protein sequencees |
EnsemblGenome_PRO:
SPAC19A8.12.1:pep
RefSeq:
NP_593780.1
|
Others |
UniRef100:
UniRef100_O13828
UniRef90:
UniRef90_O13828
UniRef50:
UniRef50_O13828
|
{{proteinIndex+1}} | mRNA | Protein | UniprotKB | Description | ||||
---|---|---|---|---|---|---|---|---|
Refseq |
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