Type | Description |
---|---|
Definition | Sus1p |
Date | Results | Publications |
---|---|---|
2020-06-20 10:32:00 | Study portrays the biophysical characterization of Sus1 from S. cerevisiae. Sus1 protein is a alpha-helical structure which is stable at various pH conditions. The results reported the alpha-helix to beta-sheet transition at low pH as well as at high pH. Also, Sus1 secondary structure was found to be stable till 55% alcohol concentration while tertiary structure was stable up to 20% concentration. | 32134955 |
2018-10-20 10:35:00 | Study provides support for a model in which SAGA/TREX-2 factor Sus1 acts as a global transcriptional regulator in yeast but has differential activity at yeast genes as a function of their transcription rate or during stress conditions. | 29598828 |
2018-10-13 11:16:00 | results provide solid evidence for a role of Sus1 in negatively regulating telomere length through the modulation of H2BK123 mono-ubiquitination and its interaction with the nuclear pore complex | 29116388 |
2018-10-06 11:37:00 | Exon three-way junction structure exerted a role in SUS1 transcript metabolism that includes splicing and transcript degradation. | 29966763 |
2017-08-19 11:52:00 | Examination of pre-mRNA splicing efficiency in these mutants reveals the requirement of Npl3 methylation for the efficient splicing of SUS1 intron 1, but not of ECM33 or ASC1. | 28392442 |
Type | IDs |
---|---|
Gene |
UniProtKB-ID:
SUS1_YEAST
UniprotKB:
Q6WNK7
UniParc:
UPI000023FD4C
EMBL:
BK006936,
Z35981,
Z35980,
AY278445
EnsemblGenome:
YBR111W-A
KO:
sce:YBR111W-A
|
Nucleutide sequences |
EMBL-CDS:
AAQ19492.1,
DAA07231.1
EnsemblGenome_TRS:
YBR111W-A_mRNA
|
Protein sequencees |
EnsemblGenome_PRO:
YBR111W-A
RefSeq:
NP_878049.2
|
Others |
UniRef100:
UniRef100_Q6WNK7
UniRef90:
UniRef90_Q6WNK7
UniRef50:
UniRef50_Q6WNK7
|
{{proteinIndex+1}} | mRNA | Protein | UniprotKB | Description | ||||
---|---|---|---|---|---|---|---|---|
Refseq |
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