+ |
CDK4 | up-regulates
phosphorylation
|
PELP1 |
0.36 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-167770 |
Ser477 |
ADALKLRsPRGSPDG |
Homo sapiens |
Breast Cancer Cell |
pmid |
sentence |
20807815 |
Using site-directed mutagenesis and in vitro kinase assays, we identified ser(477) and ser(991) of pelp1 as cdk phosphorylation sites. we identified pelp1 as a novel substrate of cdks and found that cdk phosphorylation is important for the proper function of pelp1 in modulating hormone-driven cell cycle progression and also for optimal e2f transactivation function. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-167774 |
Ser991 |
PALPPPEsPPKVQPE |
Homo sapiens |
Breast Cancer Cell |
pmid |
sentence |
20807815 |
Using site-directed mutagenesis and in vitro kinase assays, we identified ser(477) and ser(991) of pelp1 as cdk phosphorylation sites. we identified pelp1 as a novel substrate of cdks and found that cdk phosphorylation is important for the proper function of pelp1 in modulating hormone-driven cell cycle progression and also for optimal e2f transactivation function. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
CDK2 | up-regulates
phosphorylation
|
PELP1 |
0.376 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-167766 |
Ser991 |
PALPPPEsPPKVQPE |
Homo sapiens |
|
pmid |
sentence |
20807815 |
We identified ser(477) and ser(991) of pelp1 as cdk phosphorylation sites. we conclude that pelp1 is a novel substrate of interphase cdks and that its phosphorylation is important for the proper function of pelp1 in modulating hormone-driven cell cycle progression and also for optimal e2f transactivation function. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PELP1 | form complex
binding
|
Rix1 complex |
0.792 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265469 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
22190735 |
LAS1L was first described as a nucleolar protein required for maturation of the 60S preribosomal subunit. In this paper, we demonstrate that LAS1L interacts with PELP1, TEX10, and WDR18, the mammalian homologues of the budding yeast Rix1 complex, along with NOL9 and SENP3, to form a novel nucleolar complex that cofractionates with the 60S preribosomal subunit. our data identify a novel mammalian complex required for 60S ribosomal subunit synthesis, providing further insight into the intricate, yet poorly described, process of ribosome biogenesis in higher eukaryotes. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PELP1 | up-regulates quantity by expression
transcriptional regulation
|
NR3C1 |
0.534 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251681 |
|
|
Homo sapiens |
|
pmid |
sentence |
18682536 |
MNAR functionally interacts with both NH2- and COOH-terminal GR domains to modulate transactivation |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MDN1 | up-regulates quantity by stabilization
binding
|
PELP1 |
0.385 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261357 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
27814492 |
MDN1 Is Physically and Functionally Associated with the Mammalian PELP1 Complex. To more specifically determine a function of mammalian MDN1 in the subnuclear distribution of PELP1-containing pre-60S-particles, we examined PELP1 localization in control cells or cells depleted from MDN1. Importantly, in the absence of MDN1, PELP1 became sequestered in enlarged nucleoli, indicating that MDN1 is involved in the nucleolar release of PELP1-containing pre-60S ribosomes |
|
Publications: |
1 |
Organism: |
Homo Sapiens |