+ |
NUP35 | form complex
binding
|
NPC |
0.624 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262080 |
|
|
|
|
pmid |
sentence |
27016207 |
The protein inventory of the NPC has been studied for a very diverse set of eukaryotes, including trypanosomes, fungi, plants, animals, and humans [4], [5], [6], [7], [8], [9]. In all cases, about 30 different Nups were found (Fig. 2). |
|
Publications: |
1 |
+ |
CDK1 | down-regulates activity
phosphorylation
|
NUP35 |
0.56 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-278917 |
|
|
Homo sapiens |
|
pmid |
sentence |
29065306 |
Collectively, these data show that mitotic hyperphosphorylation of Nup53 by CDK1 and PLK1 contributes to its removal from NPCs.|The combined mutation of the CDK1 and PLK1 sites to phosphomimetic residues almost completely abolished NPC integration of Nup53, indicating that hyperphosphorylation of Nup53 might be incompatible with its NPC association. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PLK1 | down-regulates activity
phosphorylation
|
NUP35 |
0.414 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-279252 |
|
|
Homo sapiens |
|
pmid |
sentence |
29065306 |
Collectively, these data show that mitotic hyperphosphorylation of Nup53 by CDK1 and PLK1 contributes to its removal from NPCs.|The combined mutation of the CDK1 and PLK1 sites to phosphomimetic residues almost completely abolished NPC integration of Nup53, indicating that hyperphosphorylation of Nup53 might be incompatible with its NPC association. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |