+ |
NEK6 | down-regulates activity
phosphorylation
|
NUP98 |
0.321 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273892 |
Ser608 |
VLKNLNNsNLFSPVN |
in vitro |
|
pmid |
sentence |
21335236 |
To elucidate which of the identified sites can be targeted by CDK1/cyclin B1 and Nek6 in vitro (Figure S1D), we performed phosphorylation reactions using recombinant kinases and unlabeled ATP followed by phosphopeptide mapping (Table S1). MS analysis confirmed phosphorylation of S591 and S822 by Nek6 as well as phosphorylation of T529, T536, S595, S606, and T653 by CDK1. Phosphomimetic Mutants of Nup98 Show Defects in NPC Localization |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273893 |
Ser839 |
TSRCLIKsPDRLADI |
in vitro |
|
pmid |
sentence |
21335236 |
To elucidate which of the identified sites can be targeted by CDK1/cyclin B1 and Nek6 in vitro (Figure S1D), we performed phosphorylation reactions using recombinant kinases and unlabeled ATP followed by phosphopeptide mapping (Table S1). MS analysis confirmed phosphorylation of S591 and S822 by Nek6 as well as phosphorylation of T529, T536, S595, S606, and T653 by CDK1. Phosphomimetic Mutants of Nup98 Show Defects in NPC Localization |
|
Publications: |
2 |
Organism: |
In Vitro |
+ |
CDK1 | down-regulates activity
phosphorylation
|
NUP98 |
0.408 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-172217 |
Ser612 |
LNNSNLFsPVNRDSE |
Homo sapiens |
|
pmid |
sentence |
21335236 |
We show that npc disassembly is a phosphorylation-driven process, dependent on cdk1 activity and supported by members of the nima-related kinase (nek) family. mitotic hyperphosphorylation of nup98 is accomplished by multiple kinases, including cdk1 and neks. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-172221 |
Ser623 |
RDSENLAsPSEYPEN |
Homo sapiens |
|
pmid |
sentence |
21335236 |
We show that npc disassembly is a phosphorylation-driven process, dependent on cdk1 activity and supported by members of the nima-related kinase (nek) family. mitotic hyperphosphorylation of nup98 is accomplished by multiple kinases, including cdk1 and neks. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-172225 |
Thr670 |
IAKPIPQtPESAGNK |
Homo sapiens |
|
pmid |
sentence |
21335236 |
We show that npc disassembly is a phosphorylation-driven process, dependent on cdk1 activity and supported by members of the nima-related kinase (nek) family. mitotic hyperphosphorylation of nup98 is accomplished by multiple kinases, including cdk1 and neks. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
DHX9 | up-regulates activity
binding
|
NUP98 |
0.364 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260954 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
28221134 |
Here we report on the identification of the DExH/D-box helicase DHX9 as an intranuclear Nup98 binding partner. Various results, including in vitro assays, show that the FG/GLFG region of Nup98 binds to N- and C-terminal regions of DHX9 in an RNA facilitated manner. Importantly, binding of Nup98 stimulates the ATPase activity of DHX9, and a transcriptional reporter assay suggests Nup98 supports DHX9-stimulated transcription. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
6 | down-regulates activity
binding
|
NUP98 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260976 |
|
|
Homo sapiens |
|
pmid |
sentence |
32353860 |
Orf6 of SARS-CoV antagonizes host interferon signaling by perturbing nuclear transport, and the NUP98-RAE1 interaction with Orf6 may perform the same function for SARS-CoV-2. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
NUP98 | form complex
binding
|
NPC |
0.692 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262098 |
|
|
|
|
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). |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262074 |
|
|
|
|
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: |
2 |
+ |
RAE1 | up-regulates activity
binding
|
NUP98 |
0.882 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260868 |
|
|
Homo sapiens |
|
pmid |
sentence |
16036565 |
Nup98 is a major interacting partner of Rae1 and known to beinvolved in mRNA export. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
Interferon-type-I | up-regulates quantity by expression
transcriptional regulation
|
NUP98 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260870 |
|
|
Homo sapiens |
|
pmid |
sentence |
16036565 |
Nup98/Nup96 (41) and Rae1 (17)are up regulated by interferons, which revert the mRNAexport block induced by VSV M protein |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
NUP98 | up-regulates
|
mRNA-nucleus_export |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260872 |
|
|
Homo sapiens |
|
pmid |
sentence |
20498086 |
The export of mRNAs is a multistep process, involving the packaging of mRNAs into messenger ribonucleoprotein particles (mRNPs), their transport through nuclear pore complexes, and mRNP remodeling events prior to translation. Ribonucleic acid export 1 (Rae1) and Nup98 are evolutionarily conserved mRNA export factors that are targeted by the vesicular stomatitis virus matrix protein to inhibit host cell nuclear export. these data suggest that the Rae1*Nup98 complex directly binds to the mRNP at several stages of the mRNA export pathway. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |