+ |
CDK1 | up-regulates activity
phosphorylation
|
RANBP2 |
0.451 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-259118 |
Ser2246 |
SSSVHASerPLASSP |
in vitro |
|
pmid |
sentence |
26051540 |
Cdk1 phosphorylates conserved sites within RanBP2 and activates BicD2 binding and early dynein recruitment. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-259119 |
Ser2251 |
ASPLASSerPVRKNL |
in vitro |
|
pmid |
sentence |
26051540 |
Cdk1 phosphorylates conserved sites within RanBP2 and activates BicD2 binding and early dynein recruitment. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-259120 |
Ser2276 |
SFKSALSerPSKSPA |
in vitro |
|
pmid |
sentence |
26051540 |
Cdk1 phosphorylates conserved sites within RanBP2 and activates BicD2 binding and early dynein recruitment. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-259121 |
Ser2280 |
LSPSKSerPAKLN |
in vitro |
|
pmid |
sentence |
26051540 |
Cdk1 phosphorylates conserved sites within RanBP2 and activates BicD2 binding and early dynein recruitment. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-259117 |
Thr2153 |
LDIPLQThrPHKLVD |
in vitro |
|
pmid |
sentence |
26051540 |
Cdk1 phosphorylates conserved sites within RanBP2 and activates BicD2 binding and early dynein recruitment. |
|
Publications: |
5 |
Organism: |
In Vitro |
+ |
RANBP2 | up-regulates quantity
relocalization
|
BICD2 |
0.52 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-259122 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
20386726 |
We show that the dynein/dynactin adaptor BICD2 is specifically recruited to the NPC in G2phase through a direct interaction with the NPC componentRanBP2. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RANBP2 | form complex
binding
|
NPC |
0.613 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262088 |
|
|
|
|
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 |
+ |
RANBP2 | up-regulates activity
binding
|
TNPO1 |
0.467 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262111 |
|
|
Homo sapiens |
U2-OS Cell |
pmid |
sentence |
32161167 |
Nup358(806–1306), but not other regions, efficiently recruits importin β and transportin 1 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RANBP2 | down-regulates quantity
relocalization
|
CDKN1B |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-259115 |
|
|
Homo sapiens |
Cholangiocarcinoma Cell Line |
pmid |
sentence |
28882106 |
RanBP2 can increase the sumoylation of p27kip1. In our study, the target protein p27kip1 mainly acts as a tumor-suppressor gene in the nucleus, RanBP2 and SUMO1 act as oncogenes by promoting the nuclear-cytoplasmic translocation and debilitate the G1-arrest brought by p27kip1 accumulation in the nucleus. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PRKN | down-regulates quantity by destabilization
ubiquitination
|
RANBP2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-259116 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
16332688 |
Our findings suggested that the intracellular levels of RanBP2 and its functional activity may be modulated by Parkin-mediated ubiquitination and proteasomal pathways. Furthermore, Parkin controls the intracellular levels of sumoylated HDAC4, as a result of the ubiquitination and degradation of RanBP2. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |