+ |
SIRT7 | down-regulates activity
deacetylation
|
RAN |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275849 |
Lys37 |
HLTGEFEkKYVATLG |
|
|
pmid |
sentence |
31075303 |
N this study, we demonstrated that SIRT7 interacts with a small GTPase, Ras-related nuclear antigen (Ran), and deacetylates Ran at K37. |The nuclear export by CRM1 requires an interaction with the small GTPase Ras-related nuclear antigen (Ran), which cycles between GTP- and GDP-bound states. The binding of Ran GTP to CRM1 in the nucleus increases the affinity of CRM1 for cargo proteins [[18], [19], [20]]. Interestingly, Ran is a lysine-acetylated protein |
|
Publications: |
1 |
+ |
PLK1 | up-regulates
phosphorylation
|
RAN |
0.268 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-149073 |
Ser135 |
DRKVKAKsIVFHRKK |
Homo sapiens |
|
pmid |
sentence |
16930555 |
Plk1 is capable of phosphorylating co-immunoprecipitated ran in vitro on serine-135 and ran is phosphorylated in vivo at the same site during mitosis when plk1 is normally activated. Deregulation of ran phosphorylation disrupts normal spindle structure and segregation of chromosomes. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PAK4 |
phosphorylation
|
RAN |
0.312 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-167671 |
Ser135 |
DRKVKAKsIVFHRKK |
Homo sapiens |
|
pmid |
sentence |
20805321 |
We show that ran is a substrate for p21-activated kinase 4 (pak4) and that its phosphorylation on serine-135 increases during mitosis. our study suggests that pak4-mediated phosphorylation of gdp- or gtp-bound ran regulates the assembly of ran-dependent complexes on the mitotic spindle |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PAK4 | up-regulates
phosphorylation
|
RAN |
0.312 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-167667 |
Ser135 |
DRKVKAKsIVFHRKK |
Homo sapiens |
|
pmid |
sentence |
20805321 |
We show that ran is a substrate for p21-activated kinase 4 (pak4) and that its phosphorylation on serine-135 increases during mitosis.Altogether, our findings strongly suggest that pak4-mediated phosphorylation of gdp- or gtp-bound ran modulates the assembly of complexes that are required at specific subcellular localizations for ran to carry out its functions during mitotic progression. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RAN | up-regulates activity
binding
|
XPOT |
0.808 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261392 |
|
|
Homo sapiens |
|
pmid |
sentence |
9660920 |
The first step in export appears to be the formation of a trimeric tRNA/exportin-t/RanGTP complex. tRNA and RanGTP bind to exportin-t in a highly cooperative manner: tRNA increases the affinity of exportin-t for RanGTP apparently 300-fold (Figure 5A); conversely, RanGTP has to increase the affinity of exportin-t for tRNA by the same factor. RanGTP appears to have at least two functions in this complex. First, it stabilizes the tRNA/exportin-t interaction (see Figure 4B). Second, exportin-t apparently has to bind RanGTP for rapid exit from the nucleus |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MYCBP2 | up-regulates activity
guanine nucleotide exchange factor
|
RAN |
0.3 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261204 |
|
|
Mus musculus |
|
pmid |
sentence |
26304119 |
MYCBP2 Is a Nuclear GEF for Ran in DRG Neurons—Next, we studied whether or not MYCBP2 modulates the interaction between Ran/RanGAP1. MYCBP2 contains an N-terminal RCC1-like domain (Fig. 8C) (13), and RCC1 is a known GEF for Ran, indicating a potential functional interaction between MYCBP2 and Ran. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
RAN | up-regulates activity
binding
|
XPO1 |
0.926 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275848 |
|
|
|
|
pmid |
sentence |
31075303 |
The nuclear export by CRM1 requires an interaction with the small GTPase Ras-related nuclear antigen (Ran), which cycles between GTP- and GDP-bound states. The binding of Ran GTP to CRM1 in the nucleus increases the affinity of CRM1 for cargo proteins |
|
Publications: |
1 |