| + |
CSNK2A1 | up-regulates 
phosphorylation
|
RANGAP1 |
0.314 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-143948 |
Ser358 |
AKVLASLsDDEDEEE |
Homo sapiens |
|
| pmid |
sentence |
| 16428860 |
Phosphorylation of rangap1 stabilizes its interaction with ran and ranbp1. Serine-358 (358s) was identified as the major phosphorylation site. Experiments using purified recombinant kinase and specific inhibitors such as drb and apigenin strongly suggest that casein kinase ii (ck2) is the responsible kinase |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CyclinB/CDK1 | up-regulates
phosphorylation
|
RANGAP1 |
0.446 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216781 |
Ser428 |
EPAPVLSsPPPADVS |
Homo sapiens |
|
| pmid |
sentence |
| 15037602 |
Here, we show that rangap1 is phosphorylated on residues t409, s428, and s442. Phosphorylation occurs before nuclear envelope breakdown and is maintained throughout mitosis . Alternatively, phosphorylated rangap1 may recruit specific sumo target proteins to ranbp2's catalytic domain. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216785 |
Ser442 |
STFLAFPsPEKLLRL |
Homo sapiens |
|
| pmid |
sentence |
| 15037602 |
Here, we show that rangap1 is phosphorylated on residues t409, s428, and s442. Phosphorylation occurs before nuclear envelope breakdown and is maintained throughout mitosis . Alternatively, phosphorylated rangap1 may recruit specific sumo target proteins to ranbp2's catalytic domain. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216789 |
Thr409 |
GQGEKSAtPSRKILD |
Homo sapiens |
|
| pmid |
sentence |
| 15037602 |
Here, we show that rangap1 is phosphorylated on residues t409, s428, and s442. Phosphorylation occurs before nuclear envelope breakdown and is maintained throughout mitosis. The m-phase kinase cyclin b/cdk1 phosphorylates rangap1 efficiently in vitro, and t409 phosphorylation correlates with nuclear accumulation of cyclin b1 in vivo. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
CDK1 | up-regulates
phosphorylation
|
RANGAP1 |
0.472 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-123516 |
Ser428 |
EPAPVLSsPPPADVS |
Homo sapiens |
|
| pmid |
sentence |
| 15037602 |
Here, we show that rangap1 is phosphorylated on residues t409, s428, and s442. Phosphorylation occurs before nuclear envelope breakdown and is maintained throughout mitosis . Alternatively, phosphorylated rangap1 may recruit specific sumo target proteins to ranbp2's catalytic domain. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-123520 |
Ser442 |
STFLAFPsPEKLLRL |
Homo sapiens |
|
| pmid |
sentence |
| 15037602 |
Here, we show that rangap1 is phosphorylated on residues t409, s428, and s442. Phosphorylation occurs before nuclear envelope breakdown and is maintained throughout mitosis . Alternatively, phosphorylated rangap1 may recruit specific sumo target proteins to ranbp2's catalytic domain. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-123524 |
Thr409 |
GQGEKSAtPSRKILD |
Homo sapiens |
|
| pmid |
sentence |
| 15037602 |
Here, we show that rangap1 is phosphorylated on residues t409, s428, and s442. Phosphorylation occurs before nuclear envelope breakdown and is maintained throughout mitosis. The m-phase kinase cyclin b/cdk1 phosphorylates rangap1 efficiently in vitro, and t409 phosphorylation correlates with nuclear accumulation of cyclin b1 in vivo. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
RANGAP1 | down-regulates quantity by destabilization 
relocalization
|
MYCBP2 |
0.319 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261203 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 26304119 |
SUMOylated RanGAP1 Inhibits MYCBP2 Activity and Mediates Its Transport to the Nucleus. Surprisingly, we did not find MYCBP2-dependent ubiquitylation of SUMOylated RanGAP1 but instead a strong inhibition of the ubiquitin ligase activity of MYCBP2 in the presence of SUMOylated RanGAP1, as determined by the presence of ubiquitylated proteins. this effect was specific for SUMOylated RanGAP1, because the unmodified form of RanGAP1 did not affect MYCBP2-dependent protein ubiquitylation. , SUMOylated RanGAP1 inhibited the ubiquitin ligase activity of MYCBP2, and it is tempting to speculate that SUMOylated RanGAP1 inhibits the ubiquitin ligase activity of MYCBP2 to ensure MYCBP2 silencing during its transport to the nucleus |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
3.0
RANGAP1
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