+ |
GSK3A | up-regulates activity
phosphorylation
|
NIFK |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262697 |
Thr234 |
TVDSQGPtPVCTPTF |
in vitro |
|
pmid |
sentence |
16244663 |
The forkhead-associated (FHA) domain of human Ki67 interacts with the human nucleolar protein hNIFK, recognizing a 44-residue fragment, hNIFK226-269, phosphorylated at Thr234. Here we show that high-affinity binding requires sequential phosphorylation by two kinases, CDK1 and GSK3, yielding pThr238, pThr234 and pSer230. phosphorylation of Thr234 by GSK3 proceeds only after Thr238 is already phosphorylated by CDK1. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
GSK3B | up-regulates activity
phosphorylation
|
NIFK |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262698 |
Thr234 |
TVDSQGPtPVCTPTF |
in vitro |
|
pmid |
sentence |
16244663 |
The forkhead-associated (FHA) domain of human Ki67 interacts with the human nucleolar protein hNIFK, recognizing a 44-residue fragment, hNIFK226-269, phosphorylated at Thr234. Here we show that high-affinity binding requires sequential phosphorylation by two kinases, CDK1 and GSK3, yielding pThr238, pThr234 and pSer230. phosphorylation of Thr234 by GSK3 proceeds only after Thr238 is already phosphorylated by CDK1. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
CDK1 | up-regulates activity
phosphorylation
|
NIFK |
0.284 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262696 |
Thr238 |
QGPTPVCtPTFLERR |
in vitro |
|
pmid |
sentence |
16244663 |
The forkhead-associated (FHA) domain of human Ki67 interacts with the human nucleolar protein hNIFK, recognizing a 44-residue fragment, hNIFK226-269, phosphorylated at Thr234. Here we show that high-affinity binding requires sequential phosphorylation by two kinases, CDK1 and GSK3, yielding pThr238, pThr234 and pSer230. phosphorylation of Thr234 by GSK3 proceeds only after Thr238 is already phosphorylated by CDK1. |
|
Publications: |
1 |
Organism: |
In Vitro |