| + |
PRKAA1 | up-regulates activity 
phosphorylation
|
KIF4A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265991 |
Ser801 |
KLRRRTFsLTEVRGQ |
in vitro |
|
| pmid |
sentence |
| 28992084 |
We found that the strong direct substrate KIF4A is phosphorylated by AMPK at Ser801.Using in vitro kinase assays, we found that active AMPK and Aurora B phosphorylated KIF4A at Ser801 and Thr799 respectively in a time-dependent manner (Figure 5D). KIF4A is phosphoregulated by AMPK and Aurora B. Although AMPK phosphorylation increased the ATPase activity of KIF4A, Aurora B phosphorylation resulted in a stronger increase (Figure 5I), which might be consistent with the more powerful kinase function of Aurora B during mitosis. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
CyclinB/CDK1 | up-regulates activity
phosphorylation
|
KIF4A |
0.468 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265995 |
Thr1161 |
FFNPVCAtPNSKILK |
in vitro |
|
| pmid |
sentence |
| 29771379 |
Kif4A T1161 was phosphorylated by Cdk1/Cyclin B1 in vitro. We show that Cdk phosphorylation of Kif4A licenses its chromosome localization. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
CDK1 | up-regulates activity
phosphorylation
|
KIF4A |
0.508 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265994 |
Thr1161 |
FFNPVCAtPNSKILK |
Homo sapiens |
|
| pmid |
sentence |
| 29771379 |
Identification of Cdk phosphorylation of Kif4A at T1161 in early mitosis. We show that Cdk phosphorylation of Kif4A licenses its chromosome localization. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AURKB | up-regulates activity
phosphorylation
|
KIF4A |
0.539 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265992 |
Thr799 |
PPKLRRRtFSLTEVR |
in vitro |
|
| pmid |
sentence |
| 28992084 |
Using in vitro kinase assays, we found that active AMPK and Aurora B phosphorylated KIF4A at Ser801 and Thr799 respectively in a time-dependent manner (Figure 5D). KIF4A is phosphoregulated by AMPK and Aurora B. Although AMPK phosphorylation increased the ATPase activity of KIF4A, Aurora B phosphorylation resulted in a stronger increase (Figure 5I), which might be consistent with the more powerful kinase function of Aurora B during mitosis. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
AURKA | up-regulates activity
phosphorylation
|
KIF4A |
0.433 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265993 |
Thr799 |
PPKLRRRtFSLTEVR |
in vitro |
|
| pmid |
sentence |
| 31881080 |
We show that Aurora A phosphorylates the condensin I-dependent pool of KIF4A and thus actively promotes chromosome congression from the spindle poles to the metaphase plate. In vitro kinase assays showed that recombinant KIF4A can be phosphorylated by Aurora A and that this activity is inhibited by the specific Aurora A inhibitor MLN8537 (Fig. 7 C). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
APC-c | down-regulates quantity by destabilization 
ubiquitination
|
KIF4A |
0.292 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266112 |
|
|
in vitro |
|
| pmid |
sentence |
| 24510915 |
Biochemical studies on the kinesins confirmed KIFC1, KIF18A, KIF2C, and KIF4A as APC/C substrates. Furthermore, we showed that the APC/CCDH1-dependent degradation of KIFC1 regulates the bipolar spindle formation and proper cell division. Our in vitro degradation assays showed a time-dependent degradation for four of the five potential substrates tested: KIF18A, KIF2C, KIFC1 and KIF4A were readily degraded in vitro, however remained stable in the presence of either APC/C inhibitor (Fig(Fig4A4A and Supplementary Fig S3A). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
KIF4A | up-regulates 
|
Spindle_assembly |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265986 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15297875 |
These results suggest that KIF4 and its binding partner PRC1 play essential roles in the organization of central spindles and midzone formation. KIF4 deficiency leads to mislocalization of PRC1, MKLP1, CENP-E and chromosomal passenger proteins |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
KIF4A | up-regulates activity
binding
|
PRC1 |
0.589 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265988 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15297875 |
These results suggest that KIF4 and its binding partner PRC1 play essential roles in the organization of central spindles and midzone formation. KIF4 deficiency leads to mislocalization of PRC1, MKLP1, CENP-E and chromosomal passenger proteins |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
KIF4A
- 
- 