| + |
AURKB | down-regulates 
phosphorylation
|
KIF2C |
0.72 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-155894 |
Ser111 |
KESLRSRsTRMSTVS |
Homo sapiens |
|
| pmid |
sentence |
| 17567953 |
Here, we show that the binding of mcak to chromosome arms is also regulated by aurora b and that aurora b-dependent chromosome arm and centromere localization is regulated by distinct two-site phosphoregulatory mechanisms. Mcak association with chromosome arms is promoted by phosphorylation of t95 on mcak, whereas phosphorylation of s196 on mcak promotes dissociation from the arms. Although targeting of mcak to centromeres requires phosphorylation of s110 on mcak, dephosphorylation of t95 on mcak increases the binding of mcak to centromeres. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-155898 |
Ser192 |
VNSVRRKsCLVKEVE |
Homo sapiens |
|
| pmid |
sentence |
| 17567953 |
Here, we show that the binding of mcak to chromosome arms is also regulated by aurora b and that aurora b-dependent chromosome arm and centromere localization is regulated by distinct two-site phosphoregulatory mechanisms. Mcak association with chromosome arms is promoted by phosphorylation of t95 on mcak, whereas phosphorylation of s196 on mcak promotes dissociation from the arms. Although targeting of mcak to centromeres requires phosphorylation of s110 on mcak, dephosphorylation of t95 on mcak increases the binding of mcak to centromeres. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PAK1 | down-regulates
phosphorylation
|
KIF2C |
0.394 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-199080 |
Ser111 |
KESLRSRsTRMSTVS |
Homo sapiens |
|
| pmid |
sentence |
| 23055517 |
Here we found that mcak is a cognate substrate of pak1 wherein pak1 phosphorylates mcak on serines 192 and 111 both in vivo and in vitro. Furthermore, we found that pak1 phosphorylation of mcak on serines 192 and 111 preferentially regulates its microtubule depolymerization activity and localization to centrosomes |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-199084 |
Ser192 |
VNSVRRKsCLVKEVE |
Homo sapiens |
|
| pmid |
sentence |
| 23055517 |
Here we found that mcak is a cognate substrate of pak1 wherein pak1 phosphorylates mcak on serines 192 and 111 both in vivo and in vitro. Furthermore, we found that pak1 phosphorylation of mcak on serines 192 and 111 preferentially regulates its microtubule depolymerization activity and localization to centrosomes |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PLK1 | down-regulates quantity by destabilization
phosphorylation
|
KIF2C |
0.804 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276862 |
Ser621 |
ALIPGNLsKEEEELS |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 25504441 |
Our studies suggest new mechanisms by which Plk1 regulates MCAK: the degradation of MCAK is controlled by Plk1 phosphorylation on S621, whereas its activity is modulated by Plk1 phosphorylation on S632/S633 in mitosis.We have recently shown that S621 in MCAK is the major phosphorylation site of Plk1, which is responsible for regulating MCAK's degradation by promoting the association of MCAK with APC/CCdc20. In the present study, we have addressed another two residues phosphorylated by Plk1, namely S632/S633 in the C-terminus of MCAK. Our data suggest that Plk1 phosphorylates S632/S633 and regulates its catalytic activity in mitosis. This phosphorylation is required for proper spindle assembly during early phases of mitosis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PLK1 | up-regulates activity 
phosphorylation
|
KIF2C |
0.804 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276863 |
Ser632 |
EELSSQMsSFNEAMT |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 25504441 |
Our studies suggest new mechanisms by which Plk1 regulates MCAK: the degradation of MCAK is controlled by Plk1 phosphorylation on S621, whereas its activity is modulated by Plk1 phosphorylation on S632/S633 in mitosis.We have recently shown that S621 in MCAK is the major phosphorylation site of Plk1, which is responsible for regulating MCAK's degradation by promoting the association of MCAK with APC/CCdc20. In the present study, we have addressed another two residues phosphorylated by Plk1, namely S632/S633 in the C-terminus of MCAK. Our data suggest that Plk1 phosphorylates S632/S633 and regulates its catalytic activity in mitosis. This phosphorylation is required for proper spindle assembly during early phases of mitosis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276861 |
Ser633 |
ELSSQMSsFNEAMTQ |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 25504441 |
Our studies suggest new mechanisms by which Plk1 regulates MCAK: the degradation of MCAK is controlled by Plk1 phosphorylation on S621, whereas its activity is modulated by Plk1 phosphorylation on S632/S633 in mitosis.We have recently shown that S621 in MCAK is the major phosphorylation site of Plk1, which is responsible for regulating MCAK's degradation by promoting the association of MCAK with APC/CCdc20. In the present study, we have addressed another two residues phosphorylated by Plk1, namely S632/S633 in the C-terminus of MCAK. Our data suggest that Plk1 phosphorylates S632/S633 and regulates its catalytic activity in mitosis. This phosphorylation is required for proper spindle assembly during early phases of mitosis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276931 |
Ser715 |
MQLEEQAsRQISSKK |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 26206521 |
Active PLK1, in turn, phosphorylates MCAK at Ser715 which promotes its microtubule depolymerase activity essential for faithful chromosome segregation. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
AURKB | up-regulates
phosphorylation
|
KIF2C |
0.72 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-155890 |
Ser95 |
IQKQKRRsVNSKIPA |
Homo sapiens |
|
| pmid |
sentence |
| 17567953 |
Here, we show that the binding of mcak to chromosome arms is also regulated by aurora b and that aurora b-dependent chromosome arm and centromere localization is regulated by distinct two-site phosphoregulatory mechanisms. Mcak association with chromosome arms is promoted by phosphorylation of t95 on mcak, whereas phosphorylation of s196 on mcak promotes dissociation from the arms. Although targeting of mcak to centromeres requires phosphorylation of s110 on mcak, dephosphorylation of t95 on mcak increases the binding of mcak to centromeres. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK1 | down-regulates
phosphorylation
|
KIF2C |
0.673 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-164761 |
Thr537 |
LGQNKAHtPFRESKL |
Homo sapiens |
|
| pmid |
sentence |
| 20368358 |
We show here that cyclin-dependent kinase 1 (cdk1) phosphorylates t537 in the core domain of mcak and attenuates its microtubule-destabilizing activity in vitro and in vivo. Phosphorylation of mcak by cdk1 promotes the release of mcak from centrosomes and is required for proper spindle formation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
APC-c | down-regulates quantity by destabilization
ubiquitination
|
KIF2C |
0.281 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276864 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 25504441 |
Our studies suggest new mechanisms by which Plk1 regulates MCAK: the degradation of MCAK is controlled by Plk1 phosphorylation on S621, whereas its activity is modulated by Plk1 phosphorylation on S632/S633 in mitosis.We have recently shown that S621 in MCAK is the major phosphorylation site of Plk1, which is responsible for regulating MCAK's degradation by promoting the association of MCAK with APC/CCdc20. In the present study, we have addressed another two residues phosphorylated by Plk1, namely S632/S633 in the C-terminus of MCAK. Our data suggest that Plk1 phosphorylates S632/S633 and regulates its catalytic activity in mitosis. This phosphorylation is required for proper spindle assembly during early phases of mitosis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266111 |
|
|
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: |
2 |
Organism: |
Homo Sapiens, In Vitro |
| + |
KIF2C | up-regulates 
|
Minus-end directed microtubule movement |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272535 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19773780 |
In general, N-kinesins and C-kinesins drive microtubule plus end- and minus end-directed motilities, respectively, and M-kinesins depolymerize microtubules1,9 (Box 1).|Forty-five genes that encode kinesin superfamily proteins (also known as KIFs) have been discovered in the mouse and human genomes.|KIFs are molecular motors that directionally transport various cargos, including membranous organelles, protein complexes and mRNAs, along the microtubule system. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
KIF2C | up-regulates
|
Plus-end directed sliding movement |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272529 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19773780 |
In general, N-kinesins and C-kinesins drive microtubule plus end- and minus end-directed motilities, respectively, and M-kinesins depolymerize microtubules1,9 (Box 1).|Forty-five genes that encode kinesin superfamily proteins (also known as KIFs) have been discovered in the mouse and human genomes.|KIFs are molecular motors that directionally transport various cargos, including membranous organelles, protein complexes and mRNAs, along the microtubule system. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
KIF2C
- 
- 