+ |
CyclinE/CDK2 |
phosphorylation
|
PRC1 |
0.351 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250745 |
Thr470 |
LYGSAPRtPSKRRGL |
|
|
pmid |
sentence |
9885575 |
We have shown that PRC1 is a good in vitro substrate for several CDKs, and that it is also phosphorylated in a cell cycle–dependent manner in vivo at Thr-481 (major mitosis. and Thr-470 (minor site), which are the in vitro phosphorylation sites. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250746 |
Thr481 |
RRGLAPNtPGKARKL |
|
|
pmid |
sentence |
9885575 |
We have shown that PRC1 is a good in vitro substrate for several CDKs, and that it is also phosphorylated in a cell cycle–dependent manner in vivo at Thr-481 (major mitosis. and Thr-470 (minor site), which are the in vitro phosphorylation sites. |
|
Publications: |
2 |
+ |
CDK16 | up-regulates activity
phosphorylation
|
PRC1 |
0.35 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273017 |
Thr481 |
RRGLAPNtPGKARKL |
Homo sapiens |
MDA-MB-231 Cell |
pmid |
sentence |
35449080 |
Mechanistically, CDK16 exerts its function by phosphorylating protein regulator of cytokinesis 1 (PRC1) to regulate spindle formation during mitosis.|Indeed, immunoblot analysis showed that PRC1 phosphorylation at the T481 site (CDK-dependent major phosphorylation site) fluctuated with the abundance of CDK16 protein in the cell cycle process |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CyclinY/CDK16 | up-regulates activity
phosphorylation
|
PRC1 |
0.35 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273013 |
Thr481 |
RRGLAPNtPGKARKL |
Homo sapiens |
MDA-MB-231 Cell |
pmid |
sentence |
35449080 |
Mechanistically, CDK16 exerts its function by phosphorylating protein regulator of cytokinesis 1 (PRC1) to regulate spindle formation during mitosis.|Indeed, immunoblot analysis showed that PRC1 phosphorylation at the T481 site (CDK-dependent major phosphorylation site) fluctuated with the abundance of CDK16 protein in the cell cycle process |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PRC1 | up-regulates activity
binding
|
KIF14 |
0.618 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266423 |
|
|
Homo sapiens |
|
pmid |
sentence |
16431929 |
KIF14 interacts with PRC1 and citron kinase. We find that KIF14 targets to the central spindle via its interaction with PRC1 and has an essential function in cytokinesis. I |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PRC1 | up-regulates
|
Spindle_assembly |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265987 |
|
|
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 |
+ |
PRC1 | up-regulates activity
binding
|
CENPE |
0.601 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265990 |
|
|
Homo sapiens |
|
pmid |
sentence |
15297875 |
These data indicate that PRC1 binds to KIF4, MKLP1 and CENP-E during late mitosis; however, it apparently does not interact simultaneously with more than one of these motor proteins. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PRC1 | up-regulates activity
binding
|
KIF23 |
0.589 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265989 |
|
|
Homo sapiens |
|
pmid |
sentence |
15297875 |
These data indicate that PRC1 binds to KIF4, MKLP1 and CENP-E during late mitosis; however, it apparently does not interact simultaneously with more than one of these motor proteins. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
KIF4A | up-regulates activity
binding
|
PRC1 |
0.585 |
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 |