+ |
AURKA | up-regulates activity
phosphorylation
|
TPX2 |
0.963 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265089 |
Ser121 |
PAQPQRRsLRLSAQK |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
26240182 |
Here we show that TPX2, a microtubule-bundling protein and activator of Aurora A, plays an important role. TPX2 was phosphorylated by Aurora A during mitosis. Its phospho-null mutant caused short metaphase spindles coupled with low microtubule flux rate. Interestingly, phosphorylation of TPX2 regulated its interaction with CLASP1 but not Kif2a.|This suggests that TPX2 phosphorylation positively regulates the function of CLASP1.| This is in accord with a phosphoproteomics study that identified S121 and S125 as potential phosphorylation sites for Aurora A in mitotic HeLa cells |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265088 |
Ser125 |
QRRSLRLsAQKDLEQ |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
26240182 |
Here we show that TPX2, a microtubule-bundling protein and activator of Aurora A, plays an important role. TPX2 was phosphorylated by Aurora A during mitosis. Its phospho-null mutant caused short metaphase spindles coupled with low microtubule flux rate. Interestingly, phosphorylation of TPX2 regulated its interaction with CLASP1 but not Kif2a.|This suggests that TPX2 phosphorylation positively regulates the function of CLASP1.| This is in accord with a phosphoproteomics study that identified S121 and S125 as potential phosphorylation sites for Aurora A in mitotic HeLa cells |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
CDK5 | up-regulates quantity by stabilization
phosphorylation
|
TPX2 |
0.277 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265100 |
Ser486 |
LPITVPKsPAFALKN |
Homo sapiens |
|
pmid |
sentence |
31272499 |
CDK5-mediated phosphorylation and stabilization of TPX2 promotes hepatocellular tumorigenesis |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Hepatobiliary Carcinoma Cell |
+ |
CDK2 | down-regulates activity
phosphorylation
|
TPX2 |
0.299 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265099 |
Thr72 |
NLQQAIVtPLKPVDN |
in vitro |
|
pmid |
sentence |
25688093 |
In this study, we characterize the phosphorylation of threonine 72 (Thr(72)) in human TPX2, a residue highly conserved across species. We find that Cdk1/2 phosphorylate TPX2 in vitro and in vivo. |Endogenous TPX2 phosphorylated at Thr(72) does not associate with the mitotic spindle. Furthermore, ectopic GFP-TPX2 T72A preferentially concentrates on the spindle |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
CDK1 | down-regulates activity
phosphorylation
|
TPX2 |
0.622 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265096 |
Thr72 |
NLQQAIVtPLKPVDN |
in vitro |
|
pmid |
sentence |
25688093 |
In this study, we characterize the phosphorylation of threonine 72 (Thr(72)) in human TPX2, a residue highly conserved across species. We find that Cdk1/2 phosphorylate TPX2 in vitro and in vivo. |Endogenous TPX2 phosphorylated at Thr(72) does not associate with the mitotic spindle. Furthermore, ectopic GFP-TPX2 T72A preferentially concentrates on the spindle |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
TPX2 | up-regulates activity
binding
|
CLASP1 |
0.477 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265090 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
26240182 |
Phosphorylation of TPX2 regulated its interaction with CLASP1 but not Kif2a.|This suggests that TPX2 phosphorylation positively regulates the function of CLASP1.| This is in accord with a phosphoproteomics study that identified S121 and S125 as potential phosphorylation sites for Aurora A in mitotic HeLa cells |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TPX2 | down-regulates activity
binding
|
KIF11 |
0.514 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265097 |
|
|
|
|
pmid |
sentence |
26018074 |
Dimeric, but not monomeric, Eg5 was differentially inhibited by full-length and truncated TPX2, demonstrating that dimerization or residues in the neck region are important for the interaction of TPX2 with Eg5. |
|
Publications: |
1 |