| + |
PLK1 | up-regulates activity 
phosphorylation
|
TTK |
0.392 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276220 |
Ser108 |
DKYGQNEsFARIQVR |
in vitro |
|
| pmid |
sentence |
| 26119734 |
Here, we demonstrate that Plk1 promotes checkpoint signaling at kinetochores through the phosphorylation of at least two Mps1 substrates, including KNL-1 and Mps1 itself. As a result, Plk1 activity enhances Mps1 catalytic activity as well as the recruitment of the SAC components Mad1:C-Mad2 and Bub3:BubR1 to kinetochores. Plk1 Targets Mps1 Autophosphorylation Sites In Vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276216 |
Ser214 |
TVLTAQEsFSGSLGH |
in vitro |
|
| pmid |
sentence |
| 26119734 |
Here, we demonstrate that Plk1 promotes checkpoint signaling at kinetochores through the phosphorylation of at least two Mps1 substrates, including KNL-1 and Mps1 itself. As a result, Plk1 activity enhances Mps1 catalytic activity as well as the recruitment of the SAC components Mad1:C-Mad2 and Bub3:BubR1 to kinetochores. Plk1 Targets Mps1 Autophosphorylation Sites In Vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276199 |
Ser291 |
CDVKTDDsVVPCFMK |
in vitro |
|
| pmid |
sentence |
| 26119734 |
Here, we demonstrate that Plk1 promotes checkpoint signaling at kinetochores through the phosphorylation of at least two Mps1 substrates, including KNL-1 and Mps1 itself. As a result, Plk1 activity enhances Mps1 catalytic activity as well as the recruitment of the SAC components Mad1:C-Mad2 and Bub3:BubR1 to kinetochores. Plk1 Targets Mps1 Autophosphorylation Sites In Vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276212 |
Ser321 |
SKPSGNDsCELRNLK |
in vitro |
|
| pmid |
sentence |
| 26119734 |
Here, we demonstrate that Plk1 promotes checkpoint signaling at kinetochores through the phosphorylation of at least two Mps1 substrates, including KNL-1 and Mps1 itself. As a result, Plk1 activity enhances Mps1 catalytic activity as well as the recruitment of the SAC components Mad1:C-Mad2 and Bub3:BubR1 to kinetochores. Plk1 Targets Mps1 Autophosphorylation Sites In Vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276197 |
Ser333 |
NLKSVQNsHFKEPLV |
in vitro |
|
| pmid |
sentence |
| 26119734 |
Here, we demonstrate that Plk1 promotes checkpoint signaling at kinetochores through the phosphorylation of at least two Mps1 substrates, including KNL-1 and Mps1 itself. As a result, Plk1 activity enhances Mps1 catalytic activity as well as the recruitment of the SAC components Mad1:C-Mad2 and Bub3:BubR1 to kinetochores. Plk1 Targets Mps1 Autophosphorylation Sites In Vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276198 |
Ser345 |
PLVSDEKsSELIITD |
in vitro |
|
| pmid |
sentence |
| 26119734 |
Here, we demonstrate that Plk1 promotes checkpoint signaling at kinetochores through the phosphorylation of at least two Mps1 substrates, including KNL-1 and Mps1 itself. As a result, Plk1 activity enhances Mps1 catalytic activity as well as the recruitment of the SAC components Mad1:C-Mad2 and Bub3:BubR1 to kinetochores. Plk1 Targets Mps1 Autophosphorylation Sites In Vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276200 |
Ser362 |
TLKNKTEsSLLAKLE |
in vitro |
|
| pmid |
sentence |
| 26119734 |
Here, we demonstrate that Plk1 promotes checkpoint signaling at kinetochores through the phosphorylation of at least two Mps1 substrates, including KNL-1 and Mps1 itself. As a result, Plk1 activity enhances Mps1 catalytic activity as well as the recruitment of the SAC components Mad1:C-Mad2 and Bub3:BubR1 to kinetochores. Plk1 Targets Mps1 Autophosphorylation Sites In Vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276208 |
Ser363 |
LKNKTESsLLAKLEE |
in vitro |
|
| pmid |
sentence |
| 26119734 |
Here, we demonstrate that Plk1 promotes checkpoint signaling at kinetochores through the phosphorylation of at least two Mps1 substrates, including KNL-1 and Mps1 itself. As a result, Plk1 activity enhances Mps1 catalytic activity as well as the recruitment of the SAC components Mad1:C-Mad2 and Bub3:BubR1 to kinetochores. Plk1 Targets Mps1 Autophosphorylation Sites In Vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276206 |
Ser37 |
EDLTDELsLNKISAD |
in vitro |
|
| pmid |
sentence |
| 26119734 |
Here, we demonstrate that Plk1 promotes checkpoint signaling at kinetochores through the phosphorylation of at least two Mps1 substrates, including KNL-1 and Mps1 itself. As a result, Plk1 activity enhances Mps1 catalytic activity as well as the recruitment of the SAC components Mad1:C-Mad2 and Bub3:BubR1 to kinetochores. Plk1 Targets Mps1 Autophosphorylation Sites In Vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276202 |
Thr12 |
DLSGRELtIDSIMNK |
in vitro |
|
| pmid |
sentence |
| 26119734 |
Here, we demonstrate that Plk1 promotes checkpoint signaling at kinetochores through the phosphorylation of at least two Mps1 substrates, including KNL-1 and Mps1 itself. As a result, Plk1 activity enhances Mps1 catalytic activity as well as the recruitment of the SAC components Mad1:C-Mad2 and Bub3:BubR1 to kinetochores. Plk1 Targets Mps1 Autophosphorylation Sites In Vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276219 |
Thr210 |
LSASTVLtAQESFSG |
in vitro |
|
| pmid |
sentence |
| 26119734 |
Here, we demonstrate that Plk1 promotes checkpoint signaling at kinetochores through the phosphorylation of at least two Mps1 substrates, including KNL-1 and Mps1 itself. As a result, Plk1 activity enhances Mps1 catalytic activity as well as the recruitment of the SAC components Mad1:C-Mad2 and Bub3:BubR1 to kinetochores. Plk1 Targets Mps1 Autophosphorylation Sites In Vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276204 |
Thr33 |
KFKNEDLtDELSLNK |
in vitro |
|
| pmid |
sentence |
| 26119734 |
Here, we demonstrate that Plk1 promotes checkpoint signaling at kinetochores through the phosphorylation of at least two Mps1 substrates, including KNL-1 and Mps1 itself. As a result, Plk1 activity enhances Mps1 catalytic activity as well as the recruitment of the SAC components Mad1:C-Mad2 and Bub3:BubR1 to kinetochores. Plk1 Targets Mps1 Autophosphorylation Sites In Vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276210 |
Thr371 |
LLAKLEEtKEYQEPE |
in vitro |
|
| pmid |
sentence |
| 26119734 |
Here, we demonstrate that Plk1 promotes checkpoint signaling at kinetochores through the phosphorylation of at least two Mps1 substrates, including KNL-1 and Mps1 itself. As a result, Plk1 activity enhances Mps1 catalytic activity as well as the recruitment of the SAC components Mad1:C-Mad2 and Bub3:BubR1 to kinetochores. Plk1 Targets Mps1 Autophosphorylation Sites In Vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276222 |
Thr458 |
CKTPSSNtLDDYMSC |
in vitro |
|
| pmid |
sentence |
| 26119734 |
Here, we demonstrate that Plk1 promotes checkpoint signaling at kinetochores through the phosphorylation of at least two Mps1 substrates, including KNL-1 and Mps1 itself. As a result, Plk1 activity enhances Mps1 catalytic activity as well as the recruitment of the SAC components Mad1:C-Mad2 and Bub3:BubR1 to kinetochores. Plk1 Targets Mps1 Autophosphorylation Sites In Vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276218 |
Thr46 |
NKISADTtDNSGTVN |
in vitro |
|
| pmid |
sentence |
| 26119734 |
Here, we demonstrate that Plk1 promotes checkpoint signaling at kinetochores through the phosphorylation of at least two Mps1 substrates, including KNL-1 and Mps1 itself. As a result, Plk1 activity enhances Mps1 catalytic activity as well as the recruitment of the SAC components Mad1:C-Mad2 and Bub3:BubR1 to kinetochores. Plk1 Targets Mps1 Autophosphorylation Sites In Vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276214 |
Thr564 |
LEEADNQtLDSYRNE |
in vitro |
|
| pmid |
sentence |
| 26119734 |
Here, we demonstrate that Plk1 promotes checkpoint signaling at kinetochores through the phosphorylation of at least two Mps1 substrates, including KNL-1 and Mps1 itself. As a result, Plk1 activity enhances Mps1 catalytic activity as well as the recruitment of the SAC components Mad1:C-Mad2 and Bub3:BubR1 to kinetochores. Plk1 Targets Mps1 Autophosphorylation Sites In Vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276221 |
Thr594 |
RLYDYEItDQYIYMV |
in vitro |
|
| pmid |
sentence |
| 26119734 |
Here, we demonstrate that Plk1 promotes checkpoint signaling at kinetochores through the phosphorylation of at least two Mps1 substrates, including KNL-1 and Mps1 itself. As a result, Plk1 activity enhances Mps1 catalytic activity as well as the recruitment of the SAC components Mad1:C-Mad2 and Bub3:BubR1 to kinetochores. Plk1 Targets Mps1 Autophosphorylation Sites In Vitro |
|
| Publications: |
17 |
Organism: |
In Vitro |
| + |
TTK | up-regulates activity
phosphorylation
|
TTK |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276217 |
Ser214 |
TVLTAQEsFSGSLGH |
in vitro |
|
| pmid |
sentence |
| 26119734 |
Here, we demonstrate that Plk1 promotes checkpoint signaling at kinetochores through the phosphorylation of at least two Mps1 substrates, including KNL-1 and Mps1 itself. As a result, Plk1 activity enhances Mps1 catalytic activity as well as the recruitment of the SAC components Mad1:C-Mad2 and Bub3:BubR1 to kinetochores. Plk1 Targets Mps1 Autophosphorylation Sites In Vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276213 |
Ser321 |
SKPSGNDsCELRNLK |
in vitro |
|
| pmid |
sentence |
| 26119734 |
Here, we demonstrate that Plk1 promotes checkpoint signaling at kinetochores through the phosphorylation of at least two Mps1 substrates, including KNL-1 and Mps1 itself. As a result, Plk1 activity enhances Mps1 catalytic activity as well as the recruitment of the SAC components Mad1:C-Mad2 and Bub3:BubR1 to kinetochores. Plk1 Targets Mps1 Autophosphorylation Sites In Vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276201 |
Ser362 |
TLKNKTEsSLLAKLE |
in vitro |
|
| pmid |
sentence |
| 26119734 |
Here, we demonstrate that Plk1 promotes checkpoint signaling at kinetochores through the phosphorylation of at least two Mps1 substrates, including KNL-1 and Mps1 itself. As a result, Plk1 activity enhances Mps1 catalytic activity as well as the recruitment of the SAC components Mad1:C-Mad2 and Bub3:BubR1 to kinetochores. Plk1 Targets Mps1 Autophosphorylation Sites In Vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276209 |
Ser363 |
LKNKTESsLLAKLEE |
in vitro |
|
| pmid |
sentence |
| 26119734 |
Here, we demonstrate that Plk1 promotes checkpoint signaling at kinetochores through the phosphorylation of at least two Mps1 substrates, including KNL-1 and Mps1 itself. As a result, Plk1 activity enhances Mps1 catalytic activity as well as the recruitment of the SAC components Mad1:C-Mad2 and Bub3:BubR1 to kinetochores. Plk1 Targets Mps1 Autophosphorylation Sites In Vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276207 |
Ser37 |
EDLTDELsLNKISAD |
in vitro |
|
| pmid |
sentence |
| 26119734 |
Here, we demonstrate that Plk1 promotes checkpoint signaling at kinetochores through the phosphorylation of at least two Mps1 substrates, including KNL-1 and Mps1 itself. As a result, Plk1 activity enhances Mps1 catalytic activity as well as the recruitment of the SAC components Mad1:C-Mad2 and Bub3:BubR1 to kinetochores. Plk1 Targets Mps1 Autophosphorylation Sites In Vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276203 |
Thr12 |
DLSGRELtIDSIMNK |
in vitro |
|
| pmid |
sentence |
| 26119734 |
Here, we demonstrate that Plk1 promotes checkpoint signaling at kinetochores through the phosphorylation of at least two Mps1 substrates, including KNL-1 and Mps1 itself. As a result, Plk1 activity enhances Mps1 catalytic activity as well as the recruitment of the SAC components Mad1:C-Mad2 and Bub3:BubR1 to kinetochores. Plk1 Targets Mps1 Autophosphorylation Sites In Vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276205 |
Thr33 |
KFKNEDLtDELSLNK |
in vitro |
|
| pmid |
sentence |
| 26119734 |
Here, we demonstrate that Plk1 promotes checkpoint signaling at kinetochores through the phosphorylation of at least two Mps1 substrates, including KNL-1 and Mps1 itself. As a result, Plk1 activity enhances Mps1 catalytic activity as well as the recruitment of the SAC components Mad1:C-Mad2 and Bub3:BubR1 to kinetochores. Plk1 Targets Mps1 Autophosphorylation Sites In Vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276211 |
Thr371 |
LLAKLEEtKEYQEPE |
in vitro |
|
| pmid |
sentence |
| 26119734 |
Here, we demonstrate that Plk1 promotes checkpoint signaling at kinetochores through the phosphorylation of at least two Mps1 substrates, including KNL-1 and Mps1 itself. As a result, Plk1 activity enhances Mps1 catalytic activity as well as the recruitment of the SAC components Mad1:C-Mad2 and Bub3:BubR1 to kinetochores. Plk1 Targets Mps1 Autophosphorylation Sites In Vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276215 |
Thr564 |
LEEADNQtLDSYRNE |
in vitro |
|
| pmid |
sentence |
| 26119734 |
Here, we demonstrate that Plk1 promotes checkpoint signaling at kinetochores through the phosphorylation of at least two Mps1 substrates, including KNL-1 and Mps1 itself. As a result, Plk1 activity enhances Mps1 catalytic activity as well as the recruitment of the SAC components Mad1:C-Mad2 and Bub3:BubR1 to kinetochores. Plk1 Targets Mps1 Autophosphorylation Sites In Vitro |
|
| Publications: |
9 |
Organism: |
In Vitro |
| + |
TTK | up-regulates
phosphorylation
|
TTK |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179896 |
Ser582 |
LNKLQQHsDKIIRLY |
Homo sapiens |
|
| pmid |
sentence |
| 18680479 |
We have identified 16 sites of mps1 autophosphorylation in vitro, several of which are required for catalytic activity / autophosphorylation outside the activation segment was also important for activity in vitro, since s582a/s582d and y811f mutants exhibited decreased activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-183022 |
Ser677 |
QMQPDTTsVVKDSQV |
Homo sapiens |
|
| pmid |
sentence |
| 19120698 |
Autophosphorylation appears to be a priming event for kinase activation. We identified mps1 autophosphorylation sites in the activation and the p+1 loops. Whereas activation loop autophosphorylation enhances kinase activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179900 |
Ser742 |
QQIINQIsKLHAIID |
Homo sapiens |
|
| pmid |
sentence |
| 18680479 |
We have identified 16 sites of mps1 autophosphorylation in vitro, several of which are required for catalytic activity after expression in bacteria or in cultured human cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-183026 |
Thr676 |
NQMQPDTtSVVKDSQ |
Homo sapiens |
|
| pmid |
sentence |
| 19120698 |
Autophosphorylation appears to be a priming event for kinase activation. We identified mps1 autophosphorylation sites in the activation and the p+1 loops. Whereas activation loop autophosphorylation enhances kinase activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-183030 |
Thr686 |
VKDSQVGtVNYMPPE |
Homo sapiens |
|
| pmid |
sentence |
| 19120698 |
Autophosphorylation appears to be a priming event for kinase activation. We identified mps1 autophosphorylation sites in the activation and the p+1 loops. Whereas activation loop autophosphorylation enhances kinase activity, autophosphorylation at the p+1 loop (t686) is associated with the active kinase. |
|
| Publications: |
5 |
Organism: |
Homo Sapiens |
| + |
TTK | up-regulates
phosphorylation
|
HSPA9 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-156181 |
Ser65 |
IDLGTTNsCVAVMEG |
Homo sapiens |
|
| pmid |
sentence |
| 17573779 |
Mortalin binds to mps1, and is phosphorylated by mps1 on thr62 and ser65. The phosphorylated mortalin then super-activates mps1 in a feedback manner. Mps1-associated acceleration of centrosome duplication depends on the presence of mortalin and super-activation by the thr62/ser65 phosphorylated mortalin |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-156185 |
Thr62 |
VVGIDLGtTNSCVAV |
Homo sapiens |
|
| pmid |
sentence |
| 17573779 |
Mortalin binds to mps1, and is phosphorylated by mps1 on thr62 and ser65. The phosphorylated mortalin then super-activates mps1 in a feedback manner. Mps1-associated acceleration of centrosome duplication depends on the presence of mortalin and super-activation by the thr62/ser65 phosphorylated mortalin |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
TTK | up-regulates
phosphorylation
|
CDCA8 |
0.476 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186143 |
Thr169 |
KRSSRANtVTPAVGR |
Homo sapiens |
|
| pmid |
sentence |
| 19530738 |
First, we confirmed that wild-type borealin is phosphorylated at the previously described sites t88, t94, t169, and t230 when present in complex with survivin borealin might be a substrate for mps1. In the case of wild-type borealin, the fast exchange between the monomeric and dimeric forms may allow mps1 to phosphorylate the monomer. In turn, mps1 may regulate borealin function by unfolding the c-terminal domain and/or shifting the population to the monomeric form. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186147 |
Thr230 |
DSKEIFLtVPVGGGE |
Homo sapiens |
|
| pmid |
sentence |
| 19530738 |
We found that substitutions at borealin t230, recently identified as an mps1 phosphorylation site, can modulate the dimerization state of borealin. Mutation of this single residue to alanine or valine impairs aurora b activity during mitosis and causes chromosome segregation defects |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186151 |
Thr88 |
QALEEAAtADLDITE |
Homo sapiens |
|
| pmid |
sentence |
| 19530738 |
First, we confirmed that wild-type borealin is phosphorylated at the previously described sites t88, t94, t169, and t230 when present in complex with survivin borealin might be a substrate for mps1. In the case of wild-type borealin, the fast exchange between the monomeric and dimeric forms may allow mps1 to phosphorylate the monomer. In turn, mps1 may regulate borealin function by unfolding the c-terminal domain and/or shifting the population to the monomeric form. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186155 |
Thr94 |
ATADLDItEINKLTA |
Homo sapiens |
|
| pmid |
sentence |
| 19530738 |
First, we confirmed that wild-type borealin is phosphorylated at the previously described sites t88, t94, t169, and t230 when present in complex with survivin borealin might be a substrate for mps1. In the case of wild-type borealin, the fast exchange between the monomeric and dimeric forms may allow mps1 to phosphorylate the monomer. In turn, mps1 may regulate borealin function by unfolding the c-terminal domain and/or shifting the population to the monomeric form. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-160604 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18243099 |
Direct phosphorylation of the aurora b regulator borealin by mps1 enhances aurora b activity and is essential for chromosome alignment |
|
| Publications: |
5 |
Organism: |
Homo Sapiens |
| + |
TTK | up-regulates
phosphorylation
|
TP53 |
0.519 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-184931 |
Thr18 |
EPPLSQEtFSDLWKL |
Homo sapiens |
|
| pmid |
sentence |
| 19332559 |
Ttk/hmps1 mediates the p53-dependent postmitotic checkpoint by phosphorylating p53 at thr18. phosphorylation at thr18 enhances p53-dependent activation of not only p21 but also lats2, two mediators of the postmitotic checkpoint. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CHEK2 |
phosphorylation
|
TTK |
0.299 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-183470 |
Thr288 |
SPDCDVKtDDSVVPC |
Homo sapiens |
|
| pmid |
sentence |
| 19151762 |
Phosphorylation at ttk/hmps1 thr288 is enhanced by chk2 in vitro and in vivo after ir |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CHEK2 | up-regulates
phosphorylation
|
TTK |
0.299 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-242665 |
Thr288 |
SPDCDVKtDDSVVPC |
Homo sapiens |
|
| pmid |
sentence |
| 19151762 |
Phosphorylation at ttk/hmps1 thr288 is enhanced by chk2 in vitro and in vivo after ir |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TTK | down-regulates 
phosphorylation
|
TTK |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179904 |
Thr675 |
ANQMQPDtTSVVKDS |
Homo sapiens |
|
| pmid |
sentence |
| 18680479 |
We have identified 16 sites of mps1 autophosphorylation in vitro, several of which are required for catalytic activity / mutation of thr675 to alanine increased mps1 catalytic domain activity, and this was reduced to wt levels by mutation to aspartate |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179908 |
Thr806 |
NQMAKGTtEEMKYVL |
Homo sapiens |
|
| pmid |
sentence |
| 18680479 |
We have identified 16 sites of mps1 autophosphorylation in vitro, several of which are required for catalytic activity / t806d mps1 was significantly less active than t806a, demonstrating a potential negative correlation between phosphorylation and activity at this site. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
TTK | up-regulates
phosphorylation
|
CHEK2 |
0.299 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-132665 |
Thr68 |
SSLETVStQELYSIP |
Homo sapiens |
|
| pmid |
sentence |
| 15618221 |
Ttk/hmps1 directly phosphorylates chk2 on thr-68 in vitro.ablation of ttk expression using small interfering rna results not only in reduced chk2 thr-68 phosphorylation, but also in impaired growth arrest. Our results are consistent with a model in which ttk functions upstream from chk2 in response to dna damage |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TTK | down-regulates
phosphorylation
|
ABL1 |
0.286 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-181064 |
Thr735 |
DTEWRSVtLPRDLQS |
Homo sapiens |
|
| pmid |
sentence |
| 18794806 |
Ttk phosphorylation of thr735 was associated with partial inhibition of nuclear targeting of c-abl. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TTK | up-regulates activity
phosphorylation
|
MAD2L1 |
0.741 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252036 |
|
|
|
|
| pmid |
sentence |
| 18541701 |
Mps1 is an upstream component of the spindle assembly checkpoint, which, in human cells, is required for checkpoint activation in response to spindle damage but not apparently during an unperturbed mitosis. Mps1 also recruits Mad1 and Mad2 to kinetochores.|Thus, in human cells, Mps1 catalytic activity is required for spindle checkpoint function and recruitment of Mad2. |
|
| Publications: |
1 |
| + |
1124329-14-1 | down-regulates
chemical inhibition
|
TTK |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-190137 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DNA_damage | up-regulates 
|
TTK |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-242619 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19151762 |
Cell cycle progression is monitored constantly to ensure faithful passage of genetic codes and genome stability. We have demonstrated previously that, upon DNA damage, TTK/hMps1 activates the checkpoint kinase CHK2 by phosphorylating CHK2 at Thr68 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDR2 | up-regulates quantity by expression
transcriptional regulation
|
TTK |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252021 |
|
|
|
|
| pmid |
sentence |
| 20383333 |
Additionally, cdr2 knockdown lead to a decrease (Table 3) in four other transcripts (AURKA, CENPE, SPC25 and TTK), which are involved in kinetochore and spindle biology |
|
| Publications: |
1 |
3.0
TTK
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