Relation Results

Identifier	Residue	Sequence	Organism
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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

Identifier	Residue	Organism
SIGNOR-278246		Homo sapiens
pmid	sentence
26119734	As a result, Plk1 activity enhances Mps1 catalytic activity as well as the recruitment of the spindle assembly checkpoint components Mad1:C-Mad2 and Bub3:BubR1 to kinetochores.\|When assayed in vitro, Plk1 readily phosphorylated kinase-dead Mps1, confirming earlier data (Dou et al., 2011).

Publications:

18

Organism:

In Vitro, Homo Sapiens

Identifier	Residue	Sequence	Organism
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
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
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
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
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
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
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
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
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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277350	Ser415	VEDEDQDsEEEKDND	Homo sapiens	HEK-293T Cell
pmid	sentence
28380042	Usp16 is a TTK phosphorylation substrate.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277351	Thr554	EVLTSSPtRNLNGAY	Homo sapiens	HEK-293T Cell
pmid	sentence
28380042	Usp16 is a TTK phosphorylation substrate.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
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
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
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
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
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

Identifier	Residue	Sequence	Organism
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
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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277458	Ser928	SRLATNTsAPDLKNV	Homo sapiens	HeLa Cell
pmid	sentence
31253867	We further uncovered that Mps1 is a kinase of MAP4, and E7-MAP4 binding blocks Mps1 phosphorylation of MAP4, thereby interrupting phosphorylation-dependent MAP4 degradation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277462	Thr927	LSRLATNtSAPDLKN	Homo sapiens	HeLa Cell
pmid	sentence
31253867	We further uncovered that Mps1 is a kinase of MAP4, and E7-MAP4 binding blocks Mps1 phosphorylation of MAP4, thereby interrupting phosphorylation-dependent MAP4 degradation.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
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
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
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
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	Organism
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

Identifier	Residue	Sequence	Organism
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

Identifier	Residue	Sequence	Organism
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

Identifier	Residue	Sequence	Organism
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

Identifier	Residue	Sequence	Organism
SIGNOR-279315	Thr306	LADYWKCtSCNEMNP	Homo sapiens
pmid	sentence
26531827	(D and E) MDM2 was phosphorylated by hMps1 at Thr4, Thr306 and Ser307 in vitro.\|In support, the MDM2 Ser307 to Ala mutant was less stable than the wild-type protein when coexpressed with hMps1 (Supplementary Figure S2B and C). hMps1 promotes MDM2-mediated H2B ubiquitination. (A) wild-type but not kinase-dead mutant hMps1 promotes MDM2-mediated H2B ubiquitination. 293T cells were transfected with the indicated plasmids and lysates were prepared for the Ni-NTA bead pulldown assay. 46999999="S307A"}

Identifier	Residue	Sequence	Organism
SIGNOR-279314	Thr4	tNMSVPTD	Homo sapiens
pmid	sentence
26531827	In support, the MDM2 Ser307 to Ala mutant was less stable than the wild-type protein when coexpressed with hMps1 (Supplementary Figure S2B and C). hMps1 promotes MDM2-mediated H2B ubiquitination. (A) wild-type but not kinase-dead mutant hMps1 promotes MDM2-mediated H2B ubiquitination. 293T cells were transfected with the indicated plasmids and lysates were prepared for the Ni-NTA bead pulldown assay. 46999999="S307A"}\|MDM2 Thr4 and Thr306 are phosphorylated by hMps1 upon oxidative stress.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-278255	Thr461	SKVQPSPtVHTKEAL	Homo sapiens
pmid	sentence
28072388	After Cdk1 phosphorylates Bub1 S459, Mps1 then phosphorylates Bub1 T461 (b).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-279398	Thr468	DYMSCFRtPVVKNDF	Homo sapiens
pmid	sentence
20861309	Cdk2 phosphorylates Mps1 at T468, attenuating the function of a degradation signal found in amino acids 420\u2013507 (encoded by exons 12 and 13) and allowing the accumulation of a centrosomal pool of Mps1 that represents no more than 10% of total cellular Mps1 ( xref ).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
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
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

Identifier	Residue	Sequence	Organism
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

Identifier	Residue	Sequence	Organism
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

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

Identifier	Residue	Organism
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

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

Identifier	Residue	Organism
SIGNOR-279132		Homo sapiens
pmid	sentence
11257498	Fig. 6C-1 shows that the GST-TTK fusion protein phosphorylated both tau and tubulin, but the phosphorylating activity on tau was much higher than that on tubulin.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-190137		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-279000		in vitro
pmid	sentence
18541701	Furthermore, although catalytically inactive Mps1 can restore kinetochore localization of Mad1, only the active kinase restores Mad2 localization.\|Indeed, Mps1 can phosphorylate Mad1 in vitro.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Organism
SIGNOR-278999		Homo sapiens
pmid	sentence
18342609	Strikingly, phosphorylation of Cenp-E C tail by wild-type (WT) MPS1 or CDK1-cyclin B completely reverses its inhibitory effect toward Cenp-E motor ATPase in solution.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-279352		Homo sapiens
pmid	sentence
26953350	Because Mps1 also phosphorylates ARHGEF17, the Mps1\u2013ARHGEF17 complex is short lived and promotes its own dissociation, which in turn releases Mps1 and ARHGEF17 from the kinetochore.\|ARHGEF17 and Mps1 interact during mitosis and Mps1 phosphorylates ARHGEF17.

Publications:

1

Organism:

Homo Sapiens

Name	TTK View Modifications
Full Name	Dual specificity protein kinase TTK
Synonyms	Phosphotyrosine picked threonine-protein kinase, PYT \| MPS1, MPS1L1
Primary ID	P33981
Links	- -
Type	protein
Relations	62
Inhibitors	1124329-14-1
Function	Phosphorylates proteins on serine, threonine, and tyrosine (PubMed:18243099, PubMed:29162720). Probably associated with cell proliferation (PubMed:18243099). Phosphorylates MAD1L1 to promote mitotic checkpoint signaling (PubMed:29162720). Essential for chromosome alignment by enhancing AURKB activity (via direct CDCA8 phosphorylation) at the centromere, and for the mitotic checkpoint (PubMed:18243099).

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