Relation Results

Identifier	Residue	Sequence
SIGNOR-265728	Ser103	RQDKKDKsRAPISAK
pmid	sentence
31253668	CDK1 contributes to upregulation of PRPS1 activity by phosphorylating PRPS1 at S103\|In conclusion, compared with upregulation of PRPS1 expression levels, increased PRPS1 activity, which is marked by S103 phosphorylation

Publications:

1

Identifier	Residue	Sequence	Organism
SIGNOR-278239	Ser1038	STSATQSsPAPGQSK	Homo sapiens
pmid	sentence
24530506	Loss of CDK1 decreased p300 phosphorylation, but increased the p300 level.\|Our results showed that phosphorylation of p300 by CDK1 at Ser1038 and Ser2039 repressed the proliferation and metastasis activity of lung cancer cells in vitro.

Identifier	Residue	Sequence	Organism
SIGNOR-278238	Ser2039	GLGQVGIsPLKPGTV	Homo sapiens
pmid	sentence
24530506	Loss of CDK1 decreased p300 phosphorylation, but increased the p300 level.\|Our results showed that phosphorylation of p300 by CDK1 at Ser1038 and Ser2039 repressed the proliferation and metastasis activity of lung cancer cells in vitro.

Publications:

2

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276457	Ser1038	STSATQSsPAPGQSK	Homo sapiens	Lung Cancer Cell
pmid	sentence
24530506	In this study, we found that p300 was highly phosphorylated and its level was decreased during mitosis and tumorigenesis. In vitro and in vivo experiments aimed showed that cyclin-dependent kinase 1 (CDK1) and ERK1/2 phosphorylated p300 on Ser1038 and Ser2039. Mutations of Ser1038 and Ser2039 increased p300 protein stability and levels.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276456	Ser2039	GLGQVGIsPLKPGTV	Homo sapiens	Lung Cancer Cell
pmid	sentence
24530506	In this study, we found that p300 was highly phosphorylated and its level was decreased during mitosis and tumorigenesis. In vitro and in vivo experiments aimed showed that cyclin-dependent kinase 1 (CDK1) and ERK1/2 phosphorylated p300 on Ser1038 and Ser2039. Mutations of Ser1038 and Ser2039 increased p300 protein stability and levels.

Publications:

2

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-267985	Ser104	FSFDTDRsPAPMSCD	Homo sapiens
pmid	sentence
22071694	Furthermore, active recombinant Cdk1/cyclin B1 phosphorylates BimEL and BimL in vitro and Serine 44 on BimL has been identified as a Cdk1 phosphorylation site. Collectively, these results suggest that Cdk1/cyclin B1-dependent hyper-phosphorylation of Bim during prolonged mitotic arrest is an important cell death signal.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-153300	Ser104	SQQQFGYsPGQQQTH	Homo sapiens
pmid	sentence
17310276	Ttdn1 is phosphorylated by cdk1 in vitro and in vivo. Ttdn1 is phosphorylated at multiple residues, including ser93 and ser104. Mutation of thr120 of ttdn1 abolishes its interaction with plk1, suggesting phosphorylation of thr120 in the consensus plk1-binding motif is required for its interaction with plk1

Identifier	Residue	Sequence	Organism
SIGNOR-153304	Ser93	YPGSYSRsPAGSQQQ	Homo sapiens
pmid	sentence
17310276	Ttdn1 is phosphorylated by cdk1 in vitro and in vivo. Ttdn1 is phosphorylated at multiple residues, including ser93 and ser104. Mutation of thr120 of ttdn1 abolishes its interaction with plk1, suggesting phosphorylation of thr120 in the consensus plk1-binding motif is required for its interaction with plk1

Identifier	Residue	Sequence	Organism
SIGNOR-153308	Thr120	QGSPRTStPFGSGRV	Homo sapiens
pmid	sentence
17310276	Ttdn1 is phosphorylated by cdk1 in vitro and in vivo. Ttdn1 is phosphorylated at multiple residues, including ser93 and ser104. Mutation of thr120 of ttdn1 abolishes its interaction with plk1, suggesting phosphorylation of thr120 in the consensus plk1-binding motif is required for its interaction with plk1

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276927	Ser105	TGAGAAGsPAQQHAH	Homo sapiens	HeLa Cell
pmid	sentence
26183396	In this study, we found that Cdk1 (Cyclin-dependent kinase 1) directly phosphorylated TAZ on six novel sites independent of the Hippo pathway, which further resulted in TAZ degradation through proteasome system.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276926	Ser90	QHVRSHSsPASLQLG	Homo sapiens	HeLa Cell
pmid	sentence
26183396	In this study, we found that Cdk1 (Cyclin-dependent kinase 1) directly phosphorylated TAZ on six novel sites independent of the Hippo pathway, which further resulted in TAZ degradation through proteasome system.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276925	Thr285	AVNPPTMtPDMRSIT	Homo sapiens	HeLa Cell
pmid	sentence
26183396	In this study, we found that Cdk1 (Cyclin-dependent kinase 1) directly phosphorylated TAZ on six novel sites independent of the Hippo pathway, which further resulted in TAZ degradation through proteasome system.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-276520	Ser105	TGAGAAGsPAQQHAH
pmid	sentence
26375055	We found that TAZ is phosphorylated in vitro and in vivo by the mitotic kinase CDK1 at S90, S105, T326, and T346 during the G2/M phase of the cell cycle. Interestingly, mitotic phosphorylation inactivates TAZ oncogenic activity

Identifier	Residue	Sequence
SIGNOR-276518	Ser90	QHVRSHSsPASLQLG
pmid	sentence
26375055	We found that TAZ is phosphorylated in vitro and in vivo by the mitotic kinase CDK1 at S90, S105, T326, and T346 during the G2/M phase of the cell cycle. Interestingly, mitotic phosphorylation inactivates TAZ oncogenic activity

Identifier	Residue	Sequence
SIGNOR-276519	Thr326	GCYSVPTtPEDFLSN
pmid	sentence
26375055	We found that TAZ is phosphorylated in vitro and in vivo by the mitotic kinase CDK1 at S90, S105, T326, and T346 during the G2/M phase of the cell cycle. Interestingly, mitotic phosphorylation inactivates TAZ oncogenic activity

Identifier	Residue	Sequence
SIGNOR-276521	Thr346	TGENAGQtPMNINPQ
pmid	sentence
26375055	We found that TAZ is phosphorylated in vitro and in vivo by the mitotic kinase CDK1 at S90, S105, T326, and T346 during the G2/M phase of the cell cycle. Interestingly, mitotic phosphorylation inactivates TAZ oncogenic activity

Publications:

4

Identifier	Residue	Sequence
SIGNOR-275593	Ser105	QPSSGREsPRH
pmid	sentence
24746669	Here, we show that a fraction of cyclin B1/Cdk1 proteins localizes to the matrix of mitochondria and phosphorylates a cluster of mitochondrial proteins, including the complex I (CI) subunits in the respiratory chain. Cyclin B1/Cdk1-mediated CI phosphorylation enhances CI activity, whereas deficiency of such phosphorylation in each of the relevant CI subunits results in impairment of CI function.\|These results were confirmed by generating phosphorylation defective forms of the five CI subunits through substitutions of S/T residues with Alanine (A) on either Cdk1 optimal or minimal consensus motifs (T383 on NDUFV1, S105 on NDUFV3, S364 on NDUFS2, S55/S29/T5 on NDUFB6, and T142/T120 on NDUFA12). The mutation of Cdk1 consensus motifs severely diminished their phosphorylation

Publications:

1

Identifier	Residue	Sequence	Organism
SIGNOR-262702	Ser11	KRIAKRRsPPADAIP	in vitro
pmid	sentence
15014043	Human RCC1 is phosphorylated on Ser 2 and Ser 11 in mitosis by Cdc2 kinase. We show here that Cdc2 kinase phosphorylates the serines located in or near the nuclear localization signal (NLS) of human RCC1, the nucleotide exchange factor for Ran. This phosphorylation is necessary for RCC1 to generate RanGTP on mitotic chromosomes in mammalian cells, which in turn is required for spindle assembly and chromosome segregation.

Identifier	Residue	Sequence	Organism
SIGNOR-262701	Ser2	sPKRIAKR	in vitro
pmid	sentence
15014043	Human RCC1 is phosphorylated on Ser 2 and Ser 11 in mitosis by Cdc2 kinase. We show here that Cdc2 kinase phosphorylates the serines located in or near the nuclear localization signal (NLS) of human RCC1, the nucleotide exchange factor for Ran. This phosphorylation is necessary for RCC1 to generate RanGTP on mitotic chromosomes in mammalian cells, which in turn is required for spindle assembly and chromosome segregation.

Identifier	Residue	Sequence	Organism
SIGNOR-262703	Ser387	GQDEDAWsPVEMMGK	in vitro
pmid	sentence
15014043	We show here that Cdc2 kinase phosphorylates the serines located in or near the nuclear localization signal (NLS) of human RCC1, the nucleotide exchange factor for Ran. This phosphorylation is necessary for RCC1 to generate RanGTP on mitotic chromosomes in mammalian cells, which in turn is required for spindle assembly and chromosome segregation. However, when both S2 and S11 were simultaneously mutated to As, the resulting 6His-RCC1S2,11A failed to be phosphorylated, whereas all of the other double mutants were phosphorylated (Fig. 1C). As expected, mutating all four sites to As (the 6His-RCC1S2,11,387A-T274A) also blocked phosphorylation (Fig. 1C).

Identifier	Residue	Sequence	Organism
SIGNOR-262704	Thr274	SNYHQLGtPGTESCF	in vitro
pmid	sentence
15014043	We show here that Cdc2 kinase phosphorylates the serines located in or near the nuclear localization signal (NLS) of hum an RCC1, the nucleotide exchange factor for Ran. This phosphorylation is necessary for RCC1 to generate RanGTP on mitotic chromosomes in mammalian cells, which in turn is required for spindle assembly and chromosome segregation. However, when both S2 and S11 were simultaneously mutated to As, the resulting 6His-RCC1S2,11A failed to be phosphorylated, whereas all of the other double mutants were phosphorylated (Fig. 1C). As expected, mutating all four sites to As (the 6His-RCC1S2,11,387A-T274A) also blocked phosphorylation (Fig. 1C).

Publications:

4

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-262693	Ser11	SEETPAIsPSKRARP	in vitro
pmid	sentence
8631817	DUTPase Is Phosphorylated at a Consensus Cyclin-dependent Protein Kinase Site: in Vitro Phosphorylation of Ser-11 by p34cdc2. It is conceivable that the exclusive phosphorylation of DUT-N may play a role in nuclear targeting of this protein. Taken a step further, Ser-11 may confer the ability of DUT-N to localize in specific regions of the nucleus where the dUTPase function is required. The Ser-11 Ala mutant should aid in the testing of these hypotheses.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-276156	Ser112	EKENGFSsPPQIKDE	in vitro
pmid	sentence
18408216	In vitro kinase assays demonstrated that Ser(10) can be phosphorylated by casein kinase II, Ser(21) can be phosphorylated by protein kinase Calpha, and Ser(112) and Ser(394) can be phosphorylated by Cdk1.Collectively these results indicate that topo I is phosphorylated during mitosis at multiple sites, one of which enhances DNA relaxation activity in vitro and interaction with DNA in cells.

Identifier	Residue	Sequence	Organism
SIGNOR-276157	Ser394	SKDAKVPsPPPGHKW	in vitro
pmid	sentence
18408216	In vitro kinase assays demonstrated that Ser(10) can be phosphorylated by casein kinase II, Ser(21) can be phosphorylated by protein kinase Calpha, and Ser(112) and Ser(394) can be phosphorylated by Cdk1.Collectively these results indicate that topo I is phosphorylated during mitosis at multiple sites, one of which enhances DNA relaxation activity in vitro and interaction with DNA in cells.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-113126	Ser1126	IAPSTNSsPVLKTKP	Homo sapiens
pmid	sentence
11747808	Both cdc2/cyclinb1 and mapk (erk2) efficiently phosphorylate separase at its major inhibitory site in vitro

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-273586	Ser113	LHPYSPLsPKGRPSS	Homo sapiens
pmid	sentence
30105797	Cyclin B/cyclin-dependent kinase 1 (CDK1) phosphorylates inhibitor of apoptosis stimulating protein of P53 (iASPP) to promote iASPP nucleus localization and its inhibitory effect on p53.

Identifier	Residue	Sequence	Organism
SIGNOR-273585	Ser84	EPFGSRGsPRKAATD	Homo sapiens
pmid	sentence
30105797	Cyclin B/cyclin-dependent kinase 1 (CDK1) phosphorylates inhibitor of apoptosis stimulating protein of P53 (iASPP) to promote iASPP nucleus localization and its inhibitory effect on p53.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-95256	Ser116	PQKLLGCsPALKRSH	Homo sapiens
pmid	sentence
12411508	Mitotic stabilization of cdc25a reflects its phosphorylation on ser17 and ser115 by cyclin b-cdk1, modifications required to uncouple cdc25a from its ubiquitin-proteasome-mediated turnover.

Identifier	Residue	Sequence	Organism
SIGNOR-95260	Ser18	RRLLFACsPPPASQP	Homo sapiens
pmid	sentence
12411508	Mitotic stabilization of cdc25a reflects its phosphorylation on ser17 and ser115 by cyclin b-cdk1, modifications required to uncouple cdc25a from its ubiquitin-proteasome-mediated turnover.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-72083	Ser1189	QKGELSRsPSPFTHT	Homo sapiens	Breast Cancer Cell
pmid	sentence
10550055	However, shrna-mediated depletion of cdk1 alone or small molecule cdk1 inhibition abrogated s phase cell-cycle arrest and the phosphorylation of a subset of atr/atm targets after dna damage. Loss of dna damage-induced checkpoint control was caused by a reduction in formation of brca1-containing foci. Mutation of brca1 at s1497 and s1189/s1191 resulted in loss of cdk1-mediated phosphorylation and also compromised formation of brca1-containing foci.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-187595	Ser1189	QKGELSRsPSPFTHT	Homo sapiens	Lung Cancer Cell
pmid	sentence
19683496	However, shrna-mediated depletion of cdk1 alone or small molecule cdk1 inhibition abrogated s phase cell-cycle arrest and the phosphorylation of a subset of atr/atm targets after dna damage. Loss of dna damage-induced checkpoint control was caused by a reduction in formation of brca1-containing foci. Mutation of brca1 at s1497 and s1189/s1191 resulted in loss of cdk1-mediated phosphorylation and also compromised formation of brca1-containing foci.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-187599	Ser1191	GELSRSPsPFTHTHL	Homo sapiens	Lung Cancer Cell
pmid	sentence
19683496	However, shrna-mediated depletion of cdk1 alone or small molecule cdk1 inhibition abrogated s phase cell-cycle arrest and the phosphorylation of a subset of atr/atm targets after dna damage. Loss of dna damage-induced checkpoint control was caused by a reduction in formation of brca1-containing foci. Mutation of brca1 at s1497 and s1189/s1191 resulted in loss of cdk1-mediated phosphorylation and also compromised formation of brca1-containing foci.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-72087	Ser1497	EPGVERSsPSKCPSL	Homo sapiens	Breast Cancer Cell
pmid	sentence
10550055	However, shrna-mediated depletion of cdk1 alone or small molecule cdk1 inhibition abrogated s phase cell-cycle arrest and the phosphorylation of a subset of atr/atm targets after dna damage. Loss of dna damage-induced checkpoint control was caused by a reduction in formation of brca1-containing foci. Mutation of brca1 at s1497 and s1189/s1191 resulted in loss of cdk1-mediated phosphorylation and also compromised formation of brca1-containing foci.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-187603	Ser1497	EPGVERSsPSKCPSL	Homo sapiens	Lung Cancer Cell
pmid	sentence
19683496	However, shrna-mediated depletion of cdk1 alone or small molecule cdk1 inhibition abrogated s phase cell-cycle arrest and the phosphorylation of a subset of atr/atm targets after dna damage. Loss of dna damage-induced checkpoint control was caused by a reduction in formation of brca1-containing foci. Mutation of brca1 at s1497 and s1189/s1191 resulted in loss of cdk1-mediated phosphorylation and also compromised formation of brca1-containing foci.

Publications:

5

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-116504	Ser120	LDEPNPNsPANSQAA	Homo sapiens
pmid	sentence
11953320	Hhr6a is phosphorylated in vitro by cdk-1 and -2 on ser120, a residue conserved in all hhr6a homologues, resulting in a 4-fold increase in its ubiquitin-conjugating activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-160493	Ser120	GRNIIHGsDSVESAE	Homo sapiens
pmid	sentence
18234856	Application of this approach to the discovery of cdk1-cyclin b substrates yielded identification of >70 substrates and phosphorylation sites. Many of these sites are known to be phosphorylated in vivo, but most of the proteins have not been characterized as cdk1-cyclin b substrates.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-78416	Ser122	DQHLMKCsPAQLLCS	Homo sapiens
pmid	sentence
10864927	Activation of human cdc25c at the g2/m transition occurs concomitantly with phosphorylation of five serine/threonine-proline sites: thr48, thr67, ser122, thr130, and ser214, presumably by cdc2-cyclin b.

Identifier	Residue	Sequence	Organism
SIGNOR-78420	Ser214	SRSGLYRsPSMPENL	Homo sapiens
pmid	sentence
10864927	Activation of human cdc25c at the g2/m transition occurs concomitantly with phosphorylation of five serine/threonine-proline sites: thr48, thr67, ser122, thr130, and ser214, presumably by cdc2-cyclin b.

Identifier	Residue	Sequence	Organism
SIGNOR-64960	Ser214	SRSGLYRsPSMPENL	Homo sapiens
pmid	sentence
10037602	Phosphorylation at thr-48, thr-67, ser-122, thr-130, ser-168 and ser-214 occurs at g2 and g2-m transition and is catalyzed by cdk1. Ser-168 phosphorylation levels are lower than those at the other 5 cdk1 sites. Phosphorylation by cdk1 leads to increased activity.

Identifier	Residue	Sequence	Organism
SIGNOR-36267	Ser214	SRSGLYRsPSMPENL	Homo sapiens
pmid	sentence
8119945	Phosphorylation at thr-48, thr-67, ser-122, thr-130, ser-168 and ser-214 occurs at g2 and g2-m transition and is catalyzed by cdk1. Ser-168 phosphorylation levels are lower than those at the other 5 cdk1 sites. Phosphorylation by cdk1 leads to increased activity.

Identifier	Residue	Sequence	Organism
SIGNOR-78424	Thr130	PAQLLCStPNGLDRG	Homo sapiens
pmid	sentence
10864927	Activation of human cdc25c at the g2/m transition occurs concomitantly with phosphorylation of five serine/threonine-proline sites: thr48, thr67, ser122, thr130, and ser214, presumably by cdc2-cyclin b.

Identifier	Residue	Sequence	Organism
SIGNOR-64964	Thr48	VCPDVPRtPVGKFLG	Homo sapiens
pmid	sentence
10037602	Phosphorylation at thr-48, thr-67, ser-122, thr-130, ser-168 and ser-214 occurs at g2 and g2-m transition and is catalyzed by cdk1. Ser-168 phosphorylation levels are lower than those at the other 5 cdk1 sites. Phosphorylation by cdk1 leads to increased activity.

Identifier	Residue	Sequence	Organism
SIGNOR-36271	Thr48	VCPDVPRtPVGKFLG	Homo sapiens
pmid	sentence
8119945	Phosphorylation at thr-48, thr-67, ser-122, thr-130, ser-168 and ser-214 occurs at g2 and g2-m transition and is catalyzed by cdk1. Ser-168 phosphorylation levels are lower than those at the other 5 cdk1 sites. Phosphorylation by cdk1 leads to increased activity.

Identifier	Residue	Sequence	Organism
SIGNOR-78428	Thr48	VCPDVPRtPVGKFLG	Homo sapiens
pmid	sentence
10864927	Activation of human cdc25c at the g2/m transition occurs concomitantly with phosphorylation of five serine/threonine-proline sites: thr48, thr67, ser122, thr130, and ser214, presumably by cdc2-cyclin b.

Identifier	Residue	Sequence	Organism
SIGNOR-64968	Thr67	LSILSGGtPKRCLDL	Homo sapiens
pmid	sentence
10037602	Phosphorylation at thr-48, thr-67, ser-122, thr-130, ser-168 and ser-214 occurs at g2 and g2-m transition and is catalyzed by cdk1. Ser-168 phosphorylation levels are lower than those at the other 5 cdk1 sites. Phosphorylation by cdk1 leads to increased activity.

Identifier	Residue	Sequence	Organism
SIGNOR-78432	Thr67	LSILSGGtPKRCLDL	Homo sapiens
pmid	sentence
10864927	Activation of human cdc25c at the g2/m transition occurs concomitantly with phosphorylation of five serine/threonine-proline sites: thr48, thr67, ser122, thr130, and ser214, presumably by cdc2-cyclin b.

Identifier	Residue	Sequence	Organism
SIGNOR-36275	Thr67	LSILSGGtPKRCLDL	Homo sapiens
pmid	sentence
8119945	Phosphorylation at thr-48, thr-67, ser-122, thr-130, ser-168 and ser-214 occurs at g2 and g2-m transition and is catalyzed by cdk1. Ser-168 phosphorylation levels are lower than those at the other 5 cdk1 sites. Phosphorylation by cdk1 leads to increased activity.

Publications:

11

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-69233	Ser123	KELQRQAsPSIVIAL	Homo sapiens
pmid	sentence
10403367	Cdc2 kinase preferentially phosphorylates ser-123 of rab5b. More work will be required to establish how phosphorylation of the three rab5 isoforms influences their function in the endocytic pathway

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-139465	Ser123	EEGFGSSsPVKSPAA	Homo sapiens
pmid	sentence
16085715	We show that phosphorylation of S123 (pS123) by CDK promoted the binding of Wee1A to beta-TrCP through three independent mechanisms. The pS123 not only directly interacted with basic residues in the WD40 repeat domain of beta-TrCP but also primed phosphorylation by two independent protein kinases, Plk1 and CK2 (formerly casein kinase 2)

Identifier	Residue	Sequence	Organism
SIGNOR-123824	Ser123	EEGFGSSsPVKSPAA	Homo sapiens
pmid	sentence
15070733	We have found also that the major M-phase kinases polo-like kinase 1 (Plk1) and Cdc2 are responsible for the phosphorylation of S53 and S123, respectively, and that in each case phosphorylation generates an unconventional phospho-degron (signal for degradation) that can be recognized by beta-TrCP

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-278233	Ser1234	QGYDNSEsSVRKACV	Homo sapiens
pmid	sentence
23045552	Overall, these results support the idea that phosphorylation of CLASP2 on S1234 by Cdk1, but not phosphorylation of the CLASP2 C terminal by Plk1, is required to maintain mitotic spindle bipolarity.\|We propose that Cdk1 and Plk1 mediate a CLASP2 phospho-switch that is necessary to stabilize KT-MT attachments in human cells.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-110908	Ser1237	TEYSQGAsPQPQHQL	Homo sapiens
pmid	sentence
11584018	Phosphorylation of serines 1237 and 1270 caused inhibition of dna binding in vitro. In cotransfection studies, cyclin a-cdk1 inhibited cdp/cux stable dna binding and prevented repression of the p21(waf1) reporter.

Identifier	Residue	Sequence	Organism
SIGNOR-110912	Ser1270	YQQKPYPsPKTIEDL	Homo sapiens
pmid	sentence
11584018	Phosphorylation of serines 1237 and 1270 caused inhibition of dna binding in vitro. In cotransfection studies, cyclin a-cdk1 inhibited cdp/cux stable dna binding and prevented repression of the p21(waf1) reporter.

Publications:

2

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-30244	Ser1247	KNENTEGsPQEDGVE	Homo sapiens	HeLa Cell
pmid	sentence
7635160	We show that many of the sites phosphorylated on topoisomerase iia in vivo correspond to sites phosphorylated in vitro by both p3pdcz and mitogen-activated protein (map) kinase. similarly, phosphopeptide 4 was absent from a mutant protein lacking ser1246

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-30248	Ser1354	DFVPSDAsPPKTKTS	Homo sapiens	HeLa Cell
pmid	sentence
7635160	We show that many of the sites phosphorylated on topoisomerase iia in vivo correspond to sites phosphorylated in vitro by both p3pdcz and mitogen-activated protein (map) kinase. we have also shown that phosphorylation of ser1353 and ser1360 yields different phosphopeptide maps depending upon whether one or both of these sites are phosphorylated.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-30252	Ser1361	SPPKTKTsPKLSNKE	Homo sapiens	HeLa Cell
pmid	sentence
7635160	We show that many of the sites phosphorylated on topoisomerase iia in vivo correspond to sites phosphorylated in vitro by both p3pdcz and mitogen-activated protein (map) kinase. we have also shown that phosphorylation of ser1353 and ser1360 yields different phosphopeptide maps depending upon whether one or both of these sites are phosphorylated.

Identifier	Residue	Sequence	Organism
SIGNOR-30256	Ser1393	GSVPLSSsPPATHFP	Homo sapiens
pmid	sentence
7635160	We show that many of the sites phosphorylated on topoisomerase iia in vivo correspond to sites phosphorylated in vitro by both p3pdcz and mitogen-activated protein (map) kinase. phosphopeptide 1 was eliminated by replacement of ser1392

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-272968	Ser1252	QPTLPSSsPVPIPVS	Homo sapiens	HeLa Cell
pmid	sentence
37584777	CDK1 phosphorylates AMBRA1 at T1209 and S1223. \|CDK1-mediated phosphorylation primes PLK1 phosphorylation on AMBRA1\|In this work, we show that AMBRA1 is sequentially phosphorylated at mitosis by CDK1 and PLK1 on multiple sites. In particular, CDK1 is responsible for the early phosphorylations on T1209 and S1223, and it promotes additional late phosphorylation events by PLK1 on AMBRA1. Altogether, these phosphorylation events are critical for proper spindle function and orientation. Indeed, phosphorylated AMBRA1 can interact with NUMA1 and is responsible for NUMA1 proper localization at the cell cortex. Moreover, we observe that loss of AMBRA1 leads to PLK1 protein stabilization and to an increase in phospho-NUMA1 levels which, in turn, contributes to spindle orientation defects.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-272966	Thr1238	ASWDQPGtPGREPTQ	Homo sapiens	HeLa Cell
pmid	sentence
37584777	CDK1 phosphorylates AMBRA1 at T1209 and S1223. \|CDK1-mediated phosphorylation primes PLK1 phosphorylation on AMBRA1\|In this work, we show that AMBRA1 is sequentially phosphorylated at mitosis by CDK1 and PLK1 on multiple sites. In particular, CDK1 is responsible for the early phosphorylations on T1209 and S1223, and it promotes additional late phosphorylation events by PLK1 on AMBRA1. Altogether, these phosphorylation events are critical for proper spindle function and orientation. Indeed, phosphorylated AMBRA1 can interact with NUMA1 and is responsible for NUMA1 proper localization at the cell cortex. Moreover, we observe that loss of AMBRA1 leads to PLK1 protein stabilization and to an increase in phospho-NUMA1 levels which, in turn, contributes to spindle orientation defects.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-276115	Ser126	NPEAESSsKEGELDA	in vitro
pmid	sentence
23901111	Here we show that the mitotic kinases Aurora B and Cyclin-dependent kinase 1 (Cdk1) destabilize interactions between Sororin and the cohesin subunit precocious dissociation of sisters protein 5 (Pds5) by phosphorylating Sororin, leading to release of acetylated cohesin from chromosome arms and loss of cohesion.

Identifier	Residue	Sequence	Organism
SIGNOR-276125	Ser139	DARDLEMsKKVRRSY	in vitro
pmid	sentence
23901111	Here we show that the mitotic kinases Aurora B and Cyclin-dependent kinase 1 (Cdk1) destabilize interactions between Sororin and the cohesin subunit precocious dissociation of sisters protein 5 (Pds5) by phosphorylating Sororin, leading to release of acetylated cohesin from chromosome arms and loss of cohesion.

Identifier	Residue	Sequence	Organism
SIGNOR-276120	Ser164	TSTPGRRsCFGFEGL	in vitro
pmid	sentence
23901111	Here we show that the mitotic kinases Aurora B and Cyclin-dependent kinase 1 (Cdk1) destabilize interactions between Sororin and the cohesin subunit precocious dissociation of sisters protein 5 (Pds5) by phosphorylating Sororin, leading to release of acetylated cohesin from chromosome arms and loss of cohesion.

Identifier	Residue	Sequence	Organism
SIGNOR-276124	Ser33	LRRSQRKsGSELPSI	in vitro
pmid	sentence
23901111	Here we show that the mitotic kinases Aurora B and Cyclin-dependent kinase 1 (Cdk1) destabilize interactions between Sororin and the cohesin subunit precocious dissociation of sisters protein 5 (Pds5) by phosphorylating Sororin, leading to release of acetylated cohesin from chromosome arms and loss of cohesion.

Identifier	Residue	Sequence	Organism
SIGNOR-276118	Ser83	PRRSPRIsFFLEKEN	in vitro
pmid	sentence
23901111	Here we show that the mitotic kinases Aurora B and Cyclin-dependent kinase 1 (Cdk1) destabilize interactions between Sororin and the cohesin subunit precocious dissociation of sisters protein 5 (Pds5) by phosphorylating Sororin, leading to release of acetylated cohesin from chromosome arms and loss of cohesion.

Identifier	Residue	Sequence	Organism
SIGNOR-276121	Thr151	RSYSRLEtLGSASTS	in vitro
pmid	sentence
23901111	Here we show that the mitotic kinases Aurora B and Cyclin-dependent kinase 1 (Cdk1) destabilize interactions between Sororin and the cohesin subunit precocious dissociation of sisters protein 5 (Pds5) by phosphorylating Sororin, leading to release of acetylated cohesin from chromosome arms and loss of cohesion.

Publications:

6

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-95574	Ser13	LPTVLPGsPSKTRGQ	Homo sapiens	HeLa Cell
pmid	sentence
12435275	Given that the dimeric form of tk1 is less active than the tetrameric, we propose that mitotic phosphorylation of serine-13 is of physiological importance, in that it may counteract atp-dependent activation of tk1 by affecting its quaternary structure, thus attenuating its enzymatic function at the g2/m phase.

Identifier	Residue	Sequence	Organism
SIGNOR-120368	Ser13	LPTVLPGsPSKTRGQ	Homo sapiens
pmid	sentence
14697231	Given that the dimeric form of tk1 is less active than the tetrameric, we propose that mitotic phosphorylation of serine-13 is of physiological importance, in that it may counteract atp-dependent activation of tk1 by affecting its quaternary structure, thus attenuating its enzymatic function at the g2/m phase.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-97733	Ser133	APQTQHVsPMRQVEP	Homo sapiens
pmid	sentence
12551973	The sequence flanking ser-133 of ef-1delta completely matches the consensus phosphorylation site for a cellular protein kinase, cdc2, and in vitro kinase assays revealed that purified cdc2 phosphorylates ser-133 of ef-1delta.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-276589	Ser138	SLQLGAVsPGTLTPT
pmid	sentence
26933062	Our evidence suggested that these YAP sites (Ser138, Thr143, and Ser367) were CDK1 phosphorylation sites.\|These data demonstrate that the YAP phosphorylation sites Ser138, Thr143, and Ser367 are important for proper mitosis and cytokinesis.

Identifier	Residue	Sequence	Organism
SIGNOR-279362	Ser289	PPPLAPQsPQGGVMG	Homo sapiens
pmid	sentence
24101154	Specifically, we found that YAP is phosphorylated in vitro and in vivo by the cell cycle kinase CDK1 at T119, S289, and S367 during G2/M phase of the cell cycle.

Identifier	Residue	Sequence	Organism
SIGNOR-279363	Ser367	GTQNPVSsPGMSQEL	Homo sapiens
pmid	sentence
24101154	Specifically, we found that YAP is phosphorylated in vitro and in vivo by the cell cycle kinase CDK1 at T119, S289, and S367 during G2/M phase of the cell cycle.

Identifier	Residue	Sequence
SIGNOR-276587	Ser367	GTQNPVSsPGMSQEL
pmid	sentence
26933062	Our evidence suggested that these YAP sites (Ser138, Thr143, and Ser367) were CDK1 phosphorylation sites.\|These data demonstrate that the YAP phosphorylation sites Ser138, Thr143, and Ser367 are important for proper mitosis and cytokinesis.

Identifier	Residue	Sequence	Organism
SIGNOR-279361	Thr119	AGTAGALtPQHVRAH	Homo sapiens
pmid	sentence
24101154	Specifically, we found that YAP is phosphorylated in vitro and in vivo by the cell cycle kinase CDK1 at T119, S289, and S367 during G2/M phase of the cell cycle.

Identifier	Residue	Sequence
SIGNOR-276588	Thr143	AVSPGTLtPTGVVSG
pmid	sentence
26933062	Our evidence suggested that these YAP sites (Ser138, Thr143, and Ser367) were CDK1 phosphorylation sites.\|These data demonstrate that the YAP phosphorylation sites Ser138, Thr143, and Ser367 are important for proper mitosis and cytokinesis.

Publications:

6

Organism:

, Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-102350	Ser140	AVERVTKsPGETSKP	Homo sapiens
pmid	sentence
12810701	Now, we have found that p47, which mainly localizes to the nucleus during interphase, is phosphorylated on serine-140 by cdc2 at mitosis. The phosphorylated p47 does not bind to golgi membranes.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273435	Ser1456	FKLERERsYELVRSA	Homo sapiens	MDA-MB-231 Cell
pmid	sentence
31776402	Phosphorylation of the histone demethylase KDM5B and regulation of the phenotype of triple negative breast cancer\|Here, we demonstrate that KDM5B is phosphorylated at Ser1456 by the cyclin-dependent kinase 1 (CDK1). Phosphorylation of KDM5B at Ser1456 attenuated the occupancy of KDM5B on the promoters of pluripotency genes.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-173677	Ser154	AKPEPSPsPRITRKS	Homo sapiens
pmid	sentence
21565170	We report that cyclin-dependent kinases (cdks) 1, 2 and 5 can phosphorylate ser154 of human dnmt1 in vitro. Further evidence of phosphorylation of endogenous dnmt1 at position 154 by cdks is also found in 293 cells treated with roscovitine, a specific inhibitor of cdk1, 2 and 5

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-179171	Ser157	LQKAGKLsPVKVQPK	Homo sapiens
pmid	sentence
18574241	Irp2 ser-157 is phosphorylated by cdk1/cyclin b1 during g(2)/m / ser-157 phosphorylation during g(2)/m reduces irp2 rna-binding activity

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-182753	Ser158	FVSHSHIsPIKPTEA	Homo sapiens
pmid	sentence
19066288	We also show that dlg1 is phosphorylated by both cdk1 and cdk2 on ser158 and ser442. These phosphorylated sites together affect the nuclear localisation of the protein, and implicate the role of phosphorylation on ser158 and ser442 in its putative nuclear functions as a tumour suppressor.

Identifier	Residue	Sequence	Organism
SIGNOR-182757	Ser443	FLGQTPAsPARYSPV	Homo sapiens
pmid	sentence
19066288	We also show that dlg1 is phosphorylated by both cdk1 and cdk2 on ser158 and ser442. These phosphorylated sites together affect the nuclear localisation of the protein, and implicate the role of phosphorylation on ser158 and ser442 in its putative nuclear functions as a tumour suppressor.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-279396	Ser159	SGIPDFRsPGSGLYS	Homo sapiens
pmid	sentence
26141949	Posttranscriptionally, SIRT3 enzymatic activity is further enhanced via Thr150/Ser159 phosphorylation by cyclin B1-CDK1, which is also induced by radiation and relocated to mitochondria together with SIRT3.

Identifier	Residue	Sequence	Organism
SIGNOR-279395	Thr150	MVGAGIStPSGIPDF	Homo sapiens
pmid	sentence
26141949	Both SIRT3 T150 and S159 phosphorylated by CDK1 indicates that CDK1-SIRT3 pathway may play a role in the overall mitochondrial protein acetylation involved in mitochondrial homeostasis and apoptosis.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-90451	Ser160	PVRLLGHsPVLRNIT	Homo sapiens
pmid	sentence
12107172	We demonstrate that serine 146 is required for two crucial features of cdc25b1. It is essential for cdc25b1 to function as a mitotic inducer and to prevent cdc25b1 export from the nucleus. We also show that serine 146 is phosphorylated in vitro by cdk1-cyclin b. Serine 146 phosphorylation is proposed to be a key event in the regulation of the cdc25b function

Identifier	Residue	Sequence	Organism
SIGNOR-167641	Ser321	KCQRLFRsPSMPCSV	Homo sapiens
pmid	sentence
20801879	Ser(321) is phosphorylated in mitosis by cdk1. The mitotic phosphorylation of ser(321) acts to maintain full activation of cdc25b by disrupting 14-3-3 binding to ser(323) and enhancing the dephosphorylation of ser(323) to block 14-3-3 binding to this site.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-275605	Ser1616	NSHSPAGsAAISQQD	Homo sapiens	A-549 Cell
pmid	sentence
27991932	Epidermal growth factor (EGF) treatment, and the KrasG12D and EGFRL858R mutations decrease USP24 protein stability via EGF- or CDK1-mediated phosphorylation at Ser1616, Ser2047 and Ser2604.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-275604	Ser2047	QRVSDQNsPVLPKKS	Homo sapiens	A-549 Cell
pmid	sentence
27991932	Epidermal growth factor (EGF) treatment, and the KrasG12D and EGFRL858R mutations decrease USP24 protein stability via EGF- or CDK1-mediated phosphorylation at Ser1616, Ser2047 and Ser2604.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-275603	Ser2604	HLQQGSEsPMMIGEL	Homo sapiens	A-549 Cell
pmid	sentence
27991932	Epidermal growth factor (EGF) treatment, and the KrasG12D and EGFRL858R mutations decrease USP24 protein stability via EGF- or CDK1-mediated phosphorylation at Ser1616, Ser2047 and Ser2604.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-74619	Ser165	LFQLGPPsPVKMPSP	Homo sapiens
pmid	sentence
10656688	Hpttg is phosphorylated by cdc2 at ser165 these results suggest that hpttg is induced by, and may have a role in, regulatory pathways involved in the control of cell proliferation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262700	Ser165	LFQLGPPsPVKMPSP	Homo sapiens	HeLa Cell
pmid	sentence
10656688	HPTTG is phosphorylated by Cdc2 at Ser165. we show that hPTTG is phosphorylated during mitosis. The direct phosphorylation of hPTTG by Cdc2 is interesting in itself since the substrates of this master mitotic kinase are supposed to play important roles in the initiation and progression of mitosis.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-264412	Ser1678	ITSEEERsPAKRGRK	in vitro
pmid	sentence
30685087	Nuclear import of 53BP1 is required for proper localization of 53BP1 and maintenance of genome integrity. 53BP1 has a classical bipartite nuclear localization signal (NLS) of sequence 1666-GKRKLITSEEERSPAKRGRKS-1686. Ser1678 within the 53BP1 NLS can be phosphorylated by CDK1/cyclin B, and a phosphomimetic substitution of Ser1678 with aspartate has been shown to negatively regulate nuclear import of 53BP1.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-64972	Ser168	SEMKYLGsPITTVPK	Homo sapiens
pmid	sentence
10037602	Phosphorylation at thr-48, thr-67, ser-122, thr-130, ser-168 and ser-214 occurs at g2 and g2-m transition and is catalyzed by cdk1. Ser-168 phosphorylation levels are lower than those at the other 5 cdk1 sites. Phosphorylation by cdk1 leads to increased activity.

Identifier	Residue	Sequence	Organism
SIGNOR-36279	Ser168	SEMKYLGsPITTVPK	Homo sapiens
pmid	sentence
8119945	Phosphorylation at thr-48, thr-67, ser-122, thr-130, ser-168 and ser-214 occurs at g2 and g2-m transition and is catalyzed by cdk1. Ser-168 phosphorylation levels are lower than those at the other 5 cdk1 sites. Phosphorylation by cdk1 leads to increased activity.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-261959	Ser181	LKATVTPsPVKGKGK	in vitro
pmid	sentence
12413487	putative phosphorylation site for Cdk1 is present in the DNA-binding domain peptide. This site, corresponding to Ser 181 in the NUCKS primary structure, is phosphorylated in vitro by Cdk1 with a Km of approximately 35 μM [7]. Phosphorylation of Ser 181 in the synthetic, DNA-binding domain peptide reduces its affinity for DNA-by 100%.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-259830	Ser185	NRHSPSWsPDGRRRQ	Homo sapiens
pmid	sentence
20890132	In this study, we show that Nlp can be phosphorylated by cell cycle protein kinase Cdc2/cyclin B1. The phosphorylation sites of Nlp are mapped at Ser185 and Ser589. Interestingly, the Cdc2/cyclin B1 phosphorylation site Ser185 of Nlp is required for its recognition by PLK1, which enable Nlp depart from centrosomes to allow the establishment of a mitotic scaffold at the onset of mitosis .

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-103535	Ser187	MDCLTFGsPVLMRHL	Homo sapiens	HEK-293 Cell
pmid	sentence
12853968	Phosphorylation of human fen1 by cyclin-dependent kinase modulates its role in replication fork regulation.As a functional consequence of phosphorylation by cdk1-cyclin a in vitro, endo- and exonuclease activities of fen1 are reduced whereas its dna binding is not affected.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-262699	Ser1881	SPPSGLWsPAYASH	in vitro
pmid	sentence
8672508	In vitro phosphorylation of GST fusion protein containing the carboxyl-terminal domain of gp210 by cyclin B-p34cdc2 protein kinase generates a phosphopeptide that comigrates with a mitosis-specific phosphopeptide. Ser1880 Is the Mitotic Phosphorylation Site of Gp210.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262729	Ser189	LLGVDLGsMDEEEEI	Mus musculus	NIH-3T3 Cell
pmid	sentence
14754904	Inactivation and phosphorylation mimicking of potential phosphorylation sites in mSTI1 altered the nuclear translocation. Mimicking of phosphorylation at the mSTI1 CKII phosphorylation site (S189E) promoted nuclear localization of mSTI1-EGFP. Mimicking phosphorylation at the cdc2 kinase phosphorylation site (T198E) promoted cytoplasmic localization of mSTI1-EGFP at the G1/S-phase transition,whereas removal of this site (T198A) promoted the nuclear localization of mSTI1-EGFP under the same conditions.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262727	Thr198	DEEEEIAtPPPPPPP	Mus musculus	NIH-3T3 Cell
pmid	sentence
14754904	Inactivation and phosphorylation mimicking of potential phosphorylation sites in mSTI1 altered the nuclear translocation. Mimicking of phosphorylation at the mSTI1 CKII phosphorylation site (S189E) promoted nuclear localization of mSTI1-EGFP. Mimicking phosphorylation at the cdc2 kinase phosphorylation site (T198E) promoted cytoplasmic localization of mSTI1-EGFP at the G1/S-phase transition,whereas removal of this site (T198A) promoted the nuclear localization of mSTI1-EGFP under the same conditions. A lower level of phosphorylation was observed for the double mutant, suggesting that T332 might also be phosphorylated by cdc2 kinase.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262728	Thr332	KSLAEHRtPDVLKKC	Mus musculus	NIH-3T3 Cell
pmid	sentence
14754904	Inactivation and phosphorylation mimicking of potential phosphorylation sites in mSTI1 altered the nuclear translocation. Mimicking of phosphorylation at the mSTI1 CKII phosphorylation site (S189E) promoted nuclear localization of mSTI1-EGFP. Mimicking phosphorylation at the cdc2 kinase phosphorylation site (T198E) promoted cytoplasmic localization of mSTI1-EGFP at the G1/S-phase transition,whereas removal of this site (T198A) promoted the nuclear localization of mSTI1-EGFP under the same conditions. A lower level of phosphorylation was observed for the double mutant, suggesting that T332 might also be phosphorylated by cdc2 kinase.

Publications:

3

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-64312	Ser20	DPQQLQLsPLKGLSL	Homo sapiens
pmid	sentence
9990288	Ribonucleotide reductase r2 protein is phosphorylated at serine-20 by p34cdc2 kinase. comparison of ribonucleotide reductase activities between wild type and mutated forms of the r2 proteins suggested that mutation at serine-20 did not significantly affect enzyme activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-121601	Ser200	YSGDSDAsSPRSNCS	Homo sapiens
pmid	sentence
14749395	Myod is phosphorylated on ser5 and ser200 by cyclin b-cdc2, resulting in a decrease of its stability and down-regulation of both myod and p21.

Identifier	Residue	Sequence	Organism
SIGNOR-176505	Ser200	YSGDSDAsSPRSNCS	Homo sapiens
pmid	sentence
21902831	Phosphorylation of myod at s200 is common to other cdks, such as the mitotic cyclin b/cdk1, which may prevent inappropriate myod accumulation during mitosis.

Identifier	Residue	Sequence	Organism
SIGNOR-121605	Ser5	sPPLRDVD	Homo sapiens
pmid	sentence
14749395	Myod is phosphorylated on ser5 and ser200 by cyclin b-cdc2, resulting in a decrease of its stability and down-regulation of both myod and p21.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-279014	Ser202	LLSQLYHsPARRFGG	Homo sapiens
pmid	sentence
22936947	Cdk1 inhibition promoted a cytoplasmic accumulation of HuR, while a predominately nuclear localization of HuR was observed under conditions of high Cdk1 activity.\|Kim et al. further showed that Cdk1-dependent Ser-202 phosphorylation of HuR was essential for 14-3-3\u03b8 binding to HuR.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-268297	Ser208	PASTPTYsPAPTQPA
pmid	sentence
20171170	We identified the Ser208 residue of Aki1 as a cyclin B1–Cdk1 phosphorylation site. Furthermore, cyclin B1–Cdk1 inhibitor treatment was shown to attenuate the level of Aki1 in complex with Scc1, suggesting that Aki1 phosphorylation by cyclin B1–Cdk1 contributes to Aki1–Scc1 complex formation.

Publications:

1

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-29462	Ser209	QAASNFKsPVKTIR	Homo sapiens	Lymphoma Cell
pmid	sentence
7578274	In cells, the casein kinase ii beta-subunit is phosphorylated at an autophosphorylation site and at a site (ser-209) that is maximally phosphorylated in mitotic cells. These studies provide strong biochemical evidence that p34cdc2 is the enzyme that phosphorylates ser-209 on the beta-subunit of ckii in mitotic cells.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-169318	Ser21	TPPSTALsPGKMSEA	Homo sapiens
pmid	sentence
21059642	Phosphorylation of runx1 on ser-303 by cdks leads its ubiquitin-mediated degradation during g2/m (19). We developed additional evidence that cdks phosphorylate ser-303 and found that ser-48 and ser-424 are also substrates of cdk1/cyclin b and cdk6/cyclin d3. Moreover, we demonstrated that phosphorylation of ser-48, ser-303, and ser-424 strengthens the ability of runx1 to activate transcription and to stimulate proliferation of the ba/f3 hematopoietic cell line (20).

Identifier	Residue	Sequence	Organism
SIGNOR-138908	Ser249	DTRQIQPsPPWSYDQ	Homo sapiens
pmid	sentence
16046550	We have identified four phosphorylation sites on aml1c that are necessary for transcriptional activity of aml1c in k562 and 293t cells (27).4 mutation of these four sites (serine 276, serine 293, serine 303, and threonine 300) to alanine abolishes transcriptional activation, whereas mutation of these sites to aspartic acid (which mimics phosphorylation) results in a hyperactive protein.

Identifier	Residue	Sequence	Organism
SIGNOR-138912	Ser266	QYLGSIAsPSVHPAT	Homo sapiens
pmid	sentence
16046550	Phosphorylation of ser-48, ser-303, and ser-424 by cyclin-dependent kinases (cdks) increases runx1 trans-activation activity without perturbing p300 interaction.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-169322	Ser397	SMVGGERsPPRILPP	Homo sapiens	HEK-293 Cell
pmid	sentence
21059642	Phosphorylation of runx1 on ser-303 by cdks leads its ubiquitin-mediated degradation during g2/m (19). We developed additional evidence that cdks phosphorylate ser-303 and found that ser-48 and ser-424 are also substrates of cdk1/cyclin b and cdk6/cyclin d3. Moreover, we demonstrated that phosphorylation of ser-48, ser-303, and ser-424 strengthens the ability of runx1 to activate transcription and to stimulate proliferation of the ba/f3 hematopoietic cell line (20).

Identifier	Residue	Sequence	Organism
SIGNOR-138920	Thr273	SPSVHPAtPISPGRA	Homo sapiens
pmid	sentence
16046550	Phosphorylation of ser-48, ser-303, and ser-424 by cyclin-dependent kinases (cdks) increases runx1 trans-activation activity without perturbing p300 interaction.

Publications:

5

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-264421	Ser216	VPNDYMTsPARLGSQ	Homo sapiens	HeLa Cell
pmid	sentence
21900237	We identified serine 216 of Abi1 as a target of CDK1/cyclin B kinase that is phosphorylated in cells at the onset of mitosis.\|Bcr-Abl-induced actin polymerization requires the Abi1 pathway, as the blockade of the signal transduction from Bcr-Abl to Abi1 abolishes the F-actin assembly\|serine phosphorylation of Abi1 by CDK1/cyclin B serves as a cell cycle-dependent regulatory mechanism that inhibits actin assembly

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-181310	Ser22	QASSTPLsPTRITRL	Homo sapiens
pmid	sentence
18815303	Phosphorylation by mitotic cdc2 kinase at ser-22, ser-390, and ser-392 residues on lamin a/c, or by protein kinase c (pkc) during apoptosis, leads to the depolymerization of lamin (disassembly of the nuclear lamina), which may lead to their release from the inm

Identifier	Residue	Sequence	Organism
SIGNOR-181314	Ser390	EEERLRLsPSPTSQR	Homo sapiens
pmid	sentence
18815303	Phosphorylation by mitotic cdc2 kinase at ser-22, ser-390, and ser-392 residues on lamin a/c, or by protein kinase c (pkc) during apoptosis, leads to the depolymerization of lamin (disassembly of the nuclear lamina), which may lead to their release from the inm

Identifier	Residue	Sequence	Organism
SIGNOR-181318	Ser392	ERLRLSPsPTSQRSR	Homo sapiens
pmid	sentence
18815303	Phosphorylation by mitotic cdc2 kinase at ser-22, ser-390, and ser-392 residues on lamin a/c, or by protein kinase c (pkc) during apoptosis, leads to the depolymerization of lamin (disassembly of the nuclear lamina), which may lead to their release from the inm

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-188061	Ser221	KVAAETQsPSLFGST	Homo sapiens
pmid	sentence
19767751	These results suggest that both ERK and Cdk1 directly phosphorylate Nup50 at Ser221 in intact cells\|Notably, erk phosphorylation of the fg repeat region of nup50 reduced its affinity for importin-beta family proteins, importin-beta and transportin.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-259118	Ser2246	SSSVHASerPLASSP	in vitro
pmid	sentence
26051540	Cdk1 phosphorylates conserved sites within RanBP2 and activates BicD2 binding and early dynein recruitment.

Identifier	Residue	Sequence	Organism
SIGNOR-259119	Ser2251	ASPLASSerPVRKNL	in vitro
pmid	sentence
26051540	Cdk1 phosphorylates conserved sites within RanBP2 and activates BicD2 binding and early dynein recruitment.

Identifier	Residue	Sequence	Organism
SIGNOR-259120	Ser2276	SFKSALSerPSKSPA	in vitro
pmid	sentence
26051540	Cdk1 phosphorylates conserved sites within RanBP2 and activates BicD2 binding and early dynein recruitment.

Identifier	Residue	Sequence	Organism
SIGNOR-259121	Ser2280	LSPSKSerPAKLN	in vitro
pmid	sentence
26051540	Cdk1 phosphorylates conserved sites within RanBP2 and activates BicD2 binding and early dynein recruitment.

Identifier	Residue	Sequence	Organism
SIGNOR-259117	Thr2153	LDIPLQThrPHKLVD	in vitro
pmid	sentence
26051540	Cdk1 phosphorylates conserved sites within RanBP2 and activates BicD2 binding and early dynein recruitment.

Publications:

5

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-16971	Ser23	GAGGYTQsPGGFGSP	Homo sapiens
pmid	sentence
1318195	Cdc2 family kinases phosphorylate a human cell dna replication factor, rpa, and activate dna replication. therefore, the serines on rpa p34 that were necessary for phosphorylation by cdc2 kinase were also necessary for phosphorylation in the cell

Identifier	Residue	Sequence	Organism
SIGNOR-16975	Ser29	QSPGGFGsPAPSQAE	Homo sapiens
pmid	sentence
1318195	Cdc2 family kinases phosphorylate a human cell dna replication factor, rpa, and activate dna replication. therefore, the serines on rpa p34 that were necessary for phosphorylation by cdc2 kinase were also necessary for phosphorylation in the cell

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-274073	Ser242	IPNGFGTsPLTPSAR	in vitro
pmid	sentence
12556484	In this case, only NudelS2 and NudelS5 were phosphorylated. Therefore, T219, S242, and T245 of Nudel were phosphorylation sites of Cdc2 in vitro. In contrast, Erk2 only phosphorylated T219 and T245. These two sites, with surrounding sequences such as PATP from residues 217 to 220 and PLTP from 243 to 246, respectively, are indeed typical MAPK sites

Identifier	Residue	Sequence	Organism
SIGNOR-274074	Thr219	ASLSLPAtPVGKGTE	in vitro
pmid	sentence
12556484	In this case, only NudelS2 and NudelS5 were phosphorylated. Therefore, T219, S242, and T245 of Nudel were phosphorylation sites of Cdc2 in vitro. In contrast, Erk2 only phosphorylated T219 and T245. These two sites, with surrounding sequences such as PATP from residues 217 to 220 and PLTP from 243 to 246, respectively, are indeed typical MAPK sites

Identifier	Residue	Sequence	Organism
SIGNOR-274072	Thr245	GFGTSPLtPSARISA	in vitro
pmid	sentence
12556484	In this case, only NudelS2 and NudelS5 were phosphorylated. Therefore, T219, S242, and T245 of Nudel were phosphorylation sites of Cdc2 in vitro. In contrast, Erk2 only phosphorylated T219 and T245. These two sites, with surrounding sequences such as PATP from residues 217 to 220 and PLTP from 243 to 246, respectively, are indeed typical MAPK sites

Publications:

3

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-178202	Ser249	EGGKSGKsPRRRAAS	Homo sapiens	Prostate Gland Cancer Cell
pmid	sentence
18408765	Overexpression of cdk1 inhibits the transcriptional activity of foxo1 in pca cells through s249 phosphorylation on foxo1.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252890	Ser249	EGGKSGKsPRRRAAS	Homo sapiens	Prostate Gland Cancer Cell
pmid	sentence
18408765	Overexpression of cdk1 inhibits the transcriptional activity of foxo1 in pca cells through s249 phosphorylation on foxo1.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-21548	Ser249	AVIPINGsPRTPRRG	Homo sapiens
pmid	sentence
1756735	The retinoblastoma gene product (prb) is a nuclear phosphoprotein that is thought to play a key role in the negative regulation of cellular proliferation. The active form of prb is underphosphorylated. Using synthetic peptides corresponding to potential cdc2 phosphorylation sites, we have developed a strategy which has allowed the identification of five sites. S249, t252, t373, s807 and s811 are phosphorylated in vivo, and in each case these sites correspond closely to the consensus sequence for phosphorylation by p34cdc2.

Identifier	Residue	Sequence	Organism
SIGNOR-21552	Ser807	PGGNIYIsPLKSPYK	Homo sapiens
pmid	sentence
1756735	The retinoblastoma gene product (prb) is a nuclear phosphoprotein that is thought to play a key role in the negative regulation of cellular proliferation. The active form of prb is underphosphorylated. Using synthetic peptides corresponding to potential cdc2 phosphorylation sites, we have developed a strategy which has allowed the identification of five sites. S249, t252, t373, s807 and s811 are phosphorylated in vivo, and in each case these sites correspond closely to the consensus sequence for phosphorylation by p34cdc2.

Identifier	Residue	Sequence	Organism
SIGNOR-21556	Ser811	IYISPLKsPYKISEG	Homo sapiens
pmid	sentence
1756735	The retinoblastoma gene product (prb) is a nuclear phosphoprotein that is thought to play a key role in the negative regulation of cellular proliferation. The active form of prb is underphosphorylated. Using synthetic peptides corresponding to potential cdc2 phosphorylation sites, we have developed a strategy which has allowed the identification of five sites. S249, t252, t373, s807 and s811 are phosphorylated in vivo, and in each case these sites correspond closely to the consensus sequence for phosphorylation by p34cdc2.

Identifier	Residue	Sequence	Organism
SIGNOR-21560	Thr252	PINGSPRtPRRGQNR	Homo sapiens
pmid	sentence
1756735	The retinoblastoma gene product (prb) is a nuclear phosphoprotein that is thought to play a key role in the negative regulation of cellular proliferation. The active form of prb is underphosphorylated. Using synthetic peptides corresponding to potential cdc2 phosphorylation sites, we have developed a strategy which has allowed the identification of five sites. S249, t252, t373, s807 and s811 are phosphorylated in vivo, and in each case these sites correspond closely to the consensus sequence for phosphorylation by p34cdc2.

Identifier	Residue	Sequence	Organism
SIGNOR-21564	Thr373	VNVIPPHtPVRTVMN	Homo sapiens
pmid	sentence
1756735	The retinoblastoma gene product (prb) is a nuclear phosphoprotein that is thought to play a key role in the negative regulation of cellular proliferation. The active form of prb is underphosphorylated. Using synthetic peptides corresponding to potential cdc2 phosphorylation sites, we have developed a strategy which has allowed the identification of five sites. S249, t252, t373, s807 and s811 are phosphorylated in vivo, and in each case these sites correspond closely to the consensus sequence for phosphorylation by p34cdc2.

Publications:

5

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-279803	Ser25	QAFELILsPRSKESV	Homo sapiens
pmid	sentence
8125092

Identifier	Residue	Sequence	Organism
SIGNOR-279802	Ser38	SVPEFPLsPPKKKDL	Homo sapiens
pmid	sentence
8125092

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277375	Ser251	EVSIRVGsPQPSSSG	Homo sapiens	HEK-293T Cell
pmid	sentence
29229926	During S/G2 phases, CDK1 and CDK2 (CDK1/2) phosphorylate RECQL4 on serines 89 and 251, enhancing MRE11/RECQL4 interaction and RECQL4 recruitment to DSBs.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-187876	Ser251	MIQFAINsTERKRMT	Homo sapiens
pmid	sentence
19737929	A conserved phosphorylation site within the forkhead domain of foxm1b is required for its activation by cyclin-cdk1the phosphorylation at ser-251 is critical for the activation of foxm1.

Identifier	Residue	Sequence	Organism
SIGNOR-187880	Thr611	ETLPISStPSKSVLP	Homo sapiens
pmid	sentence
19737929	A conserved phosphorylation site within the forkhead domain of foxm1b is required for its activation by cyclin-cdk1further analysis reveals that the leu-641 residue within an lxl motif is required for the recruitment of the cyclin-cdk complex, and the thr-596 residue is a critical cdk1 phosphorylation site within the activation domain of foxm1b. Cdk-dependent phosphorylation stimulates the foxm1b transcriptional activity

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-273591	Ser254	PAPQSQLsPNAKEFV	in vitro
pmid	sentence
32404348	Taken together, these observations strongly support the notion that several different CDK-cyclin complexes are involved in the phosphorylation of Tob2 at S254.A more detailed regulatory context of Tob2 phosphorylation at S254 is provided by our findings from mass-spec and in vitro kinase analyses that suggest connections to PP2B and PP2C phosphatases and CDK-cyclin complexes, particularly CDK1, CDK2, and CDK4 (Table 1; Supplemental Table S2).One possibility is that the phosphorylation of S254 helps stabilize the interaction of Tob2 with the Ccr4–Not complex, which could contribute to Tob2's ability to recruit the entire Ccr4–Not complex and thus further enhances deadenylation.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence
SIGNOR-275608	Ser2547	YEGSEEVsPPQTKDQ
pmid	sentence
32152317	Here, we find that CDC14B antagonizes CDK1-mediated activating mitotic phosphorylation of the deubiquitinase USP9X at serine residue 2563, which we show to be essential for USP9X to mediate mitotic survival. Starting from an unbiased proteome-wide screening approach, we specify Wilms' tumor protein 1 (WT1) as the relevant substrate that becomes deubiquitylated and stabilized by serine 2563-phosphorylated USP9X in mitosis.

Publications:

1

Identifier	Residue	Sequence	Organism
SIGNOR-116321	Ser258	TSCASLDsPGRIKRK	Homo sapiens
pmid	sentence
11931757	Horc1p contains three (s/t)px(k/r) consensus sites for cdk phosphorylation (ser258, ser273, and thr375). These data combined strongly suggest that skp2 promotes horc1p turnover and that the n-terminal domain of horc1p, containing most of the phosphorylation sites and overlapping with one of the skp2-interacting domains, is a regulatory element for horc1p stability.

Identifier	Residue	Sequence	Organism
SIGNOR-116325	Ser273	VAFSEITsPSKRSQP	Homo sapiens
pmid	sentence
11931757	Horc1p contains three (s/t)px(k/r) consensus sites for cdk phosphorylation (ser258, ser273, and thr375). These data combined strongly suggest that skp2 promotes horc1p turnover and that the n-terminal domain of horc1p, containing most of the phosphorylation sites and overlapping with one of the skp2-interacting domains, is a regulatory element for horc1p stability.

Identifier	Residue	Sequence	Organism
SIGNOR-116329	Thr375	AQNEATStPHRIRRK	Homo sapiens
pmid	sentence
11931757	Horc1p contains three (s/t)px(k/r) consensus sites for cdk phosphorylation (ser258, ser273, and thr375). These data combined strongly suggest that skp2 promotes horc1p turnover and that the n-terminal domain of horc1p, containing most of the phosphorylation sites and overlapping with one of the skp2-interacting domains, is a regulatory element for horc1p stability.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-100903	Ser259	KVSNLQVsPKSEDIS	Homo sapiens
pmid	sentence
12719431	Mitotic and stress-induced phosphorylation of HsPI3K-C2alpha targets the protein for degradation. Stress-dependent and mitotic phosphorylation of hspik3-c2alpha occurs on the same serine residue (ser259) within a recognition motif for proline-directed kinases. Mitotic phosphorylation of hspik3-c2alpha can be attributed to cdc2 activity, and stress-induced phosphorylation of hspik3-c2alpha is mediated by jnk/sapk

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277605	Ser261	PSGMGTSsPARRGSA	Homo sapiens	HEK-293 Cell
pmid	sentence
36104103	We demonstrated that cyclin-dependent kinase 1-mediated phosphorylation of Ser261 residue primes PD-1 protein nucleus translocation and binding with FBW7.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276346	Ser271	QGVVMAAsPGSLHSP	Homo sapiens	Prostate Cancer Cell Line
pmid	sentence
21767532	In this report data is presented demonstrating that ICER is phosphorylated by the mitotic kinase cdk1. Phosphorylation of ICER on a discrete residue targeted ICER to be monoubiquitinated. Different from unphosphorylated, phosphorylated and polyubiquitinated ICER, monoubiquitinated ICER was found to be cytosolic. Taken together, these results hinted on a mechanism for the observed abnormal subcellular localization of ICER in human prostate tumors.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-169012	Ser272	RSRLTPVsPESSSTE	Homo sapiens
pmid	sentence
20974803	Here we show that cdk1 phosphorylates p62 in vitro and in vivo at t269 and s272, which is necessary for the maintenance of appropriate cyclin b1 levels and the levels of cdk1 activity necessary to allow cells to properly enter and exit mitosis.

Identifier	Residue	Sequence	Organism
SIGNOR-169016	Thr269	GGKRSRLtPVSPESS	Homo sapiens
pmid	sentence
20974803	Here we show that cdk1 phosphorylates p62 in vitro and in vivo at t269 and s272, which is necessary for the maintenance of appropriate cyclin b1 levels and the levels of cdk1 activity necessary to allow cells to properly enter and exit mitosis.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262840	Ser274	DPLPGPGsPSHSAPD	Rattus norvegicus	NRK Cell
pmid	sentence
15834132	Here we show that GRASP65 is phosphorylated on serine 277 in interphase cells, and this is strongly enhanced in response to the addition of serum or epidermal growth factor. This is directly mediated by ERK suggesting that GRASP65 has some role in growth factor signal transduction. Phosphorylation of Ser-277 is also dramatically increased during mitosis, however this is mediated by Cdk1 and not by ERK. These results argue against Ser-277 phosphorylation alone causing the dissolution of GRASP65 oligomers and cisternal unstacking, although it may make a significant contribution to these events.

Publications:

1

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism
SIGNOR-149972	Ser276	VHPATPIsPGRASGM	Homo sapiens
pmid	sentence
17015473	Aml1/runx1 phosphorylation by cyclin-dependent kinases regulates the degradation of aml1/runx1 by the anaphase-promoting complex.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-138916	Ser276	VHPATPIsPGRASGM	Homo sapiens
pmid	sentence
16046550	Phosphorylation of ser-48, ser-303, and ser-424 by cyclin-dependent kinases (cdks) increases runx1 trans-activation activity without perturbing p300 interaction.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, IDH-TET in AML, KIT in AML

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-101043	Ser277	SHSQDLGsPERHQPV	Homo sapiens	HeLa Cell
pmid	sentence
12734188	Here we present evidence that thr292 of hrad9 is subject to cdc2-dependent phosphorylation in mitosis. Furthermore, our data are also consistent with four other hrad9 phosphorylation sites (ser277, ser328, ser336, and thr355) being regulated in part by cdc2. We also identify ser387 as a novel site of hrad9 constitutive phosphorylation and show that phosphorylation at ser387 is a prerequisite for one form of dna damage-induced hyperphosphorylation of hrad9.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-101047	Ser328	VLPSISLsPGPQPPK	Homo sapiens	HeLa Cell
pmid	sentence
12734188	Here we present evidence that thr292 of hrad9 is subject to cdc2-dependent phosphorylation in mitosis. Furthermore, our data are also consistent with four other hrad9 phosphorylation sites (ser277, ser328, ser336, and thr355) being regulated in part by cdc2. We also identify ser387 as a novel site of hrad9 constitutive phosphorylation and show that phosphorylation at ser387 is a prerequisite for one form of dna damage-induced hyperphosphorylation of hrad9.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-101051	Ser336	PGPQPPKsPGPHSEE	Homo sapiens	HeLa Cell
pmid	sentence
12734188	Here we present evidence that thr292 of hrad9 is subject to cdc2-dependent phosphorylation in mitosis. Furthermore, our data are also consistent with four other hrad9 phosphorylation sites (ser277, ser328, ser336, and thr355) being regulated in part by cdc2. We also identify ser387 as a novel site of hrad9 constitutive phosphorylation and show that phosphorylation at ser387 is a prerequisite for one form of dna damage-induced hyperphosphorylation of hrad9.

Identifier	Residue	Sequence	Organism
SIGNOR-101055	Thr292	PQLQAHStPHPDDFA	Homo sapiens
pmid	sentence
12734188	Here we present evidence that thr292 of hrad9 is subject to cdc2-dependent phosphorylation in mitosis. Furthermore, our data are also consistent with four other hrad9 phosphorylation sites (ser277, ser328, ser336, and thr355) being regulated in part by cdc2. We also identify ser387 as a novel site of hrad9 constitutive phosphorylation and show that phosphorylation at ser387 is a prerequisite for one form of dna damage-induced hyperphosphorylation of hrad9.

Identifier	Residue	Sequence	Organism
SIGNOR-101059	Thr355	EPSTVPGtPPPKKFR	Homo sapiens
pmid	sentence
12734188	Here we present evidence that thr292 of hrad9 is subject to cdc2-dependent phosphorylation in mitosis. Furthermore, our data are also consistent with four other hrad9 phosphorylation sites (ser277, ser328, ser336, and thr355) being regulated in part by cdc2. We also identify ser387 as a novel site of hrad9 constitutive phosphorylation and show that phosphorylation at ser387 is a prerequisite for one form of dna damage-induced hyperphosphorylation of hrad9.

Publications:

5

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-275979	Ser277	ASPGSLHsPQQLAEE	Mus musculus	AtT-20 Cell
pmid	sentence
11466319	The MAPKs extracellular signal-regulated kinases 1 and 2 physically interact with ICER and mediated the phosphorylation of ICER on a critical serine residue (Ser-41). A mutant form of ICER in which Ser-41 was substituted by alanine had a half-life 4-5 h longer than its wild-type counterpart. This alteration in stability was due to the inability of the Ser-41-mutant ICER to be efficiently ubiquitinated and degraded via the ubiquitin-proteasome pathway.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-278305	Ser280	LAEAALEsPRPALVR	Homo sapiens
pmid	sentence
20937695	During the early stages of mitosis in HeLa cells, Cdc2 phosphorylates EBP50 on serine residues 280 and 302.\|Phosphorylation by Cdc2 inhibits EBP50's role in forming microvilli in interphase but not mitotic cells. (A) Results from scoring JEG-3 cells for the presence of microvilli; error bars indicate mean \u00b1 SD. (B) Representative images from the microvillar rescue assay.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-175071	Ser286	TSGGVSEsPSGFSKH	Homo sapiens
pmid	sentence
21765472	Chk1 itself is also subject to cdk-mediated phosphorylation at serines 286 and 301 (s286 and 301). We show that chk1 s301 phosphorylation increases as cells progress through s and g2 and that both cdk1 and cdk2 are likely to contribute to this modification in vivo. We also find that substitution of s286 and s301 with non-phosphorylatable alanine residues strongly attenuates dna damage-induced chk1 activation and g2 checkpoint proficiency

Identifier	Residue	Sequence	Organism
SIGNOR-175075	Ser301	IQSNLDFsPVNSASS	Homo sapiens
pmid	sentence
21765472	Chk1 itself is also subject to cdk-mediated phosphorylation at serines 286 and 301 (s286 and 301). We show that chk1 s301 phosphorylation increases as cells progress through s and g2 and that both cdk1 and cdk2 are likely to contribute to this modification in vivo. We also find that substitution of s286 and s301 with non-phosphorylatable alanine residues strongly attenuates dna damage-induced chk1 activation and g2 checkpoint proficiency

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-275591	Ser29	WLKDQELsPREPVLP
pmid	sentence
24746669	Here, we show that a fraction of cyclin B1/Cdk1 proteins localizes to the matrix of mitochondria and phosphorylates a cluster of mitochondrial proteins, including the complex I (CI) subunits in the respiratory chain. Cyclin B1/Cdk1-mediated CI phosphorylation enhances CI activity, whereas deficiency of such phosphorylation in each of the relevant CI subunits results in impairment of CI function.\|These results were confirmed by generating phosphorylation defective forms of the five CI subunits through substitutions of S/T residues with Alanine (A) on either Cdk1 optimal or minimal consensus motifs (T383 on NDUFV1, S105 on NDUFV3, S364 on NDUFS2, S55/S29/T5 on NDUFB6, and T142/T120 on NDUFA12). The mutation of Cdk1 consensus motifs severely diminished their phosphorylation

Identifier	Residue	Sequence
SIGNOR-275590	Ser55	NKFLENKsPWRKMVH
pmid	sentence
24746669	Here, we show that a fraction of cyclin B1/Cdk1 proteins localizes to the matrix of mitochondria and phosphorylates a cluster of mitochondrial proteins, including the complex I (CI) subunits in the respiratory chain. Cyclin B1/Cdk1-mediated CI phosphorylation enhances CI activity, whereas deficiency of such phosphorylation in each of the relevant CI subunits results in impairment of CI function.\|These results were confirmed by generating phosphorylation defective forms of the five CI subunits through substitutions of S/T residues with Alanine (A) on either Cdk1 optimal or minimal consensus motifs (T383 on NDUFV1, S105 on NDUFV3, S364 on NDUFS2, S55/S29/T5 on NDUFB6, and T142/T120 on NDUFA12). The mutation of Cdk1 consensus motifs severely diminished their phosphorylation

Identifier	Residue	Sequence
SIGNOR-275589	Thr5	tPDEKLRL
pmid	sentence
24746669	Here, we show that a fraction of cyclin B1/Cdk1 proteins localizes to the matrix of mitochondria and phosphorylates a cluster of mitochondrial proteins, including the complex I (CI) subunits in the respiratory chain. Cyclin B1/Cdk1-mediated CI phosphorylation enhances CI activity, whereas deficiency of such phosphorylation in each of the relevant CI subunits results in impairment of CI function.\|These results were confirmed by generating phosphorylation defective forms of the five CI subunits through substitutions of S/T residues with Alanine (A) on either Cdk1 optimal or minimal consensus motifs (T383 on NDUFV1, S105 on NDUFV3, S364 on NDUFS2, S55/S29/T5 on NDUFB6, and T142/T120 on NDUFA12). The mutation of Cdk1 consensus motifs severely diminished their phosphorylation

Publications:

3

Identifier	Residue	Sequence	Organism
SIGNOR-279446	Ser3	sPEREAEA	Homo sapiens
pmid	sentence
34286694	We found that recombinant CHMP7 could be directly phosphorylated by CDK1/CCNB1 in vitro and that CDK1-phosphorylation reduced the capacity of CHMP7 to sediment (Figure 4A and B).\|We identified direct CDK1 phosphorylation of CHMP7 at Ser3 and Ser441 as a suppressor of both CHMP7\u2019s ability to interact with LEM2 and its ability to assemble, as judged by sedimentation assays.

Identifier	Residue	Sequence	Organism
SIGNOR-279445	Ser441	GLVPSSKsPKRQLEP	Homo sapiens
pmid	sentence
34286694	We found that recombinant CHMP7 could be directly phosphorylated by CDK1/CCNB1 in vitro and that CDK1-phosphorylation reduced the capacity of CHMP7 to sediment (Figure 4A and B).\|We identified direct CDK1 phosphorylation of CHMP7 at Ser3 and Ser441 as a suppressor of both CHMP7\u2019s ability to interact with LEM2 and its ability to assemble, as judged by sedimentation assays.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-123467	Ser304	LSPAFDHsPNKIMTE	Homo sapiens
pmid	sentence
15030318	Our studies identify ser-304 as a major phosphorylation site in human tcptp, and the tc45 variant as a novel mitotic cdk substrate.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-276526	Ser305	MKRKRGGsPAVTLLI
pmid	sentence
32351706	The major mitotic kinase CDK1-cyclin B complex phosphorylates human cGAS at S305 or mouse cGAS at S291, which inhibits its ability to synthesize cGAMP upon mitotic entry.

Publications:

1

Identifier	Residue	Sequence	Organism
SIGNOR-278331	Ser31	FPLGSPLsSPVFPRA	Homo sapiens
pmid	sentence
32042098	In line with this, we found that in Drp/MC mice desmin was hyperphosphorylated in Ser-31 by a hyperactivated Cdk-1.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-276423	Ser313	ATSDTLEsPPKIIPK	in vitro
pmid	sentence
23116119	In this study, we show that Ser313 phosphorylation in USP1 is required for its interaction with UAF1 and for the stimulation of USP1's activity. We further demonstrated that CDK1 is responsible for Ser313 phosphorylation, and protein phosphatase treatment of USP1 can lead to inactivation of USP1/UAF1.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-84256	Ser315	LPNNTSSsPQPKKKP	Homo sapiens
pmid	sentence
24173284	The N-terminus of E2F1 can interact directly with a region towards the C-terminus of p53, resulting in increased nuclear retention of p53 and p53-mediated transcription and apoptosis. This is inhibited by competition between p53 and cyclin A at the binding site within E2F19,10. The interaction between p53 and E2F1 is enhanced by phosphorylation of p53 on Ser315, a residue within the E2F1 binding region that is phosphorylated by cell cycle kinases such as cdk1, cdk2, cdk9 and Aurora kinase A

Identifier	Residue	Sequence	Organism
SIGNOR-167779	Ser315	LPNNTSSsPQPKKKP	Homo sapiens
pmid	sentence
24173284	The N-terminus of E2F1 can interact directly with a region towards the C-terminus of p53, resulting in increased nuclear retention of p53 and p53-mediated transcription and apoptosis. This is inhibited by competition between p53 and cyclin A at the binding site within E2F19,10. The interaction between p53 and E2F1 is enhanced by phosphorylation of p53 on Ser315, a residue within the E2F1 binding region that is phosphorylated by cell cycle kinases such as cdk1, cdk2, cdk9 and Aurora kinase A

Publications:

2

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-36022	Ser332	TDSATIVsPPPSSPP	Homo sapiens
pmid	sentence
8087847	Association of e2f with rb inhibits its transactivation potential. phosphorylation of e2f-1 on serine residues 332 and 337 prevented its interaction with rbthese residues were phosphorylated in vivo and by p34cdc2 kinase in vitro.

Identifier	Residue	Sequence	Organism
SIGNOR-36026	Ser337	IVSPPPSsPPSSLTT	Homo sapiens
pmid	sentence
8087847	Association of e2f with rb inhibits its transactivation potential. phosphorylation of e2f-1 on serine residues 332 and 337 prevented its interaction with rbthese residues were phosphorylated in vivo and by p34cdc2 kinase in vitro.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-263100	Ser334	FLLLAGLsLRGQGNF	Homo sapiens
pmid	sentence
25482198	Here, we show that SUN1, located in the INM, undergoes mitosis-specific phosphorylation on at least 3 sites within its nucleoplasmic N-terminus. We further identify Cdk1 as the kinase responsible for serine 48 and 333 phosphorylation, while serine 138 is phosphorylated by Plk1. Together, these data support a model whereby mitotic phosphorylation of SUN1 disrupts interactions with nucleoplasmic binding partners, promoting disassembly of the nuclear lamina and, potentially, its chromatin interactions.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-263099	Ser48	KLDPVFDsPRMSRRS	Homo sapiens	HeLa Cell
pmid	sentence
25482198	Here, we show that SUN1, located in the INM, undergoes mitosis-specific phosphorylation on at least 3 sites within its nucleoplasmic N-terminus. We further identify Cdk1 as the kinase responsible for serine 48 and 333 phosphorylation, while serine 138 is phosphorylated by Plk1. Together, these data support a model whereby mitotic phosphorylation of SUN1 disrupts interactions with nucleoplasmic binding partners, promoting disassembly of the nuclear lamina and, potentially, its chromatin interactions.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-55994	Ser34	RPVSSAAsVYAGAGG	Homo sapiens
pmid	sentence
9524113	We identified k18 ser33 as an interphase phosphorylation site, which increases its phosphorylation during mitosis in cultured cells and regenerating liver, and as an in vitro cdc2 kinase phosphorylation site. K18 ser33 phosphorylation dictates binding to 14_3_3 proteins

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-277185	Ser343	PTDEVGQsPAAVGLG	Homo sapiens
pmid	sentence
26459638	We found that CDK1 phosphorylates Ser343 of ERK1c, thereby allowing the binding of phosphorylated ERK1c to a complex that consists of PI4KIIIβ (also known as PI4KB) and the 14-3-3γ dimer (encoded by YWHAB).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-119705	Ser355	AALSRAHsPALGVHS	Homo sapiens
pmid	sentence
14657031	Apc activation is thought to depend on apc phosphorylation and cdc20 binding. We have identified 43 phospho_sites on apc of which at least 34 are mitosis specific. Of these, 32 sites are clustered in parts of apc1 and the tetratricopeptide repeat (tpr) subunits cdc27, cdc16, cdc23 and apc7. In vitro, at least 15 of the mitotic phospho_sites can be generated by cyclin_dependent kinase 1 (cdk1), and 3 by polo_like kinase 1 (plk1). Apc phosphorylation by cdk1, but not by plk1, is sufficient for increased cdc20 binding and apc activation

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-177982	Ser359	GTEEKCGsPQVRTLS	Homo sapiens
pmid	sentence
18337751	Phosphorylation at ser359 inhibits eef2k activity even at high calcium concentrations. we demonstrate that cdc2 contributes to controlling eef2 phosphorylation in cells. inactivation of eef2k by cdc2 may serve to keep eef2 active during mitosis

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-158604	Ser36	PRKQPPVsPGTALVG	Homo sapiens
pmid	sentence
17960875	Here, we found that hipk2 phosphorylates hmga1a at ser-35, thr-52, and thr-77, and hmga1b at thr-41 and thr-66. In addition, we demonstrated that cdc2, which is known to phosphorylate hmga1 proteins, could induce the phosphorylation of hmga1 proteins at the same ser/thr sites. we found that the hipk2-phosphorylated hmga1a reduced the binding affinity of hmga1a to human germ line promoter, and the drop in binding affinity induced by hipk2 phosphorylation was lower than that introduced by cdc2 phosphorylation.

Identifier	Residue	Sequence	Organism
SIGNOR-158608	Thr53	KEPSEVPtPKRPRGR	Homo sapiens
pmid	sentence
17960875	Here, we found that hipk2 phosphorylates hmga1a at ser-35, thr-52, and thr-77, and hmga1b at thr-41 and thr-66. In addition, we demonstrated that cdc2, which is known to phosphorylate hmga1 proteins, could induce the phosphorylation of hmga1 proteins at the same ser/thr sites. we found that the hipk2-phosphorylated hmga1a reduced the binding affinity of hmga1a to human germ line promoter, and the drop in binding affinity induced by hipk2 phosphorylation was lower than that introduced by cdc2 phosphorylation.

Identifier	Residue	Sequence	Organism
SIGNOR-22338	Thr78	KTRKTTTtPGRKPRG	Homo sapiens
pmid	sentence
1939057	Phosphorylation of the dna-binding domain of nonhistone high-mobility group i protein by cdc2 kinase: reduction of binding affinity

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-161839	Ser362	ISSVPTPsPLGPLAG	Homo sapiens	Glioblastoma Cell
pmid	sentence
19941816	The mitotic phosphorylation sites on the alpha subunit of casein kinase ii can be phosphorylated in vitro by p34cdc2.

Identifier	Residue	Sequence	Organism
SIGNOR-29521	Ser370	PLGPLAGsPVIAAAN	Homo sapiens
pmid	sentence
7592773	Four residues within this domain, thr-344, thr-360, ser-362, and ser-370, conform to the minimal consensus sequence for p34cdc2 phosphorylationthe high stoichiometry of phosphorylation suggests that phosphorylation could regulate functional properties of ckii and that it could in some way participate in the burst of phosphorylation that accompanies the activation of p34graphic at the ggraphic-m transition

Identifier	Residue	Sequence	Organism
SIGNOR-29525	Thr344	SSMPGGStPVSSANM	Homo sapiens
pmid	sentence
7592773	Four residues within this domain, thr-344, thr-360, ser-362, and ser-370, conform to the minimal consensus sequence for p34cdc2 phosphorylationthe high stoichiometry of phosphorylation suggests that phosphorylation could regulate functional properties of ckii and that it could in some way participate in the burst of phosphorylation that accompanies the activation of p34graphic at the ggraphic-m transition

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-161843	Thr360	SGISSVPtPSPLGPL	Homo sapiens	Glioblastoma Cell
pmid	sentence
19941816	It has been shown that the c-terminal domains of ck2? Are phosphorylated by cdc2 and interact with the peptidyl-prolyl isomerase pin1 in a cell cycle-dependent manner

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-275592	Ser364	KVDDAKVsPPKRAEM
pmid	sentence
24746669	Here, we show that a fraction of cyclin B1/Cdk1 proteins localizes to the matrix of mitochondria and phosphorylates a cluster of mitochondrial proteins, including the complex I (CI) subunits in the respiratory chain. Cyclin B1/Cdk1-mediated CI phosphorylation enhances CI activity, whereas deficiency of such phosphorylation in each of the relevant CI subunits results in impairment of CI function.\|These results were confirmed by generating phosphorylation defective forms of the five CI subunits through substitutions of S/T residues with Alanine (A) on either Cdk1 optimal or minimal consensus motifs (T383 on NDUFV1, S105 on NDUFV3, S364 on NDUFS2, S55/S29/T5 on NDUFB6, and T142/T120 on NDUFA12). The mutation of Cdk1 consensus motifs severely diminished their phosphorylation

Publications:

1

Identifier	Residue	Sequence	Organism
SIGNOR-154681	Ser368	PNPSTSAsPKKSPPP	Homo sapiens
pmid	sentence
17488717	Here, we demonstrate that sirt2 is phosphorylated both in vitro and in vivo on serine 368 by the cell-cycle regulator, cyclin-dependent kinase 1. Overexpression of sirt2 mediates a delay in cellular proliferation that is dependent on serine 368 phosphorylation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-60281	Ser37	REYQQRNsPGVPTGA	Homo sapiens
pmid	sentence
9753325	Cdc2 kinase directly phosphorylates the cis-golgi matrix protein gm130 and is required for golgi fragmentation in mitosis. Mitotic fragmentation of the golgi apparatus can be largely explained by disruption of the interaction between gm130 and the vesicle-docking protein p115. Here we identify a single serine (ser-25) in gm130 as the key phosphorylated target and cdc2 as the responsible kinase

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-167822	Ser373	SSRSAPAsPNHAGVL	Homo sapiens
pmid	sentence
20810654	We have mapped two cdk phosphorylation sites, serines 368 and 423, which play a role in defining foxk2 function through regulating its stability and its activity as a transcriptional repressor protein. These two cdk sites appear vital for foxk2 function because expression of a mutant lacking these sites cannot be tolerated and causes apoptosis.

Identifier	Residue	Sequence	Organism
SIGNOR-167826	Ser428	FAQSAPGsPLSSQPV	Homo sapiens
pmid	sentence
20810654	We have mapped two cdk phosphorylation sites, serines 368 and 423, which play a role in defining foxk2 function through regulating its stability and its activity as a transcriptional repressor protein. These two cdk sites appear vital for foxk2 function because expression of a mutant lacking these sites cannot be tolerated and causes apoptosis.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-124638	Ser382	DFIDAFAsPVEAEGT	Homo sapiens
pmid	sentence
15125835	Here we show that, at the onset of mitosis, cdk1 phosphorylates the peripheral golgi protein nir2 at multiple sites;of these, s382 is the most prominent. Phosphorylation of nir2 by cdk1 facilitates its dissociation from the golgi apparatus, and phospho-nir2(ps382) is localized in the cleavage furrow and midbody during cytokinesis.

Identifier	Residue	Sequence	Organism
SIGNOR-124642	Thr287	SAASNTGtPDGPEAP	Homo sapiens
pmid	sentence
15125835	T287 is phosphorylated by cdk1 during mitosis. Phosphorylation of nir2 by cdk1 facilitates its dissociation from the golgi apparatus, and phospho-nir2(ps382) is localized in the cleavage furrow and midbody during cytokinesis.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262723	Ser382	FSDPWGGsPAKPSTN	Cricetulus griseus	CHO Cell
pmid	sentence
10764745	Phosphorylation of POB1 and Epsin by p34cdc2 kinase. Their phosphorylation sites (Ser411 of POB1 and Ser357 of Epsin) were determined. Phosphorylated Epsin and EpsinS357D formed a complex with α-adaptin less efficiently than wild type Epsin.

Publications:

1

Organism:

Cricetulus Griseus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-39233	Ser386	LRGAQAAsPAKGEPS	Homo sapiens	HeLa Cell
pmid	sentence
8491187	Ptp1b is phosphorylated on ser386 by p34cdc2 in vivo.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-272970	Ser386	LRGAQAAsPAKGEPS	Homo sapiens	HeLa Cell
pmid	sentence
23348582	Cdk1-cyclin B1 directly phosphorylates PTP1B at serine 386 in a kinase assay. Recombinant Plk1 phosphorylates PTP1B on serine 286 and 393 in vitro, however, it requires a priming phosphorylation by Cdk1 at serine 386 highlighting a novel co-operation between Cdk1 and Plk1 in the regulation of PTP1B.\|Finally, phosphorylation on serine 286 enhanced PTP1B phosphatase activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-129061	Ser387	PRFSPPPsPPGPCMP	Homo sapiens
pmid	sentence
15367677	S387a mutant abolished fancg fusion protein phosphorylation by cdc2.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-168446	Ser387	YLEMDLSsPQTRYIP	Homo sapiens
pmid	sentence
20937773	In this study, we demonstrate that procaspase-8 is phosphorylated in mitotic cells by cdk1na interference-mediated silencing of cyclin b1 or treatment with the cdk1 inhibitor ro-3306 enhances the fas-mediated activation and processing of procaspase-8 in mitotic cells/cyclin b1 on ser-387

Publications:

1

Organism:

Homo Sapiens

Tissue:

Breast

Identifier	Residue	Sequence	Organism
SIGNOR-134846	Ser39	MKKIRLEsEEEGVPS	Homo sapiens
pmid	sentence
15788687	Additionally, transfection of cdc2 with a mutation at ser(39) to ala, which is the ck2 phosphorylation site, partially inhibits cell cycle progression in g(1) to g(2) phase following 6-tg treatment.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-50603	Ser394	TRQTPVDsPDDSTLS	Homo sapiens
pmid	sentence
9271440	Interestingly, phosphorylation at several ser/thr residues within the c-terminal autoinhibitory tail appears to either activate or inhibit s6k1, depending on the cell cycle phase. phosphorylation of those residues (featured by the thr-421/ser-424 site) during mitosis pursued by cdk1 inactivates s6k1 we then assessed the phosphorylation status of the mitosis-specific inhibitory residue of s6k1, thr-421/ser-424, which is targeted by mitotic cdk1.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-98211	Ser394	TRQTPVDsPDDSTLS	Homo sapiens	HeLa Cell
pmid	sentence
12586835	A physical interaction exists between cdc2 and s6k1, and this interaction is enhanced in mitotic cells. These results suggest that cdc2 provides a signal that triggers inactivation of s6k1 in mitosis, presumably serving to spare energy for costly mitotic processes at the expense of ribosomal protein synthesis.

Identifier	Residue	Sequence	Organism
SIGNOR-98215	Ser434	SFEPKIRsPRRFIGS	Homo sapiens
pmid	sentence
12586835	The activation of p70s6k is associated with multiple phosphorylations at two sets of sites. The first set, s411, s418, t421, and s424, reside within the autoinhibitory domain, mutations of s371 abolished kinase activity. In mitotic hela cells, when the activity of cdc2 is high, s6k1 is phosphorylated at multiple ser/thr, pro (s/tp) sites, including ser(371), ser(411), thr(421), and ser(424).

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-50607	Ser434	SFEPKIRsPRRFIGS	Homo sapiens	HeLa Cell
pmid	sentence
9271440	The activation of p70s6k is associated with multiple phosphorylations at two sets of sites. The first set, s411, s418, t421, and s424, reside within the autoinhibitory domain, mutations of s371 abolished kinase activity. In mitotic hela cells, when the activity of cdc2 is high, s6k1 is phosphorylated at multiple ser/thr, pro (s/tp) sites, including ser(371), ser(411), thr(421), and ser(424).

Identifier	Residue	Sequence	Organism
SIGNOR-134654	Thr444	RFIGSPRtPVSPVKF	Homo sapiens
pmid	sentence
15774499	The principal target of rapamycin-induced p70s6k inactivation is a novel phosphorylation site within a conserved hydrophobic domain.

Identifier	Residue	Sequence	Organism
SIGNOR-111507	Thr444	RFIGSPRtPVSPVKF	Homo sapiens
pmid	sentence
11705993	Interestingly, phosphorylation at several ser/thr residues within the c-terminal autoinhibitory tail appears to either activate or inhibit s6k1, depending on the cell cycle phase. phosphorylation of those residues (featured by the thr-421/ser-424 site) during mitosis pursued by cdk1 inactivates s6k1 we then assessed the phosphorylation status of the mitosis-specific inhibitory residue of s6k1, thr-421/ser-424, which is targeted by mitotic cdk1.

Publications:

6

Organism:

Homo Sapiens

Tissue:

Muscle, Skeletal Muscle

Identifier	Residue	Sequence	Organism
SIGNOR-154047	Ser395	PGLEVPSsPLRKAKR	Homo sapiens
pmid	sentence
17389604	Moreover, we found cyclin b1/cdk1 to phosphorylate nipa at ser-395 in mitosis. Mutation of both ser-359 and ser-395 impaired effective inactivation of the scfnipa complex, resulting in reduced levels of mitotic cyclin b1

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-31157	Ser4	sPLSKKRR	Homo sapiens	Breast Cancer Cell
pmid	sentence
7673335	Ubiquitin-activating enzyme, e1, is phosphorylated in mammalian cells by the protein kinase cdc2. Each serine residue was independently mutated to an alanine and analyzed by two-dimensional electrophoresis;only serine 4 was phosphorylated. Disruption of the basic amino acids within the nls resulted in loss of exclusive nuclear localization and a 90-95% decrease in the phosphorylation of ha1-e1

Identifier	Residue	Sequence	Organism
SIGNOR-47162	Ser4	sPLSKKRR	Homo sapiens
pmid	sentence
9099746	Ubiquitin-activating enzyme, e1, is phosphorylated in mammalian cells by the protein kinase cdc2. Each serine residue was independently mutated to an alanine and analyzed by two-dimensional electrophoresis;only serine 4 was phosphorylated. Disruption of the basic amino acids within the nls resulted in loss of exclusive nuclear localization and a 90-95% decrease in the phosphorylation of ha1-e1

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-32225	Ser835	ELKATLPsPDKLPGF	Homo sapiens	HeLa Cell
pmid	sentence
7724583	Ubiquitin-activating enzyme, e1, is phosphorylated in mammalian cells by the protein kinase cdc2. Thus, the serine at position 835 is a phosphorylation site. Taking these findings into consideration, we consider that cyclin b might be one of the substrates targeted by the specific ubiquitin conjugation pathway activated by the phosphorylation of e1 with cdc2 kinase.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-275489	Ser40	PTAEEKPsPRRSLSQ
pmid	sentence
33309518	Phosphorylation of multiple residues in the catalytic domain of PPM1D during mitosis, including Ser40 by Cyclin-dependent kinase 1 (CDK1), leads to ubiquitination of PPM1D and subsequent proteasomal degradation by Adenomatous polyposis coli (APC) and cell-division cycle protein 20 (CDC20)

Publications:

1

Identifier	Residue	Sequence	Organism
SIGNOR-140882	Ser425	NREKVAAsPKSPTAA	Homo sapiens
pmid	sentence
16198290	Upon mitotic entry, centrosome dissociation of cep55 is triggered by erk2/cdk1-dependent phosphorylation at s425 and s428. S425/428 phosphorylation is required for interaction with plk1, enabling phosphorylation of cep55 at s436. enabling it to relocate to the midbody to function in mitotic exit and cytokinesis.

Identifier	Residue	Sequence	Organism
SIGNOR-140886	Ser428	KVAASPKsPTAALNE	Homo sapiens
pmid	sentence
16198290	Upon mitotic entry, centrosome dissociation of cep55 is triggered by erk2/cdk1-dependent phosphorylation at s425 and s428. S425/428 phosphorylation is required for interaction with plk1, enabling phosphorylation of cep55 at s436. enabling it to relocate to the midbody to function in mitotic exit and cytokinesis.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-119873	Ser426	TQPNINDsLEITKLD	Homo sapiens
pmid	sentence
14657031	Apc activation is thought to depend on apc phosphorylation and cdc20 binding. We have identified 43 phospho_sites on apc of which at least 34 are mitosis specific. Of these, 32 sites are clustered in parts of apc1 and the tetratricopeptide repeat (tpr) subunits cdc27, cdc16, cdc23 and apc7. In vitro, at least 15 of the mitotic phospho_sites can be generated by cyclin_dependent kinase 1 (cdk1), and 3 by polo_like kinase 1 (plk1). Apc phosphorylation by cdk1, but not by plk1, is sufficient for increased cdc20 binding and apc activation

Identifier	Residue	Sequence	Organism
SIGNOR-119877	Thr446	EGKISTItPQIQAFN	Homo sapiens
pmid	sentence
14657031	Apc activation is thought to depend on apc phosphorylation and cdc20 binding. We have identified 43 phospho_sites on apc of which at least 34 are mitosis specific. Of these, 32 sites are clustered in parts of apc1 and the tetratricopeptide repeat (tpr) subunits cdc27, cdc16, cdc23 and apc7. In vitro, at least 15 of the mitotic phospho_sites can be generated by cyclin_dependent kinase 1 (cdk1), and 3 by polo_like kinase 1 (plk1). Apc phosphorylation by cdk1, but not by plk1, is sufficient for increased cdc20 binding and apc activation

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-123516	Ser428	EPAPVLSsPPPADVS	Homo sapiens
pmid	sentence
15037602	Here, we show that rangap1 is phosphorylated on residues t409, s428, and s442. Phosphorylation occurs before nuclear envelope breakdown and is maintained throughout mitosis . Alternatively, phosphorylated rangap1 may recruit specific sumo target proteins to ranbp2's catalytic domain.

Identifier	Residue	Sequence	Organism
SIGNOR-123520	Ser442	STFLAFPsPEKLLRL	Homo sapiens
pmid	sentence
15037602	Here, we show that rangap1 is phosphorylated on residues t409, s428, and s442. Phosphorylation occurs before nuclear envelope breakdown and is maintained throughout mitosis . Alternatively, phosphorylated rangap1 may recruit specific sumo target proteins to ranbp2's catalytic domain.

Identifier	Residue	Sequence	Organism
SIGNOR-123524	Thr409	GQGEKSAtPSRKILD	Homo sapiens
pmid	sentence
15037602	Here, we show that rangap1 is phosphorylated on residues t409, s428, and s442. Phosphorylation occurs before nuclear envelope breakdown and is maintained throughout mitosis. The m-phase kinase cyclin b/cdk1 phosphorylates rangap1 efficiently in vitro, and t409 phosphorylation correlates with nuclear accumulation of cyclin b1 in vivo.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-56054	Ser432	SAYGGLTsPGLSYSL	Homo sapiens
pmid	sentence
9524113	With regard to k8 phosphorylation at ser-431, it increases dramatically upon stimulation of cells with epidermal growth factor (egf) or after mitotic arrest and is the major k8 phosphorylated residue after incubating k8 immunoprecipitates with mitogen-activated protein or cdc2 kinases.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-148354	Ser439	AGSPFQSsPLSLGSR	Homo sapiens
pmid	sentence
16880739	Cdk1/cyclin b-mediated phosphorylation stabilizes srebp1 during mitosis.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-74094	Ser44	QEPTGEPsPKRPRGR	Homo sapiens
pmid	sentence
10636877	Architecture of high mobility group protein i-c dna complex and its perturbation upon phosphorylation by cdc2 kinase. Phosphorylation by cdc2 reduces binding strength of the mammalian and insect hmgi proteins to dna. After phosphorylation of the protein at ser-43 and ser-58 by cdc2 kinase multiple contacts of dbds, especially with the bases, are impaired and the protein binds to dna in a different way, extending the contacts to the sugar-phosphate backbone.

Identifier	Residue	Sequence	Organism
SIGNOR-74098	Ser59	PKGSKNKsPSKAAQK	Homo sapiens
pmid	sentence
10636877	Architecture of high mobility group protein i-c dna complex and its perturbation upon phosphorylation by cdc2 kinase. Phosphorylation by cdc2 reduces binding strength of the mammalian and insect hmgi proteins to dna. After phosphorylation of the protein at ser-43 and ser-58 by cdc2 kinase multiple contacts of dbds, especially with the bases, are impaired and the protein binds to dna in a different way, extending the contacts to the sugar-phosphate backbone.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-272972	Ser460	STSVLHSsPLNVFMG
pmid	sentence
21690413	Mechanistically, we demonstrated that Cdc2-dependent phosphorylation on a γ-tubulin ring complex (γ-TuRC) recruitment protein, Nedd1/GCP-WD, at the previously uncharacterized S460 residue induces the Nedd1-Plk1 interaction

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-272973	Thr550	PPINGSStPNPKIAS	Homo sapiens	HeLa Cell
pmid	sentence
19509060	Here we report that the function of Nedd1 is regulated by Cdk1 and Plk1. During mitosis, Nedd1 is firstly phosphorylated at T550 by Cdk1, which creates a binding site for the polo-box domain of Plk1. Then, Nedd1 is further phosphorylated by Plk1 at four sites: T382, S397, S637 and S426. The sequential phosphorylation of Nedd1 by Cdk1 and Plk1 promotes its interaction with gamma-tubulin for targeting the gammaTuRC to the centrosome and is important for spindle formation.

Publications:

2

Organism:

, Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-262724	Ser463	RPRSRSYsSTSIEEA	Cricetulus griseus
pmid	sentence
10764745	Phosphorylation of POB1 and Epsin by p34cdc2 kinase. Their phosphorylation sites (Ser411 of POB1 and Ser357 of Epsin) were determined. Phosphorylated Epsin and EpsinS357D formed a complex with α-adaptin less efficiently than wild type Epsin.

Publications:

1

Organism:

Cricetulus Griseus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-143586	Ser465	MVPGGDRsPSRMLPP	Homo sapiens	Breast Cancer Cell, Prostate Gland Cancer Cell
pmid	sentence
16407259	In vitro kinase assays using recombinant cdc2 kinase showed that runx2 was phosphorylated at ser(451) the cdc2 inhibitor roscovitine dose dependently inhibited in vivo runx2 dna-binding activity during mitosis and the runx2 mutant s451a exhibited lower dna-binding activity and reduced stimulation of anchorage-independent growth relative to wild type runx2.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-121398	Ser470	PQGQQPLsPQSGSPQ	Homo sapiens
pmid	sentence
14732590	A rare, missense polymorphism, s470n, was identified in the synapsin iii gene and appeared more frequently in individuals with schizophrenia than in controls. Ser470, was determined to be a substrate for mitogen-activated protein kinase, a downstream effector of neurotrophin action.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-18735	Ser484	SLIVPGKsPTRKKSG	Homo sapiens
pmid	sentence
1406653	Two of the sites of phosphorylation by cyclic amp (camp)-dependent kinase were localized to serine residues 490 and 499, and one site of phosphorylation by p34cdc2 was localized to serine 484.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276834	Ser533	ATGTGTFsPGASPGS	Homo sapiens	HeLa Cell
pmid	sentence
31981797	CDK1 phosphorylates PKN1 at S533, S537, S562, and S916 in vitro and in cells during drug-induced mitotic arrest. Immunofluorescence staining further confirmed that PKN1 phosphorylation occurs during normal mitosis in a CDK1-dependent manner.Knockdown of PKN1 significantly inhibited anchorage-independent growth and migration without affecting proliferation in multiple cancer cell lines.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276833	Ser537	GTFSPGAsPGSEART	Homo sapiens	HeLa Cell
pmid	sentence
31981797	CDK1 phosphorylates PKN1 at S533, S537, S562, and S916 in vitro and in cells during drug-induced mitotic arrest. Immunofluorescence staining further confirmed that PKN1 phosphorylation occurs during normal mitosis in a CDK1-dependent manner.Knockdown of PKN1 significantly inhibited anchorage-independent growth and migration without affecting proliferation in multiple cancer cell lines.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276831	Ser562	LGTDSDSsPQKSSRD	Homo sapiens	HeLa Cell
pmid	sentence
31981797	CDK1 phosphorylates PKN1 at S533, S537, S562, and S916 in vitro and in cells during drug-induced mitotic arrest. Immunofluorescence staining further confirmed that PKN1 phosphorylation occurs during normal mitosis in a CDK1-dependent manner.Knockdown of PKN1 significantly inhibited anchorage-independent growth and migration without affecting proliferation in multiple cancer cell lines.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276832	Ser916	TGEAPTLsPPRDARP	Homo sapiens	HeLa Cell
pmid	sentence
31981797	CDK1 phosphorylates PKN1 at S533, S537, S562, and S916 in vitro and in cells during drug-induced mitotic arrest. Immunofluorescence staining further confirmed that PKN1 phosphorylation occurs during normal mitosis in a CDK1-dependent manner.Knockdown of PKN1 significantly inhibited anchorage-independent growth and migration without affecting proliferation in multiple cancer cell lines.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-268338	Ser537	DNSMSVPsPTSATKT	Mus musculus	Oocyte
pmid	sentence
34048556	Once an oocyte resumes meiosis, activated CDK1 and ERK1/2 cooperatively mediate the phosphorylation of three serine residues of PAPalpha, 537, 545 and 558, thereby leading to increased activity.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-268339	Ser545	PTSATKTsPLNSSGS	Mus musculus	Oocyte
pmid	sentence
34048556	Once an oocyte resumes meiosis, activated CDK1 and ERK1/2 cooperatively mediate the phosphorylation of three serine residues of PAPalpha, 537, 545 and 558, thereby leading to increased activity.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-268340	Ser558	GSSQGRNsPAPAVTA	Mus musculus	Oocyte
pmid	sentence
34048556	Once an oocyte resumes meiosis, activated CDK1 and ERK1/2 cooperatively mediate the phosphorylation of three serine residues of PAPalpha, 537, 545 and 558, thereby leading to increased activity.

Publications:

3

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-182863	Ser540	HVSEDSSsPERTSPP	Homo sapiens
pmid	sentence
19107194	We identified cyclinb/cdk1 as a cell cycle-dependent kinase that forms a complex with and phosphorylates sirt1. Mutation of two residues phosphorylated by cyclin b/cdk1 (threonine 530 and serine 540) disturbs normal cell cycle progression and fails to rescue proliferation defects in sirt1-deficient cells

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-277603	Ser548	GQAWGRQsPRRLEDS	in vitro
pmid	sentence
35843311	Using in vitro kinase assays and phosphomutants, we determined that CDK1 phosphorylates MLK3 on Ser548 and decreases MLK3 activity during mitosis, whereas CDK2 phosphorylates MLK3 on Ser770 and increases MLK3 activity during G1/S and G2 phases.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-278264	Ser549	SNGGNLNsPPGPHSA	Homo sapiens
pmid	sentence
30089874	We found that Cdc14A is phosphorylated on Ser411, Ser453 and Ser549 by Cdk1 early in mitosis and becomes dephosphorylated during late mitotic stages.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-35492	Ser55	TSRSLYAsSPGGVYA	Homo sapiens
pmid	sentence
7983050	These results strongly suggest that cdc2 kinase is the kinase which phosphorylates vimentin ser55 in the entire cytoplasm during mitosis and that the appearance of immunoreactivities with antibody 4a4 in cell staining indeed reflect the vimentin phosphorylation by cdc2 kinase. immunofluorescent evidence using antibody 4a4 and biochemical analysis using vimentin ser55 peptide showed that the degree of disassembly of vimentin filament of various cell types at early mitotic phase correlated well with the amount of mitotically activated cdc2 kinase.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-202678	Ser552	DLEVLTSsPTRNLNG	Homo sapiens
pmid	sentence
24013421	Here, we report that cyclin-dependent kinase 1 (cdk1) phosphorylates the histone h2a deubiquitinase ubp-m at serine 552 (s552p), and, importantly, this phosphorylation is required for cell cycle progression.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-265040	Ser56	PKATVFKsPRTPPQR
pmid	sentence
23500464	At mitosis, Cdc2 kinase phosphorylates p47 on Serine-140 and p37 on Serine-56 and Threonine-59, respectively. The phosphorylated p47 and p37 are unable to bind to Golgi membranes, resulting in mitotic inhibition of the p97/p47 and the p97/p37 pathways, respectively.

Identifier	Residue	Sequence
SIGNOR-265041	Thr59	TVFKSPRtPPQRFYS
pmid	sentence
23500464	At mitosis, Cdc2 kinase phosphorylates p47 on Serine-140 and p37 on Serine-56 and Threonine-59, respectively. The phosphorylated p47 and p37 are unable to bind to Golgi membranes, resulting in mitotic inhibition of the p97/p47 and the p97/p37 pathways, respectively.

Publications:

2

Identifier	Residue	Sequence	Organism
SIGNOR-119762	Ser560	KTLKNIIsPPWDFRE	Homo sapiens
pmid	sentence
14657031	Apc activation is thought to depend on apc phosphorylation and cdc20 binding. We have identified 43 phospho_sites on apc of which at least 34 are mitosis specific. Of these, 32 sites are clustered in parts of apc1 and the tetratricopeptide repeat (tpr) subunits cdc27, cdc16, cdc23 and apc7. In vitro, at least 15 of the mitotic phospho_sites can be generated by cyclin_dependent kinase 1 (cdk1), and 3 by polo_like kinase 1 (plk1). Apc phosphorylation by cdk1, but not by plk1, is sufficient for increased cdc20 binding and apc activation

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-118576	Ser584	ETSIFTPsPCKIPPP	Homo sapiens	Kidney Cancer Cell, Brain Cancer Cell, Skin Cancer Cell
pmid	sentence
14551205	Cell cycle-regulated phosphorylation of hamartin, the product of the tuberous sclerosis complex 1 gene, by cyclin-dependent kinase 1/cyclin b.Cyclin-dependent kinase 1 phosphorylates hamartin at three sites, one of which (thr417) is in the hamartin-tuberin interaction domain. Tuberin interacts with phosphohamartin, and tuberin expression attenuates the phosphorylation of exogenous hamartin. Hamartin with alanine mutations in the three cyclin-dependent kinase 1 phosphorylation sites increased the inhibition of p70s6 kinase by the hamartin-tuberin complex

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-118580	Thr1047	SSSSELStPEKPPHQ	Homo sapiens	Kidney Cancer Cell, Brain Cancer Cell, Skin Cancer Cell
pmid	sentence
14551205	Cell cycle-regulated phosphorylation of hamartin, the product of the tuberous sclerosis complex 1 gene, by cyclin-dependent kinase 1/cyclin b.Cyclin-dependent kinase 1 phosphorylates hamartin at three sites, one of which (thr417) is in the hamartin-tuberin interaction domain. Tuberin interacts with phosphohamartin, and tuberin expression attenuates the phosphorylation of exogenous hamartin. Hamartin with alanine mutations in the three cyclin-dependent kinase 1 phosphorylation sites increased the inhibition of p70s6 kinase by the hamartin-tuberin complex

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-118584	Thr417	SLPQATVtPPRKEER	Homo sapiens	Kidney Cancer Cell, Brain Cancer Cell, Skin Cancer Cell
pmid	sentence
14551205	Cell cycle-regulated phosphorylation of hamartin, the product of the tuberous sclerosis complex 1 gene, by cyclin-dependent kinase 1/cyclin b.Cyclin-dependent kinase 1 phosphorylates hamartin at three sites, one of which (thr417) is in the hamartin-tuberin interaction domain. Tuberin interacts with phosphohamartin, and tuberin expression attenuates the phosphorylation of exogenous hamartin. Hamartin with alanine mutations in the three cyclin-dependent kinase 1 phosphorylation sites increased the inhibition of p70s6 kinase by the hamartin-tuberin complex

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-118588	Ser584	ETSIFTPsPCKIPPP	Homo sapiens
pmid	sentence
14551205	In vitro assays showed that cyclin-dependent kinase 1 phosphorylates hamartin at three sites, one of which (thr417) is in the hamartin-tuberin interaction domain.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-117339	Thr1047	SSSSELStPEKPPHQ	Homo sapiens	Kidney Cancer Cell, Brain Cancer Cell, Skin Cancer Cell
pmid	sentence
14551205	In vitro assays showed that cyclin-dependent kinase 1 phosphorylates hamartin at three sites, one of which (thr417) is in the hamartin-tuberin interaction domain.

Identifier	Residue	Sequence	Organism
SIGNOR-86696	Thr417	SLPQATVtPPRKEER	Homo sapiens
pmid	sentence
14551205	In vitro assays showed that cyclin-dependent kinase 1 phosphorylates hamartin at three sites, one of which (thr417) is in the hamartin-tuberin interaction domain.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-259831	Ser589	NRHSPSWsPDGRRRQ	Homo sapiens
pmid	sentence
20890132	In this study, we show that Nlp can be phosphorylated by cell cycle protein kinase Cdc2/cyclin B1. The phosphorylation sites of Nlp are mapped at Ser185 and Ser589. the phosphorylation at the site Ser589 by Cdc2/cyclin B1 plays an important role in Nlp protein stability probably due to its effect on protein degradation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-277294	Ser6	sPLLEVKG	in vitro
pmid	sentence
24510915	We confirmed that CDK1 phosphorylates Ser6 (Supplementary Fig S5B) and demonstrated that KIFC1 displays CDK1-mediated resistance to ubiquitination by the APC/C (Fig S5C).

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-172217	Ser612	LNNSNLFsPVNRDSE	Homo sapiens
pmid	sentence
21335236	We show that npc disassembly is a phosphorylation-driven process, dependent on cdk1 activity and supported by members of the nima-related kinase (nek) family. mitotic hyperphosphorylation of nup98 is accomplished by multiple kinases, including cdk1 and neks.

Identifier	Residue	Sequence	Organism
SIGNOR-172221	Ser623	RDSENLAsPSEYPEN	Homo sapiens
pmid	sentence
21335236	We show that npc disassembly is a phosphorylation-driven process, dependent on cdk1 activity and supported by members of the nima-related kinase (nek) family. mitotic hyperphosphorylation of nup98 is accomplished by multiple kinases, including cdk1 and neks.

Identifier	Residue	Sequence	Organism
SIGNOR-172225	Thr670	IAKPIPQtPESAGNK	Homo sapiens
pmid	sentence
21335236	We show that npc disassembly is a phosphorylation-driven process, dependent on cdk1 activity and supported by members of the nima-related kinase (nek) family. mitotic hyperphosphorylation of nup98 is accomplished by multiple kinases, including cdk1 and neks.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-94160	Ser613	EKKQITTsPITVRKN	Homo sapiens
pmid	sentence
12372621	Warts is a serine/threonine kinase and a dynamic component of the mitotic apparatus. We have found that cdc2/cyclin b forms a complex with a fraction of warts in the centrosome and phosphorylates the ser613 site of warts during mitosisit can be speculated that phosphorylation of warts by cdc2/cyclin b promotes a protein complex formation on the mitotic apparatus at early mitosis, which may be required for subsequent activation of warts kinase at the metaphase-anaphase transition.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-279394	Ser616	PIPIMPAsPQKGHAV	Homo sapiens
pmid	sentence
26352374	Drp1 is phosphorylated at the Ser616 position and activated predominantly by CDK1.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-266410	Ser653	TVPFDSEsPIRMKFT	Homo sapiens	HEK-293 Cell
pmid	sentence
31875566	To determine whether mitotic CDK phosphorylates ATAD5, a CDK1 inhibitor (RO3306) was applied to nocodazole-arrested cells (Figure S3F). CDK1 inhibition resulted in a loss of S653 phosphorylation (Figure S3F). These data meant that the S653 residue in the BET BD of ATAD5 is phosphorylated by mitotic CDK. This result suggested that the BRD4-ATAD5 interaction is inhibited during mitosis.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-279599	Ser668	DTQSRTAsPNRAGKG	Homo sapiens
pmid	sentence
24189531	In vitro kinase assays reveal that CDK1 directly phosphorylates HIF-1\u03b1 at a previously unidentified regulatory site, Ser668.\|Overexpression of CDK1 and/or cyclin B1 is sufficient to stabilize HIF-1alpha under normoxic conditions, whereas inhibition of CDK1 enhances the proteasomal degradation of HIF-1alpha, reducing its half-life and steady-state levels.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-189017	Ser668	IGEETDSsPGRKKFP	Homo sapiens
pmid	sentence
19881501	Stim1 is phosphorylated during mitosis. Removal of ten mpm-2 recognition sites by truncation at amino acid 482 abolished mpm-2 recognition of mitotic stim1, and significantly rescued stim1 rearrangement and soce response in mitosis. We identified ser 486 and ser 668 as mitosis-specific phosphorylation sites, and stim1 containing mutations of these sites to alanine also significantly rescued mitotic soce.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277576	Ser68	LIRKLPFsRLAREIC	Homo sapiens	HeLa Cell
pmid	sentence
34758320	Here, we report that the phosphorylation of CENP-A Ser68 primes the ubiquitin-proteasome-mediated proteolysis of CENP-A during mitotic phase in human cultured cells.the mitotic CENP-A degradation specifically depends on Cdk1 activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-164487	Ser684	IGIPQFHsPVGSPLK	Homo sapiens
pmid	sentence
20236090	Using ms analysis, we identified four novel phosphorylation sites, ser684, ser688, thr698 and ser705, located at the extreme c-terminus of erk3. All four sites are followed by a proline residue. We have shown that purified cyclin b-cdk1 (cyclindependent kinase 1) phosphorylates these sitesalanine substitution of the four c-terminal phosphorylation sites markedly decreased the half-life of erk3 in mitosis, thereby linking phosphorylation to the stabilization of the kinase.

Identifier	Residue	Sequence	Organism
SIGNOR-164491	Ser688	QFHSPVGsPLKSIQA	Homo sapiens
pmid	sentence
20236090	Using ms analysis, we identified four novel phosphorylation sites, ser684, ser688, thr698 and ser705, located at the extreme c-terminus of erk3. All four sites are followed by a proline residue. We have shown that purified cyclin b-cdk1 (cyclindependent kinase 1) phosphorylates these sitesalanine substitution of the four c-terminal phosphorylation sites markedly decreased the half-life of erk3 in mitosis, thereby linking phosphorylation to the stabilization of the kinase.

Identifier	Residue	Sequence	Organism
SIGNOR-164495	Ser705	TPSAMKSsPQIPHQT	Homo sapiens
pmid	sentence
20236090	Using ms analysis, we identified four novel phosphorylation sites, ser684, ser688, thr698 and ser705, located at the extreme c-terminus of erk3. All four sites are followed by a proline residue. We have shown that purified cyclin b-cdk1 (cyclindependent kinase 1) phosphorylates these sitesalanine substitution of the four c-terminal phosphorylation sites markedly decreased the half-life of erk3 in mitosis, thereby linking phosphorylation to the stabilization of the kinase.

Identifier	Residue	Sequence	Organism
SIGNOR-164499	Thr698	KSIQATLtPSAMKSS	Homo sapiens
pmid	sentence
20236090	Using ms analysis, we identified four novel phosphorylation sites, ser684, ser688, thr698 and ser705, located at the extreme c-terminus of erk3. All four sites are followed by a proline residue. We have shown that purified cyclin b-cdk1 (cyclindependent kinase 1) phosphorylates these sitesalanine substitution of the four c-terminal phosphorylation sites markedly decreased the half-life of erk3 in mitosis, thereby linking phosphorylation to the stabilization of the kinase.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-53735	Ser696	PNKELPPsPEKKTKP	Homo sapiens	HeLa Cell
pmid	sentence
9398320	Map4 is phosphorylated by cdc2 kinase in mitotic hela/ phosphorylation by cdc2 kinase decreased the microtubule-stabilizing ability of map4, suggesting that there are critical phosphorylation sites among the five major cdc2 kinase-dependent phosphorylation sites [spots 4 (ser-696), 5, 6, 9, and 10 (ser-787)].

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-53739	Ser787	KAPEKRAsPSKPASA	Homo sapiens	HeLa Cell
pmid	sentence
9398320	Map4 is phosphorylated by cdc2 kinase in mitotic hela/ phosphorylation by cdc2 kinase decreased the microtubule-stabilizing ability of map4, suggesting that there are critical phosphorylation sites among the five major cdc2 kinase-dependent phosphorylation sites [spots 4 (ser-696), 5, 6, 9, and 10 (ser-787)].

Identifier	Residue	Sequence	Organism
SIGNOR-77087	Ser787	KAPEKRAsPSKPASA	Homo sapiens
pmid	sentence
10791892	Ser787 in the proline-rich region of human map4 is a critical phosphorylation site that reduces its activity to promote tubulin polymerization. Phosphorylation on ser-787 negatively regulates map4 activity to promote microtubule assembly.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-163849	Ser696	EKNYALPsPATTEGG	Homo sapiens
pmid	sentence
20169205	Cdc2 is the raptor ser696, thr706 kinase

Identifier	Residue	Sequence	Organism
SIGNOR-163853	Thr706	TTEGGSLtPVRDSPC	Homo sapiens
pmid	sentence
20169205	Cdc2 is the raptor ser696, thr706 kinase

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277461	Ser696	PNKELPPsPEKKTKP	Homo sapiens	HeLa Cell
pmid	sentence
10791892	We have shown that MAP4 is phosphorylated in vivo in mitotic HeLa cells at eight sites. Five of these were phosphorylated by p34cdc2 kinase. Two of the five p34cdc2 kinase phosphorylation sites were shown to be Ser696 and Ser787 in the proline-rich region

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-161801	Ser70	EAMNYEGsPIKVTLA	Homo sapiens
pmid	sentence
19933706	Simultaneous inactivation of two cdk phosphorylation sites at ser10 and ser70 (npm-aa) induced g(2)/m cell cycle arrest, phosphorylation of cdk1 at tyr15 (cdc2(tyr15)) and increased cytoplasmic accumulation of cdc25c.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-121335	Ser71	KGGSTSSsPSRRRGS	Homo sapiens
pmid	sentence
14718546	The binding of the nk fragment to chromatin pretreated with an s-phase extract was suppressed by incubation with an m-phase extract. Enzyme inhibitor experiments revealed that multiple kinases participate in the suppression. One of these kinases was shown to be cdc2 experiments involving a mutant nk fragment showed that the phosphorylation of serine 71 by cdc2 kinase is responsible for the suppression.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-195233	Ser728	VVKQEQLsPKKKENN	Homo sapiens
pmid	sentence
22163316	We demonstrate that aib1 is phosphorylated on ser728 and ser867 by cdk1/cyclin b at the onset of mitosis and remains phosphorylated until exit from m phase.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-103242	Ser76	EEEDEALsPAKGQKP	Homo sapiens	HeLa Cell
pmid	sentence
12851383	We show that three residues (ser51, ser76, and ser91), which are part of cyclin-dependent kinase sites, are phosphorylated in a cell cycle-dependent manner.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-265038	Ser768	TPTKAPYsPTTSKEK
pmid	sentence
23500464	We clarified that VCIP135, an essential factor in both p97 membrane fusion pathways, is phosphorylated on Threonine-760 and Serine-767 by Cdc2 at mitosis and that this phosphorylated VCIP135 does not bind to p97.

Identifier	Residue	Sequence
SIGNOR-265037	Thr761	GPSSAPAtPTKAPYS
pmid	sentence
23500464	We clarified that VCIP135, an essential factor in both p97 membrane fusion pathways, is phosphorylated on Threonine-760 and Serine-767 by Cdc2 at mitosis and that this phosphorylated VCIP135 does not bind to p97.

Publications:

2

Identifier	Residue	Sequence	Organism
SIGNOR-273587	Ser771	ESGPRCSsPVDTECS	in vitro
pmid	sentence
29764989	We found that many interactions were abolished upon kinase inhibition; however, a subset was protected from phosphatase opposition or was unopposed, resulting in persistent interaction of the substrate with Plk1. This subset includes phosphoprotein phosphatase 6 (PP6), whose activity toward Aurora kinase A (Aurora A) was inhibited by Plk1. Our data suggest that this Plk1-PP6 interaction generates a feedback loop that coordinates and reinforces the activities of Plk1 and Aurora A during mitotic entry and is terminated by the degradation of Plk1 during mitotic exit.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277459	Ser787	KAPEKRAsPSKPASA	Homo sapiens	HeLa Cell
pmid	sentence
10791892	We have shown that MAP4 is phosphorylated in vivo in mitotic HeLa cells at eight sites. Five of these were phosphorylated by p34cdc2 kinase. Two of the five p34cdc2 kinase phosphorylation sites were shown to be Ser696 and Ser787 in the proline-rich region. Mutation of Ser787 to Glu strikingly reduced the MAP4's MT-polymerization activity, while Glu-mutation at Ser696 did not. These results suggest that Ser787 could be the critical phosphorylation site causing MTs to be dynamic at mitosis.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-280207	Ser80	QVIFCNRsPRVVLPV	Homo sapiens
pmid	sentence
36813923	Mechanistically, CDK1 directly phosphorylates pVHL at Ser80, which primes the recognition of pVHL by PIN1.\|PIN1 and CDK1 cooperatively modulate the protein turnover of pVHL, thereby conferring tumor growth, chemotherapeutic resistance and metastasis both in vitro and in vivo.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277836	Ser80	QVIFCNRsPRVVLPV	Homo sapiens	MDA-MB-231 Cell
pmid	sentence
36813923	Mechanistically, CDK1 directly phosphorylates pVHL at Ser80, which primes the recognition of pVHL by PIN1. PIN1 then binds to phosphorylated pVHL and facilitates the recruitment of the E3 ligase WSB1, therefore targeting pVHL for ubiquitination and degradation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-273584	Ser820	YSTFLTSsPIRSRSP	Homo sapiens
pmid	sentence
19386263	Phosphorylation of hCenexin1 at S796 is critical for the hCenexin1-Plk1 interaction.Here we show that a splice variant of hODF2 called hCenexin1, but not hODF2 itself, efficiently localizes to somatic centrosomes via a variant-specific C-terminal extension and recruits Plk1 through a Cdc2-dependent phospho-S796 motif within the extension. This interaction and Plk1 activity were important for proper recruitment of pericentrin and gamma-tubulin, and, ultimately, for formation of normal bipolar spindles.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-175692	Ser83	QQQQQETsPRQQQQQ	Homo sapiens	Prostate Gland Cancer Cell
pmid	sentence
21799006	At first, the data show that cdk5 enables phosphorylation of ar at ser-81 site through direct biochemical interaction and, therefore, results in the stabilization of ar proteins although ar was reported as substrates for cdk9 (5) as well as cdk1

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-139649	Ser86	TKNGLPGsRPGSPER	Homo sapiens
pmid	sentence
16103124	Moreover, app stabilized tip60 through cdk-dependent phosphorylation

Identifier	Residue	Sequence	Organism
SIGNOR-139653	Ser90	LPGSRPGsPEREVPA	Homo sapiens
pmid	sentence
16103124	Moreover, app stabilized tip60 through cdk-dependent phosphorylation

Publications:

2

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence
SIGNOR-267921	Ser91	EGMGEEPsPFRGRSR
pmid	sentence
24677263	CDK1-mediated Bcl-2 serine 70 phosphorylation enhances its pro-apoptotic function, whereas CDK1-mediated Bad serine 128 phosphorylation promotes apoptosis.

Publications:

1

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-134388	Ser96	SFSVKDPsPLYDMLR	Homo sapiens
pmid	sentence
15735705	Cdc2p34 phosphorylates mdmx on ser 96 in vitro. Mutation within this site (mdmx(s96a)) impairs, whereas phosphomimic substitution (mdmx(s96d)) increases the cytoplasmic localization of mdmx, suggesting that cdk2/cdc2p34 phosphorylation is required for export of mdmx from the nucleus

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-152133	Thr1063	VKQFDAStPKNDISP	Homo sapiens
pmid	sentence
17218258	Following phosphorylation of pich on the cdk1 site t1063, plk1 is recruited to pich and controls its localization. Starting in prometaphase, pich accumulates at kinetochores and inner centromeres.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-265994	Thr1161	FFNPVCAtPNSKILK	Homo sapiens
pmid	sentence
29771379	Identification of Cdk phosphorylation of Kif4A at T1161 in early mitosis. We show that Cdk phosphorylation of Kif4A licenses its chromosome localization.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-275588	Thr120	HKFNVTGtPEQYVPY
pmid	sentence
24746669	Here, we show that a fraction of cyclin B1/Cdk1 proteins localizes to the matrix of mitochondria and phosphorylates a cluster of mitochondrial proteins, including the complex I (CI) subunits in the respiratory chain. Cyclin B1/Cdk1-mediated CI phosphorylation enhances CI activity, whereas deficiency of such phosphorylation in each of the relevant CI subunits results in impairment of CI function.\|These results were confirmed by generating phosphorylation defective forms of the five CI subunits through substitutions of S/T residues with Alanine (A) on either Cdk1 optimal or minimal consensus motifs (T383 on NDUFV1, S105 on NDUFV3, S364 on NDUFS2, S55/S29/T5 on NDUFB6, and T142/T120 on NDUFA12). The mutation of Cdk1 consensus motifs severely diminished their phosphorylation

Identifier	Residue	Sequence
SIGNOR-275587	Thr142	QEWIPPStPYK
pmid	sentence
24746669	Here, we show that a fraction of cyclin B1/Cdk1 proteins localizes to the matrix of mitochondria and phosphorylates a cluster of mitochondrial proteins, including the complex I (CI) subunits in the respiratory chain. Cyclin B1/Cdk1-mediated CI phosphorylation enhances CI activity, whereas deficiency of such phosphorylation in each of the relevant CI subunits results in impairment of CI function.\|These results were confirmed by generating phosphorylation defective forms of the five CI subunits through substitutions of S/T residues with Alanine (A) on either Cdk1 optimal or minimal consensus motifs (T383 on NDUFV1, S105 on NDUFV3, S364 on NDUFS2, S55/S29/T5 on NDUFB6, and T142/T120 on NDUFA12). The mutation of Cdk1 consensus motifs severely diminished their phosphorylation

Publications:

2

Identifier	Residue	Sequence	Organism
SIGNOR-68544	Thr121	YKEQPLKtPGKKKKG	Homo sapiens
pmid	sentence
10373465	Phosphorylation at the cyclin-dependent kinases site (thr85) of parathyroid hormone-related protein negatively regulates its nuclear localization

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-141621	Thr125	PEVLRPEtPRPVDIG	Homo sapiens
pmid	sentence
16287866	Here, we show that the apoptotic initiator protease caspase-9 is regulated during the cell cycle through periodic phosphorylation at an inhibitory site, thr125. This site is phosphorylated by cdk1/cyclin b1 during mitosis and in response to microtubule poisons that arrest cells at this stage of the cell cycle.

Identifier	Residue	Sequence	Organism
SIGNOR-154626	Thr125	PEVLRPEtPRPVDIG	Homo sapiens
pmid	sentence
17466630	Here, we show that the apoptotic initiator protease caspase-9 is regulated during the cell cycle through periodic phosphorylation at an inhibitory site, thr125. This site is phosphorylated by cdk1/cyclin b1 during mitosis and in response to microtubule poisons that arrest cells at this stage of the cell cycle.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-275419	Thr128	RPPQKCStPCGPLRL	Homo sapiens	HeLa Cell
pmid	sentence
24413556	Phosphorylation by Cyclin B-Cdk1 allows Haspin to bind Plk1-PBD. Phosphorylation of Haspin at T128 and Plk1 target sites is required for full H3T3ph generation and normal Aurora B localization in mitosis.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-170882	Thr135	TVQQHPStPKRHTVL	Homo sapiens	HEK-293 Cell
pmid	sentence
21209322	High nacl-induced activation of cdk5 increases phosphorylation of the osmoprotective transcription factor tonebp/orebp at threonine 135, which contributes to its rapid nuclear localization. we performed in vitro kinase assays using the tonebp/orebp peptide containing t135 as substrate (figure 3b, right panel) and various recombinant kinases. The peptide is strongly phosphorylated by cdk5, less by cdk1.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-186617	Thr14	IEKIGEGtYGVVYKG	Homo sapiens
pmid	sentence
19574738	Cdk1/cdc2 activation involves tyr15/thr14 dephosphorylation by cdc25c

Identifier	Residue	Sequence	Organism
SIGNOR-186621	Tyr15	EKIGEGTyGVVYKGR	Homo sapiens
pmid	sentence
19574738	Cdk1/cdc2 activation involves tyr15/thr14 dephosphorylation by cdc25c

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-276969	Thr14	IEKIGEGtYGVVYKG	Homo sapiens
pmid	sentence
25384584	CDC25B facilitates dephosphorylation of the key cell cycle regulator CDC2 (also called CDK1) at Tyr15 or Thr14, thereby initiating the G 2 /M transition ( xref ).\|CDC25B facilitates dephosphorylation of the key cell cycle regulator CDC2 (also called CDK1) at Tyr15 or Thr14, thereby initiating the G2/M transition ( ).

Identifier	Residue	Sequence	Organism
SIGNOR-276970	Tyr15	EKIGEGTyGVVYKGR	Homo sapiens
pmid	sentence
25384584	CDC25B facilitates dephosphorylation of the key cell cycle regulator CDC2 (also called CDK1) at Tyr15 or Thr14, thereby initiating the G 2 /M transition ( xref ).\|CDC25B facilitates dephosphorylation of the key cell cycle regulator CDC2 (also called CDK1) at Tyr15 or Thr14, thereby initiating the G2/M transition ( ).

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248479	Thr14	IEKIGEGtYGVVYKG	Homo sapiens
pmid	sentence
10454565	Phosphatase activity of Cdc25A is critical for its activating capacity (data not shown). In this context, it should also be mentioned that Cdc25A is able to activate cyclin B-Cdk1 in vitro

Identifier	Residue	Sequence	Organism
SIGNOR-248480	Tyr15	EKIGEGTyGVVYKGR	Homo sapiens
pmid	sentence
10454565	Phosphatase activity of Cdc25A is critical for its activating capacity (data not shown). In this context, it should also be mentioned that Cdc25A is able to activate cyclin B-Cdk1 in vitro

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-276945	Thr14	IEKIGEGtYGVVYKG	Homo sapiens
pmid	sentence
17634129	The activity of Cdc2 is regulated by the phosphatase Cdc25C. Dephosphorylation of Cdc2 at threonine 14 and tyrosine 15 by Cdc25C results in activation of Cdc2 and initiation of an autoactivation loop between Cdc25C and Cdc2 that efficiently drives cells into mitosis.\|Cdc2 is activated by Cdc25C that removes phosphate groups from tyrosine 15 and threonine 14 .\|Dephosphorylation of Cdc2 at threonine 14 and tyrosine 15 by Cdc25C results in activation of Cdc2 and initiation of an autoactivation loop between Cdc25C and Cdc2 that efficiently drives cells into mitosis.

Identifier	Residue	Sequence	Organism
SIGNOR-276944	Tyr15	EKIGEGTyGVVYKGR	Homo sapiens
pmid	sentence
24643073	At the onset of mitosis, the protein phosphatase Cdc25C activates the Cdc2 and cyclin B1 complex by removing the inhibitory phosphate groups from Thr 14 and Tyr 15 on Cdc2.\|Dephosphorylation of Tyr15 of Cdc2 is catalyzed by Cdc25C phosphatases, and this reaction is believed to be the rate limited step for the entrance into mitosis .

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-45725	Thr14	IEKIGEGtYGVVYKG	Homo sapiens	HeLa Cell
pmid	sentence
9001210	Myt1hu preferentially phosphorylates cdc2 on threonine 14 in a cyclin-dependent manner;phosphorylation of threonine 14 and tyrosine 15 is inhibitory.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-45729	Tyr15	EKIGEGTyGVVYKGR	Homo sapiens	HeLa Cell
pmid	sentence
9001210	Myt1hu preferentially phosphorylates cdc2 on threonine 14 in a cyclin-dependent manner;phosphorylation of threonine 14 and tyrosine 15 is inhibitory.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-165768	Thr159	DGSEPTKtPGRTSST	Homo sapiens
pmid	sentence
20513426	We show that vps34 is phosphorylated on thr159 by cdk1, thr159 phosphorylation negatively regulates the ptdins3 kinase activity of vps34 and autophagy

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-38307	Thr161	GIPIRVYtHEVVTLW	Homo sapiens
pmid	sentence
8344251	The mo15 gene encodes the catalytic subunit of a protein kinase that activates cdc2 and other cyclin-dependent kinases (cdks) through phosphorylation of thr161 and its homologues

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-262695	Thr1644	VKHPGCTtPVTVKIP	Homo sapiens
pmid	sentence
11470801	Here we report the identification of a novel KRP, termed KRMP1, which undergoes in vivo phosphorylation. The carboxyl-terminal globular tail domain is strongly phosphorylated by mitotic kinase activities almost attributed to cdc2 kinase, which is responsible for phosphorylation on residue Thr-1604 of KRMP1.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276884	Thr176	HLFGFPPtPPKEVSP	Homo sapiens	HEK-293 Cell
pmid	sentence
25670854	GATA2 contains a cell division control protein 4 (Cdc4) phosphodegron (CPD), a consensus motif for ubiquitylation by Fbw7, which includes Thr(176). Ectopic expression of Fbw7 destabilized GATA2 and promoted its proteasomal degradation. Substitution of threonine 176 to alanine in GATA2 inhibited binding with Fbw7, and the ubiquitylation and degradation of GATA2 by Fbw7 was suppressed. The CPD kinase, which mediates the phosphorylation of Thr(176), was cyclin B-cyclin-dependent kinase 1 (CDK1).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-278472	Thr177	HCISTEFtPRKHGGE	Homo sapiens
pmid	sentence
31709755	In addition, overexpression of TFCP2L1 and CDK1 in T24 cells increased clonogenic activity in a clonogenic limiting dilution assay (Fig\u00a05H), confirming the importance of CDK1\u2010TFCP2L1 pathways for the stemness features of BC cells.High levels of co\u2010expression of p\u2010TFCP2L1 and CDK1 were associated with distant metastasis in our cohort of BC patients (Table\u00a01).\|Tfcp2l1 Thr177 phosphorylation by CDK1 is essential for proliferation and cell cycle progression of ESCs.\|Tfcp2l1 is phosphorylated at Thr177 by CDK1.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-264777	Thr186	KTMKGSStPVKN	in vitro
pmid	sentence
23455152	Here, we show that the p27/p25 heterodimer undergoes mitotic phosphorylation by cyclin‐dependent kinase 1 (Cdk1) at a single site, p27 Thr186, to generate an anchoring site for polo‐like kinase 1 (Plk1) at kinetochores.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-80230	Thr187	NAGSVEQtPKKPGLR	Homo sapiens
pmid	sentence
10931950	Phosphorylation of kip1 on thr-187, by cdk1 and cdk2 leads to protein ubiquitination and proteasomal degradation.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-100877	Thr19	GSRRGRAtPAQTPRS	Homo sapiens	HeLa Cell
pmid	sentence
12714602	We report here that human mcm4, a subunit of the putative dna replicative helicase, is extensively phosphorylated in hela cells when they are incubated in the presence of inhibitors of dna synthesis or are exposed to uv irradiation. The data presented here indicate that the consecutive actions of atr-chk1 and cdk2 kinases are involved in this phosphorylation in the presence of hydroxyurea. Phosphorylation of t19 correlates with lowered level of dna helicase activity of the purified mcm4,6,7 complex.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-243414	Thr194	NMMDILTtPSMAKPR	Xenopus laevis
pmid	sentence
22354989	We propose a model in which the initiating event for Gwl activation is phosphorylation by MPF of the proline-directed sites T193 and T206 in the presumptive activation loop

Identifier	Residue	Sequence	Organism
SIGNOR-249653	Thr207	PRQDYSRtPGQVLSL	Xenopus laevis
pmid	sentence
22354989	We propose a model in which the initiating event for Gwl activation is phosphorylation by MPF of the proline-directed sites T193 and T206 in the presumptive activation loop

Publications:

2

Organism:

Xenopus Laevis

Identifier	Residue	Sequence	Organism
SIGNOR-89605	Thr199	VKKSIRDtPAKNAQK	Homo sapiens
pmid	sentence
12058066	However, under the experimental conditions used here, the t199 residue was the most likely candidate to be phosphorylated by cyclin b/cdc2 these results strongly support the concept that the rna binding activity of b23.1 is inactivated by cyclin b/cdc2-mediated phosphorylation.

Identifier	Residue	Sequence	Organism
SIGNOR-235530	Thr234	SFKKQEKtPKTPKGP	Mus musculus
pmid	sentence
11278991	CDK1-cyclin B phosphorylates NPM/B23 on Thr234.

Identifier	Residue	Sequence	Organism
SIGNOR-120330	Thr234	SFKKQEKtPKTPKGP	Homo sapiens
pmid	sentence
14670079	We have recently found that nucleophosmin (npm/b23), a phosphoprotein primarily found in nucleolus, associates with unduplicated centrosomes and is a direct substrate of cdk2-cyclin e in centrosome duplication.

Identifier	Residue	Sequence	Organism
SIGNOR-89597	Thr234	SFKKQEKtPKTPKGP	Homo sapiens
pmid	sentence
12058066	Both subtypes of B23 proteins were phosphorylated during mitosis by cyclin B/cdc2. The RNA binding activity of B23.1 was repressed through cyclin B/cdc2-mediated phosphorylation at specific sites in B23. Thus, the RNA binding activity of B23.1 is stringently modulated by its phosphorylation and subtype association.

Identifier	Residue	Sequence	Organism
SIGNOR-120334	Thr237	KQEKTPKtPKGPSSV	Homo sapiens
pmid	sentence
14670079	We further demonstrate that phospho-mkk1/mkk2 antibodies recognize npm on the c-terminal region, which is phosphorylated by cdc2 (cell division control kinase-2) during g2/m-phase. biochemical and immunocytochemistry analyses verified that the phospho-mkk1/mkk2 antibodies cross-reacted with npm that was phosphorylated at thr234 and thr237 during g2/m-phase, which are the same sites that are targeted by cdc2 (cell division cycle protein-2) during mitosis.

Identifier	Residue	Sequence	Organism
SIGNOR-89601	Thr237	KQEKTPKtPKGPSSV	Homo sapiens
pmid	sentence
12058066	Both subtypes of B23 proteins were phosphorylated during mitosis by cyclin B/cdc2. The RNA binding activity of B23.1 was repressed through cyclin B/cdc2-mediated phosphorylation at specific sites in B23. Thus, the RNA binding activity of B23.1 is stringently modulated by its phosphorylation and subtype association.

Publications:

6

Organism:

Homo Sapiens, Mus Musculus

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-141565	Thr204	LTRYTRPtPVQKHAI	Homo sapiens
pmid	sentence
16280325	Thr204 to glu204 ddx3 mutant protein lost its function, suggesting that phosphorylation at thr204 affects ddx3 function. Thr204 was phosphorylated by cyclin b/cdc2. Thr323 in motif ib was also phosphorylated by cyclin b/cdc2 kinase. We propose a novel function of cyclin b/cdc2 kinase in mitosis, which is to cause a loss of ddx3 function to repress cyclin a expression and to decrease ribosome biogenesis and translation during mitosis.

Identifier	Residue	Sequence	Organism
SIGNOR-141569	Thr323	GCHLLVAtPGRLVDM	Homo sapiens
pmid	sentence
16280325	Thr204 to glu204 ddx3 mutant protein lost its function, suggesting that phosphorylation at thr204 affects ddx3 function. Thr204 was phosphorylated by cyclin b/cdc2. Thr323 in motif ib was also phosphorylated by cyclin b/cdc2 kinase. We propose a novel function of cyclin b/cdc2 kinase in mitosis, which is to cause a loss of ddx3 function to repress cyclin a expression and to decrease ribosome biogenesis and translation during mitosis.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-194825	Thr2055	MAFSILNtPKKLGNS	Homo sapiens
pmid	sentence
23921553	Cdk1-mediated phosphorylation at t2055 negatively regulates numa cortical localization and that this phosphorylation is counteracted by ppp2ca phosphatase activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273889	Thr210	SEYSMAEtLVGTPYY	Homo sapiens	HeLa Cell
pmid	sentence
21642957	We now identify Plk1 as Nek9 direct activator and propose a two-step activation mechanism that involves Nek9 sequential phosphorylation by CDK1 and Plk1. while CDK1 activity is necessary for Nek9 phosphorylation in mitosis and the resulting change in electrophoretical mobility, Nek9 Thr210 phosphorylation and mitotic activation requires both CDK1 and Plk1.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-176131	Thr221	KDEILPTtPISEQKG	Homo sapiens
pmid	sentence
21871177	These results suggest that the phosphorylation of rps3 by cdk1 occurs at thr221 during g2/m phase and, moreover, that this event is important for nuclear accumulation of rps3.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-262696	Thr238	QGPTPVCtPTFLERR	in vitro
pmid	sentence
16244663	The forkhead-associated (FHA) domain of human Ki67 interacts with the human nucleolar protein hNIFK, recognizing a 44-residue fragment, hNIFK226-269, phosphorylated at Thr234. Here we show that high-affinity binding requires sequential phosphorylation by two kinases, CDK1 and GSK3, yielding pThr238, pThr234 and pSer230. phosphorylation of Thr234 by GSK3 proceeds only after Thr238 is already phosphorylated by CDK1.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-265032	Thr244	AETHSSStPVQHPIK	Homo sapiens	HeLa Cell
pmid	sentence
30021153	Cyclin-dependent kinase 1 (Cdk1) phosphorylates WAC, priming its direct interaction with the polo-box domain of Plk1. Knockdown of WAC compromises Plk1 activity and delays mitotic entry.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-265035	Thr457	YVSPRIStPQTNTVP	Homo sapiens	HeLa Cell
pmid	sentence
30021153	Cyclin-dependent kinase 1 (Cdk1) phosphorylates WAC, priming its direct interaction with the polo-box domain of Plk1. Knockdown of WAC compromises Plk1 activity and delays mitotic entry.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-265034	Thr471	PIKPLIStPPVSSQP	Homo sapiens	HeLa Cell
pmid	sentence
30021153	Cyclin-dependent kinase 1 (Cdk1) phosphorylates WAC, priming its direct interaction with the polo-box domain of Plk1. Knockdown of WAC compromises Plk1 activity and delays mitotic entry.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-265033	Thr482	SSQPKVStPVVKQGP	Homo sapiens	HeLa Cell
pmid	sentence
30021153	Cyclin-dependent kinase 1 (Cdk1) phosphorylates WAC, priming its direct interaction with the polo-box domain of Plk1. Knockdown of WAC compromises Plk1 activity and delays mitotic entry.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277517	Thr249	AAPEPERtPVGQGSW	Homo sapiens	HeLa Cell
pmid	sentence
32214089	Here we report that hTERT is phosphorylated at threonine 249 during mitosis by the serine/threonine kinase CDK1.These observations indicate that phosphorylation at threonine 249 regulates hTERT RdRP and contributes to cancer progression in a telomere independent manner.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277832	Thr27	VCQEVLKtPVRTTAC	Homo sapiens	HEK-293 Cell
pmid	sentence
38309501	Altogether, our results suggest RNF138 is phosphorylated at position T27 in a CDK1- and CDK2-dependent manner.Altogether, our results suggest RNF138 is phosphorylated at position T27 in a CDK1- and CDK2-dependent manner.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-36112	Thr286	VEGDAAEtPPRPRTP	Homo sapiens
pmid	sentence
8114697	P34cdc2 catalyzes the in vitro phosphorylation of mkk1 on both of these threonine residues and inactivates mkk1 enzymatic activity. Both sites are phosphorylated in vivo as well

Identifier	Residue	Sequence	Organism
SIGNOR-36116	Thr292	ETPPRPRtPGRPLSS	Homo sapiens
pmid	sentence
8114697	P34cdc2 catalyzes the in vitro phosphorylation of mkk1 on both of these threonine residues and inactivates mkk1 enzymatic activity. Both sites are phosphorylated in vivo as well

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-275470	Thr287	KIGFPSTtPAKAKAN
pmid	sentence
19687009	Cdc2 phosphorylates T287\|CLIP-170, the founding member of microtubule “plus ends tracking” proteins, is involved in many critical microtubule-related functions, including recruitment of dynactin to the microtubule plus ends and formation of kinetochore-microtubule attachments during metaphase. \|These results demonstrate that Cdc2-mediated phosphorylation of CLIP-170 is essential for the normal function of this protein during cell cycle progression.

Publications:

1

Identifier	Residue	Sequence	Organism
SIGNOR-177545	Thr300	HKRSLTKtPARKSAH	Homo sapiens
pmid	sentence
22101338	We report here that cdk1 phosphorylates nusap at threonine 300 and 338 in early mitosis. Phosphorylation of nusap inhibits its microtubule-binding activity in vitro and in vivo.

Identifier	Residue	Sequence	Organism
SIGNOR-177549	Thr338	GNSAAVItPFKLTTE	Homo sapiens
pmid	sentence
22101338	We report here that cdk1 phosphorylates nusap at threonine 300 and 338 in early mitosis. Phosphorylation of nusap inhibits its microtubule-binding activity in vitro and in vivo.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-51275	Thr317	RGALVRGtPVRGAIT	Homo sapiens
pmid	sentence
9315091	Phosphorylation of sam68 by purified cdc2.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-151799	Thr320	NPGGRPItPPRNSAK	Homo sapiens
pmid	sentence
12202491	Both of these pp1 isoforms contain an arg-pro-ile/val-thr-pro-pro-arg sequence near the c terminus, a known site of phosphorylation by cdc/cdk kinases, and phosphorylation attenuates phosphatase activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-197630	Thr33	SLVDKENtPPALSGT	Homo sapiens
pmid	sentence
22632967	We found that, during g2, following cdk-mediated phosphorylation of thr33, rrm2 is degraded via scf(cyclin f) to maintain balanced dntp pools and genome stability.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-115129	Thr34	FLEGCACtPERMAEA	Homo sapiens
pmid	sentence
11861764	Survivin is a member of the inhibitor of apoptosis gene family that has been implicated in both apoptosis inhibition and regulation of mitosisin synchronized cultures, cytosolic survivin abruptly increased at mitosis, physically associated with p34(cdc2), and was phosphorylated by p34(cdc2) on thr(34), in vivo

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-174054	Thr345	LTAERIKtPPKRPGG	Homo sapiens
pmid	sentence
21659531	Cdk1, which phosphorylates ezh2 at threonines 345 and 487.Phosphorylation of thr-345 and thr-487 promotes ezh2 ubiquitination and subsequent degradation by the proteasome

Identifier	Residue	Sequence	Organism
SIGNOR-174058	Thr487	APAEDVDtPPRKKKR	Homo sapiens
pmid	sentence
21659531	Cdk1, which phosphorylates ezh2 at threonines 345 and 487.Phosphorylation of thr-345 and thr-487 promotes ezh2 ubiquitination and subsequent degradation by the proteasome

Publications:

2

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-265263	Thr346	LEEGVHLtPFRQKVS	Homo sapiens
pmid	sentence
24055156	The complex between shugoshin and protein phosphatase 2A (Sgo1-PP2A) localizes to centromeres in mitosis, binds to cohesin in a reaction requiring Cdk-dependent phosphorylation of Sgo1, dephosphorylates cohesin-bound sororin, and protects a centromeric pool of cohesin from mitotic kinases and the cohesin inhibitor Wapl.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-278376	Thr358	SYENLLRtPTPPEVT	Homo sapiens
pmid	sentence
28479321	Cdk1 treatment further enhanced the binding of Ska3 2D to Ndc80, suggesting that phosphorylation of other Cdk1 sites in Ska3 further contributes to the Ndc80C-Ska3 interaction, although this contribution is not apparent in our kinetochore localization assay.We next purified the GST-Ndc80C Bonsai construct that lacks the loop region of Ndc80 as well as the coiled coil regions of Ndc80C [17].\|Thus, Ska3 can be phosphorylated by Cdk1 on T358 and T360 sites in vitro.We next tested whether Ska3 was required for Ska1 or Ska2 localization.

Identifier	Residue	Sequence	Organism
SIGNOR-278375	Thr360	ENLLRTPtPPEVTKI	Homo sapiens
pmid	sentence
28479321	Cdk1 treatment further enhanced the binding of Ska3 2D to Ndc80, suggesting that phosphorylation of other Cdk1 sites in Ska3 further contributes to the Ndc80C-Ska3 interaction, although this contribution is not apparent in our kinetochore localization assay.We next purified the GST-Ndc80C Bonsai construct that lacks the loop region of Ndc80 as well as the coiled coil regions of Ndc80C [17].\|Thus, Ska3 can be phosphorylated by Cdk1 on T358 and T360 sites in vitro.We next tested whether Ska3 was required for Ska1 or Ska2 localization.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-140549	Thr373	VSMLSLNtPNSNRKR	Homo sapiens
pmid	sentence
16170345	We show that phosphorylation of ect2 at threonine-341 (t341) affects the autoregulatory mechanism of ect2. In g2/m phase, ect2 was phosphorylated at t341 most likely by cyclin b/cyclin-dependent kinase 1 (cdk1) ect2 is biologically active even when it is not phosphorylated at t341

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-78311	Thr376	QVAPRAGtPGFRAPE	Homo sapiens
pmid	sentence
10846177	Hucdc7 and ask proteins can also be phosphorylated by cdks in vitro. Among four possible cdk phosphorylation sites of hucdc7, replacement of thr-376, corresponding to the activating threonine of cdk, with alanine (t376a mutant) dramatically reduces kinase activity, indicative of kinase activation by phosphorylation of this residue.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-275594	Thr383	HESCGQCtPCREGVD
pmid	sentence
24746669	Here, we show that a fraction of cyclin B1/Cdk1 proteins localizes to the matrix of mitochondria and phosphorylates a cluster of mitochondrial proteins, including the complex I (CI) subunits in the respiratory chain. Cyclin B1/Cdk1-mediated CI phosphorylation enhances CI activity, whereas deficiency of such phosphorylation in each of the relevant CI subunits results in impairment of CI function.\|These results were confirmed by generating phosphorylation defective forms of the five CI subunits through substitutions of S/T residues with Alanine (A) on either Cdk1 optimal or minimal consensus motifs (T383 on NDUFV1, S105 on NDUFV3, S364 on NDUFS2, S55/S29/T5 on NDUFB6, and T142/T120 on NDUFA12). The mutation of Cdk1 consensus motifs severely diminished their phosphorylation

Publications:

1

Identifier	Residue	Sequence	Organism
SIGNOR-143387	Thr412	DTEIANStPNPKPAA	Homo sapiens
pmid	sentence
16378098	Here, we report that cdk1 phosphorylates thr 59 and thr 388 on inner centromere protein (incenp), which regulates the localization and kinase activity of aurora-b from prophase to metaphase. The replacement of endogenous incenp with t388a resulted in the delay of progression from metaphase to anaphase.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-141175	Thr444	TKSSKSStPVPSKQS	Homo sapiens
pmid	sentence
16247472	Here we show that two mitotic kinases, cdk1 and polo-like kinase 1 (plk1), phosphorylate ect2 in vitro.Moreover, ect2 t412a, but not phosphomimic t412d, displayed a diminished accumulation of gtp-bound rhoa compared with wt ect2, suggesting that phosphorylation of thr-412 is critical for the catalytic activity of ect2.

Identifier	Residue	Sequence	Organism
SIGNOR-141179	Thr846	RAFSFSKtPKRALRR	Homo sapiens
pmid	sentence
16247472	Thr-814 to ala greatly diminished the ability of p34cdk1/cyclin b to phosphorylate recombinant ect2-c protein (figure 1b, left panel). These data suggest that thr-814 is a major cdk1 phosphorylation site in ect2-c in vitrothe sequence thr-pro-lys-arg (tpkr) starting at amino acid 814we found that the t814a mutation slightly reduces the exchange activity of ect2 on rac1

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-187766	Thr4539	GGLIEPDtPGRVPLD	Homo sapiens
pmid	sentence
19709076	Identification of plectin as a substrate of p34cdc2 kinase and mapping of a single phosphorylation site. threonine 4542 was identified as the major target for the kinase. Phosphorylation of plectin by cyclin-dependent kinase 1/cyclin b (cdk1/cycb) kinase has been reported to abolish its cross-linking function during mitosis. Here, we induced phosphorylation of plectin in prepared fractions of hela cells by adding activated cdk1/cycb kinase. Consequently, there was significant dissociation of the centrosome from the nuclear membrane.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-41319	Thr4539	GGLIEPDtPGRVPLD	Homo sapiens	HeLa Cell
pmid	sentence
8626512	Identification of plectin as a substrate of p34cdc2 kinase and mapping of a single phosphorylation site. threonine 4542 was identified as the major target for the kinase. Phosphorylation of plectin by cyclin-dependent kinase 1/cyclin b (cdk1/cycb) kinase has been reported to abolish its cross-linking function during mitosis. Here, we induced phosphorylation of plectin in prepared fractions of hela cells by adding activated cdk1/cycb kinase. Consequently, there was significant dissociation of the centrosome from the nuclear membrane.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-100964	Thr463	QGAPLLStPKRERMV	Homo sapiens
pmid	sentence
12727876	Cdc2-mediated phosphorylation of kid controls its distribution to spindle and chromosomes. We identify ser427 and thr463 as m phase-specific phosphorylation sites and cdc2-cyclin b as a thr463 kinase. Kid with a thr463 to alanine mutation fails to be localized on chromosomes and is only detected along spindles, although it retains the ability to bind dna or chromosomes

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-265504	Thr506	KESKLERtPQKNVQG	Chlorocebus aethiops	COS Cell
pmid	sentence
12930972	Phosphorylation of the PCNA binding domain of the large subunit of replication factor C on Thr506 by cyclin-dependent kinases regulates binding to PCNA\|Replication factor C (RF-C) complex binds to DNA primers and loads PCNA onto DNA, thereby increasing the processivity of DNA polymerases. \|Phosphorylation of either RF-Cp145 as a part of the RF-C complex or RF-Cp145 domain B by cdk-cyclin kinases inhibits their ability to bind PCNA.

Publications:

1

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-266387	Thr508	AQPPRTQtPPLGQTP	Homo sapiens	HEK-293 Cell
pmid	sentence
29530922	To test whether CDK1 phosphorylates T508, Flag-DAP5 was purified from dox-induced HEK293 cells and incubated with active recombinant JNK2 or CDK1 in the presence of ATP (Fig. 3G). DAP5(T508) was phosphorylated only upon incubation with CDK1 (Fig. 3G).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
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

Identifier	Residue	Sequence	Organism
SIGNOR-76837	Thr56	FSSQPGHtPHPAASR	Homo sapiens
pmid	sentence
10766756	Using synthetic peptides and mutant cell lines, we identified threonine 56, one of two consensus sites for cdc2 within the bcl-2 sequence, as a residue phosphorylated by cdc2. Mutation at threonine 56 abrogated the cell cycle inhibitory effect of bcl-2 without affecting anti-apoptotic function.Taken together, our present findings indicate that phosphorylation of bcl-2 at threonine 56 by cdc2 is required for bcl-2-mediated cell cycle inhibition, which may have some roles during mitosis in the normal cell cycle.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-119821	Thr565	NQGETPTtEVPAPFF	Homo sapiens
pmid	sentence
14657031	Apc activation is thought to depend on apc phosphorylation and cdc20 binding. We have identified 43 phospho_sites on apc of which at least 34 are mitosis specific. Of these, 32 sites are clustered in parts of apc1 and the tetratricopeptide repeat (tpr) subunits cdc27, cdc16, cdc23 and apc7. In vitro, at least 15 of the mitotic phospho_sites can be generated by cyclin_dependent kinase 1 (cdk1), and 3 by polo_like kinase 1 (plk1). Apc phosphorylation by cdk1, but not by plk1, is sufficient for increased cdc20 binding and apc activation

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-201913	Thr592	DVIAPLItPQKKEWN	Homo sapiens
pmid	sentence
23602554	Cyclin a2/cdk1 phosphorylates samhd1 at the threonine 592 residue both in vitro and in vivo. Phosphorylation of samhd1 thr592 correlates with loss of its ability to restrict hiv-1.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-147065	Thr609	SAAQLAStPFHKLPV	Homo sapiens
pmid	sentence
16760428	The plk1-bub1 interaction requires the polo-box domain (pbd) of plk1 and is enhanced by cyclin-dependent kinase 1 (cdk1)-mediated phosphorylation of bub1 at t609

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273523	Thr618	EEASSPStGQPSLCS	Homo sapiens	HEK-293 Cell
pmid	sentence
22405274	Cdk1 phosphorylation of Tex14 is required for the Tex14-Plk1 interaction

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273524	Thr727	SNLNNMStTEEYLIS	Homo sapiens	HEK-293 Cell
pmid	sentence
22405274	Cdk1 phosphorylation of Tex14 is required for the Tex14-Plk1 interaction

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273522	Thr728	NLNNMSTtEEYLISK	Homo sapiens	HEK-293 Cell
pmid	sentence
22405274	Cdk1 phosphorylation of Tex14 is required for the Tex14-Plk1 interaction

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-265258	Thr62	RRPESFTtPEGPKPR	Homo sapiens
pmid	sentence
18490441	Phosphorylation of threonine 61 by cyclin a/Cdk1 triggers degradation of stem-loop binding protein at the end of S phase

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-157642	Thr620	RAARFVStPFHEIMS	Homo sapiens
pmid	sentence
17785528	Here, we demonstrate that bubr1 is phosphorylated on the cdk1 site t620, which triggers the recruitment of plk1 and phosphorylation of bubr1 by plk1 both in vitro and in vivo. Phosphorylation does not appear to be required for spindle checkpoint function but instead is important for the stability of kinetochore-microtubule (kt-mt) interactions

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-185317	Thr623	FKELKFLtPVRRSRR	Homo sapiens
pmid	sentence
19369249	Among these, thr-622 was specifically phosphorylated by cdk1-cyclin b1 both in vitro and in vivo. these findings suggest that cdk1-cyclin b1-mediated phosphorylation of tmap is important for and contributes to proper regulation of microtubule dynamics and establishment of functional bipolar spindles during mitosis.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-110416	Thr70	RNSPVTKtPPRDLPT	Homo sapiens
pmid	sentence
11553333	Phosphorylation of 4e-bp1 is critical in causing its dissociation from eif-4e, leaving 4e available to form translationally active eif-4f complexes, switching on mrna translation. We show that the cyclin-dependent kinase, cdc2, phosphorylates 4e-bp1 at thr-70 and that phosphorylation of this site is permissive for ser-65 phosphorylation. Crucially, the increased phosphorylation of 4e-bp1 during mitosis results in its complete dissociation from eif-4e.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277837	Thr717	PSPKVIKtPVVKKTE	Homo sapiens	HeLa Cell
pmid	sentence
36967563	Mechanically, PTX and VCR activate cyclin-dependent kinase 1, which in turn induces MORC2 phosphorylation at threonine 717 (T717) and T733. Phosphorylated MORC2 enhances its interation with HSPA8 and LAMP2A, two essential components of the chaperone-mediated autophagy (CMA) mechinery, resulting in its autophagic degradation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277838	Thr733	PIKLSPAtPSRKRSV	Homo sapiens	HeLa Cell
pmid	sentence
36967563	Mechanically, PTX and VCR activate cyclin-dependent kinase 1, which in turn induces MORC2 phosphorylation at threonine 717 (T717) and T733. Phosphorylated MORC2 enhances its interation with HSPA8 and LAMP2A, two essential components of the chaperone-mediated autophagy (CMA) mechinery, resulting in its autophagic degradation.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
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

Identifier	Residue	Sequence	Organism
SIGNOR-47483	Thr736	VEVDPMLtPEERHLN	Homo sapiens
pmid	sentence
9109675	A cytoplasmic domain peptide from aplp2 is phosphorylated in vitro by protein kinase c and cdc2 kinase. Aplp2 is phosphorylated by cdc2 kinase at a site homologous to the cdc2 kinase site phosphorylated in app.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Brain

Identifier	Residue	Sequence	Organism
SIGNOR-163738	Thr739	SEGSGTAtPSALITT	Homo sapiens
pmid	sentence
20150555	Moreover, we showed that sp1 is a novel mitotic substrate of cdk1/cyclin b1 and is phosphorylated by it at thr 739 before the onset of mitosis.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Muscle, Smooth Muscle

Pathways:

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-271839	Thr767	ESFKRLVtPRKKSKS	Homo sapiens	HEK-293 Cell
pmid	sentence
23063527	Mass spectrometry, molecular, and cellular approaches show that CDK1/Cyclin B1 phosphorylates Gravin on threonine 766 to prime the recruitment of the polo-like kinase Plk1 at defined phases of mitosis.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-265501	Thr77	SSSCGKDtPSKKRKL	Homo sapiens	HEK-293 Cell
pmid	sentence
26942677	We report that CDK1-cyclin B1 phosphorylates the RNMT regulatory domain on T77 during G2/M phase of the cell cycle. RNMT T77 phosphorylation activates the enzyme both directly and indirectly by inhibiting interaction with KPNA2, an RNMT inhibitor.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-160743	Thr85	TRSQQQPtPVTPKKY	Homo sapiens
pmid	sentence
18250300	Here, we show that the interaction between plk1 and hbo1 is mitosis-specific and that plk1 phosphorylates hbo1 on ser-57 in vitro and in vivo. During mitosis, cdk1 phosphorylates hbo1 on thr-85/88, creating a docking site for plk1 to be recruited. Significantly, the overexpression of hbo1 mutated at the plk1 phosphorylation site (s57a) leads to cell-cycle arrest in the g1/s phase, inhibition of chromatin loading of the minichromosome maintenance (mcm) complex, and a reduced dna replication rate.

Identifier	Residue	Sequence	Organism
SIGNOR-160747	Thr88	QQQPTPVtPKKYPLR	Homo sapiens
pmid	sentence
18250300	Here, we show that the interaction between plk1 and hbo1 is mitosis-specific and that plk1 phosphorylates hbo1 on ser-57 in vitro and in vivo. During mitosis, cdk1 phosphorylates hbo1 on thr-85/88, creating a docking site for plk1 to be recruited. Significantly, the overexpression of hbo1 mutated at the plk1 phosphorylation site (s57a) leads to cell-cycle arrest in the g1/s phase, inhibition of chromatin loading of the minichromosome maintenance (mcm) complex, and a reduced dna replication rate.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-99742	Thr86	AASASPYtPEHAASV	Homo sapiens
pmid	sentence
12676926	Cyclin-dependent kinases phosphorylate p73 at threonine 86 in a cell cycle-dependent manner and negatively regulate p73.Furthermore, cyclin a/cdk1/2, cyclin b/cdk1/2, and cyclin e/cdk2 complexes can phosphorylate multiple p73 isoforms in vitro at threonine 86.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-130439	Thr9	EGISNFKtPSKLSEK	Homo sapiens
pmid	sentence
15541388	Topk-thr-9 was phosphorylated by cdk1/cyclin b and topk significantly associates with mitotic spindles.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-87097	Thr90	CHLAWVNtPKKQGGL	Homo sapiens
pmid	sentence
11986303	Peroxiredoxin (prx) i is a member of the peroxiredoxin family of peroxidases and contains a consensus site (thr(90)-pro-lys-lys) for phosphorylation by cyclin-dependent kinases (cdks). This protein has now been shown to be phosphorylated specifically on thr(90) by several cdks, including cdc2, in vitro. Phosphorylation of prx i on thr(90) reduced the peroxidase activity of this protein by 80%.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-165867	Thr92	EVPDVTAtPARLLFF	Homo sapiens
pmid	sentence
20526282	Mcl-1 is phosphorylated at two sites in mitosis, ser64 and thr92. Phosphorylation of thr92 by cyclin-dependent kinase 1 (cdk1)-cyclin b1 initiates degradation of mcl-1 in cells arrested in mitosis by microtubule poisons.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-273887	Thr926	LDIPTGTtPQRKSYL	Homo sapiens
pmid	sentence
19001501	Nek6 phosphorylated Eg5 at several sites in vitro and one of these sites, Ser1033, is phosphorylated in vivo during mitosis. Whereas CDK1 phosphorylates nearly all Eg5 at Thr926 during mitosis, Nek6 phosphorylates approximately 3% of Eg5, primarily at the spindle poles.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-50169	Thr926	LDIPTGTtPQRKSYL	Homo sapiens
pmid	sentence
9235942	The kinesin-related motor hseg5 is essential for centrosome separation, and its association with centrosomes appears to be regulated by phosphorylation of tail residue threonine 927 by the p34(cdc2) protein kinase.Phosphorylation also enhanced the specific binding of p150(glued) to the tail domain of hseg5 in vitro

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-88671	Tyr15	EKIGEGTyGVVYKGR	Homo sapiens
pmid	sentence
12049736	Phosphorylation on tyrosine-15 of p34(cdc2) by erbb2 inhibits p34(cdc2) activation and is involved in resistance to taxol-induced apoptosis

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-279134	Tyr15	EKIGEGTyGVVYKGR	Homo sapiens
pmid	sentence
11029659	Recombinant Wee1B effectively phosphorylated cyclin B-associated Cdk1 on tyrosine-15, resulting in an inactivation of the kinase activity of Cdk1.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-139491	Tyr15	EKIGEGTyGVVYKGR	Homo sapiens
pmid	sentence
16096060	The wee1 kinase phosphorylates and inhibits cyclin-dependent kinase 1 (cdk1), thereby delaying entry into mitosis until appropriate conditions have been met

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-164809	Tyr4	yTKIEKIG	Homo sapiens
pmid	sentence
20395957	Our findings demonstrate that (i) pkr, ser/thr kinase, phosphorylates its new substrate cdc2 at the tyr 4 residue, (ii) pkr-mediated tyr 4-phosphorylation facilitates cdc2 ubiquitination and proteosomal degradation

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-267987		Homo sapiens	KB-3-1 Cell
pmid	sentence
19917720	Cyclin-Dependent Kinase 1-Mediated Bcl-xL/Bcl-2 Phosphorylation Acts as a Functional Link Coupling Mitotic Arrest and Apoptosis\|These findings suggest a model whereby a switch in the duration of CDK1 activation, from transient during mitosis to sustained during mitotic arrest, dramatically increases the extent of Bcl-xL/Bcl-2 phosphorylation, resulting in inactivation of their antiapoptotic function. Thus, phosphorylation of antiapoptotic Bcl-2 proteins acts as a sensor for CDK1 signal duration and as a functional link coupling mitotic arrest to apoptosis.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Organism
SIGNOR-128442		Homo sapiens
pmid	sentence
15340381	P21 and p27 are key inhibitors of both cdk1 and cdk2.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Organism	Cell Line
SIGNOR-261284		Homo sapiens	HeLa Cell
pmid	sentence
1902553	We now present biochemical evidence for a mitosis-specific p34cdc2 phosphorylation of RablAp and Rab4p.We also show that the distribution of RablAp and Rab4p between cytosolic and membrane-bound forms is different in interphase and mitotic cells.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-68221		Homo sapiens
pmid	sentence
10362260	Gadd45 has now been found to directly inhibit the activity of cdc2/cyclin b1 complex

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-191322		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-277162		Homo sapiens
pmid	sentence
18347064	PP4c efficiently dephosphorylates Cdk1 sites of NDEL1 but does not dephosphorylate the Aurora A site.\|We also found that PP4c negatively regulates Cdk1 activity in interphase.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-128445		Homo sapiens
pmid	sentence
15340381	P21 and p27 are key inhibitors of both cdk1 and cdk2.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Organism
SIGNOR-190431		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-205593		Homo sapiens
pmid	sentence
25603287	The central mitotic kinase, cyclin-dependent kinase-1 (human cdk1 is present through all stages of the cell cycle, but its activity is cell-cycle regulated by phosphorylation/dephosphorylation and cyclin binding.Cdk1-cyclin b phosphorylates ser/thr residues directly preceding pro; thus, it is classified as a proline-directed kinase.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-146734		Homo sapiens
pmid	sentence
16682949	We found that nde1 is subjected to phosphorylation in vivo. In particular, we identified six putative cdc2 phosphorylation sites in nde1 and found that alteration of these sites diminishes phosphorylation by cdc2 in vitro and affects the stability of su48-nde1 interactions and the centrosomal localization of nde1.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-262726		Homo sapiens	Aortic Smooth Muscle
pmid	sentence
11687586	RGC-32 was physically associated with cyclin-dependent kinase p34CDC2 and increased the kinase activity in vivo and in vitro. In addition, RGC-32 was phosphorylated by p34CDC2-cyclin B1 in vitro. Mutation of RGC-32 protein at Thr-91 prevented the p34CDC2-mediated phosphorylation and resulted in loss of p34CDC2 kinase enhancing activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-200400		Homo sapiens
pmid	sentence
23314252	We show here that eco1 degradation requires the sequential actions of cdk1 and two additional kinases , cdc7-dbf4 and the gsk-3 homolog mck1.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-279598		Homo sapiens
pmid	sentence
30816115	In this study, we found that Cdk1 phosphorylated DIAPH1, which inhibited the interaction between DIAPH1 and profilin1 (PFN1) during metaphase.\|Thus, the results suggest that the level of cortical F-actin has to be finely maintained by Cdk1 mediated positive and negative regulation of DIAPH1.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-264878
pmid	sentence
30925160	CK1a1, JNK1 and CDK1 had the highest site-specific activity for ORP4L, while CDK1, GSK3a, CK1a1 and GSK3b showed the highest specificity for the site when corrected for background activity with ORP4L-S4A. Because of the complexity of the serine/proline-rich site, we did not determine which serine(s) in ORP4L were phosphorylated by candidate kinases.\|We conclude that phosphorylation of a unique serine/proline motif in the ORD induces a conformation change in ORP4L that enhances interaction with vimentin and cholesterol extraction from membranes.

Publications:

1

Identifier	Residue	Organism
SIGNOR-206124		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-279601		Homo sapiens
pmid	sentence
21473853	MT-polymerizing activity was decreased from samples with DDA3 phosphorylated by Cdk1 ( xref , lanes 4 vs 6) and Aurora A ( xref , lanes 14 vs 16).\|Taken together, the mitotic Cdk1 and Aurora A kinases inhibit MT polymerization activities and MT bundling activities of DDA3.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-275617
pmid	sentence
37197505	CDK2 is the predominant activating complex form of CCNO, but CCNO can bind to CDK1 to form an activating complex in the absence of CDK2.

Publications:

1

Identifier	Residue	Organism
SIGNOR-244847		Homo sapiens
pmid	sentence
8114697	P34cdc2 catalyzes the in vitro phosphorylation of mkk1 on both of these threonine residues and inactivates mkk1 enzymatic activity. Both sites are phosphorylated in vivo as well

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Organism
SIGNOR-279012		Homo sapiens
pmid	sentence
30154440	Therefore, CDK1 may trigger CFP1 degradation through some indirect mechanisms rather than CFP1 phosphorylation.\|This result suggests that, although CDK1 triggers both phosphorylation and degradation of CFP1 protein, phosphorylation of CFP1 by CDK1 is not a prerequisite for its degradation during cell division.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-259792		in vitro
pmid	sentence
22037378	Our data set represents the most detailed comprehensive assessment of the reactivity of known and clinical kinase inhibitors across the kinome published to date. \| The data also show that for at least 15 of the 27 kinases that are the primary, intended targets for the compounds tested and that are represented in the assay panel, selective inhibitors, as assessed by both absolute selectivity across the kinome and selectivity relative to the primary target, are among the 72 tested here.

Identifier	Residue	Organism
SIGNOR-258272		in vitro
pmid	sentence
22037378	Our data set represents the most detailed comprehensive assessment of the reactivity of known and clinical kinase inhibitors across the kinome published to date. \| The data also show that for at least 15 of the 27 kinases that are the primary, intended targets for the compounds tested and that are represented in the assay panel, selective inhibitors, as assessed by both absolute selectivity across the kinome and selectivity relative to the primary target, are among the 72 tested here.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Organism
SIGNOR-192458		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-191529		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-206568		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-189981		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-34541		Homo sapiens
pmid	sentence
7880537	Cdc25 dephosphorylates cdc2/cdk1 within the activation loop of the kinase domain to achieve full activity of the cyclin-cdk complex

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-252244		Mus musculus	3T3-L1 Cell
pmid	sentence
25533466	We concluded that FBXL10 recruits the noncanonical PRC1 complex to directly repress Cdk1, Uhrf1, and Pparg that may account for the FBXL10-mediated inhibition of adipogenesis.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Organism
SIGNOR-267570		Homo sapiens
pmid	sentence
29870721	Here we show that cyclin A/cdk1 kinase is the factor triggering mitosis.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-258071		in vitro
pmid	sentence
22037378	Our data set represents the most detailed comprehensive assessment of the reactivity of known and clinical kinase inhibitors across the kinome published to date. \| The data also show that for at least 15 of the 27 kinases that are the primary, intended targets for the compounds tested and that are represented in the assay panel, selective inhibitors, as assessed by both absolute selectivity across the kinome and selectivity relative to the primary target, are among the 72 tested here.

Identifier	Residue	Organism
SIGNOR-262218		in vitro
pmid	sentence
29901072	AT7519, a pyrazole 3-carboxyamide compound, was developed by Astex and acts as an inhibitor of CDK1, CDK2, CDK4, CDK6 and CDK9.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Organism	Cell Line
SIGNOR-252249		Mus musculus	3T3-L1 Cell
pmid	sentence
25533466	We concluded that FBXL10 recruits the noncanonical PRC1 complex to directly repress Cdk1, Uhrf1, and Pparg that may account for the FBXL10-mediated inhibition of adipogenesis.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Organism
SIGNOR-278916		Homo sapiens
pmid	sentence
27203178	The main cell cycle kinase Cdk1 directly phosphorylates and activates the trehalase Nth1 to trigger the flux of storage carbohydrates into central carbon metabolism.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-274077		in vitro
pmid	sentence
12556484	We found that Nudel and NudE were also phosphorylated in M phase (Fig. (Fig.22 and and3).3). First, Nudel and NudE were specifically phosphorylated in M phase. Moreover, both proteins were phosphorylated by Cdc2 and Erk2 in vitro.Due to conservation of the S/TP motifs, NudE may also be phosphorylated at similar sites by these kinases, though it contains an additional potential Cdk site at S282 (SPNR).

Publications:

1

Organism:

In Vitro

Identifier	Residue	Organism
SIGNOR-163127		Homo sapiens
pmid	sentence
20068082	Cdk1/cdc2 activation involves tyr15/thr14 dephosphorylation, regulated by wee1- and myt1-mediated phosphorylation and cdc25c-mediated dephosphorylation. Cdc25a may also be involved in cdk1 dephosphorylation in the g2/m-phase checkpoint.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-277141		Homo sapiens
pmid	sentence
26653855	Thus, Fcp1 coordinates Cdk1 and Gwl inactivation to derepress PP2A-B55, generating a dephosphorylation switch that drives mitosis progression.\|We can not exclude that, in addition to S90 and S453, other Cdk1 phosphorylation sites in Gwl are dephosphorylated by Fcp1; nevertheless, assaying S67-Ensa kinase activity of V5-GwlS90A and V5-GwlS453A mutant proteins, isolated from transfected and prometaphase arrested HeLa cells, revealed that both mutants had significantly reduced S67-Ensa kinase activity compared to V5-GwlWT (XREF_FIG).\|We show here that activation of PP2A-B55, a major mitosis exit phosphatase, required the phosphatase Fcp1 downstream Cdk1 inactivation in human cells.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-279498		Homo sapiens
pmid	sentence
10831611	As predicted by our hypothesis, the Cdc2 dependent phosphorylation has been shown to allow the full-length zyxin to interact with h-warts and LATS1 (XREF_FIG A).\|Phosphorylation of Zyxin by Cdc2 Regulates Binding to h-warts and LATS1.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-279013		Homo sapiens
pmid	sentence
23217712	(D) Phosphorylation of Cln3 by Cdk1 is independent of Ssa1 T36.\|Thereby, both Cdk1 and Pho85can promote Cln3 degradation, though under distinct circumstances.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-279677		Homo sapiens
pmid	sentence
22405274	Cdk1 phosphorylation of Tex14 is required for the Tex14-Plk1 interaction.\|While, mutation of individual PBDs in Tex14 partially reduces Cdk1 dependent phosphorylation levels and inhibits the ability of Tex14 to interact with Plk1 and to localize to KTs, mutation of all identified PBDs has a much more significant impact on binding.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-278240		Homo sapiens
pmid	sentence
26183396	Our studies suggest that phosphorylation and degradation of TAZ by Cdk1 may play important roles in apoptosis induced by antitubulin drugs.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-253864		Homo sapiens	HEP-3B Cell
pmid	sentence
14618416	To assess transactivating activity of E2F1/DP-1, we also analyzed expression of ten putative transcriptional targets of this complex in HCCs. Expression levels of TFDP1 and E2F1 correlated with those of seven transcriptional targets ( TYMS, DHFR, PCNA, RRM1, CCNE1, CDC2, and MYBL2) that play important roles in the G1/S transition, and down-regulation of TFDP1 inhibited growth of Hep3B cells.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-279143		Homo sapiens
pmid	sentence
12791267	We find that both Emi1 phosphorylation by cyclin and Cdc2 and phosphorylation on a consensus site (DSGxxS) direct recruitment of betaTrCP and subsequent Emi1 ubiquitination and destruction.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-267986		Homo sapiens	KB-3-1 Cell
pmid	sentence
19917720	Cyclin-Dependent Kinase 1-Mediated Bcl-xL/Bcl-2 Phosphorylation Acts as a Functional Link Coupling Mitotic Arrest and Apoptosis\|These findings suggest a model whereby a switch in the duration of CDK1 activation, from transient during mitosis to sustained during mitotic arrest, dramatically increases the extent of Bcl-xL/Bcl-2 phosphorylation, resulting in inactivation of their antiapoptotic function. Thus, phosphorylation of antiapoptotic Bcl-2 proteins acts as a sensor for CDK1 signal duration and as a functional link coupling mitotic arrest to apoptosis.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Organism
SIGNOR-278917		Homo sapiens
pmid	sentence
29065306	Collectively, these data show that mitotic hyperphosphorylation of Nup53 by CDK1 and PLK1 contributes to its removal from NPCs.\|The combined mutation of the CDK1 and PLK1 sites to phosphomimetic residues almost completely abolished NPC integration of Nup53, indicating that hyperphosphorylation of Nup53 might be incompatible with its NPC association.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-193546		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-278241		Homo sapiens
pmid	sentence
27030811	On the other hand, CDK1 enhances USP22 activity to stabilize CCNB1 during the G2/M phase.\|Phosphorylation of USP22 by CDK1 enhances its activity in deubiquitinating CCNB1.

Publications:

1

Organism:

Homo Sapiens

Pathways: