Relation Results

Identifier	Residue	Sequence	Organism
SIGNOR-216856	Ser100	SKIYSYMsPNKCSGM	Homo sapiens
pmid	sentence
20966048	First, we found that pr-set7 is phosphorylated at ser 29 (s29) specifically by the cyclin-dependent kinase 1 (cdk1)/cyclinb complex, s29 phosphorylation also functions to stabilize pr-set7 by directly inhibiting its interaction with the anaphase-promoting complex (apc), an e3 ubiquitin ligase.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-276524	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-276522	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-276523	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-276525	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-275601	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-216761	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.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Cell cycle: G2/M phase transition

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276093	Ser12	KTLYSFFsPSPARKR	Homo sapiens	HeLa Cell
pmid	sentence
18079698	We investigated the ability of four active CDK/cyclin pairs to phosphorylate UNG2 in vitro.When UNG2 was subjected to in vitro phosphorylation by either of these sets of CDK/cyclins, multiple phosphorylated forms of UNG2 were observed (Figure 5B). Mass spectrometry analyses revealed that the ‘early' CDK4/cyclin D and CDK2/cyclin E kinases were able to phosphorylate all three UNG2 Ser/Thr residues observed in vivo (only CDK2/cyclin E shown). Of these, only S64 was phosphorylated by the ‘late' CDK2/cyclin A and CDK1/cyclin B kinases.Mass spectrometry analyses revealed that the ‘early' CDK4/cyclin D and CDK2/cyclin E kinases were able to phosphorylate all three UNG2 Ser/Thr residues observed in vivo (only CDK2/cyclin E shown). Of these, only S64 was phosphorylated by the ‘late' CDK2/cyclin A and CDK1/cyclin B kinases (Figure 5B, upper panels) in agreement with the accumulation of this phosphorylation in G2 (Figure 3B). In addition, (unspecific) phosphorylation by all kinases was observed at S12 and S14.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276096	Ser14	LYSFFSPsPARKRHA	Homo sapiens	HeLa Cell
pmid	sentence
18079698	We investigated the ability of four active CDK/cyclin pairs to phosphorylate UNG2 in vitro.When UNG2 was subjected to in vitro phosphorylation by either of these sets of CDK/cyclins, multiple phosphorylated forms of UNG2 were observed (Figure 5B). Mass spectrometry analyses revealed that the ‘early' CDK4/cyclin D and CDK2/cyclin E kinases were able to phosphorylate all three UNG2 Ser/Thr residues observed in vivo (only CDK2/cyclin E shown). Of these, only S64 was phosphorylated by the ‘late' CDK2/cyclin A and CDK1/cyclin B kinases.Mass spectrometry analyses revealed that the ‘early' CDK4/cyclin D and CDK2/cyclin E kinases were able to phosphorylate all three UNG2 Ser/Thr residues observed in vivo (only CDK2/cyclin E shown). Of these, only S64 was phosphorylated by the ‘late' CDK2/cyclin A and CDK1/cyclin B kinases (Figure 5B, upper panels) in agreement with the accumulation of this phosphorylation in G2 (Figure 3B). In addition, (unspecific) phosphorylation by all kinases was observed at S12 and S14.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276092	Ser23	ARKRHAPsPEPAVQG	Homo sapiens	HeLa Cell
pmid	sentence
18079698	We investigated the ability of four active CDK/cyclin pairs to phosphorylate UNG2 in vitro.When UNG2 was subjected to in vitro phosphorylation by either of these sets of CDK/cyclins, multiple phosphorylated forms of UNG2 were observed (Figure 5B). Mass spectrometry analyses revealed that the ‘early' CDK4/cyclin D and CDK2/cyclin E kinases were able to phosphorylate all three UNG2 Ser/Thr residues observed in vivo (only CDK2/cyclin E shown). Of these, only S64 was phosphorylated by the ‘late' CDK2/cyclin A and CDK1/cyclin B kinases.Mass spectrometry analyses revealed that the ‘early' CDK4/cyclin D and CDK2/cyclin E kinases were able to phosphorylate all three UNG2 Ser/Thr residues observed in vivo (only CDK2/cyclin E shown). Of these, only S64 was phosphorylated by the ‘late' CDK2/cyclin A and CDK1/cyclin B kinases (Figure 5B, upper panels) in agreement with the accumulation of this phosphorylation in G2 (Figure 3B). In addition, (unspecific) phosphorylation by all kinases was observed at S12 and S14.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276094	Ser64	EPGTPPSsPLSAEQL	Homo sapiens	HeLa Cell
pmid	sentence
18079698	We investigated the ability of four active CDK/cyclin pairs to phosphorylate UNG2 in vitro.When UNG2 was subjected to in vitro phosphorylation by either of these sets of CDK/cyclins, multiple phosphorylated forms of UNG2 were observed (Figure 5B). Mass spectrometry analyses revealed that the ‘early' CDK4/cyclin D and CDK2/cyclin E kinases were able to phosphorylate all three UNG2 Ser/Thr residues observed in vivo (only CDK2/cyclin E shown). Of these, only S64 was phosphorylated by the ‘late' CDK2/cyclin A and CDK1/cyclin B kinases.Mass spectrometry analyses revealed that the ‘early' CDK4/cyclin D and CDK2/cyclin E kinases were able to phosphorylate all three UNG2 Ser/Thr residues observed in vivo (only CDK2/cyclin E shown). Of these, only S64 was phosphorylated by the ‘late' CDK2/cyclin A and CDK1/cyclin B kinases (Figure 5B, upper panels) in agreement with the accumulation of this phosphorylation in G2 (Figure 3B). In addition, (unspecific) phosphorylation by all kinases was observed at S12 and S14.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276095	Thr60	AGQEEPGtPPSSPLS	Homo sapiens	HeLa Cell
pmid	sentence
18079698	We investigated the ability of four active CDK/cyclin pairs to phosphorylate UNG2 in vitro.When UNG2 was subjected to in vitro phosphorylation by either of these sets of CDK/cyclins, multiple phosphorylated forms of UNG2 were observed (Figure 5B). Mass spectrometry analyses revealed that the ‘early' CDK4/cyclin D and CDK2/cyclin E kinases were able to phosphorylate all three UNG2 Ser/Thr residues observed in vivo (only CDK2/cyclin E shown). Of these, only S64 was phosphorylated by the ‘late' CDK2/cyclin A and CDK1/cyclin B kinases.Mass spectrometry analyses revealed that the ‘early' CDK4/cyclin D and CDK2/cyclin E kinases were able to phosphorylate all three UNG2 Ser/Thr residues observed in vivo (only CDK2/cyclin E shown). Of these, only S64 was phosphorylated by the ‘late' CDK2/cyclin A and CDK1/cyclin B kinases (Figure 5B, upper panels) in agreement with the accumulation of this phosphorylation in G2 (Figure 3B). In addition, (unspecific) phosphorylation by all kinases was observed at S12 and S14.

Publications:

5

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-216825	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-216741	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-216765	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-216769	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-216773	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-216777	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.

Publications:

5

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-267471	Ser123	EEGFGSSsPVKSPAA
pmid	sentence
23051732	Cdk1 phosphorylates Wee1 on Ser-123, which primes additional phosphorylation by other kinases, leading to the formation of phosphodegrons responsible for SCF (Skp1/cullin/F-box) ubiquitin-mediated degradation of Wee1

Publications:

1

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-272969	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-272967	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
SIGNOR-276592	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
SIGNOR-276590	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
SIGNOR-276591	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:

3

Identifier	Residue	Sequence	Organism
SIGNOR-216888	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	Cell Line
SIGNOR-276921	Ser159	SGIPDFRsPGSGLYS	Homo sapiens	HCT-116 Cell
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	Cell Line
SIGNOR-276922	Thr150	MVGAGIStPSGIPDF	Homo sapiens	HCT-116 Cell
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.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-216753	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

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-275611	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-275610	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-275609	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-264444	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	Cell Line
SIGNOR-276719	Ser174	LESSPTAsGSSVSPG	Homo sapiens	HeLa Cell
pmid	sentence
35469017	CDK1–cyclin B1 mediates KIND1 and KIND2 phosphorylation at mitotic entry . MS of KIND1 and KIND2 immunoprecipitates from STLC-arrested HeLa cells confirmed the phosphorylation of KIND1-S179 and KIND2-S181 and revealed phosphorylation of closely adjacent serine residues (KIND1: SSphS174GphS176PVphS179PGLYSK; KIND2: GphS175GphS177IYphS180phS181PGLYSK), although to a weaker extent (Supplementary Table 2).

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276720	Ser176	SSPTASGsSVSPGLY	Homo sapiens	HeLa Cell
pmid	sentence
35469017	CDK1–cyclin B1 mediates KIND2 phosphorylation at mitotic entry.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276721	Ser179	TASGSSVsPGLYSKT	Homo sapiens	HeLa Cell
pmid	sentence
35469017	CDK1–cyclin B1 mediates KIND2 phosphorylation at mitotic entry.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276716	Ser175	GPLITPGsGSIYSSP	Homo sapiens	HeLa Cell
pmid	sentence
35469017	CDK1–cyclin B1 mediates KIND2 phosphorylation at mitotic entry.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276713	Ser177	LITPGSGsIYSSPGL	Homo sapiens	HeLa Cell
pmid	sentence
35469017	CDK1–cyclin B1 mediates KIND1 and KIND2 phosphorylation at mitotic entry . MS of KIND1 and KIND2 immunoprecipitates from STLC-arrested HeLa cells confirmed the phosphorylation of KIND1-S179 and KIND2-S181 and revealed phosphorylation of closely adjacent serine residues (KIND1: SSphS174GphS176PVphS179PGLYSK; KIND2: GphS175GphS177IYphS180phS181PGLYSK), although to a weaker extent (Supplementary Table 2).

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276715	Ser180	PGSGSIYsSPGLYSK	Homo sapiens	HeLa Cell
pmid	sentence
35469017	CDK1–cyclin B1 mediates KIND2 phosphorylation at mitotic entry.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276714	Ser186	YSSPGLYsKTMTPTY	Homo sapiens	HeLa Cell
pmid	sentence
35469017	CDK1–cyclin B1 mediates KIND2 phosphorylation at mitotic entry.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-216860	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	Cell Line
SIGNOR-216920	Ser200	YSGDSDAsSPRSNCS	Homo sapiens	Myoblast
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	Cell Line
SIGNOR-216924	Ser5	sPPLRDVD	Homo sapiens	Myoblast
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
SIGNOR-268296	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-216916	Ser21	TPPSTALsPGKMSEA	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-216912	Ser397	SMVGGERsPPRILPP	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).

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-264452	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-216833	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-216837	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
SIGNOR-275612	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-250644	Ser272	EEPSPLPsPTASPNH	in vitro
pmid	sentence
11113134	Amphiphysin is phosphorylated by cdk5 in a region including serines 272, 276, and 285. Amphiphysin 1 is also phosphorylated by the cdc2/cyclin B kinase complex in the same region and undergoes mitotic phosphorylation in dividing cells.

Identifier	Residue	Sequence	Organism
SIGNOR-250645	Ser276	PLPSPTAsPNHTLAP	in vitro
pmid	sentence
11113134	Amphiphysin is phosphorylated by cdk5 in a region including serines 272, 276, and 285. Amphiphysin 1 is also phosphorylated by the cdc2/cyclin B kinase complex in the same region and undergoes mitotic phosphorylation in dividing cells.

Identifier	Residue	Sequence	Organism
SIGNOR-250646	Ser285	NHTLAPAsPAPARPR	in vitro
pmid	sentence
11113134	Amphiphysin is phosphorylated by cdk5 in a region including serines 272, 276, and 285. Amphiphysin 1 is also phosphorylated by the cdc2/cyclin B kinase complex in the same region and undergoes mitotic phosphorylation in dividing cells.

Publications:

3

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-216932	Ser272	RSRLTPVsPESSSTE	Homo sapiens	Lung Cancer Cell
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	Cell Line
SIGNOR-216936	Thr269	GGKRSRLtPVSPESS	Homo sapiens	Lung Cancer Cell
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-274083	Ser282	RNLVYDQsPNRTGGP	Homo sapiens	HEK-293 Cell
pmid	sentence
16682949	Here, we demonstrate that Su48 can associate with Nde1. Moreover, 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.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-274087	Thr191	QKQEKPRtPMPSSVE	Homo sapiens	HEK-293 Cell
pmid	sentence
16682949	Here, we demonstrate that Su48 can associate with Nde1. Moreover, 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.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-274082	Thr215	ATGSVPStPIAHRGP	Homo sapiens	HEK-293 Cell
pmid	sentence
16682949	Here, we demonstrate that Su48 can associate with Nde1. Moreover, 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.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-274085	Thr228	GPSSSLNtPGSFRRG	Homo sapiens	HEK-293 Cell
pmid	sentence
16682949	Here, we demonstrate that Su48 can associate with Nde1. Moreover, 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.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-274084	Thr243	LDDSTGGtPLTPAAR	Homo sapiens	HEK-293 Cell
pmid	sentence
16682949	Here, we demonstrate that Su48 can associate with Nde1. Moreover, 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.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-274086	Thr246	STGGTPLtPAARISA	Homo sapiens	HEK-293 Cell
pmid	sentence
16682949	Here, we demonstrate that Su48 can associate with Nde1. Moreover, 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:

6

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-275599	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-275598	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-275597	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
SIGNOR-275600	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-260606	Ser373	FEVSFLDsPGAQAQA	Rattus norvegicus
pmid	sentence
15678101	The pS376 antibody gave the strongest staining when Golgi apparatus fragmentation is initiated during prophase and in metaphase when it has become converted into a haze of small vesicles and some larger tubulovesicular remnants (Figure 4A). Therefore, GRASP65, like GM130, is phosphorylated in mitotic entry on Cdk1–cyclin B sites during the period when the Golgi apparatus is fragmented.

Publications:

1

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-272971	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-216737	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-216880	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	Cell Line
SIGNOR-250719	Ser396	NIKSEPVsPPRDRTT	10T1/2 Cell
pmid	sentence
16478538	Phosphorylation-facilitated sumoylation of MEF2C negatively regulates its transcriptional activity. \| Intriguingly, we show that phosphorylation of S396 in MEF2C, a residue in close proximity to the major sumoylation site (K391) and known to be phosphorylated in vivo, enhances sumoylation of delta- N2-MEF2C in vitro. The S396A mutation reduces sumoylation of MEF2C in vivo and enhances the transcription activity of MEF2C in reporter assays. \| CDK1/Cyclin B1 phosphorylated GST-MEF2C-ΔN2-WT to a greater extent than the MEF2C-ΔN2-S396A mutant, suggesting that Cdk1/Cyclin B1 can phosphorylate MEF2C at S396.

Publications:

1

Identifier	Residue	Sequence
SIGNOR-275490	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-216781	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-216785	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-216789	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-216821	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-216841	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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-216944	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-216949	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-216953	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	Cell Line
SIGNOR-274131	Ser585	WRGMLKTSKAEELLA	Homo sapiens	HEK-293 Cell
pmid	sentence
17301055	Drp1 was specifically phosphorylated at Ser-585 by Cdk1/cyclin B, which stimulated the mitochondrial fission in mitosis. From these results, we concluded that mitochondrial morphology is regulated by Drp1-dependent mitochondrial fission in mitotic cells

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-266113	Ser6	sPLLEVKG	in vitro
pmid	sentence
24510915	Tryptic digests of KIFC1 treated with CDK1/CYCLIN B were analyzed by LC-MS/MS revealing phosphorylation at Ser6 (Supplementary Fig S5B). These data indicate that phosphorylation by CDK1/CYLCIN B contributes to KIFC1 stability by protecting KIFC1 from APC/C-mediated ubiquitination and subsequent proteasomal degradation.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-216757	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-276408	Ser639	QQEGGFAsPRTGKGK	in vitro
pmid	sentence
22411829	Importantly, the S652ph antibody identifies phosphorylated UHRF1 in mitotic cells and consistently S652 can be phosphorylated by the M phase-specific kinase CDK1-cyclin B in vitro. UHRF1 S652 phosphorylation significantly reduces UHRF1 interaction with USP7 in vitro and in vivo, which is correlated with a decreased UHRF1 stability in the M phase of the cell cycle. In contrast, UHRF1 carrying the S652A mutation, which renders UHRF1 resistant to phosphorylation at S652, is more stable.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-216797	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-216801	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-216805	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-216809	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
SIGNOR-216892	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-250641	Ser86	TKNGLPGsRPGSPER	Homo sapiens	HeLa Cell
pmid	sentence
12468530	Baculovirus-based expression and purification of Tip60 combined with mass spectrometry allowed the identification of serines 86 and 90 as two major sites of phosphorylation in vivo. The phosphorylation of Tip60 was found to modulate its histone acetyltransferase activity. One of the identified phosphorylated serines, Ser-90, was within a consensus cyclin B/Cdc2 site. Ser-90 was specifically phosphorylatedin vitro by the cyclin B/Cdc2 complex.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250642	Ser90	LPGSRPGsPEREVPA	Homo sapiens	HeLa Cell
pmid	sentence
12468530	Baculovirus-based expression and purification of Tip60 combined with mass spectrometry allowed the identification of serines 86 and 90 as two major sites of phosphorylation in vivo. The phosphorylation of Tip60 was found to modulate its histone acetyltransferase activity. One of the identified phosphorylated serines, Ser-90, was within a consensus cyclin B/Cdc2 site. Ser-90 was specifically phosphorylatedin vitro by the cyclin B/Cdc2 complex.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276060	Ser960	SRLSPPHsPRDFTRM	Homo sapiens	HeLa Cell
pmid	sentence
17488622	The mitotic kinases Aurora A/B and Cdk1/Cyclin B phosphorylate GEF-H1, thereby inhibiting GEF-H1 catalytic activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262725	Thr111	ALLSATVtPQKAKLG	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	Sequence	Organism
SIGNOR-265995	Thr1161	FFNPVCAtPNSKILK	in vitro
pmid	sentence
29771379	Kif4A T1161 was phosphorylated by Cdk1/Cyclin B1 in vitro. We show that Cdk phosphorylation of Kif4A licenses its chromosome localization.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence
SIGNOR-275596	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-275595	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-216884	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.

Identifier	Residue	Sequence	Organism
SIGNOR-216876	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.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251509	Thr14	IEKIGEGtYGVVYKG	Homo sapiens	U2-OS Cell
pmid	sentence
10913154	Cyclin B-Cdc2 complexes are maintained in an inactive state until the end of G2 by phosphorylation of the Thr14/Tyr15 residues. Around the time of nuclear translocation of the complex, these residues are dephosphorylated, resulting in the formation of an active cyclin B-Cdc2 complex (2). As mentioned, this dephosphorylation occurs by a Cdc25 protein phosphatase. Three Cdc25 family members have been identified to date, A, B and C, the last one being the active one at the onset of mitosis. The activity of Cdc25C itself can be enhanced through phosphorylation by cyclin B-Cdc2 (9, 10). Therefore, activation of cyclin B-Cdc2 has been proposed to result in an autocatalytic feedback loop to ensure rapid activation of these complexes at the G2/M transition

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-255037	Tyr15	EKIGEGTyGVVYKGR	Homo sapiens	U2-OS Cell
pmid	sentence
10913154	Cyclin B-Cdc2 complexes are maintained in an inactive state until the end of G2 by phosphorylation of the Thr14/Tyr15 residues. Around the time of nuclear translocation of the complex, these residues are dephosphorylated, resulting in the formation of an active cyclin B-Cdc2 complex (2). As mentioned, this dephosphorylation occurs by a Cdc25 protein phosphatase. Three Cdc25 family members have been identified to date, A, B and C, the last one being the active one at the onset of mitosis. The activity of Cdc25C itself can be enhanced through phosphorylation by cyclin B-Cdc2 (9, 10). Therefore, activation of cyclin B-Cdc2 has been proposed to result in an autocatalytic feedback loop to ensure rapid activation of these complexes at the G2/M transition

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-243403	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-249652	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-216845	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-216745	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-216749	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:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-216868	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-216872	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
SIGNOR-275471	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	Cell Line
SIGNOR-263888	Thr34	KDSSRCStPGLDPER	Homo sapiens	HEK-293 Cell, HeLa Cell
pmid	sentence
24769206	We have demonstrated that MTHFR is phosphorylated on T34by CDK1/Cyclin B1 in vivo and this phosphorylation peaks duringmitosis and decreases its enzymatic activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-216864	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-250643	Thr376	QVAPRAGtPGFRAPE	in vitro
pmid	sentence
10846177	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. In vitro, Cdk2-Cyclin E, Cdk2-Cyclin A, and Cdc2-Cyclin B, but not Cdk4-Cyclin D1, phosphorylates the Thr-376 residue of huCdc7, suggesting possible regulation of huCdc7 by Cdks.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence
SIGNOR-275602	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	Cell Line
SIGNOR-216908	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.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-216904	Thr4539	GGLIEPDtPGRVPLD	Homo sapiens	HeLa Cell
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.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-216793	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
SIGNOR-216829	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-216940	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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-271840	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-216928	Thr846	RAFSFSKtPKRALRR	Homo sapiens	U2-OS Cell
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:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-216849	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
SIGNOR-250720	Thr9	EGISNFKtPSKLSEK
pmid	sentence
15541388	During mitosis, TOPK-Thr-9 was phosphorylated by cdk1/cyclin B and TOPK significantly associates with mitotic spindles. When TOPK expression was suppressed, formation of spindle midzone was thinned and dimmed and cytokinesis was disturbed.

Publications:

1

Identifier	Residue	Sequence	Organism
SIGNOR-216896	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-216900	Thr92	EVPDVTAtPARLLFF	Homo sapiens
pmid	sentence
18676833	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

Identifier	Residue	Organism
SIGNOR-216852		Homo sapiens
pmid	sentence
7588608	Consistent with the in vivo phosphorylation and inactivation by ras, erf is efficiently phosphorylated in vitro by erk2 and cdc2/cyclin b kinases, at sites similar to those detected in vivo. Furthermore, a single mutation at position 526 results in the loss of a specific phosphopeptide both in in vivo and in vitro (by erk2) labeling. Substitution of thr526 for glutamic acid also decreases the repression ability of erf

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-217511		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	Sequence	Organism	Cell Line
SIGNOR-251497
pmid	sentence
15549093	The critical target of the G2 checkpoint is the mitosis-promoting activity of the cyclin B/CDK1 kinase, whose activation after various stresses is inhibited by ATM/ATR, CHK1/CHK2 and/or p38-kinase-mediated subcellular sequestration, degradation and/or inhibition of the CDC25 family of phosphatases that normally activate CDK1 at the G2/M boundary

Publications:

1

Pathways:

Cell cycle: G2/M phase transition

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251498
pmid	sentence
10913154	P21 Inhibits Thr161 Phosphorylation of Cdc2 to Enforce the G2 DNA Damage Checkpoint\|The cyclin-dependent kinase inhibitor p21 is required for a sustained G2 arrest after activation of the DNA damage checkpoint. Here we have addressed the mechanism by which p21 can contribute to this arrest in G2. We show that p21 blocks the activating phosphorylation of Cdc2 on Thr161

Publications:

1

Pathways:

Cell cycle: G2/M phase transition

Identifier	Residue	Organism
SIGNOR-217508		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	Cell Line
SIGNOR-251510		Homo sapiens	U2-OS Cell
pmid	sentence
10913154	Cyclin B-Cdc2 complexes are maintained in an inactive state until the end of G2 by phosphorylation of the Thr14/Tyr15 residues. Around the time of nuclear translocation of the complex, these residues are dephosphorylated, resulting in the formation of an active cyclin B-Cdc2 complex (2). As mentioned, this dephosphorylation occurs by a Cdc25 protein phosphatase. Three Cdc25 family members have been identified to date, A, B and C, the last one being the active one at the onset of mitosis. The activity of Cdc25C itself can be enhanced through phosphorylation by cyclin B-Cdc2 (9, 10). Therefore, activation of cyclin B-Cdc2 has been proposed to result in an autocatalytic feedback loop to ensure rapid activation of these complexes at the G2/M transition

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-205590		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-178799		Homo sapiens
pmid	sentence
18521620	Our data additionally identify the cdk1 site s252 as critical for the recruitment of plk1 to hbora. collectively, our findings lead us to propose that hbora contributes to integrate the functions of three major mitotic kinases, cdk1, plk1, and aurora a.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251496
pmid	sentence
15549093	The critical target of the G2 checkpoint is the mitosis-promoting activity of the cyclin B/CDK1 kinase, whose activation after various stresses is inhibited by ATM/ATR, CHK1/CHK2 and/or p38-kinase-mediated subcellular sequestration, degradation and/or inhibition of the CDC25 family of phosphatases that normally activate CDK1 at the G2/M boundary

Publications:

1

Pathways:

Cell cycle: G2/M phase transition

Name	CyclinB/CDK1 View Modifications
Primary ID	SIGNOR-C17
Links	CPX-2007
Type	complex
Formed by	CCNB1, CDK1
Relations	131
Pathways	Cell cycle: G2/M phase transition

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