Relation Results

Identifier	Residue	Sequence	Organism
SIGNOR-217284	Ser104	FPPLNSVsPSPLMLL	Homo sapiens
pmid	sentence
10428798	Within er af-1, serines 104, 106, and 118 represent potential cdk phosphorylation sites, and in this current study, we ascertain their importance in mediating cyclin a-cdk2-dependent enhancement of er transcriptional activity.

Identifier	Residue	Sequence	Organism
SIGNOR-217288	Ser106	PLNSVSPsPLMLLHP	Homo sapiens
pmid	sentence
10428798	Within er af-1, serines 104, 106, and 118 represent potential cdk phosphorylation sites, and in this current study, we ascertain their importance in mediating cyclin a-cdk2-dependent enhancement of er transcriptional activity.

Identifier	Residue	Sequence	Organism
SIGNOR-217292	Ser118	LHPPPQLsPFLQPHG	Homo sapiens
pmid	sentence
10428798	Within er af-1, serines 104, 106, and 118 represent potential cdk phosphorylation sites, and in this current study, we ascertain their importance in mediating cyclin a-cdk2-dependent enhancement of er transcriptional activity.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-217272	Ser106	DNQLTIKsPSKRELA	Homo sapiens
pmid	sentence
10339564	Based on these results, we propose that phosphorylation of hscdc6 by cdks regulates dna replication of at least two steps: first, by promoting initiation of dna replication and, second, through nuclear exclusion preventing dna rereplication. hscdc6 is an excellent substrate for cdk2 in vitro and is phosphorylated in vivo at three sites (ser-54, ser-74, and ser-106)

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276091	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-276089	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-276088	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-276090	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.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-273597	Ser12	RRRARVGsPSGDAAS	in vitro
pmid	sentence
23933132	In vitro kinase assays showed that the S phase-associated Cdk2/cyclin A complex was able to phosphorylate Polμ. We identified Ser12, Thr21 (located in the BRCT domain) and Ser372 (located in loop1) as the target residues. Mutation of these residues to alanine indicated that Ser372 is the main phosphorylation site.Our evidences suggest that Polμ could be regulated in vivo by phosphorylation of the BRCT domain (Ser12/Thr21) and of Ser372, affecting the function of loop1.

Identifier	Residue	Sequence	Organism
SIGNOR-273596	Ser372	HQHSCCEsPTRLAQQ	in vitro
pmid	sentence
23933132	In vitro kinase assays showed that the S phase-associated Cdk2/cyclin A complex was able to phosphorylate Polμ. We identified Ser12, Thr21 (located in the BRCT domain) and Ser372 (located in loop1) as the target residues. Mutation of these residues to alanine indicated that Ser372 is the main phosphorylation site.Our evidences suggest that Polμ could be regulated in vivo by phosphorylation of the BRCT domain (Ser12/Thr21) and of Ser372, affecting the function of loop1.

Identifier	Residue	Sequence	Organism
SIGNOR-273598	Thr21	SGDAASStPPSTRFP	in vitro
pmid	sentence
23933132	In vitro kinase assays showed that the S phase-associated Cdk2/cyclin A complex was able to phosphorylate Polμ. We identified Ser12, Thr21 (located in the BRCT domain) and Ser372 (located in loop1) as the target residues. Mutation of these residues to alanine indicated that Ser372 is the main phosphorylation site.Our evidences suggest that Polμ could be regulated in vivo by phosphorylation of the BRCT domain (Ser12/Thr21) and of Ser372, affecting the function of loop1.

Publications:

3

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-270807	Ser164	GLAKSFGsPNRAYTH	in vitro
pmid	sentence
11113184	Activating phosphorylation of CDK7 by CDC2 and CDK2. The ability of pure CDK2-cyclin A to activate CDK7 in T170-dependent fashion (Fig. (Fig.3C,3C, lane 2) strongly suggested a direct phosphorylation mechanism. Tryptic phosphopeptide mapping confirmed that both CDK2-cyclin A (Fig. (Fig.4A)4A) and CDC2-cyclin B (Fig. (Fig.4D)4D) phosphorylated CDK7 on both S164 and T170.

Identifier	Residue	Sequence	Organism
SIGNOR-270806	Thr170	GSPNRAYtHQVVTRW	in vitro
pmid	sentence
11113184	Activating phosphorylation of CDK7 by CDC2 and CDK2. The ability of pure CDK2-cyclin A to activate CDK7 in T170-dependent fashion (Fig. (Fig.3C,3C, lane 2) strongly suggested a direct phosphorylation mechanism. Tryptic phosphopeptide mapping confirmed that both CDK2-cyclin A (Fig. (Fig.4A)4A) and CDC2-cyclin B (Fig. (Fig.4D)4D) phosphorylated CDK7 on both S164 and T170.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276910	Ser175	SFVTPPQsHFVRVST	Homo sapiens	HEK-293T Cell
pmid	sentence
26028025	We now provide evidence that BLM undergoes K48-linked ubiquitylation and subsequent degradation during mitosis due to the E3 ligase, Fbw7α. Fbw7α carries out its function after GSK3β- and CDK2/cyclin A2-dependent phosphorylation events on Thr171 and Ser175 of BLM which lies within a well-defined phosphodegron, a sequence which is conserved in all primates.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276907	Thr171	ETSKSFVtPPQSHFV	Homo sapiens	HEK-293T Cell
pmid	sentence
26028025	We now provide evidence that BLM undergoes K48-linked ubiquitylation and subsequent degradation during mitosis due to the E3 ligase, Fbw7α. Fbw7α carries out its function after GSK3β- and CDK2/cyclin A2-dependent phosphorylation events on Thr171 and Ser175 of BLM which lies within a well-defined phosphodegron, a sequence which is conserved in all primates.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-273592	Ser191	GRAQLLWsPWSPLDQ	in vitro
pmid	sentence
15159402	GST-INCA1 was phosphorylated in vitro by cyclin A2-CDK2 but not by CDK2 or either cyclin alone. Mutation of Ser23, Thr167, and Ser176 strongly reduced in vitro phosphorylation of INCA1.Cyclin A1 and Cyclin A2 in Complex with CDK2 Phosphorylated INCA1 in Vitro Predominantly at Ser176

Identifier	Residue	Sequence	Organism
SIGNOR-273593	Ser23	CSRVVSRsPPPRLPS	in vitro
pmid	sentence
15159402	GST-INCA1 was phosphorylated in vitro by cyclin A2-CDK2 but not by CDK2 or either cyclin alone. Mutation of Ser23, Thr167, and Ser176 strongly reduced in vitro phosphorylation of INCA1.Cyclin A1 and Cyclin A2 in Complex with CDK2 Phosphorylated INCA1 in Vitro Predominantly at Ser176

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250752	Ser20	RRLSSSEsPQRDPPP	Homo sapiens	HeLa Cell
pmid	sentence
11395479	We observed that a CDA1 mutant with the two consensus CDK phosphorylation sites abolished (S20A and T340A) disabled its capacity to inhibit cell growth, indicating that these sites are important for the function of this protein. Furthermore, we showed that these sites are phosphorylated by cyclin/CDKs in vitro, suggesting that these kinases may regulate CDA1 function in vivo.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250753	Thr340	GRLVSHStPIRWHRG	Homo sapiens	HeLa Cell
pmid	sentence
11395479	We observed that a CDA1 mutant with the two consensus CDK phosphorylation sites abolished (S20A and T340A) disabled its capacity to inhibit cell growth, indicating that these sites are important for the function of this protein. Furthermore, we showed that these sites are phosphorylated by cyclin/CDKs in vitro, suggesting that these kinases may regulate CDA1 function in vivo.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-217340	Ser276	VHPATPIsPGRASGM	Homo sapiens
pmid	sentence
17015473	Previous studies have shown that phosphorylation of aml1, particularly at serines 276 and 303, affects its transcriptional activation. Here, we report that phosphorylation of aml1 serines 276 and 303 can be blocked in vivo by inhibitors of the cyclin-dependent kinases (cdks) cdk1 and cdk2. Furthermore, these residues can be phosphorylated in vitro by purified cdk1/cyclin b and cdk2/cyclin a.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-217300	Ser315	LPNNTSSsPQPKKKP	Homo sapiens
pmid	sentence
14640983	We used non-radioactive electrophoretic mobility shift assays to show that c-terminal phosphorylation of p53 protein by cdk2/cyclin a on ser315 or by pkc on ser378 can efficiently stimulate p53 binding to dna in vitro.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-217344	Ser32	RSEDARSsPSQRRRG	Homo sapiens	HeLa Cell
pmid	sentence
12714602	We reported that the dna helicase activity of the human and mouse mcm4-6-7 complex, a sub-complex of the mcm2-7 heterohexamer, is inhibited by the phosphorylation by cdk2-cyclin a we identified six sites, including ser-32, ser-53, and thr-109, in the amino-terminal region of mouse mcm4 that are required for the phosphorylation with cdk2-cyclin a.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-217348	Ser54	ELQPMPTsPGVDLQS	Homo sapiens	HeLa Cell
pmid	sentence
12714602	We reported that the dna helicase activity of the human and mouse mcm4-6-7 complex, a sub-complex of the mcm2-7 heterohexamer, is inhibited by the phosphorylation by cdk2-cyclin a we identified six sites, including ser-32, ser-53, and thr-109, in the amino-terminal region of mouse mcm4 that are required for the phosphorylation with cdk2-cyclin a.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-217352	Thr110	PRSGVRGtPVRQRPD	Homo sapiens	HeLa Cell
pmid	sentence
12714602	We reported that the dna helicase activity of the human and mouse mcm4-6-7 complex, a sub-complex of the mcm2-7 heterohexamer, is inhibited by the phosphorylation by cdk2-cyclin a we identified six sites, including ser-32, ser-53, and thr-109, in the amino-terminal region of mouse mcm4 that are required for the phosphorylation with cdk2-cyclin a.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-263227	Ser327	ELPTRVSsPVFGATS	Homo sapiens	HeLa Cell
pmid	sentence
15485915	Ser327 site is a Ser-Pro site, a preferred phosphorylation site by cyclin-dependent kinases\|Unlike wild-type CtIP, the S327A mutant did not bind to BRCA1 BRCT domains in vitro (Fig. (Fig.1C)1C) and failed to associate with BRCA1 in vivo (Fig. (Fig.1D),1D), suggesting that residue Ser327 of CtIP is critical for the CtIP-BRCA1 interaction.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-217268	Ser328	VLPSISLsPGPQPPK	Homo sapiens
pmid	sentence
23028682	The forced activation of cyclin a-cdk2 in these cells by the overexpression of cyclin a,triggered rad9 phosphorylation at serine 328 and thereby promoted the interaction of rad9 with bcl-xl and the subsequent initiation of the apoptotic program.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-274051	Ser36	HPGFDAEsYTFTVPR
pmid	sentence
23972993	Priming phosphorylation of Cdh1 by the Cdk2/cyclin A kinase complex allows Plk1 to bind to Cdh1 and phosphorylate Cdh1 at Ser138 and Ser146. Phosphorylation of Cdh1 at Ser138 and Ser146 then triggers its interaction with, and subsequent ubiquitination by, SCFbeta-TRCP

Identifier	Residue	Sequence
SIGNOR-274052	Thr40	DAESYTFtVPRRHLE
pmid	sentence
23972993	Priming phosphorylation of Cdh1 by the Cdk2/cyclin A kinase complex allows Plk1 to bind to Cdh1 and phosphorylate Cdh1 at Ser138 and Ser146. Phosphorylation of Cdh1 at Ser138 and Ser146 then triggers its interaction with, and subsequent ubiquitination by, SCFbeta-TRCP

Publications:

2

Identifier	Residue	Sequence	Organism
SIGNOR-217304	Ser389	INKKQATsPASKKPA	Homo sapiens
pmid	sentence
11698641	Phosphorylation of ubf at serine 388 is required for interaction with rna polymerase i and activation of rdna transcription. After g(1) progression ubf is phosphorylated at serine 388 by cdk2/cyclin e and cdk2/cyclin a. Conversion of serine 388 to glycine abolishes ubf activity

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250751	Ser392	FKTEGPDsD	in vitro
pmid	sentence
10884347	Our previous data has shown that cyclin A-cdk2 is the major enzyme responsible for modifying p53 at Ser315 in vivo after irradiation damage and in this report we dissect the mechanism of cyclinA-cdk2 binding to and phosphorylation of p53.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252440	Ser477	PQFSYSAsGTA	Homo sapiens	MCF-7 Cell
pmid	sentence
24670654	Phosphorylation of S477 and T479 at the Akt extreme carboxy terminus by cyclin-dependent kinase 2 (Cdk2)/cyclin A or mTORC2, under distinct physiological conditions, promotes Akt activation through facilitating, or functionally compensating for, S473 phosphorylation

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252443	Thr479	FSYSASGtA	Homo sapiens	MCF-7 Cell
pmid	sentence
24670654	Phosphorylation of S477 and T479 at the Akt extreme carboxy terminus by cyclin-dependent kinase 2 (Cdk2)/cyclin A or mTORC2, under distinct physiological conditions, promotes Akt activation through facilitating, or functionally compensating for, S473 phosphorylation

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252450	Ser477	PQFSYSAsGTA	Homo sapiens	MCF-7 Cell
pmid	sentence
24670654	Phosphorylation of S477 and T479 at the Akt extreme carboxy terminus by cyclin-dependent kinase 2 (Cdk2)/cyclin A or mTORC2, under distinct physiological conditions, promotes Akt activation through facilitating, or functionally compensating for, S473 phosphorylation

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252453	Thr479	FSYSASGtA	Homo sapiens	MCF-7 Cell
pmid	sentence
24670654	Phosphorylation of S477 and T479 at the Akt extreme carboxy terminus by cyclin-dependent kinase 2 (Cdk2)/cyclin A or mTORC2, under distinct physiological conditions, promotes Akt activation through facilitating, or functionally compensating for, S473 phosphorylation

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-217320	Ser5	sPVRSVRK	Homo sapiens
pmid	sentence
9029153	Id2 acts by forming heterodimers that are unable to bind to specific (e-box) dna sequences. Here we show that this activity can be overcome by phosphorylation of a serine residue within a consensus target site for cyclin-dependent kinases (cdks). In vitro, id2 can be phosphorylated by either cyclin e-cdk2 or cyclin a-cdk2_

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-217328	Ser54	RVKALPLsPRKRLGD	Homo sapiens
pmid	sentence
9889196	Phosphorylation of mammalian cdc6 by cyclin a/cdk2 regulates its subcellular localization/based on our data we suggest that the phosphorylation of cdc6 by cyclin a/cdk2 is a negative regulatory event that could be implicated in preventing re-replication during s phase and g2.

Identifier	Residue	Sequence	Organism
SIGNOR-217276	Ser54	RVKALPLsPRKRLGD	Homo sapiens
pmid	sentence
10339564	Hscdc6 is an excellent substrate for cdk2 in vitro and is phosphorylated in vivo at three sites (ser-54, ser-74, and ser-106)\|An HsCdc6A1A2A3 mutant, which mimics unphosphorylated HsCdc6, is exclusively nuclear, and its expression inhibits initiation of DNA replication. An HsCdc6E1E2E3 mutant, which mimics phosphorylated HsCdc6, is exclusively cytoplasmic and is not associated with the chromatin/nuclear matrix fraction.

Identifier	Residue	Sequence	Organism
SIGNOR-217280	Ser74	TPHLPPCsPPKQGKK	Homo sapiens
pmid	sentence
10339564	Hscdc6 is an excellent substrate for cdk2 in vitro and is phosphorylated in vivo at three sites (ser-54, ser-74, and ser-106)\|An HsCdc6A1A2A3 mutant, which mimics unphosphorylated HsCdc6, is exclusively nuclear, and its expression inhibits initiation of DNA replication. An HsCdc6E1E2E3 mutant, which mimics phosphorylated HsCdc6, is exclusively cytoplasmic and is not associated with the chromatin/nuclear matrix fraction.

Identifier	Residue	Sequence	Organism
SIGNOR-217332	Ser74	TPHLPPCsPPKQGKK	Homo sapiens
pmid	sentence
9889196	Phosphorylation of mammalian cdc6 by cyclin a/cdk2 regulates its subcellular localization/based on our data we suggest that the phosphorylation of cdc6 by cyclin a/cdk2 is a negative regulatory event that could be implicated in preventing re-replication during s phase and g2.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-277522	Ser559	PYETYEGsPVSKGIL	Homo sapiens
pmid	sentence
32712628	Here, we report that RRM1 is phosphorylated at Ser 559 by CDK2/cyclin A during S/G2 phase. And this S559 phosphorylation of RRM1enhances RNR enzymatic activity and is required for maintaining sufficient dNTPs during normal DNA replication.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-217252	Ser577	RKPGLRRsPIKKVRK	Homo sapiens
pmid	sentence
9840932	The cell-cycle regulated transcription factor b-myb is phosphorylated by cyclin a/cdk2 at sites that enhance its transactivation properties. we show that b-myb is phosphorylated at thr447, thr490, thr497 and ser581 by cyclin a/cdk5

Identifier	Residue	Sequence	Organism
SIGNOR-217256	Thr444	NSLTPKStPVKTLPF	Homo sapiens
pmid	sentence
9840932	The cell-cycle regulated transcription factor b-myb is phosphorylated by cyclin a/cdk2 at sites that enhance its transactivation properties. we show that b-myb is phosphorylated at thr447, thr490, thr497 and ser581 by cyclin a/cdk3

Identifier	Residue	Sequence	Organism
SIGNOR-217260	Thr487	SQKVVVTtPLHRDKT	Homo sapiens
pmid	sentence
9840932	The cell-cycle regulated transcription factor b-myb is phosphorylated by cyclin a/cdk2 at sites that enhance its transactivation properties. we show that b-myb is phosphorylated at thr447, thr490, thr497 and ser581 by cyclin a/cdk2

Identifier	Residue	Sequence	Organism
SIGNOR-217264	Thr494	TPLHRDKtPLHQKHA	Homo sapiens
pmid	sentence
9840932	The cell-cycle regulated transcription factor b-myb is phosphorylated by cyclin a/cdk2 at sites that enhance its transactivation properties. we show that b-myb is phosphorylated at thr447, thr490, thr497 and ser581 by cyclin a/cdk4

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248240	Ser59	GGQESQPsPLALLAA	Mus musculus	NIH-3T3 Cell
pmid	sentence
11598016	Mutation of Sp1 Ser59 abrogates the cyclin ACDK augmentation of Sp1-dependent transcriptional transactivation

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-265046	Ser628	MVNSCITsPSTPSKK	Homo sapiens	HEK-293 Cell, HeLa Cell
pmid	sentence
21596315	There is positive reinforcement of this signaling mechanism because phosphorylation of Ser628 by CDK2/cyclin E and CDK2/cyclin A complexes produces maximal USP37 activity

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262730	Ser83	VEQELPSsPKQPICF	Homo sapiens	U2-OS Cell
pmid	sentence
27065328	Mechanistically, Cep76 phosphorylation inhibits activation of polo-like kinase 1 (Plk1), thereby blocking premature centriole disengagement and subsequent amplification. we conclude that Cep76 inhibits centriole disengagement and consequently amplification by blocking Plk1 activation at the centrosome.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262603	Ser83	VEQELPSsPKQPICF	Homo sapiens	HEK-293 Cell
pmid	sentence
27065328	Cep76 is phosphorylated by cyclin A/CDK2 at a single site S83. These data suggest that the phosphomimetic mutant is functional and that phosphorylation at S83 is critical for Cep76 to suppress centriole amplification.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-217296	Thr116	LASELAKtPQKSVSF	Homo sapiens
pmid	sentence
11931757	We also found that horc2p is phosphorylated in vitro by cyclin a/cdk2, specifically at residues thr116 and thr226. 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-217308	Thr226	SAPVGKEtPSKRMKR	Homo sapiens
pmid	sentence
11931757	We also found that horc2p is phosphorylated in vitro by cyclin a/cdk2, specifically at residues thr116 and thr226. 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:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-267621	Thr157	GKVEITYtPSDGTQK
pmid	sentence
34929314	During the cell cycle S phase, Cyclin A-CDK2 phosphorylates IDH1 on its Threonine 157 residue (Threonine 197 in IDH2) to facilitate its recognition and ubiquitination by Skp2 E3 ubiquitin, followed by degradation through 26S proteasome

Publications:

1

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276614	Thr194	NMMDILTtPSMAKPR	Homo sapiens	HEK-293T Cell
pmid	sentence
24391510	We demonstrate that PP2A/B55 is required for Gwl dephosphorylation at the essential Cdk site Thr194.Gwl phosphorylation by CycA/Cdk2 in vitro. Flag WT and Thr194A Gwl was transiently expressed and purified from asynchronous HEK 293T cells and incubated with recombinant CycA/Cdk2, following treatment with alkaline phosphatase (aPh) in the indicated samples. The proteins were analysed by immuno-blotting with anti-Gwl and Gwl pThr194 antibodies

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-267622	Thr197	GTFKMVFtPKDGSGV
pmid	sentence
34929314	During the cell cycle S phase, Cyclin A-CDK2 phosphorylates IDH1 on its Threonine 157 residue (Threonine 197 in IDH2) to facilitate its recognition and ubiquitination by Skp2 E3 ubiquitin, followed by degradation through 26S proteasome

Publications:

1

Identifier	Residue	Sequence	Organism
SIGNOR-217316	Thr235	SSSSPPGtPSPADAK	Homo sapiens
pmid	sentence
22369944	Mass spectrometric analysis revealed that cdk2/cyclina phosphorylates c/ebpbeta on thr(188) and is required for phosphorylation (on ser(184) or thr(179)) of c/ebpbeta by gsk3beta and maintenance of dna binding activity.

Identifier	Residue	Sequence	Organism
SIGNOR-217312	Thr235	SSSSPPGtPSPADAK	Homo sapiens
pmid	sentence
17601773	Mass spectrometric analysis revealed that cdk2/cyclina phosphorylates c/ebpbeta on thr(188) and is required for phosphorylation (on ser(184) or thr(179)) of c/ebpbeta by gsk3beta and maintenance of dna binding activity.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-250725	Thr376	QVAPRAGtPGFRAPE
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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273595	Thr553	GPGRVLPtPTEKDVF	Homo sapiens	HEK-293 Cell
pmid	sentence
18688254	Pol λ phosphorylation prevents degradation. Recently, we identified Pol λ as an interaction partner of cyclin-dependent kinase 2 (CDK2) that is central to the cell cycle G1/S transition and S-phase progression. This interaction leads to in vitro phosphorylation of Pol λ, and its in vivo phosphorylation pattern during cell cycle progression mimics the modulation of CDK2/cyclin A. Experiments with phosphorylation-defective mutants suggest that phosphorylation of Thr 553 is important for maintaining Pol λ stability,

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-265259	Thr62	RRPESFTtPEGPKPR	Homo sapiens	HeLa Cell
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-217324	Thr821	KISEGLPtPTKMTPR	Homo sapiens
pmid	sentence
9139732	We demonstrate that phosphorylation by either cdk2-cyclin a, which phosphorylates t821, or cdk4-cyclin d1, which phosphorylates threonine 826, can disable prb for subsequent binding of an lxcxe protein.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-182569		Homo sapiens
pmid	sentence
19056339	We therefore compared human cyclin a1- and cyclin a2-containing cdk complexes in vitro by determining kinetic constants and by examining the complexes for their ability to phosphorylate prb and p53. Differences in biochemical activity were observed in cdk2 but not cdk1 when complexed with cyclin a1 versus cyclin a2. Further, cdk1/cyclin a1 is a better kinase complex for phosphorylating potentially physiologically relevant substrates prb and p53 than cdk2/cyclin a2.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-182566		Homo sapiens
pmid	sentence
19056339	We therefore compared human cyclin a1- and cyclin a2-containing cdk complexes in vitro by determining kinetic constants and by examining the complexes for their ability to phosphorylate prb and p53. Differences in biochemical activity were observed in cdk2 but not cdk1 when complexed with cyclin a1 versus cyclin a2. Further, cdk1/cyclin a1 is a better kinase complex for phosphorylating potentially physiologically relevant substrates prb and p53 than cdk2/cyclin a2.

Publications:

1

Organism:

Homo Sapiens

Name	CyclinA2/CDK2 View Modifications
Primary ID	SIGNOR-C83
Links	CPX-2006
Type	complex
Formed by	CDK2, CCNA2
Relations	61

The SIGnaling Network
Open Resource

Summary

Viewer

Search Tools

▶Modifications Tables

Relations