Relation Results

Identifier	Residue	Sequence	Organism
SIGNOR-170451	Ser1007	QHNFSVAsPLTLSQD	Homo sapiens
pmid	sentence
21148318	We identified rbp1 as a novel cdk substrate. Rbp1 is phosphorylated by cdk2 on serines 864 and 1007, which are n- and c-terminal to the lxcxe motif, respectively. Cdk2-mediated phosphorylation of rbp1 or prb destabilizes their interaction in vitro, with concurrent phosphorylation of both proteins leading to their dissociation

Identifier	Residue	Sequence	Organism
SIGNOR-170455	Ser864	RKILGQSsPEKKIRI	Homo sapiens
pmid	sentence
21148318	In the present study we identified rbp1 as a novel cdk substrate. Rbp1 is phosphorylated by cdk2 on serines 864 and 1007, which are n- and c-terminal to the lxcxe motif, respectively. Cdk2-mediated phosphorylation of rbp1 or prb destabilizes their interaction in vitro, with concurrent phosphorylation of both proteins leading to their dissociation

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-69710	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-69714	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-69718	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.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-200867	Ser294	RAANLWPsPLMIKRS	Homo sapiens	Breast Cancer Cell
pmid	sentence
23390529	The pi3k/akt pathway is necessary to activate cdk2, which phosphorylates eralphaser294, and mediates the binding between pin1 and eralpha

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-104660	Ser1044	YPFVRTGsPRRIQLS	Homo sapiens
pmid	sentence
11157749	We now identify 22 in vivo phosphorylation sites of p130, targeted by diverse kinases, and present evidence for three cyclin-dependent kinase 4(6) [cdk4(6)] specific phosphorylations, which appear critical for controlling the growth-restraining activity of p130. site-directed mutagenesis of s1044 to an alanine resulted in the specific loss of d5 when this mutant was ectopically expressed in t98g cells and labelled by [32p]orthophosphate (figure 4b), proving that phosphorylation of s1044 gave rise to the tryptic phosphopeptide d5: tgspr.

Identifier	Residue	Sequence	Organism
SIGNOR-104667	Ser1068	HKNETMLsPREKIFY	Homo sapiens
pmid	sentence
11157749	We now identify 22 in vivo phosphorylation sites of p130, targeted by diverse kinases, and present evidence for three cyclin-dependent kinase 4(6) [cdk4(6)] specific phosphorylations, which appear critical for controlling the growth-restraining activity of p130.

Identifier	Residue	Sequence	Organism
SIGNOR-104671	Ser1080	IFYYFSNsPSKRLRE	Homo sapiens
pmid	sentence
11157749	We now identify 22 in vivo phosphorylation sites of p130, targeted by diverse kinases, and present evidence for three cyclin-dependent kinase 4(6) [cdk4(6)] specific phosphorylations, which appear critical for controlling the growth-restraining activity of p130.

Identifier	Residue	Sequence	Organism
SIGNOR-104675	Ser413	VRYIKENsPCVTPVS	Homo sapiens
pmid	sentence
11157749	We now identify 22 in vivo phosphorylation sites of p130, targeted by diverse kinases, and present evidence for three cyclin-dependent kinase 4(6) [cdk4(6)] specific phosphorylations, which appear critical for controlling the growth-restraining activity of p130.

Identifier	Residue	Sequence	Organism
SIGNOR-104679	Ser639	DEICIAGsPLTPRRV	Homo sapiens
pmid	sentence
11157749	We now identify 22 in vivo phosphorylation sites of p130, targeted by diverse kinases, and present evidence for three cyclin-dependent kinase 4(6) [cdk4(6)] specific phosphorylations, which appear critical for controlling the growth-restraining activity of p130.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-104683	Ser662	GLGRSITsPTTLYDR	Homo sapiens	U2-OS Cell
pmid	sentence
11157749	We now identify 22 in vivo phosphorylation sites of p130, targeted by diverse kinases, and present evidence for three cyclin-dependent kinase 4(6) [cdk4(6)] specific phosphorylations, which appear critical for controlling the growth-restraining activity of p130.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-104687	Ser688	RLFVENDsPSDGGTP	Homo sapiens	U2-OS Cell
pmid	sentence
11157749	We now identify 22 in vivo phosphorylation sites of p130, targeted by diverse kinases, and present evidence for three cyclin-dependent kinase 4(6) [cdk4(6)] specific phosphorylations, which appear critical for controlling the growth-restraining activity of p130.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-104691	Ser952	DSRSHQNsPTELNKD	Homo sapiens	U2-OS Cell
pmid	sentence
11157749	We now identify 22 in vivo phosphorylation sites of p130, targeted by diverse kinases, and present evidence for three cyclin-dependent kinase 4(6) [cdk4(6)] specific phosphorylations, which appear critical for controlling the growth-restraining activity of p130.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-104695	Thr1097	SMIRTGEtPTKKRGI	Homo sapiens	U2-OS Cell
pmid	sentence
11157749	We now identify 22 in vivo phosphorylation sites of p130, targeted by diverse kinases, and present evidence for three cyclin-dependent kinase 4(6) [cdk4(6)] specific phosphorylations, which appear critical for controlling the growth-restraining activity of p130.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-104699	Thr417	KENSPCVtPVSTATH	Homo sapiens	U2-OS Cell
pmid	sentence
11157749	We now identify 22 in vivo phosphorylation sites of p130, targeted by diverse kinases, and present evidence for three cyclin-dependent kinase 4(6) [cdk4(6)] specific phosphorylations, which appear critical for controlling the growth-restraining activity of p130.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-104703	Thr642	CIAGSPLtPRRVTEV	Homo sapiens	U2-OS Cell
pmid	sentence
11157749	We now identify 22 in vivo phosphorylation sites of p130, targeted by diverse kinases, and present evidence for three cyclin-dependent kinase 4(6) [cdk4(6)] specific phosphorylations, which appear critical for controlling the growth-restraining activity of p130.

Identifier	Residue	Sequence	Organism
SIGNOR-104707	Thr694	DSPSDGGtPGRMPPQ	Homo sapiens
pmid	sentence
11157749	We now identify 22 in vivo phosphorylation sites of p130, targeted by diverse kinases, and present evidence for three cyclin-dependent kinase 4(6) [cdk4(6)] specific phosphorylations, which appear critical for controlling the growth-restraining activity of p130.

Publications:

12

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-67540	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-104656	Ser1112	LLEDGSEsPAKRICP	Homo sapiens	U2-OS Cell
pmid	sentence
11157749	When expressed in u2os cells, the phosphorylation-deficient mutant p130(delta)(cdk4), in which the cdk4 specific sites were mutated to alanine residues, imposed a more sustained g1 arrest than a constitutively active prb(delta)(cdk), known to repress all cellular e2f activity

Identifier	Residue	Sequence	Organism
SIGNOR-87492	Ser1112	LLEDGSEsPAKRICP	Homo sapiens
pmid	sentence
12006580	When expressed in u2os cells, the phosphorylation-deficient mutant p130(delta)(cdk4), in which the cdk4 specific sites were mutated to alanine residues, imposed a more sustained g1 arrest than a constitutively active prb(delta)(cdk), known to repress all cellular e2f activity

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-116508	Ser120	LDEPNPNsPANSQAA	Homo sapiens
pmid	sentence
11953320	Hhr6a is phosphorylated in vitro by cdk-1 and -2 on ser120, a residue conserved in all hhr6a homologues, resulting in a 4-fold increase in its ubiquitin-conjugating activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-139469	Ser123	EEGFGSSsPVKSPAA	Homo sapiens
pmid	sentence
16085715	Phosphorylation of serines 53 and 123 (s53 and s123) of wee1a by polo-like kinase 1 (plk1) and cdk, respectively, are required for binding to beta-trcp. During the s and g2 phases, s123 (wee1) is phosphorylated by a cdk (possibly cdk2).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276039	Ser123	EEGFGSSsPVKSPAA	Homo sapiens	HeLa Cell
pmid	sentence
16085715	PS123 primes CK2 to phosphorylate S121, resulting in creation of a β-TrCP phosphodegron (EEGFGpS121) that is responsible for the instability of Wee1A during interphase.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-95578	Ser13	LPTVLPGsPSKTRGQ	Homo sapiens
pmid	sentence
12435275	Given that the dimeric form of tk1 is less active than the tetrameric, we propose that mitotic phosphorylation of serine-13 is of physiological importance, in that it may counteract atp-dependent activation of tk1 by affecting its quaternary structure, thus attenuating its enzymatic function at the g2/m phase.

Identifier	Residue	Sequence	Organism
SIGNOR-120372	Ser13	LPTVLPGsPSKTRGQ	Homo sapiens
pmid	sentence
14697231	Given that the dimeric form of tk1 is less active than the tetrameric, we propose that mitotic phosphorylation of serine-13 is of physiological importance, in that it may counteract atp-dependent activation of tk1 by affecting its quaternary structure, thus attenuating its enzymatic function at the g2/m phase.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-144000	Ser13	ESFTMASsPAQRRRG	Homo sapiens
pmid	sentence
16446360	In this work, by in vitro kinase reactions and mass spectrometry analysis of the products, we have mapped phosphorylation sites in the n terminus of mcm2 by cdc7, cdk2, cdk1, and ck2

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-149416	Ser130	SGEQAEGsPGGPGDS	Homo sapiens
pmid	sentence
15964852	Cdk2 destabilizes p21 via the cy2 cyclin-binding motif and p21 phosphorylation at ser-130.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-197593	Ser1460	APRPVPGsPARDAPA	Homo sapiens
pmid	sentence
22610972	Finally, phosphorylation of tax1bp2 at serine-763 by cyclin-dependent kinase (cdk)2 abolished the tax1bp2-mediated p38 activation and tumor-suppressive activity, indicating that tax1bp2 can adapt cdk2 signaling to the p38/p53/p21 pathway.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-72091	Ser1497	EPGVERSsPSKCPSL	Homo sapiens
pmid	sentence
10550055	However, shrna-mediated depletion of cdk1 alone or small molecule cdk1 inhibition abrogated s phase cell-cycle arrest and the phosphorylation of a subset of atr/atm targets after dna damage. Loss of dna damage-induced checkpoint control was caused by a reduction in formation of brca1-containing foci. Mutation of brca1 at s1497 and s1189/s1191 resulted in loss of cdk1-mediated phosphorylation and also compromised formation of brca1-containing foci.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-187607	Ser1497	EPGVERSsPSKCPSL	Homo sapiens	Lung Cancer Cell
pmid	sentence
19683496	However, shrna-mediated depletion of cdk1 alone or small molecule cdk1 inhibition abrogated s phase cell-cycle arrest and the phosphorylation of a subset of atr/atm targets after dna damage. Loss of dna damage-induced checkpoint control was caused by a reduction in formation of brca1-containing foci. Mutation of brca1 at s1497 and s1189/s1191 resulted in loss of cdk1-mediated phosphorylation and also compromised formation of brca1-containing foci.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Cell Line
SIGNOR-250732	Ser151	DVSPYSLsPVSNKSQ	HEK-293 Cell
pmid	sentence
12560341	A nuclear localization signal conserved in various species was identified in CDH1, and it sufficiently targets green fluorescent protein to the nucleus. Interestingly, a CDH1-4D mutant mimicking the hyperphosphorylated form was constitutively found in the cytoplasm. In further support of the notion that phosphorylation inhibits nuclear import, the nuclear localization signal of CDH1 with two phospho-accepting serine/threonine residues changed into aspartates was unable to drive heterologous protein into the nucleus.

Identifier	Residue	Sequence
SIGNOR-250733	Ser163	KSQKLLRsPRKPTRK
pmid	sentence
12560341	A nuclear localization signal conserved in various species was identified in CDH1, and it sufficiently targets green fluorescent protein to the nucleus. Interestingly, a CDH1-4D mutant mimicking the hyperphosphorylated form was constitutively found in the cytoplasm. In further support of the notion that phosphorylation inhibits nuclear import, the nuclear localization signal of CDH1 with two phospho-accepting serine/threonine residues changed into aspartates was unable to drive heterologous protein into the nucleus.

Publications:

2

Identifier	Residue	Sequence	Organism
SIGNOR-173681	Ser154	AKPEPSPsPRITRKS	Homo sapiens
pmid	sentence
21565170	We report that cyclin-dependent kinases (cdks) 1, 2 and 5 can phosphorylate ser154 of human dnmt1 in vitro. Further evidence of phosphorylation of endogenous dnmt1 at position 154 by cdks is also found in 293 cells treated with roscovitine, a specific inhibitor of cdk1, 2 and 5

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-74466	Ser154	PMDGSFEsPHTMDMS	Homo sapiens
pmid	sentence
10652300	Here we present evidence from in vitro and in vivo assay systems that the degradation of human cyclin a can be inhibited by kinase-inactive mutants of cdk2 and cdc2cdk2 can phosphorylate cyclin a on ser-154

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-182761	Ser158	FVSHSHIsPIKPTEA	Homo sapiens
pmid	sentence
19066288	We also show that dlg1 is phosphorylated by both cdk1 and cdk2 on ser158 and ser442. These phosphorylated sites together affect the nuclear localisation of the protein, and implicate the role of phosphorylation on ser158 and ser442 in its putative nuclear functions as a tumour suppressor. phosphorylation on ser158 and ser442 enhances nuclear expression of dlg1

Identifier	Residue	Sequence	Organism
SIGNOR-182765	Ser443	FLGQTPAsPARYSPV	Homo sapiens
pmid	sentence
19066288	We also show that dlg1 is phosphorylated by both cdk1 and cdk2 on ser158 and ser442. These phosphorylated sites together affect the nuclear localisation of the protein, and implicate the role of phosphorylation on ser158 and ser442 in its putative nuclear functions as a tumour suppressor. phosphorylation on ser158 and ser442 enhances nuclear expression of dlg1

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-84832	Ser164	GLAKSFGsPNRAYTH	Homo sapiens
pmid	sentence
11113184	Cdk2 phosphorylates serine-164 in the cdk7 t loop.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-265958	Ser170	RDSEGFNsPKQCDSS	in vitro
pmid	sentence
12361598	GST-tagged recombinant CP110 (GST-wt) was robustly phosphorylated by cyclin E/CDK2 (Figure 2A). Expression of a mutant derivative of CP110 refractory to CDK phosphorylation provokes marked polyploidy. We localized the majority (nine of ten) of potential CDK2 phosphorylation sites in CP110 to an amino-terminal fragment (GST-ΔN1; Figure 1B)

Identifier	Residue	Sequence	Organism
SIGNOR-265960	Ser366	GSYAKLPsPEPSMSP	in vitro
pmid	sentence
12361598	GST-tagged recombinant CP110 (GST-wt) was robustly phosphorylated by cyclin E/CDK2 (Figure 2A). Expression of a mutant derivative of CP110 refractory to CDK phosphorylation provokes marked polyploidy. We localized the majority (nine of ten) of potential CDK2 phosphorylation sites in CP110 to an amino-terminal fragment (GST-ΔN1; Figure 1B)

Identifier	Residue	Sequence	Organism
SIGNOR-265962	Ser372	PSPEPSMsPKMHRRR	in vitro
pmid	sentence
12361598	GST-tagged recombinant CP110 (GST-wt) was robustly phosphorylated by cyclin E/CDK2 (Figure 2A). Expression of a mutant derivative of CP110 refractory to CDK phosphorylation provokes marked polyploidy. We localized the majority (nine of ten) of potential CDK2 phosphorylation sites in CP110 to an amino-terminal fragment (GST-ΔN1; Figure 1B)

Identifier	Residue	Sequence	Organism
SIGNOR-265956	Ser400	PINACELsPKGKEQA	in vitro
pmid	sentence
12361598	GST-tagged recombinant CP110 (GST-wt) was robustly phosphorylated by cyclin E/CDK2 (Figure 2A). Expression of a mutant derivative of CP110 refractory to CDK phosphorylation provokes marked polyploidy. We localized the majority (nine of ten) of potential CDK2 phosphorylation sites in CP110 to an amino-terminal fragment (GST-ΔN1; Figure 1B)

Identifier	Residue	Sequence	Organism
SIGNOR-265957	Ser45	FHGVAILsPLLNIEK	in vitro
pmid	sentence
12361598	GST-tagged recombinant CP110 (GST-wt) was robustly phosphorylated by cyclin E/CDK2 (Figure 2A). Expression of a mutant derivative of CP110 refractory to CDK phosphorylation provokes marked polyploidy. We localized the majority (nine of ten) of potential CDK2 phosphorylation sites in CP110 to an amino-terminal fragment (GST-ΔN1; Figure 1B)

Identifier	Residue	Sequence	Organism
SIGNOR-265963	Ser516	ASSQCIAsPNFGTVS	in vitro
pmid	sentence
12361598	GST-tagged recombinant CP110 (GST-wt) was robustly phosphorylated by cyclin E/CDK2 (Figure 2A). Expression of a mutant derivative of CP110 refractory to CDK phosphorylation provokes marked polyploidy. We localized the majority (nine of ten) of potential CDK2 phosphorylation sites in CP110 to an amino-terminal fragment (GST-ΔN1; Figure 1B)

Identifier	Residue	Sequence	Organism
SIGNOR-265961	Thr194	FPKTSSAtPQETLIS	in vitro
pmid	sentence
12361598	GST-tagged recombinant CP110 (GST-wt) was robustly phosphorylated by cyclin E/CDK2 (Figure 2A). Expression of a mutant derivative of CP110 refractory to CDK phosphorylation provokes marked polyploidy. We localized the majority (nine of ten) of potential CDK2 phosphorylation sites in CP110 to an amino-terminal fragment (GST-ΔN1; Figure 1B)

Identifier	Residue	Sequence	Organism
SIGNOR-265959	Thr566	NTRQQMDtPMVSCGN	in vitro
pmid	sentence
12361598	GST-tagged recombinant CP110 (GST-wt) was robustly phosphorylated by cyclin E/CDK2 (Figure 2A). Expression of a mutant derivative of CP110 refractory to CDK phosphorylation provokes marked polyploidy. We localized the majority (nine of ten) of potential CDK2 phosphorylation sites in CP110 to an amino-terminal fragment (GST-ΔN1; Figure 1B)

Publications:

8

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-84949	Ser184	NEEAKRKsPKKKEKC	Homo sapiens
pmid	sentence
11102515	In particular, we have recently found that the cdk2/cyclin e complex can phosphorylate coilin in vitro . there is but a single consensus cdk2/cyclin e phosphorylation site in coilin, located at serine 184. when serine 184 was mutated to an alanine (s184a), mimicking a dephosphorylated state, a nucleolar mislocalization similar to that of gfp-coilin(1_248) was observed

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277366	Ser19	QRVQAMKsPDHNGED	Homo sapiens	MDA-MB-231 Cell
pmid	sentence
28842430	In the present study, we found that S19 site phosphorylation of PTPN12 by CDK2 discharged its antitumor activity by down-regulation of its inhibitory role in cell migration, but not affecting its other regulatory functions.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-160626	Ser197	SFGLSAMsPTKAAVD	Homo sapiens	Leukemia Cell
pmid	sentence
18246121	Here we show that the main cyclin-dependent kinase involved at the g(1) to s transition (cdk2) phosphorylates plzf at two consensus sites found within pest domains present in the hinge region of the protein. This phosphorylation triggers the ubiquitination and subsequent degradation of plzf, which impairs plzf transcriptional repression ability and antagonizes its growth inhibitory effects.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-160630	Thr282	RGKEGPGtPTRSSVI	Homo sapiens	Leukemia Cell
pmid	sentence
18246121	Here we show that the main cyclin-dependent kinase involved at the g(1) to s transition (cdk2) phosphorylates plzf at two consensus sites found within pest domains present in the hinge region of the protein. This phosphorylation triggers the ubiquitination and subsequent degradation of plzf, which impairs plzf transcriptional repression ability and antagonizes its growth inhibitory effects.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-84980	Ser20	HVAGGPPsPEVGSPL	Homo sapiens
pmid	sentence
11110801	In vitro phosphorylation of pr with cdk2 has revealed five additional in vitro cdk2 phosphorylation sites: ser(25), ser(213), thr(430), ser(554), and ser(676).

Identifier	Residue	Sequence	Organism
SIGNOR-84984	Ser213	SGAPVKPsPQAAAVE	Homo sapiens
pmid	sentence
11110801	In vitro phosphorylation of pr with cdk2 has revealed five additional in vitro cdk2 phosphorylation sites: ser(25), ser(213), thr(430), ser(554), and ser(676).

Identifier	Residue	Sequence	Organism
SIGNOR-84988	Ser25	PPSPEVGsPLLCRPA	Homo sapiens
pmid	sentence
11110801	In vitro phosphorylation of pr with cdk2 has revealed five additional in vitro cdk2 phosphorylation sites: ser(25), ser(213), thr(430), ser(554), and ser(676).

Identifier	Residue	Sequence	Organism
SIGNOR-84992	Ser554	PDSEASQsPQYSFES	Homo sapiens
pmid	sentence
11110801	In vitro phosphorylation of pr with cdk2 has revealed five additional in vitro cdk2 phosphorylation sites: ser(25), ser(213), thr(430), ser(554), and ser(676).

Identifier	Residue	Sequence	Organism
SIGNOR-84996	Ser676	LSQRFTFsPGQDIQL	Homo sapiens
pmid	sentence
11110801	In vitro phosphorylation of pr with cdk2 has revealed five additional in vitro cdk2 phosphorylation sites: ser(25), ser(213), thr(430), ser(554), and ser(676).

Identifier	Residue	Sequence	Organism
SIGNOR-85000	Thr430	PPLPPRAtPSRPGEA	Homo sapiens
pmid	sentence
11110801	In vitro phosphorylation of pr with cdk2 has revealed five additional in vitro cdk2 phosphorylation sites: ser(25), ser(213), thr(430), ser(554), and ser(676).

Publications:

6

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-176509	Ser200	YSGDSDAsSPRSNCS	Homo sapiens
pmid	sentence
21902831	Cyclin e/cdk2 can phosphorylate myod at serine 200, which causes ubiquitination and degradation of this transcription factor during g1, preventing its accumulation and a commitment to differentiation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-249426	Ser203	DLEFSSGsPGKETNE	in vitro
pmid	sentence
9199329	Cyclin-dependent kinase (CDK) and mitogen-activated protein kinase (MAPK) phosphorylate the rat glucocorticoid receptor in vitro at distinct sites that together correspond to the major phosphorylated receptor residues observed in vivo; MAPK phosphorylates receptor residues threonine 171 and serine 246, whereas multiple CDK complexes modify serines 224 and 232.\|MAPKs and CDKs exert opposite effects on receptor transcriptional enhancement. From our results, we speculate that activators of the MAPK pathway, such as growth factors, insulin, and certain oncoproteins, or inhibitors of CDK function, such as tumor growth factor beta (TGF_), p21, and p27, might attenuate receptor-induced transcrip- tional responses. In contrast, negative regulators of MAPK, such as pKA, as well as activators of CDK, such as the cyclins or CAKs, should potentiate receptor action.

Identifier	Residue	Sequence	Organism
SIGNOR-249427	Ser211	PGKETNEsPWRSDLL	in vitro
pmid	sentence
9199329	Cyclin-dependent kinase (CDK) and mitogen-activated protein kinase (MAPK) phosphorylate the rat glucocorticoid receptor in vitro at distinct sites that together correspond to the major phosphorylated receptor residues observed in vivo; MAPK phosphorylates receptor residues threonine 171 and serine 246, whereas multiple CDK complexes modify serines 224 and 232.\|MAPKs and CDKs exert opposite effects on receptor transcriptional enhancement. From our results, we speculate that activators of the MAPK pathway, such as growth factors, insulin, and certain oncoproteins, or inhibitors of CDK function, such as tumor growth factor beta (TGF_), p21, and p27, might attenuate receptor-induced transcrip- tional responses. In contrast, negative regulators of MAPK, such as pKA, as well as activators of CDK, such as the cyclins or CAKs, should potentiate receptor action.

Publications:

2

Organism:

In Vitro

Pathways:

Adipogenesis

Identifier	Residue	Sequence	Organism
SIGNOR-250749	Ser204	NHSMDAGsPNLSPNP	in vitro
pmid	sentence
15241418	Thus, we have shown that Smad3 is phosphorylated by CDK4 and CDK2. Mutation of its CDK phosphorylation sites increases its transcriptional activity and antiproliferative function. \| Thr 8 and the four sites in the linker (Thr 178, Ser 203, Ser 207 and Ser 212). Each of the five sites was phosphorylated by both CDK4 and CDK2 in vitro, and only Thr 8, Thr 178 and Ser 212 were phosphorylated by CDK4 and CDK2 in vivo phosphorylated by both CDK4 and CDK2 in vitro, and only Thr 8, Thr 178 and Ser 212 were phosphorylated by CDK4 and CDK2 in vivo.

Identifier	Residue	Sequence	Organism
SIGNOR-250750	Ser208	DAGSPNLsPNPMSPA	in vitro
pmid	sentence
15241418	Thus, we have shown that Smad3 is phosphorylated by CDK4 and CDK2. Mutation of its CDK phosphorylation sites increases its transcriptional activity and antiproliferative function. We propose that under physiological conditions, phosphorylation of Smad3 by CDK inhibits its transcriptional activity, contributing to a decreased level of p15 and an increased level of c-Myc, thus facilitating cell cycle progression from G1 to S phase.

Publications:

2

Organism:

In Vitro

Pathways:

Adipogenesis

Identifier	Residue	Sequence	Organism
SIGNOR-150121	Ser210	TTTGQVTsPVKGASF	Homo sapiens
pmid	sentence
17040896	Dna ligase iii_ is specifically phosphorylated in replicating cells by the cell cycle kinase cdk2. However, in response to oxidative dna damage, dna ligase iii_ is dephosphorylated in a pathway that is dependent upon the dna damage-activated, phosphatidylinositol 3-phosphate (pi3)1-related kinase atm.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-126732	Ser213	NLSPNPMsPAHNNLD	Homo sapiens
pmid	sentence
15241418	We have mapped cdk4 and cdk2 phosphorylation sites to thr 8, thr 178 and ser 212 in smad3. taken together, these findings indicate that cdk phosphorylation of smad3 inhibits its transcriptional activity and antiproliferative function

Identifier	Residue	Sequence	Organism
SIGNOR-182967	Ser213	NLSPNPMsPAHNNLD	Homo sapiens
pmid	sentence
19114991	In the nucleus cdk2/4-mediated phosphorylation of smad3 occurs mostly at thr8, thr179, and ser213. Cdk-dependent phosphorylation of smad3 inhibits its transcriptional activity

Identifier	Residue	Sequence	Organism
SIGNOR-126740	Thr8	MSSILPFtPPIVKRL	Homo sapiens
pmid	sentence
15241418	We have mapped cdk4 and cdk2 phosphorylation sites to thr 8, thr 178 and ser 212 in smad3. taken together, these findings indicate that cdk phosphorylation of smad3 inhibits its transcriptional activity and antiproliferative function

Identifier	Residue	Sequence	Organism
SIGNOR-182975	Thr8	MSSILPFtPPIVKRL	Homo sapiens
pmid	sentence
19114991	In the nucleus cdk2/4-mediated phosphorylation of smad3 occurs mostly at thr8, thr179, and ser213. Cdk-dependent phosphorylation of smad3 inhibits its transcriptional activity

Publications:

4

Organism:

Homo Sapiens

Pathways:

Adipogenesis

Identifier	Residue	Sequence	Organism
SIGNOR-232134	Ser213	NLSPNPMsPAHNNLD	Homo sapiens
pmid	sentence
15241418	We have mapped CDK4 and CDK2 phosphorylation sites to Thr 8, Thr 178 and Ser 212 in Smad3. Mutation of the CDK phosphorylation sites increases Smad3 transcriptional activity

Identifier	Residue	Sequence	Organism
SIGNOR-182971	Thr179	PQSNIPEtPPPGYLS	Homo sapiens
pmid	sentence
19114991	In the nucleus cdk2/4-mediated phosphorylation of smad3 occurs mostly at thr8, thr179, and ser213. Cdk-dependent phosphorylation of smad3 inhibits its transcriptional activity

Identifier	Residue	Sequence	Organism
SIGNOR-126736	Thr179	PQSNIPEtPPPGYLS	Homo sapiens
pmid	sentence
15241418	We have mapped cdk4 and cdk2 phosphorylation sites to thr 8, thr 178 and ser 212 in smad3. taken together, these findings indicate that cdk phosphorylation of smad3 inhibits its transcriptional activity and antiproliferative function

Identifier	Residue	Sequence	Organism
SIGNOR-217734	Thr8	MSSILPFtPPIVKRL	Homo sapiens
pmid	sentence
15241418	We have mapped CDK4 and CDK2 phosphorylation sites to Thr 8, Thr 178 and Ser 212 in Smad3. Mutation of the CDK phosphorylation sites increases Smad3 transcriptional activity,

Publications:

4

Organism:

Homo Sapiens

Pathways:

Adipogenesis

Identifier	Residue	Sequence	Organism
SIGNOR-165872	Ser214	SRSGLYRsPSMPENL	Homo sapiens
pmid	sentence
20530684	The cyclin e/cdk2 complex phosphorylates cdc25c on ser(214), leading to its premature activation, which coincides with higher cyclin b/cdk1 and polo-like kinase 1 (plk1) activities in an s-phase-enriched population that result in faster mitotic entry.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-156928	Ser224	APSVSHVsPRKNPSV	Homo sapiens
pmid	sentence
17638878	Atrip is a cdk2 substrate, and cdk2-dependent phosphorylation of s224 regulates the ability of atr-atrip to promote cell cycle arrest in response to dna damage./ One possibility is s224 phosphorylation creates a binding site for another protein involved in the g2-m checkpoint response

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-156932	Ser239	VIKPEACsPQFGKTS	Homo sapiens
pmid	sentence
17638878	Two novel phosphorylation sites on atrip were identified, s224 and s239

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-121198	Ser244	QPVSAPPsPRDISME	Homo sapiens
pmid	sentence
14712216	Serine 244 phosphorylation is required for h4 apoptotic function.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-150028	Ser249	EGGKSGKsPRRRAAS	Homo sapiens
pmid	sentence
17038621	Cdk2 specifically phosphorylated foxo1 at serine-249 (ser249) in vitro and in vivo. Phosphorylation of ser249 resulted in cytoplasmic localization and inhibition of foxo1.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Adipogenesis

Identifier	Residue	Sequence	Organism
SIGNOR-138928	Ser249	DTRQIQPsPPWSYDQ	Homo sapiens
pmid	sentence
16046550	We have identified four phosphorylation sites on aml1c that are necessary for transcriptional activity of aml1c in k562 and 293t cells (27).4 mutation of these four sites (serine 276, serine 293, serine 303, and threonine 300) to alanine abolishes transcriptional activation, whereas mutation of these sites to aspartic acid (which mimics phosphorylation) results in a hyperactive protein.

Identifier	Residue	Sequence	Organism
SIGNOR-138932	Ser266	QYLGSIAsPSVHPAT	Homo sapiens
pmid	sentence
16046550	We have identified four phosphorylation sites on aml1c that are necessary for transcriptional activity of aml1c in k562 and 293t cells (27).4 mutation of these four sites (serine 276, serine 293, serine 303, and threonine 300) to alanine abolishes transcriptional activation, whereas mutation of these sites to aspartic acid (which mimics phosphorylation) results in a hyperactive protein.

Identifier	Residue	Sequence	Organism
SIGNOR-138936	Ser276	VHPATPIsPGRASGM	Homo sapiens
pmid	sentence
16046550	We have identified four phosphorylation sites on aml1c that are necessary for transcriptional activity of aml1c in k562 and 293t cells (27).4 mutation of these four sites (serine 276, serine 293, serine 303, and threonine 300) to alanine abolishes transcriptional activation, whereas mutation of these sites to aspartic acid (which mimics phosphorylation) results in a hyperactive protein.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-138940	Thr273	SPSVHPAtPISPGRA	Homo sapiens	HEK-293T Cell
pmid	sentence
16046550	We have identified four phosphorylation sites on aml1c that are necessary for transcriptional activity of aml1c in k562 and 293t cells (27).4 mutation of these four sites (serine 276, serine 293, serine 303, and threonine 300) to alanine abolishes transcriptional activation, whereas mutation of these sites to aspartic acid (which mimics phosphorylation) results in a hyperactive protein.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-252892	Ser249	EGGKSGKsPRRRAAS	Homo sapiens
pmid	sentence
17038621	Cdk2 specifically phosphorylated foxo1 at serine-249 (ser249) in vitro and in vivo. Phosphorylation of ser249 resulted in cytoplasmic localization and inhibition of foxo1.

Identifier	Residue	Organism	Cell Line
SIGNOR-252891		Homo sapiens	Breast Cancer Cell, Prostate Gland Cancer Cell, Leukemia Cell, Glioblastoma Cell
pmid	sentence
19188143	Additionally, ck1, dyrk1a, and cdk2 also phosphorylate foxos at various sites to inhibit foxos activity

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277374	Ser251	EVSIRVGsPQPSSSG	Homo sapiens	HEK-293T Cell
pmid	sentence
29229926	During S/G2 phases, CDK1 and CDK2 (CDK1/2) phosphorylate RECQL4 on serines 89 and 251, enhancing MRE11/RECQL4 interaction and RECQL4 recruitment to DSBs.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-273601	Ser254	PAPQSQLsPNAKEFV	in vitro
pmid	sentence
32404348	Taken together, these observations strongly support the notion that several different CDK-cyclin complexes are involved in the phosphorylation of Tob2 at S254.A more detailed regulatory context of Tob2 phosphorylation at S254 is provided by our findings from mass-spec and in vitro kinase analyses that suggest connections to PP2B and PP2C phosphatases and CDK-cyclin complexes, particularly CDK1, CDK2, and CDK4 (Table 1; Supplemental Table S2).One possibility is that the phosphorylation of S254 helps stabilize the interaction of Tob2 with the Ccr4–Not complex, which could contribute to Tob2's ability to recruit the entire Ccr4–Not complex and thus further enhances deadenylation.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-150839	Ser263	CKLFDSPsLCSSSTR	Homo sapiens
pmid	sentence
17110335	We show here that dna-responsive checkpoints activate pp2a/b56delta phosphatase complexes to dephosphorylate cdc25 at a site distinct from ser287 (t138), the phosphorylation of which is required for 14-3-3 release.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-149976	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-138825	Ser283	RSVPEPLsPVSSLQA	Homo sapiens
pmid	sentence
16027724	Phosphorylation of the homeotic tumor suppressor Cdx2 mediates its ubiquitin-dependent proteasome degradation\|We found that cyclin-dependent kinase 2 phosphorylated Cdx2 in vitro and in vivo.

Identifier	Residue	Sequence	Organism
SIGNOR-250728	Ser287	EPLSPVSsLQASVPG	Homo sapiens
pmid	sentence
16027724	Phosphorylation of the homeotic tumor suppressor Cdx2 mediates its ubiquitin-dependent proteasome degradation\|We found that cyclin-dependent kinase 2 phosphorylated Cdx2 in vitro and in vivo.

Identifier	Residue	Sequence	Organism
SIGNOR-250729	Ser291	PVSSLQAsVPGSVPG	Homo sapiens
pmid	sentence
16027724	Phosphorylation of the homeotic tumor suppressor Cdx2 mediates its ubiquitin-dependent proteasome degradation\|We found that cyclin-dependent kinase 2 phosphorylated Cdx2 in vitro and in vivo.

Identifier	Residue	Sequence	Organism
SIGNOR-250730	Ser295	LQASVPGsVPGVLGP	Homo sapiens
pmid	sentence
16027724	Phosphorylation of the homeotic tumor suppressor Cdx2 mediates its ubiquitin-dependent proteasome degradation\|We found that cyclin-dependent kinase 2 phosphorylated Cdx2 in vitro and in vivo.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-175079	Ser286	TSGGVSEsPSGFSKH	Homo sapiens
pmid	sentence
21765472	Chk1 itself is also subject to cdk-mediated phosphorylation at serines 286 and 301 (s286 and 301). We show that chk1 s301 phosphorylation increases as cells progress through s and g2 and that both cdk1 and cdk2 are likely to contribute to this modification in vivo. We also find that substitution of s286 and s301 with non-phosphorylatable alanine residues strongly attenuates dna damage-induced chk1 activation and g2 checkpoint proficiency

Identifier	Residue	Sequence	Organism
SIGNOR-175083	Ser301	IQSNLDFsPVNSASS	Homo sapiens
pmid	sentence
21765472	Chk1 itself is also subject to cdk-mediated phosphorylation at serines 286 and 301 (s286 and 301). We show that chk1 s301 phosphorylation increases as cells progress through s and g2 and that both cdk1 and cdk2 are likely to contribute to this modification in vivo. We also find that substitution of s286 and s301 with non-phosphorylatable alanine residues strongly attenuates dna damage-induced chk1 activation and g2 checkpoint proficiency

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-74708	Ser294	APMAPGRsPLATTVM	Homo sapiens	Breast Cancer Cell
pmid	sentence
10655479	Phosphorylation of human progesterone receptors at serine-294 by mitogen-activated protein kinase signals their degradation by the 26s proteasome

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-123471	Ser304	LSPAFDHsPNKIMTE	Homo sapiens
pmid	sentence
15030318	Our studies identify ser-304 as a major phosphorylation site in human tcptp, and the tc45 variant as a novel mitotic cdk substrate.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-184160	Ser309	SLGEGNGsPNHQPEP	Homo sapiens
pmid	sentence
19237534	In vitro, lsf is phosphorylated by cyclin e/cyclin-dependent kinase 2 (cdk2), cyclin c/cdk2, and cyclin c/cdk3, predominantly on s309. Phosphorylation by cyclin c/cyclin-dependent kinase 2 following mitogenic stimulation of murine fibroblasts inhibits transcriptional activity of lsf during g1 progression

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-119379	Ser315	LPNNTSSsPQPKKKP	Homo sapiens
pmid	sentence
24173284	The N-terminus of E2F1 can interact directly with a region towards the C-terminus of p53, resulting in increased nuclear retention of p53 and p53-mediated transcription and apoptosis. This is inhibited by competition between p53 and cyclin A at the binding site within E2F19,10. The interaction between p53 and E2F1 is enhanced by phosphorylation of p53 on Ser315, a residue within the E2F1 binding region that is phosphorylated by cell cycle kinases such as cdk1, cdk2, cdk9 and Aurora kinase A

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-100881	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
SIGNOR-100885	Ser54	ELQPMPTsPGVDLQS	Homo sapiens
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-100889	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.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-100893	Thr19	GSRRGRAtPAQTPRS	Homo sapiens	HeLa Cell
pmid	sentence
12714602	We report here that human mcm4, a subunit of the putative dna replicative helicase, is extensively phosphorylated in hela cells when they are incubated in the presence of inhibitors of dna synthesis or are exposed to uv irradiation. The data presented here indicate that the consecutive actions of atr-chk1 and cdk2 kinases are involved in this phosphorylation in the presence of hydroxyurea. Phosphorylation of t19 correlates with lowered level of dna helicase activity of the purified mcm4,6,7 complex.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-250742	Ser320	GEGGRFFsPKEKDSP
pmid	sentence
12857729	Cdk2 phosphorylates two serine residues near the DNA-binding domain of the YA subunit of NF-Y. Cyclin A-cdk2 appears to associate with NF-Y both in vitro and in vivo. Furthermore, YA protein is phosphorylated in parallel with a cell cycle-dependent activation of cdk2 kinase and cyclin A expression. YA phosphorylation is unnecessary for heterotrimer formation with the YB-YC dimer. However, NF-Y containing a phosphorylation-deficient mutant form of YA, YA-aa, has its DNA binding activity impaired. \ To examine whether cdk2 phosphorylates the two serine residues at positions 320 and 326 in YA, we replaced either or both with alanine by site-directed mutagenesis. In a kinase assay using purified GST fusion proteins in vitro, cdk2 phosphorylated the wild type and both of the single-mutant proteins (YA-as and -sa), but not the double-mutant protein (YA-aa)

Identifier	Residue	Sequence
SIGNOR-250743	Ser326	FSPKEKDsPHMQDPN
pmid	sentence
12857729	Cdk2 phosphorylates two serine residues near the DNA-binding domain of the YA subunit of NF-Y. Cyclin A-cdk2 appears to associate with NF-Y both in vitro and in vivo. Furthermore, YA protein is phosphorylated in parallel with a cell cycle-dependent activation of cdk2 kinase and cyclin A expression. YA phosphorylation is unnecessary for heterotrimer formation with the YB-YC dimer. However, NF-Y containing a phosphorylation-deficient mutant form of YA, YA-aa, has its DNA binding activity impaired. \ To examine whether cdk2 phosphorylates the two serine residues at positions 320 and 326 in YA, we replaced either or both with alanine by site-directed mutagenesis. In a kinase assay using purified GST fusion proteins in vitro, cdk2 phosphorylated the wild type and both of the single-mutant proteins (YA-as and -sa), but not the double-mutant protein (YA-aa)

Publications:

2

Identifier	Residue	Sequence	Organism
SIGNOR-199020	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-274049	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-274050	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-158612	Ser36	PRKQPPVsPGTALVG	Homo sapiens
pmid	sentence
17960875	Here, we found that hipk2 phosphorylates hmga1a at ser-35, thr-52, and thr-77, and hmga1b at thr-41 and thr-66. In addition, we demonstrated that cdc2, which is known to phosphorylate hmga1 proteins, could induce the phosphorylation of hmga1 proteins at the same ser/thr sites. we found that the hipk2-phosphorylated hmga1a reduced the binding affinity of hmga1a to human germ line promoter, and the drop in binding affinity induced by hipk2 phosphorylation was lower than that introduced by cdc2 phosphorylation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-177972	Ser368	PNPSTSAsPKKSPPP	Homo sapiens
pmid	sentence
18332217	We define ser-331 as the site phosphorylated by cyclin e-cdk2, cyclin a-cdk2, and p35-cdk5 both in vitro and in cells. Importantly, phosphorylation at ser-331 inhibits the catalytic activity of sirt2.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-167830	Ser373	SSRSAPAsPNHAGVL	Homo sapiens
pmid	sentence
20810654	We have mapped two cdk phosphorylation sites, serines 368 and 423, which play a role in defining foxk2 function through regulating its stability and its activity as a transcriptional repressor protein. These two cdk sites appear vital for foxk2 function because expression of a mutant lacking these sites cannot be tolerated and causes apoptosis.

Identifier	Residue	Sequence	Organism
SIGNOR-167834	Ser428	FAQSAPGsPLSSQPV	Homo sapiens
pmid	sentence
20810654	We have mapped two cdk phosphorylation sites, serines 368 and 423, which play a role in defining foxk2 function through regulating its stability and its activity as a transcriptional repressor protein. These two cdk sites appear vital for foxk2 function because expression of a mutant lacking these sites cannot be tolerated and causes apoptosis.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-181603	Ser38	KIGPLGLsPKKVGDD	Homo sapiens
pmid	sentence
18847512	Finally, we selected one novel substrate, the ribosomal protein rl12, for further study: site-directed mutagenesis and phosphopeptide mapping confirmed that cdk2 phosphorylates rl12 in vitro and in vivo on the same site determined by our methods.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-186414	Ser387	LSEQNRAsPLPSGLL	Homo sapiens
pmid	sentence
19561641	Phosphorylation of threonine 395 has been linked to the proteasome-mediated degradation of full length cyclin e

Identifier	Residue	Sequence	Organism
SIGNOR-118555	Ser399	GLLTPPQsGKKQSSG	Homo sapiens
pmid	sentence
14536078	Phosphorylation-triggered ubiquitination has been proposed to be the major pathway regulating cyclin e protein abundance. Cdk2 activity is required for cyclin e turnover in vivo because it phosphorylates s384. Mutation of ser384 to alanine also rendered cyclin e resistant to degradation

Identifier	Residue	Sequence	Organism
SIGNOR-186418	Thr395	PLPSGLLtPPQSGKK	Homo sapiens
pmid	sentence
19561641	Phosphorylation of threonine 395 has been linked to the proteasome-mediated degradation of full length cyclin e

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-235419	Ser389	INKKQATsPASKKPA	Mus musculus	NIH-3T3 Cell
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:

Mus Musculus

Identifier	Residue	Sequence	Cell Line
SIGNOR-250734	Ser393	RGELIPIsPSTEVGG	HEK-293 Cell
pmid	sentence
10593981	Ten phosphorylation sites carboxyl-terminal to the DNA-binding domain were identified by this method: threonines at positions 267, 408, 497, 519, 522, and 524 and serines at positions 283, 396, 455, and 581. \| Our results indicate that B-Myb can be phosphorylated in a cell-free system by both cyclin A-Cdk2 and cyclin E-Cdk2 complexes. \| These data suggest that B-Myb is a target for phosphorylation by cyclin-Cdk2 and that phosphorylation of B-Myb regulates its transcriptional activity.

Identifier	Residue	Sequence	Cell Line
SIGNOR-250735	Ser452	PVKTLPFsPSQFLNF	HEK-293 Cell
pmid	sentence
10593981	Ten phosphorylation sites carboxyl-terminal to the DNA-binding domain were identified by this method: threonines at positions 267, 408, 497, 519, 522, and 524 and serines at positions 283, 396, 455, and 581. \| Our results indicate that B-Myb can be phosphorylated in a cell-free system by both cyclin A-Cdk2 and cyclin E-Cdk2 complexes. \| These data suggest that B-Myb is a target for phosphorylation by cyclin-Cdk2 and that phosphorylation of B-Myb regulates its transcriptional activity.

Identifier	Residue	Sequence	Cell Line
SIGNOR-250736	Thr266	TDLDAVRtPEPLEEF	HEK-293 Cell
pmid	sentence
10593981	Ten phosphorylation sites carboxyl-terminal to the DNA-binding domain were identified by this method: threonines at positions 267, 408, 497, 519, 522, and 524 and serines at positions 283, 396, 455, and 581. \| Our results indicate that B-Myb can be phosphorylated in a cell-free system by both cyclin A-Cdk2 and cyclin E-Cdk2 complexes. \| These data suggest that B-Myb is a target for phosphorylation by cyclin-Cdk2 and that phosphorylation of B-Myb regulates its transcriptional activity.

Identifier	Residue	Sequence	Cell Line
SIGNOR-250737	Thr405	VGGSGIGtPPSVLKR	HEK-293 Cell
pmid	sentence
10593981	Ten phosphorylation sites carboxyl-terminal to the DNA-binding domain were identified by this method: threonines at positions 267, 408, 497, 519, 522, and 524 and serines at positions 283, 396, 455, and 581. \| Our results indicate that B-Myb can be phosphorylated in a cell-free system by both cyclin A-Cdk2 and cyclin E-Cdk2 complexes. \| These data suggest that B-Myb is a target for phosphorylation by cyclin-Cdk2 and that phosphorylation of B-Myb regulates its transcriptional activity.

Identifier	Residue	Sequence	Cell Line
SIGNOR-250739	Thr515	QKYSMDNtPHTPTPF	HEK-293 Cell
pmid	sentence
10593981	Ten phosphorylation sites carboxyl-terminal to the DNA-binding domain were identified by this method: threonines at positions 267, 408, 497, 519, 522, and 524 and serines at positions 283, 396, 455, and 581. \| Our results indicate that B-Myb can be phosphorylated in a cell-free system by both cyclin A-Cdk2 and cyclin E-Cdk2 complexes. \| These data suggest that B-Myb is a target for phosphorylation by cyclin-Cdk2 and that phosphorylation of B-Myb regulates its transcriptional activity.

Identifier	Residue	Sequence
SIGNOR-250740	Thr518	SMDNTPHtPTPFKNA
pmid	sentence
10593981	Ten phosphorylation sites carboxyl-terminal to the DNA-binding domain were identified by this method: threonines at positions 267, 408, 497, 519, 522, and 524 and serines at positions 283, 396, 455, and 581. \| Our results indicate that B-Myb can be phosphorylated in a cell-free system by both cyclin A-Cdk2 and cyclin E-Cdk2 complexes. \| These data suggest that B-Myb is a target for phosphorylation by cyclin-Cdk2 and that phosphorylation of B-Myb regulates its transcriptional activity.

Identifier	Residue	Sequence	Organism
SIGNOR-250741	Thr520	DNTPHTPtPFKNALE	Homo sapiens
pmid	sentence
10593981	Ten phosphorylation sites carboxyl-terminal to the DNA-binding domain were identified by this method: threonines at positions 267, 408, 497, 519, 522, and 524 and serines at positions 283, 396, 455, and 581. \| Our results indicate that B-Myb can be phosphorylated in a cell-free system by both cyclin A-Cdk2 and cyclin E-Cdk2 complexes. \| These data suggest that B-Myb is a target for phosphorylation by cyclin-Cdk2 and that phosphorylation of B-Myb regulates its transcriptional activity.

Publications:

7

Organism:

, Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-154051	Ser395	PGLEVPSsPLRKAKR	Homo sapiens
pmid	sentence
17389604	Moreover, we found cyclin b1/cdk1 to phosphorylate nipa at ser-395 in mitosis. Mutation of both ser-359 and ser-395 impaired effective inactivation of the scfnipa complex, resulting in reduced levels of mitotic cyclin b1

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-123231	Ser44	LENDFFNsPPRKTVR	Homo sapiens
pmid	sentence
15004009	Cdk2/cyclin e-mediated phosphorylation at ser 44 activates tif-ia

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-180759	Ser477	NSMNKLPsVSQLINP	Homo sapiens
pmid	sentence
18769144	Atm kinase is a master switch for the delta np63 alpha phosphorylation/degradation in human head and neck squamous cell carcinoma cells upon dna damage. We previously found that the pro-apoptotic dna damaging agent, cisplatin, mediated the proteasome-dependent degradation of delta np63 alpha associated with its increased phosphorylated status. We found that delta np63 alpha is phosphorylated in the time-dependent fashion at the following positions: s385, t397 and s466, which were surrounded by recognition motifs for atm, cdk2 and p70s6k kinases, respectively

Identifier	Residue	Sequence	Organism
SIGNOR-180763	Ser560	LARLGCSsCLDYFTT	Homo sapiens
pmid	sentence
18769144	Atm kinase is a master switch for the delta np63 alpha phosphorylation/degradation in human head and neck squamous cell carcinoma cells upon dna damage. We previously found that the pro-apoptotic dna damaging agent, cisplatin, mediated the proteasome-dependent degradation of delta np63 alpha associated with its increased phosphorylated status. We found that delta np63 alpha is phosphorylated in the time-dependent fashion at the following positions: s385, t397 and s466, which were surrounded by recognition motifs for atm, cdk2 and p70s6k kinases, respectively

Identifier	Residue	Sequence	Organism
SIGNOR-180767	Thr491	PQQRNALtPTTIPDG	Homo sapiens
pmid	sentence
18769144	Atm kinase is a master switch for the delta np63 alpha phosphorylation/degradation in human head and neck squamous cell carcinoma cells upon dna damage. We previously found that the pro-apoptotic dna damaging agent, cisplatin, mediated the proteasome-dependent degradation of delta np63 alpha associated with its increased phosphorylated status. We found that delta np63 alpha is phosphorylated in the time-dependent fashion at the following positions: s385, t397 and s466, which were surrounded by recognition motifs for atm, cdk2 and p70s6k kinases, respectively

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-273599	Ser49	QIQECFLsPFRKPLS	in vitro
pmid	sentence
29295984	Effect of CDK2 phosphorylation on the RAD54 activities. We find that the RAD54 N-terminal domain (NTD) is responsible for initiation of BM through two coupled, but distinct steps; specific binding to Holliday junctions and RAD54 oligomerization. Furthermore, we find that the RAD54 oligomeric state can be controlled by NTD phosphorylation at S49, a CDK2 consensus site, which inhibits RAD54 oligomerization and, consequently, BM.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-46397	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-53306	Ser5	sPVRGCYE	Homo sapiens
pmid	sentence
9372912	We now show that an analogous cell-cycle-regulated phosphorylation of id3 alters the specificity of id3 for abrogating both e-box-dependent bhlh homo- or heterodimer complex formation in vitro and e-box-dependent reporter gene function in vivo._

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262734	Ser508	FWHRKKIsPNKKPFS	Mus musculus	B-lymphocyte
pmid	sentence
11526238	To study the inducible regulation of GANP DNA-primase during cell activation, we examined phosphorylation induced by various kinds of kinases.We observed that the cell cycle-associated kinase Cdks induced phosphorylation of GANP in vitro. Examination of immunoprecipitates of Cdk2 from B cells revealed phosphorylation of GANP-PD at a consensus sequence of Cdk phosphorylation at Ser502 (S/T-P-X-K/R) (Fig. (Fig.1C1C Left; ref. 22).

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-103246	Ser51	GVVSESDsPVKRPGR	Homo sapiens	HeLa Cell
pmid	sentence
12851383	Thus, phosphorylation of serine 51 on hligi plays a critical role in regulating the interaction between hligi and rfc, which is required for efficient dna replication and repair.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-103250	Ser76	EEEDEALsPAKGQKP	Homo sapiens	HeLa Cell
pmid	sentence
12851383	We show that three residues (ser51, ser76, and ser91), which are part of cyclin-dependent kinase sites, are phosphorylated in a cell cycle-dependent manner.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-103254	Ser91	ALDCSQVsPPRPATS	Homo sapiens	HeLa Cell
pmid	sentence
12851383	We show that three residues (ser51, ser76, and ser91), which are part of cyclin-dependent kinase sites, are phosphorylated in a cell cycle-dependent manner.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-63891	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-67544	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-63895	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.

Identifier	Residue	Sequence	Organism
SIGNOR-67548	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.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-62353	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-62357	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-62361	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-62365	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-248232	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
SIGNOR-273426	Ser624	KMFKDKVsPLQNLAS
pmid	sentence
33082307	The motif harbouring S436 is a target of CDK2 and CDK3 kinases, which interacted with EVI1-WT. The methyltransferase DNMT3A bound preferentially to EVI1-WT compared with EVI1-S436A, and a hypomethylated cell population associated by EVI1-WT expression in murine haematopoietic progenitors is not maintained with EVI1-S436A.

Publications:

1

Identifier	Residue	Sequence	Organism
SIGNOR-265045	Ser628	MVNSCITsPSTPSKK	Homo sapiens
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
SIGNOR-249173	Ser64	SNLGHPEsPPRKRLK
pmid	sentence
18239684	The activity of SCF(Skp2) is regulated by the Cyclin-dependent kinase (CDK)2-mediated phosphorylation of Skp2 on Ser64 allows its expression in mid-G1 phase, even in the presence of active APC(Cdh1). Reciprocally, dephosphorylation of Skp2 by the mitotic phosphatase Cdc14B at the M --> G1 transition promotes its degradation by APC(Cdh1).

Publications:

1

Identifier	Residue	Sequence	Organism
SIGNOR-163279	Ser670	KMKNKPRsPVVELSK	Homo sapiens
pmid	sentence
20080565	We report that grk2 protein levels are transiently down-regulated during the g2/m transition by a mechanism involving cdk2-mediated phosphorylation of grk2 at serine670, which triggers binding to the prolyl-isomerase pin1 and subsequent degradation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-277192	Ser675	KTKVEPYsLTAQQSS	in vitro
pmid	sentence
26727879	UHRF1 is phosphorylated by CDK2/cyclin A. In vitro kinase assay was performed with CDK2/cyclin A using recombinant wild-type UHRF1 or UHRF1-S674A mutant

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-161805	Ser70	EAMNYEGsPIKVTLA	Homo sapiens	Leukemia Cell
pmid	sentence
19933706	Simultaneous inactivation of two cdk phosphorylation sites at ser10 and ser70 (npm-aa) induced g(2)/m cell cycle arrest, phosphorylation of cdk1 at tyr15 (cdc2(tyr15)) and increased cytoplasmic accumulation of cdc25c.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-197270	Ser76	VQDTSGTsPVHDAAR	Homo sapiens
pmid	sentence
22558186	Cdk2 and pka were found to participate in p19ink4d phosphorylation process and that they would mediate serine 76 and threonine 141 modifications respectively. Nuclear translocation of p19ink4d induced by dna damage was shown to be dependent on serine 76 phosphorylation.

Identifier	Residue	Sequence	Organism
SIGNOR-197274	Thr141	RRDARGLtPLELALQ	Homo sapiens
pmid	sentence
22558186	Cdk2 and pka were found to participate in p19ink4d phosphorylation process and that they would mediate serine 76 and threonine 141 modifications respectively.we propose a sequential phosphorylation model for p19 in which modification at s76 would enable a second phosphorylation event at t141. The phosphorylation-induced structural changes could have functional implicancies for p19 in the dna damage response

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-277604	Ser770	LISRPRPsPLRSRID	in vitro
pmid	sentence
35843311	Using in vitro kinase assays and phosphomutants, we determined that CDK1 phosphorylates MLK3 on Ser548 and decreases MLK3 activity during mitosis, whereas CDK2 phosphorylates MLK3 on Ser770 and increases MLK3 activity during G1/S and G2 phases.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-275615	Ser81	PSAARGGsPLPGPAQ	Homo sapiens	HEK-293 Cell
pmid	sentence
25364462	Phosphorylation of cyclin O, a novel cyclin family protein containing a cyclin-like domain, is involved in the activation of cyclin-dependent kinase 2\|This activity was reduced in cells overexpressing cyclin O, in which the 81st serine had been replaced with alanine (S81A). These results suggest that cyclin O is a novel cyclin family protein that regulates CDK2 kinase activity, which is mediated by the phosphorylation of the 81st serine residue of cyclin O\|CKD2 phosphorylates the 81st serine residue of cyclin O

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-145577	Ser83	DSREDEIsPPPPNPV	Homo sapiens
pmid	sentence
16582606	In this context, we have identified rialpha as a novel substrate for the g(1)/s-cyclin-dependent kinase, cdk2/cyclin e, and found that rialpha is specifically phosphorylated at the serine residue.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-167766	Ser991	PALPPPEsPPKVQPE	Homo sapiens
pmid	sentence
20807815	We identified ser(477) and ser(991) of pelp1 as cdk phosphorylation sites. we conclude that pelp1 is a novel substrate of interphase cdks and that its phosphorylation is important for the proper function of pelp1 in modulating hormone-driven cell cycle progression and also for optimal e2f transactivation function.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276901	Thr112	DVYVTTHtPRNARDE	Homo sapiens	HEK-293T Cell
pmid	sentence
25948581	Here we reported that CDK2 could phosphorylate RNF4 on T26 and T112 and enhance RNF4 E3 ligase activity, which is important for MDC1 degradation and proper HR repair during S phase.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276900	Thr26	RTREATStPEISLEA	Homo sapiens	HEK-293T Cell
pmid	sentence
25948581	Here we reported that CDK2 could phosphorylate RNF4 on T26 and T112 and enhance RNF4 E3 ligase activity, which is important for MDC1 degradation and proper HR repair during S phase.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-116364	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-116476	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.

Identifier	Residue	Sequence	Organism
SIGNOR-196048	Thr226	SAPVGKEtPSKRMKR	Homo sapiens
pmid	sentence
22334659	Phosphorylation at thr-116 and thr-226 of orc2 occurs by cyclin-dependent kinase during the s phase and is maintained until the m phase. Phosphorylation of orc2 at thr-116 and thr-226 dissociated the orc2-5 from chromatin.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-68548	Thr121	YKEQPLKtPGKKKKG	Homo sapiens
pmid	sentence
10373465	Phosphorylation at the cyclin-dependent kinases site (thr85) of parathyroid hormone-related protein negatively regulates its nuclear localization

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-82137	Thr1270	SDLPVPRtPGSGAGE	Homo sapiens
pmid	sentence
10995387	Importantly, mutation of cdk2 phosphorylation sites to alanine abrogates the ability of p220 to activate the histone h2b promoter.

Identifier	Residue	Sequence	Organism
SIGNOR-82141	Thr1350	ISRTTSAtPLKDNTQ	Homo sapiens
pmid	sentence
10995387	Importantly, mutation of cdk2 phosphorylation sites to alanine abrogates the ability of p220 to activate the histone h2b promoter.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248481	Thr14	VEKIGEGtYGVVYKA	Homo sapiens
pmid	sentence
10454565	The phosphatase activity of Cdc25A is necessary for Cdk2 activation, most likely due to dephosphorylation on Tyr-15 and Thr-14 of Cdk2.

Identifier	Residue	Sequence	Organism
SIGNOR-248482	Tyr15	EKIGEGTyGVVYKAR	Homo sapiens
pmid	sentence
10454565	The phosphatase activity of Cdc25A is necessary for Cdk2 activation, most likely due to dephosphorylation on Tyr-15 and Thr-14 of Cdk2.

Identifier	Residue	Organism	Cell Line
SIGNOR-245449		Homo sapiens	MCF-7 Cell
pmid	sentence
11154267	Expression of Cdc25A mRNA and protein was induced by E(2) in control and p16(INK4a)-expressing MCF-7 cells; however, functional activity of Cdc25A was inhibited in cells expressing p16(INK4a). Inhibition of Cdc25A activity in p16(INK4a)-expressing cells was associated with depressed Cdk2 activity

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-195521	Thr14	VEKIGEGtYGVVYKA	Homo sapiens
pmid	sentence
22263797	Cell division cycle 25 a (cdc25a), a dual-specificity protein phosphatase, is one of the most crucial cell cycle regulators, which removes the inhibitory phosphorylation in cyclin-dependent kinases (cdks), such as cdk2, cdk4, and cdk6, and positively regulates the activities of cdks that lead to cell cycle progression.

Identifier	Residue	Sequence	Organism
SIGNOR-95252	Thr14	VEKIGEGtYGVVYKA	Homo sapiens
pmid	sentence
12411508	Cell division cycle 25 a (cdc25a), a dual-specificity protein phosphatase, is one of the most crucial cell cycle regulators, which removes the inhibitory phosphorylation in cyclin-dependent kinases (cdks), such as cdk2, cdk4, and cdk6, and positively regulates the activities of cdks that lead to cell cycle progression.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276634	Thr156	HLFTFPPtPPKDVSP	Homo sapiens	HeLa Cell
pmid	sentence
24820417	Phosphorylation of GATA3 Thr-156 was detected in mouse thymocytes, and cyclin-dependent kinase 2 (CDK2) was identified as a respondent for phosphorylation at Thr-156.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-244614	Thr160	GVPVRTYtHEVVTLW	Homo sapiens
pmid	sentence
12359725	In addition to its role in stimulating cyclin d1 expression and nuclear translocation of cdk2, erk regulates thr-160 phosphorylation of cdk2-cyclin e.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Adipogenesis

Identifier	Residue	Sequence	Organism
SIGNOR-94003	Thr160	GVPVRTYtHEVVTLW	Homo sapiens
pmid	sentence
12359725	In addition to its role in stimulating cyclin d1 expression and nuclear translocation of cdk2, erk regulates thr-160 phosphorylation of cdk2-cyclin e.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248724	Thr160	GVPVRTYtHEVVTLW	Homo sapiens
pmid	sentence
11463386	The CDK-interacting protein phosphatase KAP dephosphorylates phosphoThr-160 (pThr-160) of the CDK2 activation segment, the site of regulatory phosphorylation that is essential for kinase activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-118986	Thr160	GVPVRTYtHEVVTLW	Homo sapiens
pmid	sentence
14597612	P42 is essential for the phosphorylation of thr-160 and activation of cdk2.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-269330	Thr160	GVPVRTYtHEVVTLW	in vitro
pmid	sentence
10085115	Phosphorylation of monomeric human CDK2 by CAK1 is more efficient than phosphorylation of the binary CDK2-cyclin A complex. Phosphorylated CDK2 exhibits histone H1 kinase activity corresponding to approximately 0.3% of that observed with the fully activated phosphorylated CDK2-cyclin A complex. Fluorescence measurements have shown that Thr160 phosphorylation increases the affinity of CDK2 for both histone substrate and ATP and decreases its affinity for ADP.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-153636	Thr160	GVPVRTYtHEVVTLW	Homo sapiens
pmid	sentence
17361108	Our results demonstrate that cdk2 is capable of autophosphorylation at thr160.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Adipogenesis

Identifier	Residue	Sequence	Organism
SIGNOR-250768	Thr160	GVPVRTYtHEVVTLW	in vitro
pmid	sentence
10085115	Phosphorylation of monomeric human CDK2 by CAK1 is more efficient than phosphorylation of the binary CDK2-cyclin A complex. Phosphorylated CDK2 exhibits histone H1 kinase activity corresponding to approximately 0.3% of that observed with the fully activated phosphorylated CDK2-cyclin A complex. Fluorescence measurements have shown that Thr160 phosphorylation increases the affinity of CDK2 for both histone substrate and ATP and decreases its affinity for ADP.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-85013	Thr170	GSPNRAYtHQVVTRW	Homo sapiens
pmid	sentence
11113184	Threonine-170 of cdk7 is phosphorylated in vitro by cdk2. Full activation of cdk7 requires phorylation of a conserved threonine residue at position 170 in its own t loop.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-154188	Thr187	NAGSVEQtPKKPGLR	Homo sapiens
pmid	sentence
17409098	Ubiquitination and subsequent degradation play a critical role in regulating the levels of p27 during cell cycle progression. Here we provide evidence suggesting that both cdk2/e and phosphorylation of thr(187) on p27 are essential for the recognition of p27 by the scf(skp2/cks1) complex, the ubiquitin-protein isopeptide ligase (e3).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-89609	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-235725	Thr234	SFKKQEKtPKTPKGP	Mus musculus
pmid	sentence
11278991	We have recently found that nucleophosmin (npm/b23), a phosphoprotein primarily found in nucleolus, associates with unduplicated centrosomes and is a direct substrate of cdk2-cyclin e in centrosome duplication. Upon phosphorylation by CDK2-cyclin E, NPM/B23 dissociates from centrosomes, which is a prerequisite step for centrosomes to initiate duplication.

Publications:

2

Organism:

Homo Sapiens, Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-196372	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-156509	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

Pathways:

Adipogenesis

Identifier	Residue	Sequence	Organism
SIGNOR-90434	Thr244	GRAKGSEtPGATPGS	Homo sapiens
pmid	sentence
12105215	To map the set of phosphorylation sites in sap155-(223-322) that determine its interaction with nipp1, we have identified phosphorylation sites of cyclin e-cdk2 by the sequencing of proteolytically derived phosphopeptide). Three phosphorylation sites were identified as thr244, thr248, and thr313

Identifier	Residue	Sequence	Organism
SIGNOR-90438	Thr248	GSETPGAtPGSKIWD	Homo sapiens
pmid	sentence
12105215	To map the set of phosphorylation sites in sap155-(223-322) that determine its interaction with nipp1, we have identified phosphorylation sites of cyclin e-cdk2 by the sequencing of proteolytically derived phosphopeptides. Three phosphorylation sites were identified as thr244, thr248, and thr313

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-90442	Thr313	HGSGWAEtPRTDRGG	Homo sapiens
pmid	sentence
12105215	We indeed found that sap155-(223_322) and sap155-(1_491) are excellent substrates for in vitrophosphorylation by cyclin e-cdk2 as well as cyclin b-cdk1

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-92265	Thr320	NPGGRPItPPRNSAK	Homo sapiens
pmid	sentence
12202491	Both of these pp1 isoforms contain an arg-pro-ile/val-thr-pro-pro-arg sequence near the c terminus, a known site of phosphorylation by cdc/cdk kinases, and phosphorylation attenuates phosphatase activity

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-178058	Thr39	LKKIRLDtETEGVPS	Homo sapiens
pmid	sentence
18354084	Akt phosphorylates cdk2 at threonine 39 residue both in vitro and in vivo. Although cdk2 threonine 39 phosphorylation mediated by akt enhances cyclin-a binding, it is dispensable for its basal binding and the kinase activity.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Adipogenesis

Identifier	Residue	Sequence	Organism
SIGNOR-244176	Thr39	LKKIRLDtETEGVPS	Homo sapiens
pmid	sentence
18354084	Akt phosphorylates cdk2 at threonine 39 residue both in vitro and in vivo. Although cdk2 threonine 39 phosphorylation mediated by akt enhances cyclin-a binding, it is dispensable for its basal binding and the kinase activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-255656	Thr416	EANSRCQtPIKMKPN	Homo sapiens	HEK-293 Cell
pmid	sentence
23241245	Here, we demonstrate that the phosphorylation of EZH2 by cyclin-dependent kinases at Thr416 creates a docking site for the ForkHead-associated domain of NIPP1.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Cell Line
SIGNOR-250738	Thr440	LDSCNSLtPKSTPVK	HEK-293 Cell
pmid	sentence
10095772	In summary, our work has identified several phosphorylation sites for cyclin A/Cdk2 in B-Myb and shown that mutation of at least one of these sites has a strong effect on the inducibility of the B-Myb transactivation potential by cyclin A/Cdk2.

Publications:

1

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276169	Thr553	GPGRVLPtPTEKDVF	Homo sapiens	HEK-293T Cell
pmid	sentence
18688254	Phosphorylation of DNA polymerase λ is required to maintain its stability. Recently, we identified Pol lambda as an interaction partner of cyclin-dependent kinase 2 (CDK2) that is central to the cell cycle G1/S transition and S-phase progression. Experiments with phosphorylation-defective mutants suggest that phosphorylation of Thr 553 is important for maintaining Pol lambda stability, as it is targeted to the proteasomal degradation pathway through ubiquitination unless this residue is phosphorylated.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-105548	Thr555	LSPSVLTtPSKIEPM	Homo sapiens
pmid	sentence
11238922	Hira bound to and was phosphorylated by cyclin a- and e-cdk2 in vitrohira became phosphorylated on threonine 555 in s phase when cyclin-cdk2 kinases are active.ectopic expression of hira in cells caused arrest in s phase and this is consistent with the notion that it is a cyclin-cdk2 substrate that has a role in control of the cell cycle.

Publications:

1

Organism:

Homo Sapiens

Tissue:

U2-OS Cell

Identifier	Residue	Sequence	Cell Line
SIGNOR-250731	Thr611	ETLPISStPSKSVLP	U2-OS Cell
pmid	sentence
15024056	We demonstrated that FoxM1B transcriptional activity requires binding of either S-phase or M-phase Cdk-cyclin complexes to mediate efficient Cdk phosphorylation of the FoxM1B Thr 596 residue, which is essential for recruitment of p300/CBP coactivator proteins.

Publications:

1

Identifier	Residue	Sequence	Organism
SIGNOR-265099	Thr72	NLQQAIVtPLKPVDN	in vitro
pmid	sentence
25688093	In this study, we characterize the phosphorylation of threonine 72 (Thr(72)) in human TPX2, a residue highly conserved across species. We find that Cdk1/2 phosphorylate TPX2 in vitro and in vivo. \|Endogenous TPX2 phosphorylated at Thr(72) does not associate with the mitotic spindle. Furthermore, ectopic GFP-TPX2 T72A preferentially concentrates on the spindle

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-176656	Thr722	EEMPQVHtPKTADSQ	Homo sapiens
pmid	sentence
21965652	In this study, we demonstrate that mcm3 is a substrate of cyclin e/cdk2 and can be phosphorylated by cyclin e/cdk2 at thr-722.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-47895	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.

Identifier	Residue	Organism
SIGNOR-176512		Homo sapiens
pmid	sentence
21902831	Cycline/cdk2 blocks myod-induced gene expression through the phosphorylation of rb, preventing rb from binding and transactivating myod, and triggering s phase entry instead of differentiation.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-183840	Thr847	FRYIPPNtPENFWEV	Homo sapiens
pmid	sentence
19202191	Collectively, these findings thereby provided strong support for ctip thr-847 indeed being a cdk target. it is established that both cdk-dependent and checkpoint-dependent phosphorylations are required for activation of sae2/ctip in vivo

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-99746	Thr86	AASASPYtPEHAASV	Homo sapiens
pmid	sentence
12676926	Cyclin-dependent kinases phosphorylate p73 at threonine 86 in a cell cycle-dependent manner and negatively regulate p73.Furthermore, cyclin a/cdk1/2, cyclin b/cdk1/2, and cyclin e/cdk2 complexes can phosphorylate multiple p73 isoforms in vitro at threonine 86.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-87101	Thr90	CHLAWVNtPKKQGGL	Homo sapiens	HeLa Cell
pmid	sentence
11986303	Peroxiredoxin (prx) i is a member of the peroxiredoxin family of peroxidases and contains a consensus site (thr(90)-pro-lys-lys) for phosphorylation by cyclin-dependent kinases (cdks). This protein has now been shown to be phosphorylated specifically on thr(90) by several cdks, including cdc2, in vitro. Phosphorylation of prx i on thr(90) reduced the peroxidase activity of this protein by 80%.Prx i was also phosphorylated, with an efficiency similar to that observed with cdc2, when incubated in vitro with cdk2, cdk4, or cdk6 that had been immunoprecipitated from hela cell lysates with specific antibodies (data not shown).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-254695	Tyr15	EKIGEGTyGVVYKAR	in vitro
pmid	sentence
25624455	PTPRG activation by the P1-WD peptide affected the tyrosine phosphorylation of several signaling molecules. Data analysis identified 31 molecules whose phosphorylation was modified in a statistically significant manner (Table I). inhibition of ABL1, BMX, BTK, DAB1, ITGB1, JAK2, KDR, KIT, LIMK1, MET, PDGFRB, SHC1, and VCL correlates with tyrosine dephosphorylation. In contrast, SRC inhibition correlates with hyperphosphorylation of the inhibitory Tyr530 residue and with dephosphorylation of the activatory Tyr419. Moreover, CDK2 and CTTN inhibition correlates with a hyperphosphorylation of the inhibitory Tyr15 and Tyr470, respectively. In contrast, a subgroup of 13 proteins, including BLNK, DOK2, ERBB2, GRIN2B, INSR, PDGFRA, PRKCD, PXN, STAT1, STAT2, STAT3, STAT5A, and ZAP70, appears to be activated by PTPRG activity.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-83139	Tyr15	EKIGEGTyGVVYKAR	Homo sapiens	HeLa Cell
pmid	sentence
11029659	Identification and characterization of human wee1b, a new member of the wee1 family of cdk-inhibitory kinases.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-191532		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-271724		Homo sapiens	HeLa Cell
pmid	sentence
26297806	Primary microcephaly (MCPH) associated proteins CDK5RAP2, CEP152, WDR62 and CEP63 colocalize at the centrosome. We found that they interact to promote centriole duplication and form a hierarchy in which each is required to localize another to the centrosome, with CDK5RAP2 at the apex, and CEP152, WDR62 and CEP63 at sequentially lower positions. MCPH proteins interact with distinct centriolar satellite proteins; CDK5RAP2 interacts with SPAG5 and CEP72, CEP152 with CEP131, WDR62 with MOONRAKER, and CEP63 with CEP90 and CCDC14. These satellite proteins localize their cognate MCPH interactors to centrosomes and also promote centriole duplication. Consistent with a role for satellites in microcephaly, homozygous mutations in one satellite gene, CEP90, may cause MCPH. The satellite proteins, with the exception of CCDC14, and MCPH proteins promote centriole duplication by recruiting CDK2 to the centrosome.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-183655		Homo sapiens
pmid	sentence
19188143	Additionally, ck1, dyrk1a, and cdk2 also phosphorylate foxos at various sites to inhibit foxos activity

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-154191		Homo sapiens
pmid	sentence
17409098	P27, an important cell cycle regulator, blocks the g(1)/s transition in cells by binding and inhibiting cdk2/cyclin a and cdk2/cyclin e complexes (cdk2/e).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-193549		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-258087		in vitro
pmid	sentence
22037378	Our data set represents the most detailed comprehensive assessment of the reactivity of known and clinical kinase inhibitors across the kinome published to date. \| The data also show that for at least 15 of the 27 kinases that are the primary, intended targets for the compounds tested and that are represented in the assay panel, selective inhibitors, as assessed by both absolute selectivity across the kinome and selectivity relative to the primary target, are among the 72 tested here.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Organism
SIGNOR-191325		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-201506		Homo sapiens
pmid	sentence
23437375	Our results suggest that ad-induced cyclin e activates cdk2 that targets the transcriptional repressor prb/cyclin e activates the cdk2 kinase necessary for the actual initiation of dna replication

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-277140		Homo sapiens
pmid	sentence
26474275	CDC25B is also able to dephosphorylate and activate CDK2-Cyclin A and CDK2-Cyclin E complexes [ xref \u2013 xref ].

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-190179		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-271725		Homo sapiens	HeLa Cell
pmid	sentence
26297806	Primary microcephaly (MCPH) associated proteins CDK5RAP2, CEP152, WDR62 and CEP63 colocalize at the centrosome. We found that they interact to promote centriole duplication and form a hierarchy in which each is required to localize another to the centrosome, with CDK5RAP2 at the apex, and CEP152, WDR62 and CEP63 at sequentially lower positions. MCPH proteins interact with distinct centriolar satellite proteins; CDK5RAP2 interacts with SPAG5 and CEP72, CEP152 with CEP131, WDR62 with MOONRAKER, and CEP63 with CEP90 and CCDC14. These satellite proteins localize their cognate MCPH interactors to centrosomes and also promote centriole duplication. Consistent with a role for satellites in microcephaly, homozygous mutations in one satellite gene, CEP90, may cause MCPH. The satellite proteins, with the exception of CCDC14, and MCPH proteins promote centriole duplication by recruiting CDK2 to the centrosome.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-253693		Homo sapiens	Hep-G2 Cell
pmid	sentence
21544813	Screening by quantitative reverse-transcription PCR and PCR arrays revealed that cyclin E1, CDK2, Fos and Jun were negatively regulated by ARNT, whereas CDKN1C, CNKN2A, CDKN2B, MAPK11 and MAPK14 were positively regulated in HCC

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-189984		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-187457		Homo sapiens
pmid	sentence
19665013	The eukaryotic cell cycle is controlled by different cyclins and their associated kinases (murray and hunt, 1993). In mammalian cells, levels of cycline and its associated kinase, cdk2, rise in late g1/early s-phase when dna replication is initiated

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-259793		in vitro
pmid	sentence
22037378	Our data set represents the most detailed comprehensive assessment of the reactivity of known and clinical kinase inhibitors across the kinome published to date. \| The data also show that for at least 15 of the 27 kinases that are the primary, intended targets for the compounds tested and that are represented in the assay panel, selective inhibitors, as assessed by both absolute selectivity across the kinome and selectivity relative to the primary target, are among the 72 tested here.

Identifier	Residue	Organism
SIGNOR-258273		in vitro
pmid	sentence
22037378	Our data set represents the most detailed comprehensive assessment of the reactivity of known and clinical kinase inhibitors across the kinome published to date. \| The data also show that for at least 15 of the 27 kinases that are the primary, intended targets for the compounds tested and that are represented in the assay panel, selective inhibitors, as assessed by both absolute selectivity across the kinome and selectivity relative to the primary target, are among the 72 tested here.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Organism
SIGNOR-277107		in vitro
pmid	sentence
10934208	Moreover, purified recombinant PP2C alpha and PP2C beta 2 proteins efficiently dephosphorylated monomeric Cdk2/Cdk6 in vitro.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Organism	Cell Line
SIGNOR-275616		Homo sapiens	HEK-293 Cell
pmid	sentence
25364462	Phosphorylation of cyclin O, a novel cyclin family protein containing a cyclin-like domain, is involved in the activation of cyclin-dependent kinase 2\|This activity was reduced in cells overexpressing cyclin O, in which the 81st serine had been replaced with alanine (S81A). These results suggest that cyclin O is a novel cyclin family protein that regulates CDK2 kinase activity, which is mediated by the phosphorylation of the 81st serine residue of cyclin O

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-277153		Homo sapiens
pmid	sentence
20538721	CDK2 can be dephosphorylated and inactivated by protein phosphatase type 2C beta isoform long (PP2Cbetal), a unique phosphatase that was originally cloned from human liver.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-119478		Homo sapiens
pmid	sentence
14643450	Cells overexpressing prl-2 exhibited enhanced cyclin-dependent kinase 2 (cdk2) activity

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-271726		Homo sapiens	HeLa Cell
pmid	sentence
26297806	Primary microcephaly (MCPH) associated proteins CDK5RAP2, CEP152, WDR62 and CEP63 colocalize at the centrosome. We found that they interact to promote centriole duplication and form a hierarchy in which each is required to localize another to the centrosome, with CDK5RAP2 at the apex, and CEP152, WDR62 and CEP63 at sequentially lower positions. MCPH proteins interact with distinct centriolar satellite proteins; CDK5RAP2 interacts with SPAG5 and CEP72, CEP152 with CEP131, WDR62 with MOONRAKER, and CEP63 with CEP90 and CCDC14. These satellite proteins localize their cognate MCPH interactors to centrosomes and also promote centriole duplication. Consistent with a role for satellites in microcephaly, homozygous mutations in one satellite gene, CEP90, may cause MCPH. The satellite proteins, with the exception of CCDC14, and MCPH proteins promote centriole duplication by recruiting CDK2 to the centrosome.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-119418		Homo sapiens
pmid	sentence
14643450	Cells overexpressing either prl-1 or prl-2 exhibited enhanced cyclin-dependent kinase 2 (cdk2) activity and significantly lower p21cip1/waf1 protein levels

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-264058		Homo sapiens
pmid	sentence
25526788	LRRC4/NGL-2 can delay the cell cycle in late G1 by increasing the expression of cell cycle inhibitory molecules (p21, p27) and reducing the expression of cell cycle regulatory proteins (CyclinD1, CDK2, CyclinE, CDK4) via the inhibition of K-Ras/c-Raf/ERK/MAPK, PI-3K/AKT/NF- κB, p70S6/PKC and STAT3, and the upregulation of the JNK2/c-Jun/mp53 signaling pathway.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Brain

Identifier	Residue	Organism
SIGNOR-206127		Homo sapiens
pmid	sentence
Other

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-258176		in vitro
pmid	sentence
22037378	Our data set represents the most detailed comprehensive assessment of the reactivity of known and clinical kinase inhibitors across the kinome published to date. \| The data also show that for at least 15 of the 27 kinases that are the primary, intended targets for the compounds tested and that are represented in the assay panel, selective inhibitors, as assessed by both absolute selectivity across the kinome and selectivity relative to the primary target, are among the 72 tested here.

Identifier	Residue	Organism
SIGNOR-262219		in vitro
pmid	sentence
29901072	AT7519, a pyrazole 3-carboxyamide compound, was developed by Astex and acts as an inhibitor of CDK1, CDK2, CDK4, CDK6 and CDK9.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Organism	Cell Line
SIGNOR-263310		Homo sapiens	HEK-293 Cell
pmid	sentence
33015044	Speedy/RINGO A, a noncanonical activator of CDK2, was recently identified as a key regulator for CDK2 recruitment to meiotic telomeres

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-206151		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-206361		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-258171		in vitro
pmid	sentence
22037378	Our data set represents the most detailed comprehensive assessment of the reactivity of known and clinical kinase inhibitors across the kinome published to date. \| The data also show that for at least 15 of the 27 kinases that are the primary, intended targets for the compounds tested and that are represented in the assay panel, selective inhibitors, as assessed by both absolute selectivity across the kinome and selectivity relative to the primary target, are among the 72 tested here.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Organism
SIGNOR-264650		Homo sapiens
pmid	sentence
12202491	Both of these pp1 isoforms contain an arg-pro-ile/val-thr-pro-pro-arg sequence near the c terminus, a known site of phosphorylation by cdc/cdk kinases, and phosphorylation attenuates phosphatase activity

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-276759		in vitro
pmid	sentence
25361894	Our study also showed that Cables1 increases the level of p21 and decreases the level of pRb, but does not affect the other cell cycle-related proteins we studied. Induction of apoptosis by Cables1, which occurs partially through inhibiting Cdk2 activity and upregulating p21, is prevented by Akt phosphorylation and 14-3-3 binding.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Organism
SIGNOR-64431		Homo sapiens
pmid	sentence
10022885	However, induction of p16(ink4a) also causes marked inhibition of cdk2 activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-264781
pmid	sentence
22427660	The ubiquitously expressed CDK2AP1 protein is the only known specific inhibitor of CDK2, making it an important component of cell cycle regulation during G1-to-S phase transition.

Publications:

1

Identifier	Residue	Organism
SIGNOR-192461		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-206571		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-190434		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-73537		Homo sapiens
pmid	sentence
10611320	Tgf-beta treatment resulted in the specific inactivation of cyclin cdk2 complexes caused by absence of the activating thr(160) phosphorylation on cdk2.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Adipogenesis

Identifier	Residue	Organism	Cell Line
SIGNOR-149711		Homo sapiens	Myoblast
pmid	sentence
16982699	Considering that akt1 phosphorylates p21, this dissociation likely results from phosphorylation of p21 and release of cdk2.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-206835		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-207084		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-272310		Homo sapiens	Lymphocyte
pmid	sentence
29720484	We confirmed the formation of ubiquitin and CDK2 by different systems and further identified the E3 ligase KLHL6 as a mediator of the ubiquitination and degradation of CDK2.

Publications:

1

Organism:

Homo Sapiens

Name	CDK2 View Modifications
Full Name	Cyclin-dependent kinase 2
Synonyms	Cell division protein kinase 2, p33 protein kinase \| CDKN2
Primary ID	P24941
Links	- -
Type	protein
Relations	243
Pathways	Adipogenesis
Inhibitors	alvocidib; 4-[[5-amino-1-[(2,6-difluorophenyl)-oxomethyl]-1,2,4-triazol-3-yl]amino]benzenesulfonamide; N-(5-{[(5-tert-butyl-1,3-oxazol-2-yl)methyl]sulfanyl}-1,3-thiazol-2-yl)piperidine-4-carboxamide; Dinaciclib; 4-(2-methyl-3-propan-2-yl-4-imidazolyl)-N-(4-methylsulfonylphenyl)-2-pyrimidinamine; 4-(2,6-dichlorobenzamido)-N-(piperidin-4-yl)-pyrazole-3-carboxamide; R547; N-[6,6-dimethyl-5-[(1-methyl-4-piperidinyl)-oxomethyl]-1,4-dihydropyrrolo[3,4-c]pyrazol-3-yl]-3-methylbutanamide; PHA-848125; alvocidib hydrochloride; seliciclib; BMS-265246; 6-bromo-3-(1-methyl-4-pyrazolyl)-5-(3-piperidinyl)-7-pyrazolo[1,5-a]pyrimidinamine
Function	Serine/threonine-protein kinase involved in the control of the cell cycle; essential for meiosis, but dispensable for mitosis. Phosphorylates CTNNB1, USP37, p53/TP53, NPM1, CDK7, RB1, BRCA2, MYC, NPAT, EZH2. Triggers duplication of centrosomes and DNA. Acts at the G1-S transition to promote the E2F transcriptional program and the initiation of DNA synthesis, and modulates G2 progression; controls the timing of entry into mitosis/meiosis by controlling the subsequent activation of cyclin B/CDK1 by phosphorylation, and coordinates the activation of cyclin B/CDK1 at the centrosome and in the nucleus. Crucial role in orchestrating a fine balance between cellular proliferation, cell death, and DNA repair in human embryonic stem cells (hESCs). Activity of CDK2 is maximal during S phase and G2; activated by interaction with cyclin E during the early stages of DNA synthesis to permit G1-S transition, and subsequently activated by cyclin A2 (cyclin A1 in germ cells) during the late stages of DNA replication to drive the transition from S phase to mitosis, the G2 phase. EZH2 phosphorylation promotes H3K27me3 maintenance and epigenetic gene silencing. Phosphorylates CABLES1 (By similarity). Cyclin E/CDK2 prevents oxidative stress-mediated Ras-induced senescence by phosphorylating MYC. Involved in G1-S phase DNA damage checkpoint that prevents cells with damaged DNA from initiating mitosis; regulates homologous recombination-dependent repair by phosphorylating BRCA2, this phosphorylation is low in S phase when recombination is active, but increases as cells progress towards mitosis. In response to DNA damage, double-strand break repair by homologous recombination a reduction of CDK2-mediated BRCA2 phosphorylation. Phosphorylation of RB1 disturbs its interaction with E2F1. NPM1 phosphorylation by cyclin E/CDK2 promotes its dissociates from unduplicated centrosomes, thus initiating centrosome duplication. Cyclin E/CDK2-mediated phosphorylation of NPAT at G1-S transition and until prophase stimulates the NPAT-mediated activation of histone gene transcription during S phase. Required for vitamin D-mediated growth inhibition by being itself inactivated. Involved in the nitric oxide- (NO) mediated signaling in a nitrosylation/activation-dependent manner. USP37 is activated by phosphorylation and thus triggers G1-S transition. CTNNB1 phosphorylation regulates insulin internalization. Phosphorylates FOXP3 and negatively regulates its transcriptional activity and protein stability (By similarity). Phosphorylates CDK2AP2 (PubMed:12944431). Phosphorylates ERCC6 which is essential for its chromatin remodeling activity at DNA double-strand breaks (PubMed:29203878).

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