PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
20957523-2	2011	It can specifically methylate histone H3 at lysine 4 and activate the transcription of a set of downstream genes, including several oncogenes (e.g., N-myc, CrkL, Wnt10b, RIZ and hTERT) and genes involved in the control of cell cycle (e.g., CyclinG1 and CDK2) and signal transduction (e.g., STAT1, MAP3K11 and PIK3CB).	Lysine	44-50	cyclin dependent kinase 2	Homo sapiens	253-257	
14506259-3	2003	The catalytic efficiency of CDK2-cyclin A is impaired 2000-, 10-, and 150-fold, when Pro+1, Lys+2, or Lys+3, respectively, is substituted with Ala in a short synthetic peptide substrate.	Lysine	92-95	cyclin dependent kinase 2	Homo sapiens	28-32	
19773423-9	2009	Moreover, we also observed that PCAF acetylates cdk2 at lysine 33.	Lysine	56-62	cyclin dependent kinase 2	Homo sapiens	48-52	
19773423-10	2009	As this lysine is essential for the interaction with ATP, acetylation of this residue inhibits cdk2 activity.	Lysine	8-14	cyclin dependent kinase 2	Homo sapiens	95-99	
19472189-2	2009	It could specifically methylate histone H3 at lysine 4 and activate the transcription of a set of downstream genes, including of several oncogenes (e.g., N-Myc, CrkL, Wnt10b, RIZ, and hTERT) and genes involved in the control of cell cycle (e.g., Cyclin G1 and CDK2) and signal transduction (e.g., STAT1, MAP3K11, and PIK3CB).	Lysine	46-52	cyclin dependent kinase 2	Homo sapiens	260-264	
16191191-5	2005	In contrast to Cdk2-cyclin A, which has a well-defined consensus target site ((S/T)PX(K/R)) that strongly favors substrates containing a lysine at the +3 position of substrates, Cdk2-Speedy/Ringo A2 displayed a broad substrate specificity at this position.	Lysine	137-143	cyclin dependent kinase 2	Homo sapiens	15-19	
15505811-5	2004	Besides the differences in loop flexibility and solvent accessibility, the dynamic stabilities of the hydrogen bonds between the inhibitors and the side chain of the lysine residue at the bottom of the active site also correlate well with the relative binding affinities of the inhibitors for the two CDKs.	Lysine	166-172	cyclin dependent kinase 2	Homo sapiens	301-305	
14506259-4	2003	Yet, in physiological substrates of both CDK2-cyclin A and CDK2-cyclin E, it is found that Lys+2, and, occasionally, both Lys+2 and Lys+3 together are replaced with suboptimal determinants.	Lysine	91-94	cyclin dependent kinase 2	Homo sapiens	41-45	
14506259-4	2003	Yet, in physiological substrates of both CDK2-cyclin A and CDK2-cyclin E, it is found that Lys+2, and, occasionally, both Lys+2 and Lys+3 together are replaced with suboptimal determinants.	Lysine	91-94	cyclin dependent kinase 2	Homo sapiens	59-63	
11532001-4	2001	We find that an ionic interaction participates in the recognition of the P + 3 position of the substrate and confirms an observation from structural studies indicating that a key element of this recognition is an interaction between the lysine at the P + 3 position and the Thr160 phosphate of Cdk2.	Lysine	237-243	cyclin dependent kinase 2	Homo sapiens	294-298	
12501191-3	2002	Substrate specificity often employs a dual recognition strategy in which the sequence flanking the phospho-acceptor site (Ser.Pro.X.Arg/Lys) is recognized by CDK2, while the cyclin A component of the complex contains a hydrophobic site that binds Arg/Lys.X.Leu ("RXL" or "KXL") substrate recruitment motifs.	Lysine	136-139	cyclin dependent kinase 2	Homo sapiens	158-162	
11427888-5	2001	A phosphate ion held by Arg 96, Arg 180 and Lys 205 occupies the same position as the phosphate group of the phosphothreonine in activated p38gamma, CDK2 or ERK2.	Lysine	44-47	cyclin dependent kinase 2	Homo sapiens	149-153	
11418614-4	2001	Conversely, mutation of the lysine 1136 inhibited the ability of the cells to increase cyclin E and cdk2 expression, to maintain long term phosphorylation of the ERK MAPK, and to enter S-phase but had no effect on the ability of the cells to phosphorylate the p38 MAPK or to migrate on type I collagen in response to EGF.	Lysine	28-34	cyclin dependent kinase 2	Homo sapiens	100-104	
29907572-9	2018	p17 interacts with cyclins by its cyclin-binding motif, 125RXL127 Sequence and mutagenic analyses of p17 indicated that a 140WXFD143 motif and residues Asp-113 and Lys-122 in p17 are critical for CDK2 and CDK6 binding, leading to their sequestration in the cytoplasm.	Lysine	164-167	cyclin dependent kinase 2	Homo sapiens	196-200	
33858315-14	2022	Binding mode analysis for CDK2 inhibition studies indicate that hydrogen bonding interaction with Lys 33 and Leu83 are important for the activity.	Lysine	98-101	cyclin dependent kinase 2	Homo sapiens	26-30	
10633045-5	2000	The anilino group of the CDK2-bound compound was essentially coplanar with the quinazoline ring system and occupied a pocket between Lys-33 and Phe-80.	Lysine	133-136	cyclin dependent kinase 2	Homo sapiens	25-29	
26320860-2	2015	4-((6-(Cyclohexylmethoxy)-9H-purin-2-yl)amino)benzenesulfonamide (NU6102) is a potent and selective ATP-competitive inhibitor of CDK2 in which the sulfonamide moiety is positioned close to a pair of lysine residues.	Lysine	199-205	cyclin dependent kinase 2	Homo sapiens	129-133