Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Cyclin-dependent kinase 2  

UniProtKB / Swiss-Prot ID :  CDK2_HUMAN

Gene Name (Synonyms) : 
CDK2, CDKN2  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm, cytoskeleton, centrosome. Nucleus, Cajal body. Cytoplasm. Endosome. Note=Localized at the centrosomes in late G2 phase after separation of the centrosomes but before the start of prophase. Nuclear-cytoplasmic trafficking is mediated during the 

Protein 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. Interacts with cyclins A, B1, B3, D, or E. 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. 

Protein Sequence MENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVKLLDVI...
Predicted Secondary Structure CCCEEEEEEEECCCCEEEEEEEECCCCCEEEEEEECCHHCCHHHHHHHHHHHHHHHHCCCCCEEEEEEEE...
Protein Variant
LocationDescription
15Y -> S (in dbSNP:rs3087335). VAR_016157
18V -> L (in dbSNP:rs11554376). VAR_053927
45P -> L (in a glioblastoma multiformesample; somatic mutation).
290T -> S (in dbSNP:rs2069413). VAR_019988
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
1N-acetylmethionine.----MENFQ
----CCCEE
9.54UniProtKB
Link
6N6-acetyllysineENFQKVEKI
CCEEEEEEE
48.50HPRD
Link
6N6-acetyllysineENFQKVEKI
CCEEEEEEE
48.50Phosphositeplus
Link
6N6-acetyllysine.ENFQKVEKI
CCEEEEEEE
48.50UniProtKB
Link
14DePhosphothreonineIGEGTYGVV
EECCCCEEE
16.89HPRD
Link
14PhosphothreonineIGEGTYGVV
EECCCCEEE
16.89HPRD
Link
14PhosphothreonineIGEGTYGVV
EECCCCEEE
16.89PhosphoELM
Link
14PhosphothreonineIGEGTYGVV
EECCCCEEE
16.89Phosphositeplus
Link
14Phosphothreonine.IGEGTYGVV
EECCCCEEE
16.89UniProtKB
Link
15DePhosphotyrosineGEGTYGVVY
ECCCCEEEE
20.84HPRD
Link
15PhosphotyrosineGEGTYGVVY
ECCCCEEEE
20.84HPRD
Link
15PhosphotyrosineGEGTYGVVY
ECCCCEEEE
20.84HPRD
Link
15PhosphotyrosineGEGTYGVVY
ECCCCEEEE
20.84PhosphoELM
Link
15PhosphotyrosineGEGTYGVVY
ECCCCEEEE
20.84Phosphositeplus
Link
15PhosphotyrosineGEGTYGVVY
ECCCCEEEE
20.84SysPTM
Link
15Phosphotyrosine (WEE1)GEGTYGVVY
ECCCCEEEE
20.84HPRD
Link
15Phosphotyrosine; by WEE1.GEGTYGVVY
ECCCCEEEE
20.84UniProtKB
Link
19PhosphotyrosineYGVVYKARN
CEEEEEEEE
9.12PhosphoELM
Link
19PhosphotyrosineYGVVYKARN
CEEEEEEEE
9.12Phosphositeplus
Link
19Phosphotyrosine (CDK2)YGVVYKARN
CEEEEEEEE
9.12HPRD
Link
19Phosphotyrosine.YGVVYKARN
CEEEEEEEE
9.12UniProtKB
Link
20Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GVVYKARNK
EEEEEEEEC
29.29Phosphositeplus
Link
24Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KARNKLTGE
EEEECCCCC
41.70Phosphositeplus
Link
33Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)VVALKKIRL
EEEEEEECC
36.10Phosphositeplus
Link
33Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VVALKKIRL
EEEEEEECC
36.10Phosphositeplus
Link
39PhosphothreonineIRLDTETEG
ECCHHCCHH
49.77HPRD
Link-
39PhosphothreonineIRLDTETEG
ECCHHCCHH
49.77Phosphositeplus
Link-
46PhosphoserineEGVPSTAIR
HHHHHHHHH
28.23HPRD
Link
46PhosphoserineEGVPSTAIR
HHHHHHHHH
28.23Phosphositeplus
Link
46PhosphoserineEGVPSTAIR
HHHHHHHHH
28.23SysPTM
Link
46Phosphoserine.EGVPSTAIR
HHHHHHHHH
28.23UniProtKB
Link
56Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ISLLKELNH
HHHHHHCCC
66.50Phosphositeplus
Link
129Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)HRDLKPQNL
EEECCHHHE
49.17Phosphositeplus
Link
142Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EGAIKLADF
CCCEEEEEE
36.77Phosphositeplus
Link
158PhosphothreonineVPVRTYTHE
CCCCEEEEE
32.76HPRD
Link-
158PhosphothreonineVPVRTYTHE
CCCCEEEEE
32.76Phosphositeplus
Link-
158Phosphothreonine.VPVRTYTHE
CCCCEEEEE
32.76UniProtKB
Link-
159PhosphotyrosinePVRTYTHEV
CCCEEEEEE
8.78HPRD
Link-
159PhosphotyrosinePVRTYTHEV
CCCEEEEEE
8.78PhosphoELM
Link-
159PhosphotyrosinePVRTYTHEV
CCCEEEEEE
8.78Phosphositeplus
Link-
159Phosphotyrosine.PVRTYTHEV
CCCEEEEEE
8.78UniProtKB
Link-
160DePhosphothreonineVRTYTHEVV
CCEEEEEEE
15.79HPRD
Link-
160PhosphothreonineVRTYTHEVV
CCEEEEEEE
15.79HPRD
Link-
160PhosphothreonineVRTYTHEVV
CCEEEEEEE
15.79HPRD
Link-
160PhosphothreonineVRTYTHEVV
CCEEEEEEE
15.79PhosphoELM
Link-
160PhosphothreonineVRTYTHEVV
CCEEEEEEE
15.79Phosphositeplus
Link-
160Phosphothreonine (CDK20)VRTYTHEVV
CCEEEEEEE
15.79HPRD
Link-
160Phosphothreonine (CDK7)VRTYTHEVV
CCEEEEEEE
15.79HPRD
Link-
160Phosphothreonine; by CAK and CCRK.VRTYTHEVV
CCEEEEEEE
15.79UniProtKB
Link-
165PhosphothreonineHEVVTLWYR
EEEEECCCC
19.42Phosphositeplus
Link
168PhosphotyrosineVTLWYRAPE
EECCCCCHH
10.46Phosphositeplus
Link
179PhosphotyrosineLGCKYYSTA
CCCCCCCCH
13.51Phosphositeplus
Link
237Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)MPDYKPSFP
HHHHHHCCC
41.38Phosphositeplus
Link
250Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QDFSKVVPP
CCHHHHCCC
47.44Phosphositeplus
Link
273Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)YDPNKRISA
CCCCCCCCH
57.40Phosphositeplus
Link
278Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)RISAKAALA
CCCHHHHHC
27.66Phosphositeplus
Link
291Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QDVTKPVPH
CCCCCCCCC
43.81Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
PCNA_HUMANphysical interactionMINT-16050MINT10930425
PCNA_HUMANphysical interactionMINT-16051MINT10930425
DNL1_HUMANphysical interactionMINT-16079MINT10930425
CCNA2_HUMANphysical interactionMINT-17592MINT10930425
CCNE1_HUMANphysical interactionMINT-2983466MINT10330164
BRCA1_HUMANphosphorylation reactionMINT-14685MINT10373534
CDN1A_HUMANphysical interactionMINT-2635357MINT16765349
CDN1A_HUMANphysical interactionMINT-3370697MINT16962592
CDN1A_HUMANphysical interactionMINT-50415MINT15232106
CDN1A_HUMANphysical interactionMINT-73323MINT9284049
CDN1B_HUMANphysical interactionMINT-3379700MINT17053782
EP300_HUMANphysical interactionMINT-2983422MINT10330164
EP300_HUMANphysical interactionMINT-2983446MINT10330164
EP300_HUMANphysical interactionMINT-2983397MINT10330164
EP300_HUMANdirect interactionMINT-2983372MINT10330164
CAF1A_HUMANdirect interactionMINT-2842495MINT16826239
ORC2_HUMANphysical interactionMINT-50414MINT15232106
CDKN3_HUMANphysical interactionMINT-17387MINT8242750
CDKN3_HUMANphysical interactionMINT-17388MINT8242750
CDN1A_HUMANphysical interactionDIP:999EDIP8242751
Q96TE0_HUMANphysical interactionDIP:550EDIP8684460
CCNA2_HUMANphysical interaction
physical interaction
physical interaction
physical interaction
physical interaction
DIP:551EDIP10559988
12244298
7630397
7630397
10930425
GSTM2_HUMANphysical interactionDIP:73EDIP8606778
CDKN3_HUMANphysical interactionDIP:40159EDIP11463386
CDK7_HUMANdirect interactionDIP:57013EDIP16327805
CDK2_HUMANphysical interactionEBI-1070846
intact17353931
CDN1B_HUMANdirect interaction
physical interaction
direct interaction
direct interaction
physical interaction
physical interaction
physical interacti
EBI-1226516
EBI-1226497
EBI-1
intact15890360
15890360
15890360
17254966
17254966
17254967
17254967
17254967
17254967
17418410
17418410
16326706
PP1A_HUMANphysical interactionEBI-1206893
intact17274640
CCNE2_HUMANphysical interaction
physical interaction
physical interaction
physical interaction
direct interaction
direct interaction
EBI-1245754
EBI-1245683
EBI-1
intact9840943
9840943
9840943
9840943
14681455
15232106
RB_HUMANphosphorylation
phosphorylation
EBI-520074
EBI-520059
intact8756624
8756624
CCNB3_HUMANdirect interactionEBI-767837
intact14681455
CCNA1_HUMANdirect interactionEBI-767663
intact14681455
UBC12_HUMANphysical interactionEBI-1081960
intact17353931
F113A_HUMANphysical interactionEBI-1075189
intact17353931
NEDD8_HUMANphysical interactionEBI-1075209
intact17353931
FBRL_HUMANphysical interactionEBI-1074959
intact17353931
41_HUMANphysical interactionEBI-1080869
intact17353931
Q6FGD7_HUMANphysical interactionEBI-1077475
intact17353931
Q6FGI1_HUMANphysical interactionEBI-1084580
intact17353931
MYH8_HUMANphysical interactionEBI-1076177
intact17353931
CL030_HUMANphysical interactionEBI-1083428
intact17353931
RS16_HUMANphysical interactionEBI-1081777
intact17353931
MOES_HUMANphysical interactionEBI-1084403
intact17353931
C1TC_HUMANphysical interactionEBI-1077033
intact17353931
OGT1_HUMANphysical interactionEBI-1084905
intact17353931
PABP1_HUMANphysical interactionEBI-1085006
intact17353931
PFTK2_HUMANphysical interactionEBI-1086042
intact17353931
S10A8_HUMANphysical interactionEBI-1075606
intact17353931
SORT_HUMANphysical interactionEBI-1079024
intact17353931
Q6IBU1_HUMANphysical interactionEBI-1077901
intact17353931
PUR9_HUMANphysical interactionEBI-1077909
intact17353931
PEBP1_HUMANphysical interactionEBI-1079850
intact17353931
FABP5_HUMANphysical interactionEBI-1085494
intact17353931
CCNB2_HUMANdirect interactionEBI-375413
intact15232106
SMAD3_HUMANin vitro
in vivo
HPRD:00310HPRD15241418
BRCA1_HUMANin vitro
in vivo
HPRD:00310HPRD10373534
CEBPA_HUMANin vitro
in vivo
HPRD:00310HPRD11684017
CDN1A_HUMANin vitroHPRD:00310HPRD12839982
CKS1_HUMANin vitro
yeast 2-hybrid
HPRD:00310HPRD8601310
12140288
PRC1_HUMANin vitro
in vivo
HPRD:00310HPRD9885575
CCNE1_HUMANin vitro
in vivo
HPRD:00310HPRD1388288
14536078
MYOD1_HUMANin vitroHPRD:00310HPRD9710583
PTHR_HUMANin vitro
in vivo
HPRD:00310HPRD10373465
RB_HUMANin vitroHPRD:00310HPRD8756624
9315635
9139732
8626527
10207050
NFYA_HUMANin vitro
in vivo
HPRD:00310HPRD12857729
P53_HUMANin vitro
in vivo
HPRD:00310HPRD10884347
12064478
10747897
10348343
UBE2A_HUMANin vivoHPRD:00310HPRD11953320
HIRA_HUMANin vitro
in vivo
HPRD:00310HPRD11238922
P80C_HUMANin vitro
in vivo
HPRD:00310HPRD11102515
ID3_HUMANin vitro
in vivo
HPRD:00310HPRD9372912
ID2_HUMANin vitro
in vivo
HPRD:00310HPRD9029153
UBF1_HUMANin vitro
in vivo
HPRD:00310HPRD11698641
10202152
CDN1B_HUMANin vitroHPRD:00310HPRD12972555
9192873
17254966
MYBB_HUMANin vitro
in vivo
HPRD:00310HPRD9840932
10095772
10593981
ORC1_HUMANin vitroHPRD:00310HPRD11931757
P73_HUMANin vitro
in vivo
HPRD:00310HPRD12676926
FOXM1_HUMANin vitroHPRD:00310HPRD15024056
CDC6_HUMANin vitro
in vivo
HPRD:00310HPRD9889196
10339564
FZR_HUMANin vitro
in vivo
HPRD:00310HPRD12560341
PTN2_HUMANin vitro
in vivo
HPRD:00310HPRD15030318
CDC7_HUMANin vitroHPRD:00310HPRD10846177
CE110_HUMANin vitroHPRD:00310HPRD12361598
CCNH_HUMANin vitroHPRD:00310HPRD9464540
CDX2_HUMANin vitro
in vivo
HPRD:00310HPRD16027724
DPOD1_HUMANin vitroHPRD:00310HPRD9545286
KAP0_HUMANin vitro
in vivo
HPRD:00310HPRD16582606
MCM4_HUMANin vitro
in vivo
HPRD:00310HPRD16519687
16517729
DPOD2_HUMANin vitroHPRD:00310HPRD16479163
CDC27_HUMANENSP00000266970STRING
UB2D1_HUMANENSP00000266970STRING
CDC6_HUMANENSP00000266970STRING
CDC23_HUMANENSP00000266970STRING
MCM5_HUMANENSP00000266970STRING
MYBB_HUMANENSP00000266970STRING
ORC6_HUMANENSP00000266970STRING
CDC37_HUMANENSP00000266970STRING
RFA3_HUMANENSP00000266970STRING
CCND1_HUMANENSP00000266970STRING
CDN1B_HUMANENSP00000266970STRING
MCM3_HUMANENSP00000266970STRING
SKP1_HUMANENSP00000266970STRING
ID2_HUMANENSP00000266970STRING
ORC2_HUMANENSP00000266970STRING
CDC7_HUMANENSP00000266970STRING
P80C_HUMANENSP00000266970STRING
CDN1A_HUMANENSP00000266970STRING
MYOD1_HUMANENSP00000266970STRING
RFA1_HUMANENSP00000266970STRING
CCNA1_HUMANENSP00000266970STRING
E2F5_HUMANENSP00000266970STRING
CDK7_HUMANENSP00000266970STRING
CCNH_HUMANENSP00000266970STRING
MAT1_HUMANENSP00000266970STRING
CCND2_HUMANENSP00000266970STRING
CDKA1_HUMANENSP00000266970STRING
ANC5_HUMANENSP00000266970STRING
RBL2_HUMANENSP00000266970STRING
PMYT1_HUMANENSP00000266970STRING
CCNE1_HUMANENSP00000266970STRING
E2F3_HUMANENSP00000266970STRING
CC45L_HUMANENSP00000266970STRING
MCM6_HUMANENSP00000266970STRING
ORC4_HUMANENSP00000266970STRING
MCM2_HUMANENSP00000266970STRING
CHKA_HUMANENSP00000266970STRING
DBF4A_HUMANENSP00000266970STRING
DBF4A_HUMANENSP00000266970STRING
RB_HUMANENSP00000266970STRING
P53_HUMANENSP00000266970STRING
CCNA2_HUMANENSP00000266970STRING
CCNB3_HUMANENSP00000266970STRING
LYN_HUMANENSP00000266970STRING
UHRF2_HUMANENSP00000266970STRING
ATM_HUMANENSP00000266970STRING
MS4A3_HUMANENSP00000266970STRING
CCNB2_HUMANENSP00000266970STRING
NPM_HUMANENSP00000266970STRING
ORC5_HUMANENSP00000266970STRING
WEE1_HUMANENSP00000266970STRING
CDT1_HUMANENSP00000266970STRING
MPIP1_HUMANENSP00000266970STRING
UB2E1_HUMANENSP00000266970STRING
MCM7_HUMANENSP00000266970STRING
CCNE2_HUMANENSP00000266970STRING
APC10_HUMANENSP00000266970STRING
CASP3_HUMANENSP00000266970STRING
CKS1_HUMANENSP00000266970STRING
ANC2_HUMANENSP00000266970STRING
ANC4_HUMANENSP00000266970STRING
CCNC_HUMANENSP00000266970STRING
MPIP3_HUMANENSP00000266970STRING
ATRIP_HUMANENSP00000266970STRING
CHK2_HUMANENSP00000266970STRING
SMAD3_HUMANENSP00000266970STRING
CDKN3_HUMANENSP00000266970STRING
ANC1_HUMANENSP00000266970STRING
APC11_HUMANENSP00000266970STRING
ATR_HUMANENSP00000266970STRING
E2F1_HUMANENSP00000266970STRING
APC7_HUMANENSP00000266970STRING
CDC16_HUMANENSP00000266970STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
DrugBank
DB06616Bosutinib
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND LYS-6, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Cell cycle regulation of CDK2 activity by phosphorylation of Thr160and Tyr15.";
Gu Y., Rosenblatt J., O'Morgan D.O.;
EMBO J. 11:3995-4005(1992).
Cited for: PHOSPHORYLATION AT THR-14; TYR-15 AND THR-160, AND MUTAGENESIS OFTHR-14; TYR-15 AND THR-160.
"p42, a novel cyclin-dependent kinase-activating kinase in mammaliancells.";
Liu Y., Wu C., Galaktionov K.;
J. Biol. Chem. 279:4507-4514(2004).
Cited for: PHOSPHORYLATION AT THR-160.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-15 AND TYR-19, AND MASSSPECTROMETRY.
"Proteomics analysis of protein kinases by target class-selectiveprefractionation and tandem mass spectrometry.";
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R.,Keri G., Wehland J., Daub H.;
Mol. Cell. Proteomics 6:537-547(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14; TYR-15; TYR-19 ANDTHR-160, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-15 AND SER-46, AND MASSSPECTROMETRY.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-15, AND MASSSPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14; TYR-15; TYR-19;SER-46; THR-158 AND TYR-159, AND MASS SPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-15 AND THR-160, AND MASSSPECTROMETRY.
"Nuclear targeting of cyclin-dependent kinase 2 reveals essentialroles of cyclin-dependent kinase 2 localization and cyclin E invitamin D-mediated growth inhibition.";
Flores O., Wang Z., Knudsen K.E., Burnstein K.L.;
Endocrinology 151:896-908(2010).
Cited for: FUNCTION IN VITAMIN D-MEDIATED GROWTH INHIBITION, SUBCELLULARLOCATION, ENZYME REGULATION, AND PHOSPHORYLATION AT THR-160.
"Cdc25 phosphatases are required for timely assembly of CDK1-cyclin Bat the G2/M transition.";
Timofeev O., Cizmecioglu O., Settele F., Kempf T., Hoffmann I.;
J. Biol. Chem. 285:16978-16990(2010).
Cited for: PHOSPHORYLATION AT THR-160 BY CAK, AND DEPHOSPHORYLATION BY CDC25A.
"Triazolo[1,5-a]pyrimidines as novel CDK2 inhibitors: proteinstructure-guided design and SAR.";
Richardson C.M., Williamson D.S., Parratt M.J., Borgognoni J.,Cansfield A.D., Dokurno P., Francis G.L., Howes R., Moore J.D.,Murray J.B., Robertson A., Surgenor A.E., Torrance C.J.;
Bioorg. Med. Chem. Lett. 16:1353-1357(2006).
Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH INHIBITORS, ANDPHOSPHORYLATION AT THR-160.
"Discovery of a potent CDK2 inhibitor with a novel binding mode, usingvirtual screening and initial, structure-guided lead scoping.";
Richardson C.M., Nunns C.L., Williamson D.S., Parratt M.J.,Dokurno P., Howes R., Borgognoni J., Drysdale M.J., Finch H.,Hubbard R.E., Jackson P.S., Kierstan P., Lentzen G., Moore J.D.,Murray J.B., Simmonite H., Surgenor A.E., Torrance C.J.;
Bioorg. Med. Chem. Lett. 17:3880-3885(2007).
Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH INHIBITORS, ANDPHOSPHORYLATION AT THR-160.
"How tyrosine 15 phosphorylation inhibits the activity of cyclin-dependent kinase 2-cyclin A.";
Welburn J.P.I., Tucker J.A., Johnson T., Lindert L., Morgan M.,Willis A., Noble M.E.M., Endicott J.A.;
J. Biol. Chem. 282:3173-3181(2007).
Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH ATP, ANDPHOSPHORYLATION AT THR-14; TYR-15 AND THR-160.
"Briefly bound to activate: transient binding of a second catalyticmagnesium activates the structure and dynamics of CDK2 kinase forcatalysis.";
Bao Z.Q., Jacobsen D.M., Young M.A.;
Structure 19:675-690(2011).
Cited for: X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 1-296 IN COMPLEX WITH ATPAND MAGNESIUM, AND PHOSPHORYLATION AT THR-160.
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