IndraLab

Statements

CDK2 phosphorylates NPM1 on T199. 32 / 32
1 6 | 13 12
reach
"Hyperphosphorylation of NPM T199 by Cdk2 strongly correlated with constitutive centrosome duplication cycle and centrosome amplification."
21272329
biopax:phosphositeplus
No evidence text available
sparser
"During the cell cycle, NPM is phosphorylated by cdk2-cyclin E on threonine 199 (T199) which causes the dissociation of NPM away from the centrosome and permits duplication."
26123729
reach
"Since HBx is reported to potentiate the activity of CDK2 kinase [41] which phosphorylates NPM at Thr 199 [55], we next monitored the phosphorylation status of NPM in its presence."
25918010
reach
"T199 phosphorylation of NPM1 is mediated by the cyclin dependent kinases CDK1 and CDK2, which in turn play a key role in NPM1 dissociation from nucleolar components."
22285574
reach
"In our study, HBx induced CDK2 activity increased the phosphorylation of NPM at Thr 199 which correlated well with its increased intracellular stability."
25918010
sparser
"Since HBx is reported to potentiate the activity of CDK2 kinase [41] which phosphorylates NPM at Thr 199 [55] , we next monitored the phosphorylation status of NPM in its presence."
25918010
sparser
"Hyperphosphorylation of NPM T199 by Cdk2 strongly correlated with constitutive centrosome duplication cycle and centrosome amplification."
21272329
hprd
No evidence text available
18212344
reach
"Furthermore, hyperactive Cdk2 and Cdk4 deregulate the licensing of the centrosome duplication cycle in p53-null cells by hyperphosphorylating nucleophosmin (NPM) at Thr199, as evidenced by observations that ablation of Cdk2, Cdk4, or both Cdk2 and Cdk4 abrogates that excessive phosphorylation."
19933848
sparser
"Early work by Fukasawa and collaborators showed that NPM1 is one of the most conspicuous targets of Cdk2 in unduplicated centrosomes and that phosphorylation of NPM1 on T199 by Cdk2-cyclin E leads to its dissociation from centrosomes ( xref , xref )."
24282781
sparser
"As previously reported, phosphorylation of NPM1 by CDK2-cyclin E on threonine 199 triggers its dissociation from unduplicated centrosomes in the G1 phase, which promotes initiation of centrosome duplication [ xref ]."
34201061
sparser
"After Cdk2 and Cyclin E phosphorylate Thr199 in NPM, NPM dissociates from centrosomes, which in turn triggers centrosome duplication (Grisendi et al., xref )."
30478982
reach
"These observations reveal that RABL6A specifically regulates Cdk2 mediated phosphorylation of NPM at T199."
24282525
sparser
"Cdk2 phosphorylates NPM on T199 and phosphorylation of this site initiates centrosome duplication."
23627734
reach
"In late G1, activated CDK2 and cyclin E phosphorylates NPM1 at T199, causing NPM1 to dissociate from centrosomes, an event essential for centrosome duplication 16."
25922180
sparser
"Phosphorylation of NPM1 on Thr199 by cyclin-dependent kinase 2 (CDK2)/cyclin E is critical for the physical separation of the paired centrioles, which triggers the initiation of centrosome duplication [ xref ]."
34201061
hprd
No evidence text available
19651622
reach
"30 NPM1 is phosphorylated on Thr199 by Cdk2 and cyclin E late in G 1 phase, 31 which causes dissociation of the majority of NPM1 from the centrosomes, a step required for centrosome duplication to occur."
25531824
reach
"NPM1 is phosphorylated at Threonine 199 by the cyclin dependent kinases CDK1 and CDK2 during the cell cycle [XREF_BIBR]."
27553022
hprd
No evidence text available
17287340
reach
"In late G1, activated CDK2 and cyclin E phosphorylates NPM1 at T199, causing NPM1 to dissociate from centrosomes, an event essential for centrosome duplication."
25922180
hprd
No evidence text available
17924679
sparser
"After Cdk2 and cyclin E phosphorylate Thr199 in NPM, NPM dissociates from centrosomes, which in turn triggers centrosome duplication at the late G1 phase."
24290756
hprd
No evidence text available
20068231
reach
"Enhanced phosphorylation of NPM at Thr 199 by CDK2 kinase in the presence of HBx seemed to play a crucial role in preventing its interaction with caspase-3, leading to the accumulation of intracellula[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
25918010
sparser
"Enhanced phosphorylation of NPM at Thr 199 by CDK2 kinase in the presence of HBx seemed to play a crucial role in preventing its interaction with caspase-3, leading to the accumulation of intracellul[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
25918010
reach
"One common event leading to centrosome overduplication is cyclin dependent kinase 2 (Cdk2)-mediated hyperphosphorylation of threonine 199 (T199) within nucleophosmin and B23 (NPM) XREF_BIBR, a major regulator of genomic stability XREF_BIBR."
24282525
hprd
No evidence text available
11278991
sparser
"NPM1 is phosphorylated at Threonine 199 by the cyclin-dependent kinases CDK1 and CDK2 during the cell cycle [ xref ]."
27553022
reach
"Previous studies show that CDK4, CDK6 and CDK2 phosphorylate NPM at Thr199 initiating the separation of centrosomes, as the first step in centrosome duplication."
27998958
sparser
"Previous studies have shown that the human NPM’s phosphorylation by cyclin E–cyclin-dependent kinase 2 (cdk2) on threonine (Thr) 199 regulates its translocation from the centrosome during cell cycle progression."
19561638