+ |
NEK2 | up-regulates
phosphorylation
|
SGO1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-156878 |
Ser14 |
LKKSFQDsLEDIKKR |
Homo sapiens |
|
pmid |
sentence |
17621308 |
Here we show that nek2a phosphorylates human sgo1 and such phosphorylation is essential for faithful chromosome congression in mitosis. phosphorylation sites were mapped to ser(14) and ser(507) |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-156882 |
Ser507 |
TDLCFLNsPIFKQKK |
Homo sapiens |
|
pmid |
sentence |
17621308 |
Here we show that nek2a phosphorylates human sgo1 and such phosphorylation is essential for faithful chromosome congression in mitosis. phosphorylation sites were mapped to ser(14) and ser(507) |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
NEK2 | up-regulates
phosphorylation
|
NDC80 |
0.611 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-94322 |
Ser165 |
LGYPFALsKSSMYTV |
Homo sapiens |
|
pmid |
sentence |
12386167 |
Phosphorylation of the mitotic regulator protein hec1 by nek2 kinase is essential for faithful chromosome segregation.Hec1 (highly expressed in cancer) plays essential roles in chromosome segregation by interacting through its coiled-coil domains with several proteins that modulate the g(2)/m phase.Nek2 phosphorylates hec1 on serine residue 165, both in vitro and in vivo. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
NEK2 | up-regulates
phosphorylation
|
NEK2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-151755 |
Ser171 |
RILNHDTsFAKTFVG |
Homo sapiens |
|
pmid |
sentence |
17197699 |
Enzymatic activity, induced; |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-151759 |
Thr170 |
ARILNHDtSFAKTFV |
Homo sapiens |
|
pmid |
sentence |
17197699 |
Thus, it appears that autophosphorylation of thr-170 and/or ser-171 in nek2 may fine-tune overall activity of nek2 in vivo. regardless, the importance of thr-175 suggested by its conservation in many other kinases is underlined by the t175a mutant that shows reduced kinase activity and a significant reduction in efficiency of cs. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-151763 |
Thr175 |
HDTSFAKtFVGTPYY |
Homo sapiens |
|
pmid |
sentence |
17197699 |
Enzymatic activity, induced; |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
NEK2 | down-regulates
phosphorylation
|
CEP250 |
0.766 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-204833 |
Ser2392 |
AGLHHSLsHSLLAVA |
Homo sapiens |
|
pmid |
sentence |
24695856 |
Our data support a model in which centrosome disjunction is triggered by the hyperphosphorylation of c-nap1, a major linker component. This occurs in response to a shift in the balance of activities of the nek2?_Pp1 bi-stable switch. C-nap1 hyperphosphorylation triggers the loss of both oligomerization and, crucially, interaction with the core centriole proximal-end protein, cep135. All three of these sites were identified in our in vivo analysis but only two (s2234 and s2394) were identified as nek2 phosphorylation sites in vitro. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-204837 |
Ser2394 |
LHHSLSHsLLAVAQA |
Homo sapiens |
|
pmid |
sentence |
24695856 |
C-nap1 hyperphosphorylation triggers the loss of both oligomerization and, crucially, interaction with the core centriole proximal-end protein, cep135. All three of these sites were identified in our in vivo analysis but only two (s2234 and s2394) were identified as nek2 phosphorylation sites in vitro. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
NEK2 | down-regulates
phosphorylation
|
NEK2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-151767 |
Ser241 |
RRIPYRYsDELNEII |
Homo sapiens |
|
pmid |
sentence |
17197699 |
Enzymatic activity, inhibited; |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-151771 |
Thr179 |
FAKTFVGtPYYMSPE |
Homo sapiens |
|
pmid |
sentence |
17197699 |
Enzymatic activity, inhibited; |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
NEK2 | up-regulates activity
phosphorylation
|
GAS2L1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273683 |
Ser352 |
HPRSRRYsGDSDSSA |
Homo sapiens |
|
pmid |
sentence |
32289147 |
Nek2A mediates G2/M phosphorylation of GAS2L1. GAS2L1 and its Ser352 phosphorylation are required for proper spindle organization and chromosome segregation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
STK3 | up-regulates
phosphorylation
|
NEK2 |
0.246 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-169539 |
Ser438 |
EKNYQLKsRQILGMR |
Homo sapiens |
|
pmid |
sentence |
21076410 |
Our data suggest that mst2 phosphorylates nek2a thereby recruiting nek2a to centrosomes and promoting phosphorylation and displacement of centrosomal linker proteins |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
NEK2 | down-regulates activity
phosphorylation
|
LRRC45 |
0.38 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273707 |
Ser661 |
VLAYVQAsPVRTLSP |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
24035387 |
Moreover, LRRC45 interacts with both C-Nap1 and rootletin and is phosphorylated by Nek2A at S661 during mitosis. After phosphorylation, both LRRC45 centrosomal localization and fiber-like structures are significantly reduced, which subsequently leads to centrosome separation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
NEK2 | up-regulates quantity by stabilization
phosphorylation
|
YAP1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276586 |
Thr143 |
AVSPGTLtPTGVVSG |
|
|
pmid |
sentence |
35705994 |
NEK2 promotes the migration and proliferation of ESCC via stabilization of YAP1 by phosphorylation at Thr-143 |
|
Publications: |
1 |
+ |
NEK2 | up-regulates quantity by stabilization
phosphorylation
|
CD274 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277315 |
Thr194 |
EEKLFNVtSTLRINT |
Mus musculus |
Pancreatic Cancer Cell |
pmid |
sentence |
34315872 |
NEK2 interacts with PD-L1, phosphorylating the T194/T210 residues and preventing ubiquitin-proteasome pathway-mediated degradation of PD-L1 in ER lumen. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277314 |
Thr210 |
TNEIFYCtFRRLDPE |
Mus musculus |
Pancreatic Cancer Cell |
pmid |
sentence |
34315872 |
NEK2 interacts with PD-L1, phosphorylating the T194/T210 residues and preventing ubiquitin-proteasome pathway-mediated degradation of PD-L1 in ER lumen. |
|
Publications: |
2 |
Organism: |
Mus Musculus |
+ |
NEK2 | down-regulates
phosphorylation
|
PPP1CC |
0.502 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-78306 |
Thr307 |
EKKKPNAtRPVTPPR |
Homo sapiens |
|
pmid |
sentence |
10880350 |
Pp1 is a substrate for nek2 and phosphorylation of pp1gamma(1) on two c-terminal sites reduces its phosphatase activity. / threonine-307 and -318 appear to be equally well phosphorylated by nek2 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-78603 |
Thr318 |
TPPRGMItKQAKK |
Homo sapiens |
|
pmid |
sentence |
10880350 |
Pp1 is a substrate for nek2 and phosphorylation of pp1gamma(1) on two c-terminal sites reduces its phosphatase activity. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
PP1 | down-regulates
dephosphorylation
|
NEK2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264667 |
|
|
Homo sapiens |
|
pmid |
sentence |
17283141 |
Nek2 is activated by autophosphorylation, and its dephosphorylation is catalyzed by pp1 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PCM1 | up-regulates
relocalization
|
NEK2 |
0.4 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-133337 |
|
|
Homo sapiens |
|
pmid |
sentence |
15659651 |
Recruitment of nek2 and c-nap1 to the centrosome is dependent on pcm-1 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
NEK2 | down-regulates
phosphorylation
|
PP1 |
0.503 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264655 |
|
|
Homo sapiens |
|
pmid |
sentence |
10880350 |
Pp1 is a substrate for nek2 and phosphorylation of pp1gamma(1) on two c-terminal sites reduces its phosphatase activity. / threonine-307 and -318 appear to be equally well phosphorylated by nek2 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
NEK2 | down-regulates activity
phosphorylation
|
CCDC102B |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275626 |
|
|
|
|
pmid |
sentence |
30404835 |
CCDC102B is recruited to the centrosome by C-Nap1 (also known as CEP250) and interacts with the centrosome linker components rootletin and LRRC45. CCDC102B decorates and facilitates the formation of rootletin filaments. Furthermore, CCDC102B is phosphorylated by Nek2A (an isoform encoded by NEK2) and is disassociated from the centrosome at the onset of mitosis. |
|
Publications: |
1 |
+ |
NEK2 | up-regulates
phosphorylation
|
NEK11 |
0.402 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-124944 |
|
|
Homo sapiens |
|
pmid |
sentence |
15161910 |
Nek2 directly phosphorylated nek11 in the c-terminal non-catalytic region and elevated nek11 kinase activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PPP1CA | down-regulates
dephosphorylation
|
NEK2 |
0.382 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-152949 |
|
|
Homo sapiens |
|
pmid |
sentence |
17283141 |
Nek2 is activated by autophosphorylation, and its dephosphorylation is catalyzed by pp1 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |