+ |
NLK | up-regulates activity
phosphorylation
|
YAP1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273909 |
Ser128 |
QHVRAHSsPASLQLG |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
27979971 |
Here, we report that osmotic stress stimulates transient YAP nuclear localization and increases YAP activity even when YAP Ser127 is phosphorylated. Osmotic stress acts via the NLK kinase to induce YAP Ser128 phosphorylation. Phosphorylation of YAP at Ser128 interferes with its ability to bind to 14-3-3, resulting in YAP nuclear accumulation and induction of downstream target gene expression. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
NLK | down-regulates
phosphorylation
|
LEF1 |
0.751 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-97808 |
Ser166 |
TYSDEHFsPGSHPSH |
Homo sapiens |
|
pmid |
sentence |
12556497 |
Regulation of lymphoid enhancer factor 1/t-cell factor by mitogen-activated protein kinase-related nemo-like kinase-dependent phosphorylation in wnt/beta-catenin signaling.Nlk phosphorylates lef-1/tcf on two serine/threonine residues located in its central region. Mutation of both residues to alanine enhanced lef-1 transcriptional activity and rendered it resistant to inhibition by nlk. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-97812 |
Thr155 |
SHAVHPLtPLITYSD |
Homo sapiens |
|
pmid |
sentence |
12556497 |
Regulation of lymphoid enhancer factor 1/t-cell factor by mitogen-activated protein kinase-related nemo-like kinase-dependent phosphorylation in wnt/beta-catenin signaling.Nlk phosphorylates lef-1/tcf on two serine/threonine residues located in its central region. Mutation of both residues to alanine enhanced lef-1 transcriptional activity and rendered it resistant to inhibition by nlk. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
NLK | down-regulates activity
phosphorylation
|
FOXO1 |
0.601 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273907 |
Ser329 |
STISGRLsPIMTEQD |
Chlorocebus aethiops |
COS-1 Cell |
pmid |
sentence |
20061393 |
Here, we report that the transforming growth factor-beta-activated kinase (TAK1)-Nemo-like kinase (NLK) pathway negatively regulates FOXO1. We show that NLK binds and phosphorylates FOXO1 at Pro-directed Ser/Thr residues in the transactivation domain. The phosphorylation by TAK1-NLK pathway inhibits the transcriptional activity of FOXO1 and excludes FOXO1 from the nucleus, which is independent of phosphatidylinositol 3-kinase/Akt pathway. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
NLK | up-regulates
phosphorylation
|
STAT3 |
0.354 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-155828 |
Ser727 |
NTIDLPMsPRTLDSL |
Homo sapiens |
Breast Cancer Cell |
pmid |
sentence |
17563747 |
Phosphorylation of s727 induces pin1 binding which increases transcription. Pin1 binding increases stat3 interaction with p300 and dna. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
NLK | down-regulates activity
phosphorylation
|
RPTOR |
0.334 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273908 |
Ser863 |
LTQSAPAsPTNKGVH |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
26588989 |
NLK inhibits mTORC1 lysosomal localization and thereby suppresses mTORC1 activation. Mechanistically, NLK phosphorylates Raptor on S863 to disrupt its interaction with the Rag GTPase, which is important for mTORC1 lysosomal recruitment. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
NLK | down-regulates
phosphorylation
|
TCF7L2 |
0.763 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-97819 |
Thr201 |
PHHVHPLtPLITYSN |
Homo sapiens |
|
pmid |
sentence |
12556497 |
Nlk phosphorylates lef-1/tcf on two serine/threonine residues located in its central region. Mutation of both residues to alanine enhanced lef-1 transcriptional activity and rendered it resistant to inhibition by nlk. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-97873 |
Thr212 |
TYSNEHFtPGNPPPH |
Homo sapiens |
|
pmid |
sentence |
12556497 |
Nlk phosphorylates lef-1/tcf on two serine/threonine residues located in its central region. Mutation of both residues to alanine enhanced lef-1 transcriptional activity and rendered it resistant to inhibition by nlk. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
NLK | down-regulates quantity
phosphorylation
|
LEF1 |
0.751 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271596 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
16714285 |
NLK Augments the Ubiquitylation Activity of NARF against TCF/LEF. ctivation of NLK induced by unknown ligands leads to the phosphorylation of TCF/LEF. NARF then acts on TCF/LEF as an E3 ubiquitin-ligase and, together with E1 and E2 ubiquitylation enzymes, catalyze the ubiquitylation of TCF/LEF. Finally, ubiquitylated TCF/LEF is degraded by the 26 S proteasome. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
NLK | form complex
binding
|
SETDB1/NLK/CHD7 |
0.423 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-253525 |
|
|
Mus musculus |
|
pmid |
sentence |
21952300 |
The non-canonical WNT ligand WNT5A activates the histone methyltransferase SET domain bifurcated 1 (SETDB1)42. SETDB1 forms a complex with chromodomain helicase DNA-binding 7 (CHD7) and NEMO-like kinase (NLK) to inhibit the ability of PPARγ to transcriptionally activate its downstream metabolic target genes in the MSC cell line ST2 and in 3T3‑L1 cells42,43. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
NLK | down-regulates
phosphorylation
|
TCF4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-24147 |
|
|
Homo sapiens |
|
pmid |
sentence |
2861485 |
Whereas lef-1 and tcf-4 phosphorylation by nlk (nemo-like kinase) leads to less lef/tcf/beta-catenin complex binding to dna and to lef-1/tcf-4 degradation |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
NLK | down-regulates quantity
phosphorylation
|
TCF7L2 |
0.763 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271597 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
16714285 |
NLK Augments the Ubiquitylation Activity of NARF against TCF/LEF. ctivation of NLK induced by unknown ligands leads to the phosphorylation of TCF/LEF. NARF then acts on TCF/LEF as an E3 ubiquitin-ligase and, together with E1 and E2 ubiquitylation enzymes, catalyze the ubiquitylation of TCF/LEF. Finally, ubiquitylated TCF/LEF is degraded by the 26 S proteasome. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
FZD3 | up-regulates
binding
|
NLK |
0.36 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-167862 |
|
|
Homo sapiens |
|
pmid |
sentence |
20828404 |
Upon ligand binding, non-canonical wnt signaling controls tissue polarity and cell movement through the activation of rhoa, c-jun n-terminal kinase (jnk), and nemo-like kinase (nlk) signaling cascades. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAP3K7 | up-regulates
phosphorylation
|
NLK |
0.635 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-96425 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
12482967 |
The tak1-nlk-mapk-related pathway antagonizes signalling between beta-catenin and transcription factor tcf. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
NLK | down-regulates
phosphorylation
|
NOTCH1 |
0.391 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-163697 |
|
|
Homo sapiens |
|
pmid |
sentence |
20118921 |
Nlk-phosphorylated notch1icd is impaired in its ability to form a transcriptionally_ active_ ternary_ complex. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |