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Rabbit Anti-Phospho-Nemo-like kinase (Thr298)/FITC Conjugated antibody
background:
Nemo-like kinase (NLK) plays a role in cell fate determination and is required for differentiation of bone marrow stromal cells. It acts downstream of MAP3K7 and HIPK2 to negatively regulate the canonical Wnt/beta-catenin signaling pathway and the phosphorylation and destruction of the MYB transcription factor. It may suppress a wide range of transcription factors by phosphorylation of the coactivator, CREBBP. (referenced from swissprot)
Function:
Serine/threonine-protein kinase that regulates a number of transcription factors with key roles in cell fate determination. Positive effector of the non-canonical Wnt signaling pathway, acting downstream of WNT5A, MAP3K7/TAK1 and HIPK2. Activation of this pathway causes binding to and phosphorylation of the histone methyltransferase SETDB1. The NLK-SETDB1 complex subsequently interacts with PPARG, leading to methylation of PPARG target promoters at histone H3K9 and transcriptional silencing. The resulting loss of PPARG target gene transcription inhibits adipogenesis and promotes osteoblastogenesis in mesenchymal stem cells (MSCs). Negative regulator of the canonical Wnt/beta-catenin signaling pathway. Binds to and phosphorylates TCF7L2/TCF4 and LEF1, promoting the dissociation of the TCF7L2/LEF1/beta-catenin complex from DNA, as well as the ubiquitination and subsequent proteolysis of LEF1. Together these effects inhibit the transcriptional activation of canonical Wnt/beta-catenin target genes. Negative regulator of the Notch signaling pathway. Binds to and phosphorylates NOTCH1, thereby preventing the formation of a transcriptionally active ternary complex of NOTCH1, RBPJ/RBPSUH and MAML1. Negative regulator of the MYB family of transcription factors. Phosphorylation of MYB leads to its subsequent proteolysis while phosphorylation of MYBL1 and MYBL2 inhibits their interaction with the coactivator CREBBP. Other transcription factors may also be inhibited by direct phosphorylation of CREBBP itself. Acts downstream of IL6 and MAP3K7/TAK1 to phosphorylate STAT3, which is in turn required for activation of NLK by MAP3K7/TAK1.
Subunit:
Homodimer. Homodimerization is required for intermolecular autophosphorylation, kinase activation and nuclear localization. May interact with components of cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes. Interacts with LEF1, MEF2A, MYBL1 and MYBL2. Interacts with the upstream activating kinases HIPK2 and MAP3K7/TAK1. Interaction with MAP3K7/TAK1 seems to be indirect, and may be mediated by other proteins such as STAT3, TAB1 and TAB2. Interacts with and phosphorylates a number of transcription factors including FOXO1, FOXO3, FOXO4, MYB, NOTCH1 and TCF7L2/TCF4. Interacts with DAPK3/ZIPK, and this interaction may disrupt interaction with transcription factors such as TCF7L2/TCF4. Forms a transcriptional repressor complex with CHD7, PPARG and SETDB1. Interacts with RNF138/NARF.
Subcellular Location:
Nucleus. Cytoplasm. Note=Predominantly nuclear. A smaller fraction is cytoplasmic.
Post-translational modifications:
Phosphorylated on Thr-298. Intermolecular autophosphorylation on Thr-298 activates the enzyme.
Similarity:
Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily.
Contains 1 protein kinase domain.
Database links:
Entrez Gene: 51701 Human
Entrez Gene: 3699 Mouse
Entrez Gene: 497961 Rat
Omim: 609476 Human
SwissProt: Q9UBE8 Human
SwissProt: O54949 Mouse
SwissProt: D3ZSZ3 Rat
Unigene: 208759 Human
Unigene: 9001 Mouse
Unigene: 113514 Rat
Important Note:
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
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