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Validated All-in-One™ qPCR Primer for RPS6KA1(NM_002953.3) Search again
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
Summary
This gene encodes a member of the RSK (ribosomal S6 kinase) family of serine/threonine kinases. This kinase contains 2 nonidentical kinase catalytic domains and phosphorylates various substrates, including members of the mitogen-activated kinase (MAPK) signalling pathway. The activity of this protein has been implicated in controlling cell growth and differentiation.
Gene References into function
- was found to be activated by lead in a PKC- and MAPK-dependent manner
- Regulation of an activated S6 kinase 1 variant reveals a novel mammalian target of rapamycin phosphorylation site.
- TF cytoplasmic domain-independent stimulation of protein synthesis via activation of S6 kinase contributes to FVIIa effects in pathophysiology.
- activated transiently by stromal cell-derived factor 1 alpha alone or synergistically in combination with other cytokines
- Mammalian cell size is controlled by mTOR and its downstream targets S6K1 and 4EBP1/eIF4E
- RSK1 is negatively regulated by 14-3-3beta
- overexpressed in breast tumors
- Results suggest that active fibroblast growth factor receptor 1 kinase regulates the functions of nuclear 90-kDa ribosomal S6 kinase.
- that p90 ribosomal S 6 protein kinase 1 (RSK1) mediates the PGE2-induced phosphorylation of cAMP-response element binding protein
- monitored 14 previously uncharacterized and six known phosphorylation events after phorbol ester stimulation in the ERK/p90 ribosomal S6 kinase-signaling targets, TSC1 and TSC2, and a protein kinase C-dependent pathway to TSC2 phosphorylation
- S6 kinase 1 is a novel mammalian target of rapamycin (mTOR)-phosphorylating kinase
- RSK-mediated phosphorylation of DAPK is a unique mechanism for suppressing the proapoptotic function of this death kinase in healthy cells as well as Ras/Raf-transformed cells.
- interactions between subunits of PKA and RSK1 that are dependent upon the activation state of RSK1 and determine its subcellular distribution and biological actions
- A study evaluating the impact of carbohydrate and/or protein ingestion before and after exercise on ribosomal protein S6 kinase (S6K1) and S6 phosphorylation status in human skeletal muscle tissue is presented.
- study reports the crystal structures of the unactivated RSK1 N-terminal kinase domain bound to different ligands at 2.0 A resolution
- Residues 411-735 of human RSK1, covering the C-terminal serine/threonine kinase catalytic domain and the functionally important tail, were cloned into an Escherichia coli expression vector
- The ERK-RSK1 activation by growth factors delays G2/M transition and this might be required to maintain genomic integrity during growth factor stimulation.
- RSK1 and RSK2 are required for Raptor phosphorylation in vivo and directly phosphorylate Raptor in vitro.
- betaTrCP promotes cell survival in cooperation with the ERK-RSK pathway by targeting BimEL for degradation.
