Aliases for RPS6KA3 Gene
- Ribosomal Protein S6 Kinase, 90kDa, Polypeptide 3 2 3
- RSK2 3 4 6
- MAP Kinase-Activated Protein Kinase 1b 3 4
- Insulin-Stimulated Protein Kinase 1 3 4
- MAPK-Activated Protein Kinase 1b 3 4
- Ribosomal S6 Kinase 2 3 4
- MAPKAP Kinase 1b 3 4
- S6K-Alpha-3 3 4
- EC 220.127.116.11 4 64
- MAPKAPK-1b 3 4
- P90-RSK 3 3 4
- MAPKAPK1B 3 4
- Pp90RSK2 3 4
- ISPK-1 3 4
- MRX19 3 6
External Ids for RPS6KA3 Gene
Previous Symbols for RPS6KA3 Gene
This gene encodes a member of the RSK (ribosomal S6 kinase) family of serine/threonine kinases. This kinase contains 2 non-identical 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. Mutations in this gene have been associated with Coffin-Lowry syndrome (CLS). [provided by RefSeq, Jul 2008]
GeneCards Summary for RPS6KA3 Gene
RPS6KA3 (Ribosomal Protein S6 Kinase, 90kDa, Polypeptide 3) is a Protein Coding gene. Diseases associated with RPS6KA3 include coffin-lowry syndrome and alpha-thalassemia/mental retardation syndrome. Among its related pathways are Signaling by FGFR and Signaling by FGFR. GO annotations related to this gene include protein serine/threonine kinase activity and magnesium ion binding. An important paralog of this gene is MKNK2.
UniProtKB/Swiss-Prot for RPS6KA3 Gene
Serine/threonine-protein kinase that acts downstream of ERK (MAPK1/ERK2 and MAPK3/ERK1) signaling and mediates mitogenic and stress-induced activation of the transcription factors CREB1, ETV1/ER81 and NR4A1/NUR77, regulates translation through RPS6 and EIF4B phosphorylation, and mediates cellular proliferation, survival, and differentiation by modulating mTOR signaling and repressing pro-apoptotic function of BAD and DAPK1. In fibroblast, is required for EGF-stimulated phosphorylation of CREB1 and histone H3 at Ser-10, which results in the subsequent transcriptional activation of several immediate-early genes. In response to mitogenic stimulation (EGF and PMA), phosphorylates and activates NR4A1/NUR77 and ETV1/ER81 transcription factors and the cofactor CREBBP. Upon insulin-derived signal, acts indirectly on the transcription regulation of several genes by phosphorylating GSK3B at Ser-9 and inhibiting its activity. Phosphorylates RPS6 in response to serum or EGF via an mTOR-independent mechanism and promotes translation initiation by facilitating assembly of the preinitiation complex. In response to insulin, phosphorylates EIF4B, enhancing EIF4B affinity for the EIF3 complex and stimulating cap-dependent translation. Is involved in the mTOR nutrient-sensing pathway by directly phosphorylating TSC2 at Ser-1798, which potently inhibits TSC2 ability to suppress mTOR signaling, and mediates phosphorylation of RPTOR, which regulates mTORC1 activity and may promote rapamycin-sensitive signaling independently of the PI3K/AKT pathway. Mediates cell survival by phosphorylating the pro-apoptotic proteins BAD and DAPK1 and suppressing their pro-apoptotic function. Promotes the survival of hepatic stellate cells by phosphorylating CEBPB in response to the hepatotoxin carbon tetrachloride (CCl4). Is involved in cell cycle regulation by phosphorylating the CDK inhibitor CDKN1B, which promotes CDKN1B association with 14-3-3 proteins and prevents its translocation to the nucleus and inhibition of G1 progression. In LPS-stimulated dendritic cells, is involved in TLR4-induced macropinocytosis, and in myeloma cells, acts as effector of FGFR3-mediated transformation signaling, after direct phosphorylation at Tyr-529 by FGFR3. Phosphorylates DAPK1.
p90 ribosomal S6 kinases (RSKs) are a family of protein serine/threonine kinases that regulate diverse cellular processes such as cell growth, motility, survival and proliferation. There are four isoforms of this enzyme; RSK1-4, which are directly activated by ERK1/2 in response to growth factors, many polypeptide hormones, neurotransmitters and chemokines. p90 RSKs phosphorylate numerous cytosolic and nuclear targets and act as downstream effectors of the ERK/MAPK signaling cascade. They are expressed ubiquitously in human tissues and exist in multiple subcellular compartments. Abberant activation of p90 RSKs has been linked to many human diseases, including breast and prostate cancers.