Aliases for RPS6KB1 Gene
- Ribosomal Protein S6 Kinase B1 2 3 5
- S6K1 2 3 4
- Serine/Threonine-Protein Kinase 14A 3 4
- Ribosomal Protein S6 Kinase Beta-1 3 4
- Ribosomal Protein S6 Kinase I 3 4
- P70(S6K)-Alpha 2 3
- EC 184.108.40.206 4 51
- S6K-Beta-1 3 4
- P70 S6KA 3 4
- STK14A 3 4
- PS6K 2 3
- S6K 2 3
- Ribosomal Protein S6 Kinase, 70kDa, Polypeptide 1 3
External Ids for RPS6KB1 Gene
Previous HGNC Symbols for RPS6KB1 Gene
Previous GeneCards Identifiers for RPS6KB1 Gene
This gene encodes a member of the ribosomal S6 kinase family of serine/threonine kinases. The encoded protein responds to mTOR (mammalian target of rapamycin) signaling to promote protein synthesis, cell growth, and cell proliferation. Activity of this gene has been associated with human cancer. Alternatively spliced transcript variants have been observed. The use of alternative translation start sites results in isoforms with longer or shorter N-termini which may differ in their subcellular localizations. There are two pseudogenes for this gene on chromosome 17. [provided by RefSeq, Jan 2013]
GeneCards Summary for RPS6KB1 Gene
RPS6KB1 (Ribosomal Protein S6 Kinase B1) is a Protein Coding gene. Diseases associated with RPS6KB1 include Tuberous Sclerosis and Lymphangioleiomyomatosis. Among its related pathways are Common Cytokine Receptor Gamma-Chain Family Signaling Pathways and Translation Translation regulation by Alpha-1 adrenergic receptors. Gene Ontology (GO) annotations related to this gene include transferase activity, transferring phosphorus-containing groups and protein tyrosine kinase activity. An important paralog of this gene is RPS6KB2.
UniProtKB/Swiss-Prot Summary for RPS6KB1 Gene
Serine/threonine-protein kinase that acts downstream of mTOR signaling in response to growth factors and nutrients to promote cell proliferation, cell growth and cell cycle progression. Regulates protein synthesis through phosphorylation of EIF4B, RPS6 and EEF2K, and contributes to cell survival by repressing the pro-apoptotic function of BAD. Under conditions of nutrient depletion, the inactive form associates with the EIF3 translation initiation complex. Upon mitogenic stimulation, phosphorylation by the mammalian target of rapamycin complex 1 (mTORC1) leads to dissociation from the EIF3 complex and activation. The active form then phosphorylates and activates several substrates in the pre-initiation complex, including the EIF2B complex and the cap-binding complex component EIF4B. Also controls translation initiation by phosphorylating a negative regulator of EIF4A, PDCD4, targeting it for ubiquitination and subsequent proteolysis. Promotes initiation of the pioneer round of protein synthesis by phosphorylating POLDIP3/SKAR. In response to IGF1, activates translation elongation by phosphorylating EEF2 kinase (EEF2K), which leads to its inhibition and thus activation of EEF2. Also plays a role in feedback regulation of mTORC2 by mTORC1 by phosphorylating RICTOR, resulting in the inhibition of mTORC2 and AKT1 signaling. Mediates cell survival by phosphorylating the pro-apoptotic protein BAD and suppressing its pro-apoptotic function. Phosphorylates mitochondrial URI1 leading to dissociation of a URI1-PPP1CC complex. The free mitochondrial PPP1CC can then dephosphorylate RPS6KB1 at Thr-412, which is proposed to be a negative feedback mechanism for the RPS6KB1 anti-apoptotic function. Mediates TNF-alpha-induced insulin resistance by phosphorylating IRS1 at multiple serine residues, resulting in accelerated degradation of IRS1. In cells lacking functional TSC1-2 complex, constitutively phosphorylates and inhibits GSK3B. May be involved in cytoskeletal rearrangement through binding to neurabin. Phosphorylates and activates the pyrimidine biosynthesis enzyme CAD, downstream of MTOR (PubMed:11500364, PubMed:12801526, PubMed:14673156, PubMed:15071500, PubMed:15341740, PubMed:16286006, PubMed:17052453, PubMed:17053147, PubMed:17936702, PubMed:18952604, PubMed:19085255, PubMed:19720745, PubMed:19935711, PubMed:19995915, PubMed:23429703). Following activation by mTORC1, phosphorylates EPRS and thereby plays a key role in fatty acid uptake by adipocytes and also most probably in interferon-gamma-induced translation inhibition (PubMed:28178239).
Ribosomal S6 protein kinases (RSKs) are a family of protein serine/threonine kinases that regulate diverse cellular processes such as cellular growth, motility, survival and proliferation. The RSK family can be divided into two subfamilies, namely p90 RSK and p70 S6K.