Recombinant Human S6K1 protein
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(1 Publication)
Recombinant Human S6K1 protein is a Human Full Length protein, in the 1 to 525 aa range, expressed in Baculovirus infected Sf9 cells, with >90%, suitable for SDS-PAGE, WB.
View Alternative Names
STK14A, Ribosomal protein S6 kinase beta-1, S6K-beta-1, S6K1, 70 kDa ribosomal protein S6 kinase 1, Ribosomal protein S6 kinase I, Serine/threonine-protein kinase 14A, p70 ribosomal S6 kinase alpha, P70S6K1, p70-S6K 1, p70 S6 kinase alpha, p70 S6K-alpha, p70 S6KA
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human S6K1 protein (AB167933)
SDS-PAGE analysis of ab167933.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
S6K1 functions as a downstream effector of the mammalian target of rapamycin (mTOR) complex specifically mTORC1. S6K1 interacts with several protein complexes enhancing its regulatory capacity in cellular activities. It modulates protein synthesis by phosphorylating substrates involved in translation. By controlling these processes S6K1 aids in cell size regulation and energy metabolism which are critical for maintaining cellular homeostasis and adaptation to nutrient availability.
Pathways
S6K1 plays an essential role in the mTOR signaling pathway a central regulator of cell growth and metabolism. S6K1 functions in close connection with proteins such as mTOR and Raptor within this pathway. Additionally it is involved in the insulin signaling pathway where it works with proteins like insulin receptor substrate (IRS). Both pathways highlight S6K1's role in nutrient sensing and response emphasizing its significance in energy and protein homeostasis.
Specifications
Form
Liquid
Additional notes
Affinity purified.
General info
Function
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 (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 : 22017876, PubMed : 23429703, PubMed : 28178239). Regulates protein synthesis through phosphorylation of EIF4B, RPS6 and EEF2K, and contributes to cell survival by repressing the pro-apoptotic function of BAD (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 : 22017876, PubMed : 23429703, PubMed : 28178239). Under conditions of nutrient depletion, the inactive form associates with the EIF3 translation initiation complex (PubMed : 16286006). Upon mitogenic stimulation, phosphorylation by the mechanistic target of rapamycin complex 1 (mTORC1) leads to dissociation from the EIF3 complex and activation (PubMed : 16286006). 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 (PubMed : 16286006). Also controls translation initiation by phosphorylating a negative regulator of EIF4A, PDCD4, targeting it for ubiquitination and subsequent proteolysis (PubMed : 17053147). Promotes initiation of the pioneer round of protein synthesis by phosphorylating POLDIP3/SKAR (PubMed : 15341740). In response to IGF1, activates translation elongation by phosphorylating EEF2 kinase (EEF2K), which leads to its inhibition and thus activation of EEF2 (PubMed : 11500364). Also plays a role in feedback regulation of mTORC2 by mTORC1 by phosphorylating RICTOR, resulting in the inhibition of mTORC2 and AKT1 signaling (PubMed : 19720745, PubMed : 19935711, PubMed : 19995915). Also involved in feedback regulation of mTORC1 and mTORC2 by phosphorylating DEPTOR (PubMed : 22017876). Mediates cell survival by phosphorylating the pro-apoptotic protein BAD and suppressing its pro-apoptotic function (By similarity). Phosphorylates mitochondrial URI1 leading to dissociation of a URI1-PPP1CC complex (PubMed : 17936702). 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 (PubMed : 17936702). Mediates TNF-alpha-induced insulin resistance by phosphorylating IRS1 at multiple serine residues, resulting in accelerated degradation of IRS1 (PubMed : 18952604). In cells lacking functional TSC1-2 complex, constitutively phosphorylates and inhibits GSK3B (PubMed : 17052453). May be involved in cytoskeletal rearrangement through binding to neurabin (By similarity). Phosphorylates and activates the pyrimidine biosynthesis enzyme CAD, downstream of MTOR (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).
Sequence similarities
Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. S6 kinase subfamily.
Post-translational modifications
Phosphorylation at Thr-412 is regulated by mTORC1. The phosphorylation at this site is maintained by an agonist-dependent autophosphorylation mechanism (PubMed:18925875, PubMed:19085255, PubMed:22017876, PubMed:23429703, PubMed:29236692). Activated by phosphorylation at Thr-252 by PDPK1 (PubMed:19864428, PubMed:9445476). Dephosphorylation by PPP1CC at Thr-412 in mitochondrion (PubMed:17936702).
Subcellular localisation
Mitochondrion outer membrane
Target data
Publications (1)
Recent publications for all applications. Explore the full list and refine your search
Cell death & disease 12:822 PubMed34462427
2021
Applications
Unspecified application
Species
Unspecified reactive species
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