Rps6kb1
entrez
72508
canonical
uniprot
Q8BSK8
canonical
ensembl
ENSMUSG00000020516
resolver
ensp
ENSMUSP00000053188
resolver
ensp
ENSMUSP00000119715
resolver
ensp
ENSMUSP00000308747
resolver
ensp
ENSMUSP00000308750
resolver
ensp
ENSMUSP00000308794
resolver
enst
ENSMUST00000058286
resolver
genesymbol
Rps6kb1
resolver
uniprot
F7A6D6
resolver
uniprot
Q3UXD8
resolver
uniprot
Q5SWG1
resolver
uniprot
Q8C3J7
resolver
uniprot
Q8CHX0
resolver
uniprot_entry
F7A6D6_MOUSE
resolver
uniprot_entry
KS6B1_MOUSE
resolver
uniprot_entry
Q3UXD8_MOUSE
resolver
uniprot_entry
Q8C3J7_MOUSE
resolver
uniprot_sec
Q5SWG1
resolver
uniprot_sec
Q8CHX0
resolver
activity_regulation
ACTIVITY REGULATION: Activation requires multiple phosphorylation events on serine/threonine residues. Activation appears to be first mediated by phosphorylation of multiple sites in the autoinhibitory domain, which facilitates phosphorylation at Thr-412, disrupting the autoinhibitory mechanism and allowing phosphorylation of Thr-252 by PDPK1. The active conformation of the kinase is believed to be stabilized by a mechanism involving three conserved phosphorylation sites located in the kinase domain activation loop (Thr-252) and in the AGC-kinase C-terminal domain (Ser-394 in the middle of the tail/linker region and Thr-412 within a hydrophobic motif at its end). Activated by mTORC1; isoform Alpha I and isoform Alpha II are sensitive to rapamycin, which inhibits activating phosphorylation at Thr-412. Activated by PDPK1 (By similarity). {ECO:0000250}.
uniprot
proteins
amino_acid_sequence
MRRRRRRDGFYLAPDFRHREAEDMAGVFDIDLDQPEDAGSEDELEEGGQLNESMDHGGVGPYELGMEHCEKFEISETSVNRGPEKIRPECFELLRVLGKGGYGKVFQVRKVTGANTGKIFAMKVLKKAMIVRNAKDTAHTKAERNILEEVKHPFIVDLIYAFQTGGKLYLILEYLSGGELFMQLEREGIFMEDTACFYLAEISMALGHLHQKGIIYRDLKPENIMLNHQGHVKLTDFGLCKESIHDGTVTHTFCGTIEYMAPEILMRSGHNRAVDWWSLGALMYDMLTGAPPFTGENRKKTIDKILKCKLNLPPYLTQEARDLLKKLLKRNAASRLGAGPGDAGEVQAHPFFRHINWEELLARKVEPPFKPLLQSEEDVSQFDSKFTRQTPVDSPDDSTLSESANQVFLGFTYVAPSVLESVKEKFSFEPKIRSPRRFIGSPRTPVSPVKFSPGDFWGRGASASTANPQTPVEYPMETSGIEQMDVTVSGEASAPLPIRQPNSGPYKKQAFPMISKRPEHLRMNL
uniprot
proteins
ec_number
2.7.11.1
uniprot
proteins
function
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:11493700, PubMed:11500364, PubMed:15060135, PubMed:24161930). Regulates protein synthesis through phosphorylation of EIF4B, RPS6 and EEF2K, and contributes to cell survival by repressing the pro-apoptotic function of BAD (PubMed:11493700, PubMed:11500364). Under conditions of nutrient depletion, the inactive form associates with the EIF3 translation initiation complex (By similarity). Upon mitogenic stimulation, phosphorylation by the mechanistic target of rapamycin complex 1 (mTORC1) leads to dissociation from the EIF3 complex and activation (By similarity). 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 (By similarity). Also controls translation initiation by phosphorylating a negative regulator of EIF4A, PDCD4, targeting it for ubiquitination and subsequent proteolysis (By similarity). Promotes initiation of the pioneer round of protein synthesis by phosphorylating POLDIP3/SKAR (By similarity). 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 MAPKAP1/SIN1, MTOR and RICTOR, resulting in the inhibition of mTORC2 and AKT1 signaling (PubMed:24161930). Also involved in feedback regulation of mTORC1 and mTORC2 by phosphorylating DEPTOR (By similarity). Mediates cell survival by phosphorylating the pro-apoptotic protein BAD and suppressing its pro-apoptotic function (PubMed:11493700). Phosphorylates mitochondrial URI1 leading to dissociation of a URI1-PPP1CC complex (By similarity). 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 (By similarity). Mediates TNF-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 (By similarity). May be involved in cytoskeletal rearrangement through binding to neurabin (By similarity). Phosphorylates and activates the pyrimidine biosynthesis enzyme CAD, downstream of MTOR (By similarity). 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). {ECO:0000250|UniProtKB:P23443, ECO:0000250|UniProtKB:P67999, ECO:0000269|PubMed:11493700, ECO:0000269|PubMed:11500364, ECO:0000269|PubMed:15060135, ECO:0000269|PubMed:18952604, ECO:0000269|PubMed:24161930, ECO:0000269|PubMed:28178239}.
uniprot
proteins
mass_dalton
59146
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Thr-412 is regulated by mTORC1. The phosphorylation at this site is maintained by an agonist-dependent autophosphorylation mechanism. Activated by phosphorylation at Thr-252 by PDPK1. Dephosphorylation by PPP1CC at Thr-412 in mitochondrion (By similarity). {ECO:0000250}.
uniprot
proteins
protein_family
AGC Ser/Thr protein kinase family
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
S6 kinase subfamily
uniprot
proteins
pubmed
11493700
uniprot
proteins
pubmed
11500364
uniprot
proteins
pubmed
15060135
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
18952604
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
24161930
uniprot
proteins
pubmed
28178239
uniprot
proteins
sequence_length
525
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Synapse, synaptosome {ECO:0000250}. Mitochondrion outer membrane {ECO:0000269|PubMed:11493700}. Mitochondrion {ECO:0000250}. Note=Colocalizes with URI1 at mitochondrion. {ECO:0000250}.
uniprot
proteins