Rps6ka3
entrez
110651
canonical
uniprot
P18654
canonical
ensembl
ENSMUSG00000031309
resolver
ensp
ENSMUSP00000033671
resolver
ensp
ENSMUSP00000108112
resolver
enst
ENSMUST00000033671
resolver
enst
ENSMUST00000112493
resolver
genesymbol
Rps6ka3
resolver
genesymbol_syn
Mapkapk1b
resolver
genesymbol_syn
Rps6ka-rs1
resolver
genesymbol_syn
Rsk2
resolver
uniprot
B1AXN4
resolver
uniprot
B1AXN9
resolver
uniprot
Q03140
resolver
uniprot
Q8K3J8
resolver
uniprot_entry
B1AXN9_MOUSE
resolver
uniprot_entry
KS6A3_MOUSE
resolver
uniprot_sec
B1AXN4
resolver
uniprot_sec
Q03140
resolver
uniprot_sec
Q8K3J8
resolver
activity_regulation
ACTIVITY REGULATION: Upon extracellular signal or mitogen stimulation, phosphorylated at Thr-577 in the C-terminal kinase domain (CTKD) by MAPK1/ERK2 and MAPK3/ERK1. The activated CTKD then autophosphorylates Ser-386, allowing binding of PDPK1, which in turn phosphorylates Ser-227 in the N-terminal kinase domain (NTDK) leading to the full activation of the protein and subsequent phosphorylation of the substrates by the NTKD (By similarity). {ECO:0000250}.
uniprot
proteins
amino_acid_sequence
MPLAQLADPWQKMAVESPSDSAENGQQIMDEPMGEEEINPQTEEGSIKEIAITHHVKEGHEKADPSQFELLKVLGQGSFGKVFLVKKISGSDARQLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLFKRNPANRLGAGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKPATGRPEDTFYFDPEFTAKTPKDSPGIPPSANAHQLFRGFSFVAITSDDESQAMQTVGVHSIVQQLHRNSIQFTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPESIRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTPEEILARIGSGKFSLSGGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWIVHWDQLPQYQLNRQDAPHLVKGAMAATYSALNRNQSPVLEPVGRSTLAQRRGIKKITSTAL
uniprot
proteins
ec_number
2.7.11.1
uniprot
proteins
function
FUNCTION: 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 (PubMed:10856237, PubMed:15109498). 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 (By similarity). In response to mitogenic stimulation (EGF and PMA), phosphorylates and activates NR4A1/NUR77 and ETV1/ER81 transcription factors and the cofactor CREBBP (By similarity). Upon insulin-derived signal, acts indirectly on the transcription regulation of several genes by phosphorylating GSK3B at 'Ser-9' and inhibiting its activity (By similarity). Phosphorylates RPS6 in response to serum or EGF via an mTOR-independent mechanism and promotes translation initiation by facilitating assembly of the preinitiation complex (By similarity). In response to insulin, phosphorylates EIF4B, enhancing EIF4B affinity for the EIF3 complex and stimulating cap-dependent translation (By similarity). 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 (By similarity). Mediates cell survival by phosphorylating the pro-apoptotic proteins BAD and DAPK1 and suppressing their pro-apoptotic function (By similarity). Promotes the survival of hepatic stellate cells by phosphorylating CEBPB in response to the hepatotoxin carbon tetrachloride (CCl4) (By similarity). 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 (PubMed:14504289). 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 (PubMed:17785202, PubMed:17906627). Negatively regulates EGF-induced MAPK1/3 phosphorylation via phosphorylation of SOS1 (PubMed:22827337). Phosphorylates SOS1 at 'Ser-1134' and 'Ser-1161' that create YWHAB and YWHAE binding sites and which contribute to the negative regulation of MAPK1/3 phosphorylation (PubMed:22827337). Phosphorylates EPHA2 at 'Ser-897', the RPS6KA-EPHA2 signaling pathway controls cell migration (By similarity). Acts as a regulator of osteoblast differentiation by mediating phosphorylation of ATF4, thereby promoting ATF4 transactivation activity (PubMed:15109498). {ECO:0000250|UniProtKB:P51812, ECO:0000269|PubMed:10856237, ECO:0000269|PubMed:14504289, ECO:0000269|PubMed:15109498, ECO:0000269|PubMed:17785202, ECO:0000269|PubMed:17906627, ECO:0000269|PubMed:22827337}.
uniprot
proteins
mass_dalton
83694
uniprot
proteins
mutagenesis
MUTAGEN 227; /note="S->E: Loss of phosphorylation and activation by PDPK1."; /evidence="ECO:0000269|PubMed:10480933"; MUTAGEN 386; /note="S->A: Loss of phosphorylation by PDPK1; loss of activation by PDPK1 and EGF."; /evidence="ECO:0000269|PubMed:10480933, ECO:0000269|PubMed:10856237"; MUTAGEN 386; /note="S->E: Loss of interaction with PDPK1 and phosphorylation at S-227."; /evidence="ECO:0000269|PubMed:10480933, ECO:0000269|PubMed:10856237"; MUTAGEN 529; /note="Y->F: Attenuates activation by MAPK1/ERK1 and MAPK3/ERK2."; /evidence="ECO:0000269|PubMed:17785202
uniprot
proteins
post_translational_modification
PTM: Activated by phosphorylation at Ser-227 by PDPK1. Autophosphorylated on Ser-386, as part of the activation process. May be phosphorylated at Thr-365 and Ser-369 by MAPK1/ERK2 and MAPK3/ERK1. Can also be activated via phosphorylation at Ser-386 by MAPKAPK2. {ECO:0000269|PubMed:10480933, ECO:0000269|PubMed:17785202, ECO:0000269|PubMed:17906627}.; PTM: N-terminal myristoylation results in an activated kinase in the absence of added growth factors. {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
10480933
uniprot
proteins
pubmed
10856237
uniprot
proteins
pubmed
12016217
uniprot
proteins
pubmed
14504289
uniprot
proteins
pubmed
15109498
uniprot
proteins
pubmed
17785202
uniprot
proteins
pubmed
17906627
uniprot
proteins
pubmed
18084304
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
19956600
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
22827337
uniprot
proteins
pubmed
2779569
uniprot
proteins
sequence_length
740
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P51812}. Cytoplasm {ECO:0000250|UniProtKB:P51812}.
uniprot
proteins