RPS6KA3
entrez
6197
canonical
uniprot
P51812
canonical
ensembl
ENSG00000177189
resolver
ensp
ENSP00000368884
resolver
ensp
ENSP00000407655
resolver
ensp
ENSP00000493487
resolver
ensp
ENSP00000493862
resolver
ensp
ENSP00000494220
resolver
ensp
ENSP00000494769
resolver
ensp
ENSP00000494967
resolver
ensp
ENSP00000495462
resolver
ensp
ENSP00000495776
resolver
ensp
ENSP00000495974
resolver
ensp
ENSP00000496271
resolver
ensp
ENSP00000622762
resolver
ensp
ENSP00000663144
resolver
enst
ENST00000379565
resolver
enst
ENST00000457145
resolver
enst
ENST00000642835
resolver
enst
ENST00000643085
resolver
enst
ENST00000643337
resolver
enst
ENST00000643402
resolver
enst
ENST00000644368
resolver
enst
ENST00000644893
resolver
enst
ENST00000645270
resolver
enst
ENST00000646610
resolver
enst
ENST00000647265
resolver
genesymbol
RPS6KA3
resolver
genesymbol_syn
ISPK1
resolver
genesymbol_syn
MAPKAPK1B
resolver
genesymbol_syn
RSK2
resolver
hgnc
HGNC:10432
resolver
uniprot
A0A2R8Y5G4
resolver
uniprot
A0A2R8YGF5
resolver
uniprot
A0A384MDW3
resolver
uniprot
B1AXG1
resolver
uniprot
B2R9V4
resolver
uniprot
B4DG22
resolver
uniprot
B7ZB17
resolver
uniprot
Q4VAP3
resolver
uniprot
Q59H26
resolver
uniprot
Q5JPK8
resolver
uniprot
Q7Z3Z7
resolver
uniprot_entry
A0A2R8Y5G4_HUMAN
resolver
uniprot_entry
A0A2R8YGF5_HUMAN
resolver
uniprot_entry
A0A384MDW3_HUMAN
resolver
uniprot_entry
B1AXG1_HUMAN
resolver
uniprot_entry
B4DG22_HUMAN
resolver
uniprot_entry
B7ZB17_HUMAN
resolver
uniprot_entry
KS6A3_HUMAN
resolver
uniprot_sec
B2R9V4
resolver
uniprot_sec
Q4VAP3
resolver
uniprot_sec
Q59H26
resolver
uniprot_sec
Q5JPK8
resolver
uniprot_sec
Q7Z3Z7
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.
uniprot
proteins
amino_acid_sequence
MPLAQLADPWQKMAVESPSDSAENGQQIMDEPMGEEEINPQTEEVSIKEIAITHHVKEGHEKADPSQFELLKVLGQGSFGKVFLVKKISGSDARQLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLFKRNPANRLGAGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKPATGRPEDTFYFDPEFTAKTPKDSPGIPPSANAHQLFRGFSFVAITSDDESQAMQTVGVHSIVQQLHRNSIQFTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPESIRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTPEEILARIGSGKFSLSGGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWIVHWDQLPQYQLNRQDAPHLVKGAMAATYSALNRNQSPVLEPVGRSTLAQRRGIKKITSTAL
uniprot
proteins
disease_involvement
DISEASE: Coffin-Lowry syndrome (CLS) [MIM:303600]: An X-linked disorder characterized by intellectual disability associated with facial and digital dysmorphisms, progressive skeletal malformations, growth retardation, hearing deficit and paroxysmal movement disorders. {ECO:0000269|PubMed:10094187, ECO:0000269|PubMed:10528858, ECO:0000269|PubMed:14986828, ECO:0000269|PubMed:15214012, ECO:0000269|PubMed:8955270, ECO:0000269|PubMed:9837815}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Intellectual developmental disorder, X-linked 19 (XLID19) [MIM:300844]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. {ECO:0000269|PubMed:10319851, ECO:0000269|PubMed:17100996}. Note=The disease is caused by variants affecting the gene represented in this entry.
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:16213824, PubMed:16223362, PubMed:17360704, PubMed:9770464). 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 (PubMed:10436156, PubMed:9770464). In response to mitogenic stimulation (EGF and PMA), phosphorylates and activates NR4A1/NUR77 and ETV1/ER81 transcription factors and the cofactor CREBBP (PubMed:16223362). Upon insulin-derived signal, acts indirectly on the transcription regulation of several genes by phosphorylating GSK3B at 'Ser-9' and inhibiting its activity (PubMed:8250835). Phosphorylates RPS6 in response to serum or EGF via an mTOR-independent mechanism and promotes translation initiation by facilitating assembly of the preinitiation complex (PubMed:17360704). In response to insulin, phosphorylates EIF4B, enhancing EIF4B affinity for the EIF3 complex and stimulating cap-dependent translation (PubMed:18508509, PubMed:18813292). 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 (PubMed:18722121). Mediates cell survival by phosphorylating the pro-apoptotic proteins BAD and DAPK1 and suppressing their pro-apoptotic function (PubMed:16213824). Promotes the survival of hepatic stellate cells by phosphorylating CEBPB in response to the hepatotoxin carbon tetrachloride (CCl4) (PubMed:18508509, PubMed:18813292). 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 (By similarity). 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 (By similarity). Negatively regulates EGF-induced MAPK1/3 phosphorylation via phosphorylation of SOS1 (By similarity). 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 (By similarity). Phosphorylates EPHA2 at 'Ser-897', the RPS6KA-EPHA2 signaling pathway controls cell migration (PubMed:26158630). Acts as a regulator of osteoblast differentiation by mediating phosphorylation of ATF4, thereby promoting ATF4 transactivation activity (By similarity). {ECO:0000250|UniProtKB:P18654, ECO:0000269|PubMed:10436156, ECO:0000269|PubMed:16213824, ECO:0000269|PubMed:16223362, ECO:0000269|PubMed:17360704, ECO:0000269|PubMed:18722121, ECO:0000269|PubMed:26158630, ECO:0000269|PubMed:8250835, ECO:0000269|PubMed:9770464, ECO:0000303|PubMed:18508509, ECO:0000303|PubMed:18813292}.
uniprot
proteins
mass_dalton
83736
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.; PTM: N-terminal myristoylation results in an activated kinase in the absence of added growth factors.
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
10094187
uniprot
proteins
pubmed
10319851
uniprot
proteins
pubmed
10436156
uniprot
proteins
pubmed
10528858
uniprot
proteins
pubmed
12777533
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14986828
uniprot
proteins
pubmed
15214012
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15772651
uniprot
proteins
pubmed
16213824
uniprot
proteins
pubmed
16223362
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17100996
uniprot
proteins
pubmed
17213202
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
17360704
uniprot
proteins
pubmed
18508509
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
18722121
uniprot
proteins
pubmed
18813292
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
26158630
uniprot
proteins
pubmed
7813820
uniprot
proteins
pubmed
8141249
uniprot
proteins
pubmed
8250835
uniprot
proteins
pubmed
8955270
uniprot
proteins
pubmed
9770464
uniprot
proteins
pubmed
9837815
uniprot
proteins
sequence_length
740
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17213202}. Cytoplasm {ECO:0000269|PubMed:17213202}.
uniprot
proteins