RPS6KA5
entrez
9252
canonical
uniprot
O75582
canonical
ensembl
ENSG00000100784
resolver
ensp
ENSP00000402787
resolver
ensp
ENSP00000442803
resolver
ensp
ENSP00000479667
resolver
ensp
ENSP00000556694
resolver
ensp
ENSP00000556695
resolver
ensp
ENSP00000556697
resolver
ensp
ENSP00000616989
resolver
ensp
ENSP00000616990
resolver
genesymbol
RPS6KA5
resolver
genesymbol_syn
MSK1
resolver
hgnc
HGNC:10434
resolver
uniprot
B7Z2Y5
resolver
uniprot
O95316
resolver
uniprot
Q96AF7
resolver
uniprot_entry
KS6A5_HUMAN
resolver
uniprot_sec
B7Z2Y5
resolver
uniprot_sec
O95316
resolver
uniprot_sec
Q96AF7
resolver
activity_regulation
ACTIVITY REGULATION: Activated by phosphorylation at Ser-360, Thr-581 and Thr-700 by MAPK1/ERK2, MAPK3/ERK1 and MAPK14/p38-alpha, and by further autophosphorylation of Ser-212, Ser-376 and Ser-381 by the activated C-terminal kinase domain. The active N-terminal kinase domain finally phosphorylates downstream substrates, as well as Ser-750, Ser-752 and Ser-758 in its own C-terminal region. {ECO:0000269|PubMed:15568999, ECO:0000269|PubMed:9687510}.
uniprot
proteins
amino_acid_sequence
MEEEGGSSGGAAGTSADGGDGGEQLLTVKHELRTANLTGHAEKVGIENFELLKVLGTGAYGKVFLVRKISGHDTGKLYAMKVLKKATIVQKAKTTEHTRTERQVLEHIRQSPFLVTLHYAFQTETKLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADETERAYSFCGTIEYMAPDIVRGGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSALAKDLIQRLLMKDPKKRLGCGPRDADEIKEHLFFQKINWDDLAAKKVPAPFKPVIRDELDVSNFAEEFTEMDPTYSPAALPQSSEKLFQGYSFVAPSILFKRNAAVIDPLQFHMGVERPGVTNVARSAMMKDSPFYQHYDLDLKDKPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQKEITALKLCEGHPNIVKLHEVFHDQLHTFLVMELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDENDNLEIKIIDFGFARLKPPDNQPLKTPCFTLHYAAPELLNQNGYDESCDLWSLGVILYTMLSGQVPFQSHDRSLTCTSAVEIMKKIKKGDFSFEGEAWKNVSQEAKDLIQGLLTVDPNKRLKMSGLRYNEWLQDGSQLSSNPLMTPDILGSSGAAVHTCVKATFHAFNKYKREGFCLQNVDKAPLAKRRKMKKTSTSTETRSSSSESSHSSSSHSHGKTTPTKTLQPSNPADSNNPETLFQFSDSVA
uniprot
proteins
ec_number
2.7.11.1
uniprot
proteins
function
FUNCTION: Serine/threonine-protein kinase that is required for the mitogen or stress-induced phosphorylation of the transcription factors CREB1 and ATF1 and for the regulation of the transcription factors RELA, STAT3 and ETV1/ER81, and that contributes to gene activation by histone phosphorylation and functions in the regulation of inflammatory genes (PubMed:11909979, PubMed:12569367, PubMed:12763138, PubMed:18511904, PubMed:9687510, PubMed:9873047). Phosphorylates CREB1 and ATF1 in response to mitogenic or stress stimuli such as UV-C irradiation, epidermal growth factor (EGF) and anisomycin (PubMed:11909979, PubMed:9873047). Plays an essential role in the control of RELA transcriptional activity in response to TNF and upon glucocorticoid, associates in the cytoplasm with the glucocorticoid receptor NR3C1 and contributes to RELA inhibition and repression of inflammatory gene expression (PubMed:12628924, PubMed:18511904). In skeletal myoblasts is required for phosphorylation of RELA at 'Ser-276' during oxidative stress (PubMed:12628924). In erythropoietin-stimulated cells, is necessary for the 'Ser-727' phosphorylation of STAT3 and regulation of its transcriptional potential (PubMed:12763138). Phosphorylates ETV1/ER81 at 'Ser-191' and 'Ser-216', and thereby regulates its ability to stimulate transcription, which may be important during development and breast tumor formation (PubMed:12569367). Directly represses transcription via phosphorylation of 'Ser-1' of histone H2A (PubMed:15010469). Phosphorylates 'Ser-10' of histone H3 in response to mitogenics, stress stimuli and EGF, which results in the transcriptional activation of several immediate early genes, including proto-oncogenes c-fos/FOS and c-jun/JUN (PubMed:12773393). May also phosphorylate 'Ser-28' of histone H3 (PubMed:12773393). Mediates the mitogen- and stress-induced phosphorylation of high mobility group protein 1 (HMGN1/HMG14) (PubMed:12773393). In lipopolysaccharide-stimulated primary macrophages, acts downstream of the Toll-like receptor TLR4 to limit the production of pro-inflammatory cytokines (By similarity). Functions probably by inducing transcription of the MAP kinase phosphatase DUSP1 and the anti-inflammatory cytokine interleukin 10 (IL10), via CREB1 and ATF1 transcription factors (By similarity). Plays a role in neuronal cell death by mediating the downstream effects of excitotoxic injury (By similarity). Phosphorylates TRIM7 at 'Ser-107' in response to growth factor signaling via the MEK/ERK pathway, thereby stimulating its ubiquitin ligase activity (PubMed:25851810). {ECO:0000250|UniProtKB:Q8C050, ECO:0000269|PubMed:11909979, ECO:0000269|PubMed:12569367, ECO:0000269|PubMed:12628924, ECO:0000269|PubMed:12763138, ECO:0000269|PubMed:12773393, ECO:0000269|PubMed:15010469, ECO:0000269|PubMed:18511904, ECO:0000269|PubMed:25851810, ECO:0000269|PubMed:9687510, ECO:0000269|PubMed:9873047}.
uniprot
proteins
mass_dalton
89865
uniprot
proteins
mutagenesis
MUTAGEN 195; /note="D->A: Loss of kinase activity."; /evidence="ECO:0000269|PubMed:9687510"; MUTAGEN 212; /note="S->A: Inactivates the N-terminal kinase domain."; /evidence="ECO:0000269|PubMed:15568999"; MUTAGEN 360; /note="S->A: Decreases kinase activity by 60% in response to PMA and UV-C."; /evidence="ECO:0000269|PubMed:15568999"; MUTAGEN 376; /note="S->A: Loss of kinase activity, and decreases the phosphorylation of S-360 and T-581."; /evidence="ECO:0000269|PubMed:15568999"; MUTAGEN 565; /note="D->A: Loss of kinase activity."; /evidence="ECO:0000269|PubMed:9687510"; MUTAGEN 581; /note="T->A: Loss of kinase activity, and blocks phosphorylation of S-212; S-376 and S-381 in response to PMA and UV-C."; /evidence="ECO:0000269|PubMed:15568999"; MUTAGEN 700; /note="T->A,D: Strongly reduces phosphorylation of T-581 in response to PMA and UV-C."; /evidence="ECO:0000269|PubMed:17117922
uniprot
proteins
post_translational_modification
PTM: Ser-376 and Thr-581 phosphorylation is required for kinase activity. Ser-376 and Ser-212 are autophosphorylated by the C-terminal kinase domain, and their phosphorylation is essential for the catalytic activity of the N-terminal kinase domain. Phosphorylated at Ser-360, Thr-581 and Thr-700 by MAPK1/ERK2, MAPK3/ERK1 and MAPK14/p38-alpha. Autophosphorylated at Ser-750, Ser-752 and Ser-758 by the N-terminal kinase domain. {ECO:0000269|PubMed:15568999, ECO:0000269|PubMed:17117922}.; PTM: Ubiquitinated. {ECO:0000269|PubMed:20596523}.
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
10702687
uniprot
proteins
pubmed
11909979
uniprot
proteins
pubmed
12508121
uniprot
proteins
pubmed
12569367
uniprot
proteins
pubmed
12628924
uniprot
proteins
pubmed
12763138
uniprot
proteins
pubmed
12773393
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15010469
uniprot
proteins
pubmed
15274926
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15568999
uniprot
proteins
pubmed
17117922
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
18508628
uniprot
proteins
pubmed
18511904
uniprot
proteins
pubmed
19464896
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20382163
uniprot
proteins
pubmed
20596523
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
25851810
uniprot
proteins
pubmed
9687510
uniprot
proteins
pubmed
9873047
uniprot
proteins
sequence_length
802
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Predominantly nuclear. Exported into cytoplasm in response to glucocorticoid.
uniprot
proteins