Mapkapk2
entrez
17164
canonical
uniprot
P49138
canonical
ensembl
ENSMUSG00000016528
resolver
ensp
ENSMUSP00000016672
resolver
enst
ENSMUST00000016672
resolver
genesymbol
Mapkapk2
resolver
genesymbol_syn
Rps6kc1
resolver
uniprot
Q3U2P8
resolver
uniprot
Q6P561
resolver
uniprot_entry
MAPK2_MOUSE
resolver
uniprot_entry
Q3U2P8_MOUSE
resolver
uniprot_sec
Q6P561
resolver
activity_regulation
ACTIVITY REGULATION: Activated following phosphorylation by p38-alpha/MAPK14 following various stresses. Inhibited following sumoylation. Specifically inhibited by pyrrolopyridine inhibitors (By similarity). {ECO:0000250}.
uniprot
proteins
amino_acid_sequence
MLSGSPGQTPPAPFPSPPPPAPAQPPPPFPQFHVKSGLQIRKNAITDDYKVTSQVLGLGINGKVLRIFDKRTQQKFALKMLQDCPKARREVELHWRASQCPHIVHIVDVYENLYAGRKCLLIVMECLDGGELFSRIQDRGDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILKLTDFGFAKETTSHNSLTTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAISPGMKTRIRMGQYEFPNPEWSEVSEEVKMLIRNLLKTEPTQRMTITEFMNHPWIMQSTKVPQTPLHTSRVLKEDKERWEDVKEEMTSALATMRVDYEQIKIKKIEDASNPLLLKRRKKARAVEDAALAH
uniprot
proteins
ec_number
2.7.11.1
uniprot
proteins
function
FUNCTION: Stress-activated serine/threonine-protein kinase involved in cytokine production, endocytosis, reorganization of the cytoskeleton, cell migration, cell cycle control, chromatin remodeling, DNA damage response and transcriptional regulation. Following stress, it is phosphorylated and activated by MAP kinase p38-alpha/MAPK14, leading to phosphorylation of substrates. Phosphorylates serine in the peptide sequence, Hyd-X-R-X(2)-S, where Hyd is a large hydrophobic residue. Phosphorylates ALOX5, CDC25B, CDC25C, CEP131, ELAVL1, HNRNPA0, HSP27/HSPB1, KRT18, KRT20, LIMK1, LSP1, PABPC1, PARN, PDE4A, RCSD1, RPS6KA3, TAB3 and TTP/ZFP36. Phosphorylates HSF1; leading to the interaction with HSP90 proteins and inhibiting HSF1 homotrimerization, DNA-binding and transactivation activities (By similarity). Mediates phosphorylation of HSP27/HSPB1 in response to stress, leading to dissociation of HSP27/HSPB1 from large small heat-shock protein (sHsps) oligomers and impairment of their chaperone activities and ability to protect against oxidative stress effectively. Involved in inflammatory response by regulating tumor necrosis factor (TNF) and IL6 production post-transcriptionally: acts by phosphorylating AU-rich elements (AREs)-binding proteins ELAVL1, HNRNPA0, PABPC1 and TTP/ZFP36, leading to regulation of the stability and translation of TNF and IL6 mRNAs. Phosphorylation of TTP/ZFP36, a major post-transcriptional regulator of TNF, promotes its binding to 14-3-3 proteins and reduces its ARE mRNA affinity leading to inhibition of dependent degradation of ARE-containing transcripts. Phosphorylates CEP131 in response to cellular stress following ultraviolet irradiation which promotes binding of CEP131 to 14-3-3 proteins and inhibits formation of novel centriolar satellites (By similarity). Also involved in late G2/M checkpoint following DNA damage through a process of post-transcriptional mRNA stabilization: following DNA damage, relocalizes from nucleus to cytoplasm and phosphorylates HNRNPA0 and PARN, leading to stabilization of GADD45A mRNA. Involved in toll-like receptor signaling pathway (TLR) in dendritic cells: required for acute TLR-induced macropinocytosis by phosphorylating and activating RPS6KA3. {ECO:0000250|UniProtKB:P49137, ECO:0000269|PubMed:10559880, ECO:0000269|PubMed:12456657, ECO:0000269|PubMed:14688255, ECO:0000269|PubMed:15850461, ECO:0000269|PubMed:17906627, ECO:0000269|PubMed:20724476, ECO:0000269|PubMed:21323643, ECO:0000269|PubMed:8093612}.
uniprot
proteins
mass_dalton
44050
uniprot
proteins
mutagenesis
MUTAGEN 208; /note="T->A: Strong decrease in kinase activity; when associated with A-320."; /evidence="ECO:0000269|PubMed:7592979"; MUTAGEN 208; /note="T->E: Mimicks phosphorylation state and constitutive protein kinase activity; when associated with E-320."; /evidence="ECO:0000269|PubMed:7592979"; MUTAGEN 320; /note="T->A: Strong decrease in kinase activity; when associated with A-208."; /evidence="ECO:0000269|PubMed:7592979"; MUTAGEN 320; /note="T->E: Mimicks phosphorylation state and constitutive protein kinase activity; when associated with E-208."; /evidence="ECO:0000269|PubMed:7592979"; MUTAGEN 329; /note="K->R: Leads to constitutive protein kinase activity."; /evidence="ECO:0000269|PubMed:7592979"; MUTAGEN 335; /note="W->A: Leads to constitutive protein kinase activity."; /evidence="ECO:0000269|PubMed:7592979
uniprot
proteins
post_translational_modification
PTM: Sumoylation inhibits the protein kinase activity. {ECO:0000250}.; PTM: Phosphorylated and activated by MAP kinase p38-alpha/MAPK14 at Thr-208; Ser-258 and Thr-320. {ECO:0000269|PubMed:7592979, ECO:0000269|PubMed:9628873}.
uniprot
proteins
protein_family
CAMK Ser/Thr protein kinase family
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
pubmed
10559880
uniprot
proteins
pubmed
12052889
uniprot
proteins
pubmed
12456657
uniprot
proteins
pubmed
14688255
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15850461
uniprot
proteins
pubmed
17030606
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
17906627
uniprot
proteins
pubmed
20724476
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21323643
uniprot
proteins
pubmed
7592979
uniprot
proteins
pubmed
8093612
uniprot
proteins
pubmed
8262198
uniprot
proteins
pubmed
9628873
uniprot
proteins
sequence_length
386
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Phosphorylation and subsequent activation releases the autoinhibitory helix, resulting in the export from the nucleus into the cytoplasm.
uniprot
proteins