MAPKAPK3
entrez
7867
canonical
uniprot
Q16644
canonical
ensembl
ENSG00000114738
resolver
ensp
ENSP00000350639
resolver
ensp
ENSP00000396467
resolver
ensp
ENSP00000478922
resolver
ensp
ENSP00000534577
resolver
ensp
ENSP00000534578
resolver
ensp
ENSP00000534579
resolver
ensp
ENSP00000639111
resolver
ensp
ENSP00000639113
resolver
ensp
ENSP00000639114
resolver
ensp
ENSP00000639115
resolver
ensp
ENSP00000639116
resolver
ensp
ENSP00000639117
resolver
ensp
ENSP00000639118
resolver
enst
ENST00000357955
resolver
enst
ENST00000446044
resolver
enst
ENST00000621469
resolver
enst
ENST00000864518
resolver
enst
ENST00000864519
resolver
enst
ENST00000864520
resolver
enst
ENST00000969052
resolver
enst
ENST00000969054
resolver
enst
ENST00000969055
resolver
enst
ENST00000969056
resolver
enst
ENST00000969057
resolver
enst
ENST00000969058
resolver
enst
ENST00000969059
resolver
genesymbol
MAPKAPK3
resolver
hgnc
HGNC:6888
resolver
uniprot
B5BU67
resolver
uniprot_entry
MAPK3_HUMAN
resolver
uniprot_sec
B5BU67
resolver
activity_regulation
ACTIVITY REGULATION: Activated following phosphorylation by p38-alpha/MAPK14 following various stresses. Inhibited by ligand 5B (2'-[2-(1,3-benzodioxol-5-yl)pyrimidin-4-yl]-5',6'-dihydrospiro[piperidine-4,7'-pyrrolo[3,2-c]pyridin]- 4'(1'h)-one) and ligand P4O (2-[2-(2-fluorophenyl)pyridin-4-yl]-1,5,6,7-tetrahydro- 4h-pyrrolo[3,2-c]pyridin-4-one), 2 ATP-competitive inhibitors.
uniprot
proteins
amino_acid_sequence
MDGETAEEQGGPVPPPVAPGGPGLGGAPGGRREPKKYAVTDDYQLSKQVLGLGVNGKVLECFHRRTGQKCALKLLYDSPKARQEVDHHWQASGGPHIVCILDVYENMHHGKRCLLIIMECMEGGELFSRIQERGDQAFTEREAAEIMRDIGTAIQFLHSHNIAHRDVKPENLLYTSKEKDAVLKLTDFGFAKETTQNALQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYSNTGQAISPGMKRRIRLGQYGFPNPEWSEVSEDAKQLIRLLLKTDPTERLTITQFMNHPWINQSMVVPQTPLHTARVLQEDKDHWDEVKEEMTSALATMRVDYDQVKIKDLKTSNNRLLNKRRKKQAGSSSASQGCNNQ
uniprot
proteins
disease_involvement
DISEASE: Macular dystrophy, patterned, 3 (MDPT3) [MIM:617111]: A form of retinal patterned dystrophy, characterized by retinal pigment epithelium and Bruch's membrane changes resembling a 'dry desert land'. It begins around the age of 30 and progresses to retinitis pigmentosa. MDPT3 inheritance is autosomal dominant. {ECO:0000269|PubMed:26744326}. 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: Stress-activated serine/threonine-protein kinase involved in cytokines production, endocytosis, cell migration, chromatin remodeling 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. MAPKAPK2 and MAPKAPK3, share the same function and substrate specificity, but MAPKAPK3 kinase activity and level in protein expression are lower compared to MAPKAPK2. Phosphorylates HSP27/HSPB1, KRT18, KRT20, RCSD1, RPS6KA3, TAB3 and TTP/ZFP36. Mediates phosphorylation of HSP27/HSPB1 in response to stress, leading to dissociate HSP27/HSPB1 from large small heat-shock protein (sHsps) oligomers and impair 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, such as TTP/ZFP36, leading to regulate 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 transcript. Involved in toll-like receptor signaling pathway (TLR) in dendritic cells: required for acute TLR-induced macropinocytosis by phosphorylating and activating RPS6KA3. Also acts as a modulator of Polycomb-mediated repression. {ECO:0000269|PubMed:10383393, ECO:0000269|PubMed:15563468, ECO:0000269|PubMed:18021073, ECO:0000269|PubMed:20599781, ECO:0000269|PubMed:8626550, ECO:0000269|PubMed:8774846}.
uniprot
proteins
mass_dalton
42987
uniprot
proteins
mutagenesis
MUTAGEN 73; /note="K->M: Higher affinity toward PCH2."; /evidence="ECO:0000269|PubMed:15563468
uniprot
proteins
post_translational_modification
PTM: Phosphorylated and activated by MAPK1/ERK2 and MAPK3/ERK1. Phosphorylated and activated by MAP kinase p38-alpha/MAPK14 at Thr-201, Ser-251 and Thr-313 (By similarity). {ECO:0000250}.
uniprot
proteins
protein_family
CAMK Ser/Thr protein kinase family
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
pubmed
10383393
uniprot
proteins
pubmed
10781029
uniprot
proteins
pubmed
15302577
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15563468
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
18021073
uniprot
proteins
pubmed
18508601
uniprot
proteins
pubmed
19054851
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19937655
uniprot
proteins
pubmed
20599781
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21565500
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
26744326
uniprot
proteins
pubmed
8622688
uniprot
proteins
pubmed
8626550
uniprot
proteins
pubmed
8774846
uniprot
proteins
sequence_length
382
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15302577, ECO:0000269|PubMed:26744326}. Cytoplasm {ECO:0000269|PubMed:15302577, ECO:0000269|PubMed:26744326}. Note=Predominantly located in the nucleus, when activated it translocates to the cytoplasm.
uniprot
proteins