Tag | Content |
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EKPD ID | EKS-HOS-00240 |
Classification | Group/Family | Score | E-Value | Start | End | Domain Length |
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CAMK/MAPKAPK | 427.9 | 6.7E-128 | 44 | 304 | 261 |
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Status | Reviewed |
Ensembl Protein | ENSP00000410970 |
UniProt Accession | Q16644; B5BU67; |
Protein Name | MAP kinase-activated protein kinase 3 |
Protein Synonyms/Alias | MAPK-activated protein kinase 3; MAPKAP kinase 3; MAPKAP-K3; MAPKAPK-3; MK-3; Chromosome 3p kinase; 3pK; |
Gene Name | MAPKAPK3 |
Gene Synonyms/Alias | MAPKAPK3; |
Ensembl Information | |
Organism | Homo sapiens |
Functional Description | Stress-activated serine/threonine-protein kinaseinvolved 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. |
Protein Length | 332 |
Protein Sequence (FASTA) | MDGETAEEQG GPVPPPVAPG GPGLGGAPGG RREPKKYAVT DDYQLSKQVL GLGVNGKVLE 60 | CFHRRTGQKC ALKLLYDSPK ARQEVDHHWQ ASGGPHIVCI LDVYENMHHG KRCLLIIMEC 120 | MEGGELFSRI QERGDQAFTE REAAEIMRDI GTAIQFLHSH NIAHRDVKPE NLLYTSKEKD 180 | AVLKLTDFGF AKETTQNALQ TPCYTPYYVA PEVLGPEKYD KSCDMWSLGV IMYILLCGFP 240 | PFYSNTGQAI SPGMKRRIRL GQYGFPNPEW SEVSEDAKQL IRLLLKTDPT ERLTITQFMN 300 | HPWINQSMVV PQTPLHTARV LQEDKDHWDE VK 332 |
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Nucleotide Sequence (FASTA) | ATGGATGGTG AAACAGCAGA GGAGCAGGGG GGCCCTGTGC CCCCGCCAGT TGCACCCGGC 60 | GGACCCGGCT TGGGCGGTGC TCCGGGGGGG CGGCGGGAGC CCAAGAAGTA CGCAGTGACC 120 | GACGACTACC AGTTGTCCAA GCAGGTGCTG GGCCTGGGTG TGAACGGCAA AGTGCTGGAG 180 | TGCTTCCATC GGCGCACTGG ACAGAAGTGT GCCCTGAAGC TCCTGTATGA CAGCCCCAAG 240 | GCCCGGCAGG AGGTAGACCA TCACTGGCAG GCTTCTGGCG GCCCCCATAT TGTCTGCATC 300 | CTGGATGTGT ATGAGAACAT GCACCATGGC AAGCGCTGTC TCCTCATCAT CATGGAATGC 360 | ATGGAAGGTG GTGAGTTGTT CAGCAGGATT CAGGAGCGTG GCGACCAGGC TTTCACTGAG 420 | AGAGAAGCTG CAGAGATAAT GCGGGATATT GGCACTGCCA TCCAGTTTCT GCACAGCCAT 480 | AACATTGCCC ACCGAGATGT CAAGCCTGAA AACCTACTCT ACACATCTAA GGAGAAAGAC 540 | GCAGTGCTTA AGCTCACCGA TTTTGGCTTT GCTAAGGAGA CCACCCAAAA TGCCCTGCAG 600 | ACACCCTGCT ATACTCCCTA TTATGTGGCC CCTGAGGTCC TGGGTCCAGA GAAGTATGAC 660 | AAGTCATGTG ACATGTGGTC CCTGGGTGTC ATCATGTACA TCCTCCTTTG TGGCTTCCCA 720 | CCCTTCTACT CCAACACGGG CCAGGCCATC TCCCCGGGGA TGAAGAGGAG GATTCGCCTG 780 | GGCCAGTACG GCTTCCCCAA TCCTGAGTGG TCAGAAGTCT CTGAGGATGC CAAGCAGCTG 840 | ATCCGCCTCC TGTTGAAGAC AGACCCCACA GAGAGGCTGA CCATCACTCA GTTCATGAAC 900 | CACCCCTGGA TCAACCAATC GATGGTAGTG CCACAGACCC CACTCCACAC GGCCCGAGTG 960 | CTGCAGGAGG ACAAAGACCA CTGGGACGAA GTCAAGG 997 |
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Domain Profile | S: 1 klteevlGeGisgkvlecvkkktgekyalkilkdrkkvrrevelhvqasghknivelidv 60 | +l+++vlG G++gkvlec++++tg+k+alk+l+d++k+r+ev++h+qasg ++iv ++dv | Q: 44 QLSKQVLGLGVNGKVLECFHRRTGQKCALKLLYDSPKARQEVDHHWQASGGPHIVCILDV 103 | 5789******************************************************** |
| S: 61 fensfedekrlllvlekleGGellsriqer..kaftekeasevvkdiasalkflhsknia 118 | +en+++++++ll+++e++eGGel+sriqer +afte+ea+e+++di++a++flhs+nia | Q: 104 YENMHHGKRCLLIIMECMEGGELFSRIQERgdQAFTEREAAEIMRDIGTAIQFLHSHNIA 163 | *******************************9**************************** |
| S: 119 hrDlkpenlLyeskeknapvklcDfglaketeeeeelktpcltaeyvaPevleaekeeal 178 | hrD+kpenlLy+skek+a++kl+Dfg+ake +++++l+tpc+t++yvaPevl++ek | Q: 164 HRDVKPENLLYTSKEKDAVLKLTDFGFAKE-TTQNALQTPCYTPYYVAPEVLGPEK---- 218 | *****************************7.7899*********************.... |
| S: 179 lydksCDlWslGvilyillcGypPfyskkgraiskklkeriqegkyefPeeeWsevseea 238 | ydksCD+WslGvi+yillcG+pPfys++g+ais+++k+ri+ g+y fP++eWsevse+a | Q: 219 -YDKSCDMWSLGVIMYILLCGFPPFYSNTGQAISPGMKRRIRLGQYGFPNPEWSEVSEDA 277 | .*********************************************************** |
| S: 239 kdlirklLkrdpkerltieevlnhpwv 265 | k+lir lLk+dp+erlti++++nhpw+ | Q: 278 KQLIRLLLKTDPTERLTITQFMNHPWI 304 | **************************8 |
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Domain Sequence (FASTA) | QLSKQVLGLG VNGKVLECFH RRTGQKCALK LLYDSPKARQ EVDHHWQASG GPHIVCILDV 60 | YENMHHGKRC LLIIMECMEG GELFSRIQER GDQAFTEREA AEIMRDIGTA IQFLHSHNIA 120 | HRDVKPENLL YTSKEKDAVL KLTDFGFAKE TTQNALQTPC YTPYYVAPEV LGPEKYDKSC 180 | DMWSLGVIMY ILLCGFPPFY SNTGQAISPG MKRRIRLGQY GFPNPEWSEV SEDAKQLIRL 240 | LLKTDPTERL TITQFMNHPW I 261 |
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Keyword | 3D-structure; Acetylation; ATP-binding; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Serine/threonine-protein kinase; Transferase. |
Sequence Source | Ensembl |
Orthology | |
Gene Ontology | |
KEGG | |
InterPros | |
Pfam | |
SMARTs | |
Prosites | |
Prints | |
Created Date | 20-Feb-2013 |