Tag | Content |
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EKPD ID | EKS-HOS-00239 |
Classification | Group/Family | Score | E-Value | Start | End | Domain Length |
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CAMK/MAPKAPK | 433.7 | 1.2E-129 | 64 | 325 | 262 |
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Status | Reviewed |
Ensembl Protein | ENSP00000294981 |
UniProt Accession | P49137; Q5SY30; Q5SY41; Q8IYD6; |
Protein Name | MAP kinase-activated protein kinase 2 |
Protein Synonyms/Alias | MAPK-activated protein kinase 2; MAPKAP kinase 2; MAPKAP-K2; MAPKAPK-2; MK-2; MK2; |
Gene Name | MAPKAPK2 |
Gene Synonyms/Alias | MAPKAPK2; |
Ensembl Information | |
Organism | Homo sapiens |
Functional Description | Stress-activated serine/threonine-protein kinaseinvolved in cytokines 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, ELAVL1, HNRNPA0, HSF1, HSP27/HSPB1, KRT18, KRT20, LIMK1, LSP1, PABPC1, PARN, PDE4A, 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 ELAVL1, HNRNPA0, PABPC1 and 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. 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 stabilize GADD45A mRNA. Involved in toll-like receptor signaling pathway (TLR) in dendritic cells: required for acute TLR-induced macropinocytosis by phosphorylating and activating RPS6KA3. |
Protein Length | 370 |
Protein Sequence (FASTA) | MLSNSQGQSP PVPFPAPAPP PQPPTPALPH PPAQPPPPPP QQFPQFHVKS GLQIKKNAII 60 | DDYKVTSQVL GLGINGKVLQ IFNKRTQEKF ALKMLQDCPK ARREVELHWR ASQCPHIVRI 120 | VDVYENLYAG RKCLLIVMEC LDGGELFSRI QDRGDQAFTE REASEIMKSI GEAIQYLHSI 180 | NIAHRDVKPE NLLYTSKRPN AILKLTDFGF AKETTSHNSL TTPCYTPYYV APEVLGPEKY 240 | DKSCDMWSLG VIMYILLCGY PPFYSNHGLA ISPGMKTRIR MGQYEFPNPE WSEVSEEVKM 300 | LIRNLLKTEP TQRMTITEFM NHPWIMQSTK VPQTPLHTSR VLKEDKERWE DVKGCLHDKN 360 | SDQATWLTRL 370 |
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Nucleotide Sequence (FASTA) | ATGCTGTCCA ACTCCCAGGG CCAGAGCCCG CCGGTGCCGT TCCCCGCCCC GGCCCCGCCG 60 | CCGCAGCCCC CCACCCCTGC CCTGCCGCAC CCCCCGGCGC AGCCGCCGCC GCCGCCCCCG 120 | CAGCAGTTCC CGCAGTTCCA CGTCAAGTCC GGCCTGCAGA TCAAGAAGAA CGCCATCATC 180 | GATGACTACA AGGTCACCAG CCAGGTCCTG GGGCTGGGCA TCAACGGCAA AGTTTTGCAG 240 | ATCTTCAACA AGAGGACCCA GGAGAAATTC GCCCTCAAAA TGCTTCAGGA CTGCCCCAAG 300 | GCCCGCAGGG AGGTGGAGCT GCACTGGCGG GCCTCCCAGT GCCCGCACAT CGTACGGATC 360 | GTGGATGTGT ACGAGAATCT GTACGCAGGG AGGAAGTGCC TGCTGATTGT CATGGAATGT 420 | TTGGACGGTG GAGAACTCTT TAGCCGAATC CAGGATCGAG GAGACCAGGC ATTCACAGAA 480 | AGAGAAGCAT CCGAAATCAT GAAGAGCATC GGTGAGGCCA TCCAGTATCT GCATTCAATC 540 | AACATTGCCC ATCGGGATGT CAAGCCTGAG AATCTCTTAT ACACCTCCAA AAGGCCCAAC 600 | GCCATCCTGA AACTCACTGA CTTTGGCTTT GCCAAGGAAA CCACCAGCCA CAACTCTTTG 660 | ACCACTCCTT GTTATACACC GTACTATGTG GCTCCAGAAG TGCTGGGTCC AGAGAAGTAT 720 | GACAAGTCCT GTGACATGTG GTCCCTGGGT GTCATCATGT ACATCCTGCT GTGTGGGTAT 780 | CCCCCCTTCT ACTCCAACCA CGGCCTTGCC ATCTCTCCGG GCATGAAGAC TCGCATCCGA 840 | ATGGGCCAGT ATGAATTTCC CAACCCAGAA TGGTCAGAAG TATCAGAGGA AGTGAAGATG 900 | CTCATTCGGA ATCTGCTGAA AACAGAGCCC ACCCAGAGAA TGACCATCAC CGAGTTTATG 960 | AACCACCCTT GGATCATGCA ATCAACAAAG GTCCCTCAAA CCCCACTGCA CACCAGCCGG 1020 | GTCCTGAAGG AGGACAAGGA GCGGTGGGAG GATGTCAAGG GGTGTCTTCA TGACAAGAAC 1080 | AGCGACCAGG CCACTTGGCT GACCAGGTTG TGA 1113 |
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Domain Profile | S: 1 klteevlGeGisgkvlecvkkktgekyalkilkdrkkvrrevelhvqasghknivelidv 60 | k+t++vlG Gi+gkvl++++k+t+ek+alk+l+d++k+rrevelh++as++++iv+++dv | Q: 64 KVTSQVLGLGINGKVLQIFNKRTQEKFALKMLQDCPKARREVELHWRASQCPHIVRIVDV 123 | 5799******************************************************** |
| S: 61 fensfedekrlllvlekleGGellsriqer..kaftekeasevvkdiasalkflhsknia 118 | +en ++++k+ll+v+e+l+GGel+sriq+r +afte+ease++k+i++a+++lhs nia | Q: 124 YENLYAGRKCLLIVMECLDGGELFSRIQDRgdQAFTEREASEIMKSIGEAIQYLHSINIA 183 | *******************************9**************************** |
| S: 119 hrDlkpenlLyeskeknapvklcDfglaketeeeeelktpcltaeyvaPevleaekeeal 178 | hrD+kpenlLy+sk+ na++kl+Dfg+aket+++++l+tpc+t++yvaPevl++ek | Q: 184 HRDVKPENLLYTSKRPNAILKLTDFGFAKETTSHNSLTTPCYTPYYVAPEVLGPEK---- 239 | ********************************************************.... |
| S: 179 lydksCDlWslGvilyillcGypPfyskkgraiskklkeriqegkyefPeeeWsevseea 238 | ydksCD+WslGvi+yillcGypPfys++g ais+++k+ri++g+yefP++eWsevsee+ | Q: 240 -YDKSCDMWSLGVIMYILLCGYPPFYSNHGLAISPGMKTRIRMGQYEFPNPEWSEVSEEV 298 | .*********************************************************** |
| S: 239 kdlirklLkrdpkerltieevlnhpwv 265 | k+lir+lLk++p++r+ti+e++nhpw+ | Q: 299 KMLIRNLLKTEPTQRMTITEFMNHPWI 325 | **************************8 |
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Domain Sequence (FASTA) | KVTSQVLGLG INGKVLQIFN KRTQEKFALK MLQDCPKARR EVELHWRASQ CPHIVRIVDV 60 | YENLYAGRKC LLIVMECLDG GELFSRIQDR GDQAFTEREA SEIMKSIGEA IQYLHSINIA 120 | HRDVKPENLL YTSKRPNAIL KLTDFGFAKE TTSHNSLTTP CYTPYYVAPE VLGPEKYDKS 180 | CDMWSLGVIM YILLCGYPPF YSNHGLAISP GMKTRIRMGQ YEFPNPEWSE VSEEVKMLIR 240 | NLLKTEPTQR MTITEFMNHP WI 262 |
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Keyword | 3D-structure; Alternative splicing; ATP-binding; Complete proteome; Cytoplasm; DNA damage; Isopeptide bond; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Serine/threonine-protein kinase; Transferase; Ubl conjugation. |
Sequence Source | Ensembl |
Orthology | |
Gene Ontology | |
KEGG | |
InterPros | |
Pfam | |
SMARTs | |
Prosites | |
Prints | |
Created Date | 20-Feb-2013 |