EKS-HOS-00239
Eukaryotic Protein Kinase & Protein Phosphatase Database
TagContent
EKPD IDEKS-HOS-00239
Classification
Group/FamilyScoreE-ValueStartEndDomain Length
CAMK/MAPKAPK433.71.2E-12964325262
StatusReviewed
Ensembl ProteinENSP00000294981
UniProt AccessionP49137; Q5SY30; Q5SY41; Q8IYD6;
Protein NameMAP kinase-activated protein kinase 2
Protein Synonyms/Alias MAPK-activated protein kinase 2; MAPKAP kinase 2; MAPKAP-K2; MAPKAPK-2; MK-2; MK2;
Gene NameMAPKAPK2
Gene Synonyms/Alias MAPKAPK2;
Ensembl Information
Ensembl Gene IDEnsembl Protein IDEnsembl Transcript ID
ENSG00000162889ENSP00000356070ENST00000367103
ENSG00000162889ENSP00000294981ENST00000294981
OrganismHomo sapiens
Functional DescriptionStress-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 Length370
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
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
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
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
Keyword3D-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 SourceEnsembl
Orthology
Ortholog group
Ailuropoda melanoleuca"; ?>Anolis carolinensis"; ?>Callithrix jacchus"; ?>Canis familiaris"; ?>Ciona savignyi"; ?>Danio rerio"; ?>Drosophila melanogaster"; ?>Equus caballus"; ?>Felis catus"; ?>Gadus morhua"; ?>Gallus gallus"; ?>Gasterosteus aculeatus"; ?>Gorilla gorilla"; ?>Ictidomys tridecemlineatus"; ?>Latimeria chalumnae"; ?>Loxodonta africana"; ?>Macaca mulatta"; ?>Meleagris gallopavo"; ?>Microcebus murinus"; ?>Monodelphis domestica"; ?>Mus musculus"; ?>Mustela putorius furo"; ?>Myotis lucifugus"; ?>Nomascus leucogenys"; ?>Ochotona princeps"; ?>Oreochromis niloticus"; ?>Ornithorhynchus anatinus"; ?>Oryctolagus cuniculus"; ?>Oryzias latipes"; ?>Otolemur garnettii"; ?>Pan troglodytes"; ?>Pelodiscus sinensis"; ?>Petromyzon marinus"; ?>Pongo abelii"; ?>Procavia capensis"; ?>Rattus norvegicus"; ?>Sarcophilus harrisii"; ?>Sus scrofa"; ?>Takifugu rubripes"; ?>Xenopus tropicalis"; ?>Xiphophorus maculatus"; ?>
EKS-AIM-00214
EKS-ANC-00225
EKS-CAJ-00241
EKS-CAF-00242
EKS-CIS-00014
EKS-DAR-00545
EKS-DRM-00119
EKS-EQC-00227
EKS-FEC-00222
EKS-GAM-00136
EKS-GAG-00195
EKS-GAA-00284
EKS-GOG-00233
EKS-ICT-00223
EKS-LAC-00247
EKS-LOA-00232
EKS-MAM-00234
EKS-MEG-00180
EKS-MIM-00006
EKS-MOD-00236
EKS-MUM-00237
EKS-MUP-00235
EKS-MYL-00235
EKS-NOL-00216
EKS-OCP-00011
EKS-ORN-00300
EKS-ORA-00204
EKS-ORC-00211
EKS-ORL-00281
EKS-OTG-00238
EKS-PAT-00222
EKS-PES-00210
EKS-PEM-00122
EKS-POA-00225
EKS-PRC-00011
EKS-RAN-00234
EKS-SAH-00219
EKS-SUS-00202
EKS-TAR-00296
EKS-XET-00307
EKS-XIM-00292
Gene Ontology
GO:0005829; C:cytosol
GO:0005654; C:nucleoplasm
GO:0005524; F:ATP binding
GO:0004674; F:protein serine/threonine kinase activity
GO:0004871; F:signal transducer activity
GO:0070935; P:3'-UTR-mediated mRNA stabilization
GO:0000187; P:activation of MAPK activity
GO:0035924; P:cellular response to vascular endothelial growth factor stimulus
GO:0031572; P:G2/M transition DNA damage checkpoint
GO:0010467; P:gene expression
GO:0006954; P:inflammatory response
GO:0045087; P:innate immune response
GO:0048839; P:inner ear development
GO:0044351; P:macropinocytosis
GO:0016071; P:mRNA metabolic process
GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway
GO:0048011; P:nerve growth factor receptor signaling pathway
GO:0018105; P:peptidyl-serine phosphorylation
GO:0007265; P:Ras protein signal transduction
GO:0032675; P:regulation of interleukin-6 production
GO:0032680; P:regulation of tumor necrosis factor production
GO:0032496; P:response to lipopolysaccharide
GO:0051403; P:stress-activated MAPK cascade
GO:0008063; P:Toll signaling pathway
GO:0034130; P:toll-like receptor 1 signaling pathway
GO:0034134; P:toll-like receptor 2 signaling pathway
GO:0034138; P:toll-like receptor 3 signaling pathway
GO:0034142; P:toll-like receptor 4 signaling pathway
GO:0035666; P:TRIF-dependent toll-like receptor signaling pathway
GO:0048010; P:vascular endothelial growth factor receptor signaling pathway
KEGG
hsa:9261;
InterPros
IPR011009; Kinase-like_dom.
IPR000719; Prot_kinase_cat_dom.
IPR017441; Protein_kinase_ATP_BS.
IPR002290; Ser/Thr_dual-sp_kinase_dom.
IPR008271; Ser/Thr_kinase_AS.
Pfam
PF00069; Pkinase; 1.
SMARTs
SM00220; S_TKc; 1.
Prosites
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
Prints
Created Date20-Feb-2013