EKS-MUM-00239
Eukaryotic Protein Kinase & Protein Phosphatase Database
TagContent
EKPD IDEKS-MUM-00239
Classification
Group/FamilyScoreE-ValueStartEndDomain Length
CAMK/MAPKAPK417.84.0E-12523304282
StatusReviewed
Ensembl ProteinENSMUSP00000119182
UniProt AccessionO54992; E9QQ45; Q6QME4; Q6QME5; Q6QME6; Q6QME7;
Protein NameMAP kinase-activated protein kinase 5
Protein Synonyms/Alias MAPK-activated protein kinase 5; MAPKAP kinase 5; MAPKAPK-5;
Gene NameMapkapk5
Gene Synonyms/Alias Mapkapk5;
Ensembl Information
Ensembl Gene IDEnsembl Protein IDEnsembl Transcript ID
ENSMUSG00000029454ENSMUSP00000119182ENSMUST00000153763
ENSMUSG00000029454ENSMUSP00000107411ENSMUST00000111781
ENSMUSG00000029454ENSMUSP00000116464ENSMUST00000152270
ENSMUSG00000029454ENSMUSP00000107413ENSMUST00000111783
ENSMUSG00000029454ENSMUSP00000107412ENSMUST00000111782
ENSMUSG00000029454ENSMUSP00000107416ENSMUST00000111786
ENSMUSG00000029454ENSMUSP00000031410ENSMUST00000031410
OrganismMus musculus
Functional DescriptionTumor suppressor serine/threonine-protein kinaseinvolved in mTORC1 signaling and post-transcriptional regulation. Phosphorylates FOXO3, ERK3/MAPK6, ERK4/MAPK4, HSP27/HSPB1, p53/TP53 and RHEB. Acts as a tumor suppressor by mediating Ras- induced senescence and phosphorylating p53/TP53. Involved in post- transcriptional regulation of MYC by mediating phosphorylation of FOXO3: phosphorylation of FOXO3 leads to promote nuclear localization of FOXO3, enabling expression of miR-34b and miR-34c, 2 post-transcriptional regulators of MYC that bind to the 3'UTR of MYC transcript and prevent MYC translation. Acts as a negative regulator of mTORC1 signaling by mediating phosphorylation and inhibition of RHEB. Part of the atypical MAPK signaling via its interaction with ERK3/MAPK6 or ERK4/MAPK4: the precise role of the complex formed with ERK3/MAPK6 or ERK4/MAPK4 is still unclear, but the complex follows a complex set of phosphorylation events: upon interaction with atypical MAPK (ERK3/MAPK6 or ERK4/MAPK4), ERK3/MAPK6 (or ERK4/MAPK4) is phosphorylated and then mediates phosphorylation and activation of MAPKAPK5, which in turn phosphorylates ERK3/MAPK6 (or ERK4/MAPK4). Mediates phosphorylation of HSP27/HSPB1 in response to PKA/PRKACA stimulation, inducing F-actin rearrangement.
Protein Length369
Protein Sequence
(FASTA)
MSEDSDMEKA IKETSILEEY SINWTQKLGA GISGPVRVCV KKSTQERFAL KILLDRPKAR 60
NEVRLHMMCA THPNIVQIIE VFANSVQFPH ESSPRARLLI VMEMMEGGEL FHRISQHRHF 120
TEKQASQVTK QIALALQHCH LLNIAHRDLK PENLLFKDNS LDAPVKLCDF GFAKVDQGDL 180
MTPQFTPYYV APQVLEAQRR HQKEKSGIIP TSPTPYTYNK SCDLWSLGVI IYVMLCGYPP 240
FYSKHHSRTI PKDMRKKIMT GSFEFPEEEW SQISEMAKDV VRKLLKVKPE ERLTIEGVLD 300
HPWLNSTEAL DNVLPSAQLM MDKAVVAGIQ QAHAEQLANM RIQDLKVSLK PLHSVNNPIL 360
RKRKLLGRE 369
Nucleotide Sequence
(FASTA)
ATGTCGGAGG ACAGCGACAT GGAGAAAGCC ATCAAGGAGA CCTCCATTTT AGAAGAATAT 60
AGTATCAATT GGACTCAGAA ACTGGGAGCC GGAATTAGTG GTCCAGTTAG AGTCTGTGTG 120
AAGAAATCCA CTCAAGAACG GTTTGCACTG AAAATTCTTC TTGATCGTCC AAAAGCTAGA 180
AATGAGGTGC GCCTGCACAT GATGTGTGCC ACACACCCCA ACATAGTTCA GATTATTGAA 240
GTGTTTGCTA ACAGTGTACA GTTCCCTCAT GAGTCCAGCC CCAGGGCTCG ACTCTTAATT 300
GTAATGGAGA TGATGGAAGG GGGAGAGCTA TTTCACAGAA TCAGCCAGCA CCGGCACTTT 360
ACAGAGAAGC AAGCCAGCCA AGTAACAAAG CAGATAGCCC TGGCTCTACA GCACTGTCAC 420
TTGCTAAACA TTGCGCACAG AGACCTCAAG CCTGAAAATC TGCTTTTCAA GGATAACTCT 480
CTGGACGCCC CTGTGAAATT ATGTGACTTT GGGTTTGCTA AAGTTGACCA AGGTGATTTG 540
ATGACACCCC AGTTTACCCC TTACTATGTA GCACCTCAGG TACTGGAAGC GCAGAGACGG 600
CACCAGAAGG AGAAGTCTGG CATCATACCT ACCTCGCCAA CACCCTACAC TTACAACAAG 660
AGCTGTGACT TGTGGTCCCT AGGGGTGATA ATTTATGTGA TGCTGTGCGG ATATCCTCCT 720
TTTTACTCCA AACACCATAG TCGGACTATC CCAAAGGATA TGCGGAAAAA GATCATGACA 780
GGAAGTTTCG AGTTCCCAGA AGAAGAGTGG AGCCAGATCT CAGAGATGGC TAAAGATGTT 840
GTGAGGAAGC TTCTGAAGGT CAAACCAGAG GAAAGACTCA CAATCGAGGG AGTGTTGGAC 900
CATCCCTGGC TCAACTCGAC AGAGGCCCTG GATAATGTGC TACCCTCTGC CCAGCTGATG 960
ATGGATAAGG CGGTGGTTGC GGGGATCCAG CAGGCGCACG CCGAGCAGCT GGCAAACATG 1020
AGGATCCAGG ACCTCAAGGT CAGCCTCAAA CCCCTGCACT CTGTCAACAA CCCCATTCTC 1080
AGGAAGAGGA AGCTGCTGGG GAGAGAATGA 1110
Domain Profile
S: 2     lteevlGeGisgkvlecvkkktgekyalkilkdrkkvrrevelhvqasghknivelidvf  61
         +++++lG+Gisg v+ cvkk+t+e++alkil dr+k+r+ev+lh+++++h+niv++i+vf
Q: 23    NWTQKLGAGISGPVRVCVKKSTQERFALKILLDRPKARNEVRLHMMCATHPNIVQIIEVF  82
         689*********************************************************
S: 62    ensfe......dekrlllvlekleGGellsriqerkaftekeasevvkdiasalkflhsk  115
         +ns++      +++rll+v+e++eGGel++ri+++++ftek+as+v+k+ia al+++h  
Q: 83    ANSVQfphessPRARLLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQIALALQHCHLL  142
         ****99999999************************************************
S: 116   niahrDlkpenlLyeskeknapvklcDfglaketeeeeelktpcltaeyvaPevleaeke  175
         niahrDlkpenlL+++++ +apvklcDfg+ak   ++ +l+tp++t++yvaP+vlea+++
Q: 143   NIAHRDLKPENLLFKDNSLDAPVKLCDFGFAK--VDQGDLMTPQFTPYYVAPQVLEAQRR  200
         ********************************..89***********************9
S: 176   e.............allydksCDlWslGvilyillcGypPfyskk.graiskklkeriqe  221
         +             +++y+ksCDlWslGvi+y++lcGypPfysk+ +r+i+k+++++i++
Q: 201   HqkeksgiiptsptPYTYNKSCDLWSLGVIIYVMLCGYPPFYSKHhSRTIPKDMRKKIMT  260
         99*****************************************9979*************
S: 222   gkyefPeeeWsevseeakdlirklLkrdpkerltieevlnhpwv  265
         g++efPeeeWs++se+akd++rklLk++p+erltie vl+hpw+
Q: 261   GSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL  304
         *******************************************6
Domain Sequence
(FASTA)
NWTQKLGAGI SGPVRVCVKK STQERFALKI LLDRPKARNE VRLHMMCATH PNIVQIIEVF 60
ANSVQFPHES SPRARLLIVM EMMEGGELFH RISQHRHFTE KQASQVTKQI ALALQHCHLL 120
NIAHRDLKPE NLLFKDNSLD APVKLCDFGF AKVDQGDLMT PQFTPYYVAP QVLEAQRRHQ 180
KEKSGIIPTS PTPYTYNKSC DLWSLGVIIY VMLCGYPPFY SKHHSRTIPK DMRKKIMTGS 240
FEFPEEEWSQ ISEMAKDVVR KLLKVKPEER LTIEGVLDHP WL 282
KeywordAlternative splicing; ATP-binding; Coiled coil; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Serine/threonine-protein kinase; Transferase; Tumor suppressor.
Sequence SourceEnsembl
Orthology
Ortholog group
Ailuropoda melanoleuca"; ?>Anolis carolinensis"; ?>Bos taurus"; ?>Callithrix jacchus"; ?>Canis familiaris"; ?>Cavia porcellus"; ?>Ciona intestinalis"; ?>Ciona savignyi"; ?>Danio rerio"; ?>Echinops telfairi"; ?>Equus caballus"; ?>Felis catus"; ?>Gadus morhua"; ?>Gallus gallus"; ?>Gasterosteus aculeatus"; ?>Gorilla gorilla"; ?>Homo sapiens"; ?>Ictidomys tridecemlineatus"; ?>Latimeria chalumnae"; ?>Loxodonta africana"; ?>Macaca mulatta"; ?>Meleagris gallopavo"; ?>Monodelphis domestica"; ?>Mustela putorius furo"; ?>Myotis lucifugus"; ?>Nomascus leucogenys"; ?>Oreochromis niloticus"; ?>Ornithorhynchus anatinus"; ?>Oryctolagus cuniculus"; ?>Oryzias latipes"; ?>Otolemur garnettii"; ?>Pan troglodytes"; ?>Pelodiscus sinensis"; ?>Petromyzon marinus"; ?>Pongo abelii"; ?>Rattus norvegicus"; ?>Sarcophilus harrisii"; ?>Sus scrofa"; ?>Taeniopygia guttata"; ?>Takifugu rubripes"; ?>Tarsius syrichta"; ?>Tetraodon nigroviridis"; ?>Tursiops truncatus"; ?>Vicugna pacos"; ?>Xenopus tropicalis"; ?>Xiphophorus maculatus"; ?>
EKS-AIM-00216
EKS-ANC-00223
EKS-BOT-00233
EKS-CAJ-00239
EKS-CAF-00240
EKS-CAP-00259
EKS-CII-00139
EKS-CIS-00015
EKS-DAR-00547
EKS-ECT-00007
EKS-EQC-00225
EKS-FEC-00219
EKS-GAM-00141
EKS-GAG-00196
EKS-GAA-00290
EKS-GOG-00231
EKS-HOS-00241
EKS-ICT-00221
EKS-LAC-00245
EKS-LOA-00230
EKS-MAM-00236
EKS-MEG-00181
EKS-MOD-00233
EKS-MUP-00232
EKS-MYL-00232
EKS-NOL-00218
EKS-ORN-00302
EKS-ORA-00208
EKS-ORC-00209
EKS-ORL-00280
EKS-OTG-00240
EKS-PAT-00224
EKS-PES-00212
EKS-PEM-00125
EKS-POA-00227
EKS-RAN-00231
EKS-SAH-00221
EKS-SUS-00204
EKS-TAG-00249
EKS-TAR-00299
EKS-TAS-00007
EKS-TEN-00293
EKS-TUT-00013
EKS-VIP-00005
EKS-XET-00310
EKS-XIM-00294
Gene Ontology
GO:0005737; C:cytoplasm
GO:0005634; C:nucleus
GO:0005524; F:ATP binding
GO:0002039; F:p53 binding
GO:0004674; F:protein serine/threonine kinase activity
GO:0032007; P:negative regulation of TOR signaling cascade
GO:0046777; P:protein autophosphorylation
GO:0007265; P:Ras protein signal transduction
GO:0006417; P:regulation of translation
GO:0090400; P:stress-induced premature senescence
KEGG
mmu:17165;
InterPros
IPR011009; Kinase-like_dom.
IPR000719; Prot_kinase_cat_dom.
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; FALSE_NEG.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
Prints
Created Date20-Feb-2013