EKS-HOS-00472
Eukaryotic Protein Kinase & Protein Phosphatase Database
TagContent
EKPD IDEKS-HOS-00472
Classification
Group/FamilyScoreE-ValueStartEndDomain Length
CMGC/MAPK420.41.6E-12526321296
StatusReviewed
Ensembl ProteinENSP00000345524
UniProt AccessionP45984; A8K0S3; B5BU66; B5M0B4; D3DWQ8; D3DWQ9; Q15708; Q15710; Q15711; Q8N5C5;
Protein NameMitogen-activated protein kinase 9
Protein Synonyms/Alias MAP kinase 9; MAPK 9; JNK-55; Stress-activated protein kinase 1a; SAPK1a; Stress-activated protein kinase JNK2; c-Jun N-terminal kinase 2;
Gene NameMAPK9
Gene Synonyms/Alias MAPK9; JNK2, PRKM9, SAPK1A;
Ensembl Information
Ensembl Gene IDEnsembl Protein IDEnsembl Transcript ID
ENSG00000050748ENSP00000389338ENST00000455781
ENSG00000050748ENSP00000377028ENST00000393360
ENSG00000050748ENSP00000380262ENST00000397072
ENSG00000050748ENSP00000430608ENST00000523583
ENSG00000050748ENSP00000377029ENST00000393362
ENSG00000050748ENSP00000321410ENST00000347470
ENSG00000050748ENSP00000443149ENST00000539014
ENSG00000050748ENSP00000397422ENST00000425491
ENSG00000050748ENSP00000394560ENST00000452135
ENSG00000050748ENSP00000345524ENST00000343111
OrganismHomo sapiens
Functional DescriptionSerine/threonine-protein kinase involved in variousprocesses such as cell proliferation, differentiation, migration, transformation and programmed cell death. Extracellular stimuli such as proinflammatory cytokines or physical stress stimulate the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. In this cascade, two dual specificity kinases MAP2K4/MKK4 and MAP2K7/MKK7 phosphorylate and activate MAPK9/JNK2. In turn, MAPK9/JNK2 phosphorylates a number of transcription factors, primarily components of AP-1 such as JUN and ATF2 and thus regulates AP-1 transcriptional activity. In response to oxidative or ribotoxic stresses, inhibits rRNA synthesis by phosphorylating and inactivating the RNA polymerase 1-specific transcription initiation factor RRN3. Promotes stressed cell apoptosis by phosphorylating key regulatory factors including TP53 and YAP1. In T-cells, MAPK8 and MAPK9 are required for polarized differentiation of T-helper cells into Th1 cells. Upon T-cell receptor (TCR) stimulation, is activated by CARMA1, BCL10, MAP2K7 and MAP3K7/TAK1 to regulate JUN protein levels. Plays an important role in the osmotic stress-induced epithelial tight-junctions disruption. When activated, promotes beta-catenin/CTNNB1 degradation and inhibits the canonical Wnt signaling pathway. Participates also in neurite growth in spiral ganglion neurons. MAPK9 isoforms display different binding patterns:alpha-1 and alpha-2 preferentially bind to JUN, whereas beta-1 and beta-2 bind to ATF2. However, there is no correlation between binding and phosphorylation, which is achieved at about the same efficiency by all isoforms. JUNB is not a substrate for JNK2 alpha-2, and JUND binds only weakly to it.
Protein Length382
Protein Sequence
(FASTA)
MSDSKCDSQF YSVQVADSTF TVLKRYQQLK PIGSGAQGIV CAAFDTVLGI NVAVKKLSRP 60
FQNQTHAKRA YRELVLLKCV NHKNIISLLN VFTPQKTLEE FQDVYLVMEL MDANLCQVIH 120
MELDHERMSY LLYQMLCGIK HLHSAGIIHR DLKPSNIVVK SDCTLKILDF GLARTACTNF 180
MMTPYVVTRY YRAPEVILGM GYKENVDIWS VGCIMAEMVL HKVLFPGRDY IDQWNKVIEQ 240
LGTPSAEFMK KLQPTVRNYV ENRPKYPGIK FEELFPDWIF PSESERDKIK TSQARDLLSK 300
MLVIDPDKRI SVDEALRHPY ITVWYDPAEA EAPPPQIYDA QLEEREHAIE EWKELIYKEV 360
MDWEERSKNG VVKDQPSAQM QQ 382
Nucleotide Sequence
(FASTA)
ATGAGCGACA GTAAATGTGA CAGTCAGTTT TATAGTGTGC AAGTGGCAGA CTCAACCTTC 60
ACTGTCCTAA AACGTTACCA GCAGCTGAAA CCAATTGGCT CTGGGGCCCA AGGGATTGTT 120
TGTGCTGCAT TTGATACAGT TCTTGGGATA AATGTTGCAG TCAAGAAACT AAGCCGTCCT 180
TTTCAGAACC AAACTCATGC AAAGAGAGCT TATCGTGAAC TTGTCCTCTT AAAATGTGTC 240
AATCATAAAA ATATAATTAG TTTGTTAAAT GTGTTTACAC CACAAAAAAC TCTAGAAGAA 300
TTTCAAGATG TGTATTTGGT TATGGAATTA ATGGATGCTA ACTTATGTCA GGTTATTCAC 360
ATGGAGCTGG ATCATGAAAG AATGTCCTAC CTTCTTTACC AGATGCTTTG TGGTATTAAA 420
CATCTGCATT CAGCTGGTAT AATTCATAGA GATTTGAAGC CTAGCAACAT TGTTGTGAAA 480
TCAGACTGCA CCCTGAAGAT CCTTGACTTT GGCCTGGCCC GGACAGCGTG CACTAACTTC 540
ATGATGACCC CTTACGTGGT GACACGGTAC TACCGGGCGC CCGAAGTCAT CCTGGGTATG 600
GGCTACAAAG AGAACGTGGA CATCTGGTCT GTCGGGTGCA TCATGGCAGA AATGGTCCTC 660
CATAAAGTCC TGTTCCCGGG AAGAGACTAT ATTGATCAGT GGAATAAAGT TATTGAGCAG 720
CTGGGAACAC CATCAGCAGA GTTCATGAAG AAACTTCAGC CAACTGTGAG GAATTATGTC 780
GAAAACAGAC CAAAGTATCC TGGAATCAAA TTTGAAGAAC TCTTTCCAGA TTGGATATTC 840
CCATCAGAAT CTGAGCGAGA CAAAATAAAA ACAAGTCAAG CCAGAGATCT GTTATCAAAA 900
ATGTTAGTGA TTGATCCTGA CAAGCGGATC TCTGTAGACG AAGCTCTGCG TCACCCATAC 960
ATCACTGTTT GGTATGACCC CGCCGAAGCA GAAGCCCCAC CACCTCAAAT TTATGATGCC 1020
CAGTTGGAAG AAAGAGAACA TGCAATTGAA GAATGGAAAG AGCTAATTTA CAAAGAAGTC 1080
ATGGATTGGG AAGAAAGAAG CAAGAATGGT GTTGTAAAAG ATCAGCCTTC AGCACAGATG 1140
CAGCAGTAA 1149
Domain Profile
S: 1     yeslkplgeGaygvvvsavdkrteervaikklsrpfqketsakrtlRElkllkelkheNi  60
         y++lkp+g+Ga+g+v++a+d+  + +va+kklsrpfq++t+akr++REl llk+++h+Ni
Q: 26    YQQLKPIGSGAQGIVCAAFDTVLGINVAVKKLSRPFQNQTHAKRAYRELVLLKCVNHKNI  85
         899*********************************************************
S: 61    iklldvftpeeeleelkdvYlvtelmetdLkkviksqklsdehiklllyqilrglkylHs  120
         i+ll+vftp+++lee++dvYlv+elm+++L++vi+++ l++e++++llyq+l+g+k+lHs
Q: 86    ISLLNVFTPQKTLEEFQDVYLVMELMDANLCQVIHME-LDHERMSYLLYQMLCGIKHLHS  144
         ************************************9.**********************
S: 121   anviHrDlKPsNllvnedcelkildFGlarsadkekekklteyvatrwYraPeillslke  180
         a++iHrDlKPsN++v++dc+lkildFGlar+a ++ +  +t+yv+tr+YraPe++l  + 
Q: 145   AGIIHRDLKPSNIVVKSDCTLKILDFGLARTACTNFM--MTPYVVTRYYRAPEVILG-MG  201
         ********************************99976..*****************9.99
S: 181   ytkavDiWsvGCIlaElltgkplfpgkdeidqlekilevlgtpseeflkkieseearnyi  240
         y+++vDiWsvGCI+aE++ +k+lfpg+d+idq++k++e+lgtps+ef+kk++  ++rny+
Q: 202   YKENVDIWSVGCIMAEMVLHKVLFPGRDYIDQWNKVIEQLGTPSAEFMKKLQP-TVRNYV  260
         *****************************************************.5*****
S: 241   kslpkkkkkdfeelfpk............aseealdLleklLvldpdkRisveeaLehpY  288
         +++pk++  +feelfp+            ++++a+dLl+k+Lv+dpdkRisv+eaL+hpY
Q: 261   ENRPKYPGIKFEELFPDwifpseserdkiKTSQARDLLSKMLVIDPDKRISVDEALRHPY  320
         *****************************9******************************
S: 289   l  289
         +
Q: 321   I  321
         7
Domain Sequence
(FASTA)
YQQLKPIGSG AQGIVCAAFD TVLGINVAVK KLSRPFQNQT HAKRAYRELV LLKCVNHKNI 60
ISLLNVFTPQ KTLEEFQDVY LVMELMDANL CQVIHMELDH ERMSYLLYQM LCGIKHLHSA 120
GIIHRDLKPS NIVVKSDCTL KILDFGLART ACTNFMMTPY VVTRYYRAPE VILGMGYKEN 180
VDIWSVGCIM AEMVLHKVLF PGRDYIDQWN KVIEQLGTPS AEFMKKLQPT VRNYVENRPK 240
YPGIKFEELF PDWIFPSESE RDKIKTSQAR DLLSKMLVID PDKRISVDEA LRHPYI 296
Keyword3D-structure; Alternative splicing; ATP-binding; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Serine/threonine-protein kinase; Transferase.
Sequence SourceEnsembl
Orthology
Ortholog group
Ailuropoda melanoleuca"; ?>Anolis carolinensis"; ?>Callithrix jacchus"; ?>Canis familiaris"; ?>Cavia porcellus"; ?>Equus caballus"; ?>Felis catus"; ?>Gadus morhua"; ?>Gallus gallus"; ?>Gorilla gorilla"; ?>Latimeria chalumnae"; ?>Loxodonta africana"; ?>Meleagris gallopavo"; ?>Monodelphis domestica"; ?>Mus musculus"; ?>Myotis lucifugus"; ?>Nomascus leucogenys"; ?>Ochotona princeps"; ?>Ornithorhynchus anatinus"; ?>Oryctolagus cuniculus"; ?>Oryzias latipes"; ?>Otolemur garnettii"; ?>Pan troglodytes"; ?>Pelodiscus sinensis"; ?>Pongo abelii"; ?>Rattus norvegicus"; ?>Sarcophilus harrisii"; ?>Sus scrofa"; ?>Taeniopygia guttata"; ?>
EKS-AIM-00434
EKS-ANC-00451
EKS-CAJ-00468
EKS-CAF-00464
EKS-CAP-00496
EKS-EQC-00452
EKS-FEC-00442
EKS-GAM-00272
EKS-GAG-00387
EKS-GOG-00452
EKS-LAC-00475
EKS-LOA-00468
EKS-MEG-00379
EKS-MOD-00456
EKS-MUM-00496
EKS-MYL-00454
EKS-NOL-00420
EKS-OCP-00121
EKS-ORA-00402
EKS-ORC-00437
EKS-ORL-00534
EKS-OTG-00471
EKS-PAT-00436
EKS-PES-00407
EKS-POA-00452
EKS-RAN-00478
EKS-SAH-00432
EKS-SUS-00408
EKS-TAG-00526
Gene Ontology
GO:0005829; C:cytosol
GO:0005739; C:mitochondrion
GO:0005654; C:nucleoplasm
GO:0005524; F:ATP binding
GO:0004705; F:JUN kinase activity
GO:0008134; F:transcription factor binding
GO:0045087; P:innate immune response
GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway
GO:0010628; P:positive regulation of gene expression
GO:0010744; P:positive regulation of macrophage derived foam cell differentiation
GO:0051090; P:regulation of sequence-specific DNA binding transcription factor activity
GO:0046686; P:response to cadmium ion
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
KEGG
hsa:5601;
InterPros
IPR011009; Kinase-like_dom.
IPR003527; MAP_kinase_CS.
IPR008351; MAPK_JNK.
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
PS01351; MAPK; 1.
PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
Prints
PR01772; JNKMAPKINASE.
Created Date20-Feb-2013