EKS-RAN-00478
Eukaryotic Protein Kinase & Protein Phosphatase Database
TagContent
EKPD IDEKS-RAN-00478
Classification
Group/FamilyScoreE-ValueStartEndDomain Length
CMGC/MAPK420.05.5E-12626321296
StatusReviewed
Ensembl ProteinENSRNOP00000004010
UniProt AccessionP49186;
Protein NameMitogen-activated protein kinase 9
Protein Synonyms/Alias MAP kinase 9; MAPK 9; SAPK-alpha; Stress-activated protein kinase JNK2; c-Jun N-terminal kinase 2; p54-alpha;
Gene NameMapk9
Gene Synonyms/Alias Mapk9; Jnk2, Prkm9;
Ensembl Information
Ensembl Gene IDEnsembl Protein IDEnsembl Transcript ID
ENSRNOG00000002823ENSRNOP00000003987ENSRNOT00000003987
ENSRNOG00000002823ENSRNOP00000004010ENSRNOT00000004010
OrganismRattus norvegicus
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 (By similarity).
Protein Length423
Protein Sequence
(FASTA)
MSDSKSDGQF 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 VKDQPSDAAV SSKATPSQSS SINDISSMST EHTLASDTDS SLDASTGPLE 420
GCR 423
Nucleotide Sequence
(FASTA)
ATGAGTGACA GTAAAAGCGA TGGCCAGTTT TACAGTGTGC AAGTGGCAGA CTCAACTTTC 60
ACTGTTCTAA AACGTTACCA GCAGTTGAAA CCAATTGGCT CTGGAGCCCA AGGAATTGTT 120
TGTGCTGCTT TTGATACAGT TCTTGGAATA AATGTTGCTG TCAAGAAGTT AAGTCGTCCT 180
TTTCAGAACC AAACGCATGC AAAGAGAGCC TACCGTGAAC TTGTCCTCCT AAAGTGTGTC 240
AATCATAAAA ATATAATTAG CTTGTTAAAT GTGTTCACAC CACAAAAAAC GCTAGAAGAA 300
TTCCAAGATG TGTACTTGGT TATGGAGTTA ATGGACGCTA ACTTATGTCA GGTTATTCAT 360
ATGGAGCTGG ACCATGAAAG AATGTCATAC CTCCTCTACC AGATGCTTTG TGGCATTAAG 420
CACCTGCATT CAGCTGGCAT AATTCATAGG GATTTGAAGC CTAGCAACAT TGTAGTAAAA 480
TCAGACTGTA CTCTCAAGAT CCTTGACTTT GGCCTGGCAC GGACAGCCTG TACCAACTTT 540
ATGATGACTC CCTATGTGGT AACTCGCTAC TATCGGGCTC CAGAAGTCAT CCTGGGCATG 600
GGCTACAAGG AGAATGTGGA CATCTGGTCT GTCGGGTGCA TCATGGCAGA AATGGTCCTC 660
CATAAAGTCC TGTTCCCAGG AAGAGACTAT ATTGATCAAT GGAATAAAGT TATTGAACAG 720
CTAGGAACAC CATCCGCAGA GTTCATGAAG AAACTTCAGC CAACTGTAAG GAATTATGTG 780
GAAAACAGAC CAAAGTACCC TGGAATCAAA TTTGAAGAGC TCTTTCCAGA TTGGATATTT 840
CCGTCAGAAT CCGAACGAGA CAAAATAAAA ACAAGTCAAG CCAGAGATCT GTTATCGAAA 900
ATGTTAGTGA TTGATCCGGA CAAGCGGATC TCTGTGGACG AAGCCTTGCG CCACCCGTAT 960
ATTACTGTTT GGTATGACCC CGCTGAAGCA GAAGCGCCAC CACCTCAAAT TTATGATGCC 1020
CAGTTGGAAG AAAGAGAGCA TGCGATTGAA GAGTGGAAAG AACTAATTTA CAAAGAAGTG 1080
ATGGACTGGG AAGAAAGAAG CAAGAATGGG GTGAAAGACC AGCCTTCAGA TGCAGCAGTA 1140
AGCAGCAAGG CTACTCCTTC TCAGTCGTCA TCCATCAATG ACATCTCATC CATGTCCACT 1200
GAGCACACCC TGGCCTCAGA CACAGACAGC AGTCTCGATG CCTCAACCGG ACCCCTGGAA 1260
GGCTGCCGAT GA 1272
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
KeywordAlternative splicing; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; 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"; ?>Homo sapiens"; ?>Latimeria chalumnae"; ?>Loxodonta africana"; ?>Meleagris gallopavo"; ?>Monodelphis domestica"; ?>Mus musculus"; ?>Mustela putorius furo"; ?>Myotis lucifugus"; ?>Nomascus leucogenys"; ?>Ochotona princeps"; ?>Ornithorhynchus anatinus"; ?>Oryctolagus cuniculus"; ?>Oryzias latipes"; ?>Otolemur garnettii"; ?>Pan troglodytes"; ?>Pelodiscus sinensis"; ?>Pongo abelii"; ?>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-HOS-00472
EKS-LAC-00475
EKS-LOA-00468
EKS-MEG-00379
EKS-MOD-00456
EKS-MUM-00496
EKS-MUP-00459
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-SAH-00432
EKS-SUS-00408
EKS-TAG-00526
Gene Ontology
GO:0044445; C:cytosolic part
GO:0005739; C:mitochondrion
GO:0005634; C:nucleus
GO:0005524; F:ATP binding
GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process
GO:0004705; F:JUN kinase activity
GO:0008134; F:transcription factor binding
GO:0071363; P:cellular response to growth factor stimulus
GO:0071347; P:cellular response to interleukin-1
GO:0071222; P:cellular response to lipopolysaccharide
GO:0071356; P:cellular response to tumor necrosis factor
GO:0034644; P:cellular response to UV
GO:0007417; P:central nervous system development
GO:0031175; P:neuron projection development
GO:0043065; P:positive regulation of apoptotic process
GO:0010770; P:positive regulation of cell morphogenesis involved in differentiation
GO:0032722; P:positive regulation of chemokine production
GO:0045429; P:positive regulation of nitric oxide biosynthetic process
GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process
GO:0031394; P:positive regulation of prostaglandin biosynthetic process
GO:0032308; P:positive regulation of prostaglandin secretion
GO:0001934; P:positive regulation of protein phosphorylation
GO:0045893; P:positive regulation of transcription, DNA-dependent
GO:0006626; P:protein targeting to mitochondrion
GO:0046328; P:regulation of JNK cascade
GO:0031396; P:regulation of protein ubiquitination
GO:0001836; P:release of cytochrome c from mitochondria
GO:0014075; P:response to amine stimulus
GO:0042493; P:response to drug
GO:0009612; P:response to mechanical stimulus
GO:0009636; P:response to toxin
KEGG
rno:50658;
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