ID JNK_DROME Reviewed; 372 AA.
AC P92208; O01366; Q94542;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 27-MAR-2024, entry version 204.
DE RecName: Full=Stress-activated protein kinase JNK;
DE Short=dJNK;
DE EC=2.7.11.24;
DE AltName: Full=Protein basket;
GN Name=bsk {ECO:0000312|FlyBase:FBgn0000229};
GN Synonyms=JNK {ECO:0000312|FlyBase:FBgn0000229};
GN ORFNames=CG5680 {ECO:0000312|FlyBase:FBgn0000229};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DEVELOPMENTAL STAGE, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Embryo;
RX PubMed=8946915; DOI=10.1101/gad.10.21.2745;
RA Sluss H.K., Han Z., Barrett T., Davis R.J., Ip Y.T.;
RT "A JNK signal transduction pathway that mediates morphogenesis and an
RT immune response in Drosophila.";
RL Genes Dev. 10:2745-2758(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS, AND TISSUE SPECIFICITY.
RC STRAIN=Oregon-R; TISSUE=Embryo;
RX PubMed=8946916; DOI=10.1101/gad.10.21.2759;
RA Riesgo-Escovar J.R., Jenni M., Fritz A., Hafen E.;
RT "The Drosophila Jun-N-terminal kinase is required for cell morphogenesis
RT but not for DJun-dependent cell fate specification in the eye.";
RL Genes Dev. 10:2759-2768(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo, and Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP FUNCTION.
RX PubMed=9224720; DOI=10.1101/gad.11.13.1717;
RA Riesgo-Escovar J.R., Hafen E.;
RT "Drosophila Jun kinase regulates expression of decapentaplegic via the ETS-
RT domain protein Aop and the AP-1 transcription factor DJun during dorsal
RT closure.";
RL Genes Dev. 11:1717-1727(1997).
RN [7]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=10433922; DOI=10.1242/dev.126.17.3947;
RA Zeitlinger J., Bohmann D.;
RT "Thorax closure in Drosophila: involvement of Fos and the JNK pathway.";
RL Development 126:3947-3956(1999).
RN [8]
RP FUNCTION.
RX PubMed=11784101; DOI=10.1006/dbio.2001.0502;
RA Raemet M., Lanot R., Zachary D., Manfruelli P.;
RT "JNK signaling pathway is required for efficient wound healing in
RT Drosophila.";
RL Dev. Biol. 241:145-156(2002).
RN [9]
RP INTERACTION WITH MKP-4, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT
RP THR-181 AND TYR-183.
RX PubMed=18456458; DOI=10.1016/j.cellsig.2008.03.003;
RA Sun L., Yu M.C., Kong L., Zhuang Z.H., Hu J.H., Ge B.X.;
RT "Molecular identification and functional characterization of a Drosophila
RT dual-specificity phosphatase DMKP-4 which is involved in PGN-induced
RT activation of the JNK pathway.";
RL Cell. Signal. 20:1329-1337(2008).
RN [10]
RP FUNCTION, AND INDUCTION BY WOUNDING.
RX PubMed=22227521; DOI=10.1038/emboj.2011.476;
RA Nam H.J., Jang I.H., You H., Lee K.A., Lee W.J.;
RT "Genetic evidence of a redox-dependent systemic wound response via Hayan
RT protease-phenoloxidase system in Drosophila.";
RL EMBO J. 31:1253-1265(2012).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=25836674; DOI=10.1242/bio.20148417;
RA Chittaranjan S., Xu J., Kuzyk M., Dullat H.K., Wilton J., DeVorkin L.,
RA Lebovitz C., Morin G.B., Marra M.A., Gorski S.M.;
RT "The Drosophila TIPE family member Sigmar interacts with the Ste20-like
RT kinase Misshapen and modulates JNK signaling, cytoskeletal remodeling and
RT autophagy.";
RL Biol. Open 4:672-684(2015).
RN [12]
RP FUNCTION, AND INDUCTION BY REACTIVE OXYGEN SPECIES.
RX PubMed=25594180; DOI=10.1016/j.cell.2014.12.019;
RA Liu L., Zhang K., Sandoval H., Yamamoto S., Jaiswal M., Sanz E., Li Z.,
RA Hui J., Graham B.H., Quintana A., Bellen H.J.;
RT "Glial lipid droplets and ROS induced by mitochondrial defects promote
RT neurodegeneration.";
RL Cell 160:177-190(2015).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28396149; DOI=10.1016/j.bbrc.2017.04.028;
RA Nitta Y., Sugie A.;
RT "DISCO interacting protein 2 determines direction of axon projection under
RT the regulation of c-Jun N-terminal kinase in the Drosophila mushroom
RT body.";
RL Biochem. Biophys. Res. Commun. 487:116-121(2017).
RN [14] {ECO:0000305}
RP FUNCTION.
RX PubMed=31704968; DOI=10.1038/s41598-019-52743-z;
RA Park S.H., Lee C.W., Choe K.M.;
RT "Interplay between integrins and PI4P5K Sktl is crucial for cell
RT polarization and reepithelialisation during Drosophila wound healing.";
RL Sci. Rep. 9:16331-16331(2019).
RN [15]
RP FUNCTION.
RX PubMed=37138087; DOI=10.1038/s41586-023-06039-y;
RA Xu C., Xu J., Tang H.W., Ericsson M., Weng J.H., DiRusso J., Hu Y., Ma W.,
RA Asara J.M., Perrimon N.;
RT "A phosphate-sensing organelle regulates phosphate and tissue
RT homeostasis.";
RL Nature 0:0-0(2023).
CC -!- FUNCTION: Mitogen-activated protein kinase and key component of the c-
CC Jun N-terminal kinase (JNK) pathway which phosphorylate and activate
CC transcription factors involved in a wide range of biological processes
CC including response to various stresses, cellular proliferation,
CC differentiation and migration, and regulation of cell shape
CC (PubMed:8946915, PubMed:9224720, PubMed:10433922, PubMed:11784101,
CC PubMed:22227521, PubMed:25594180, PubMed:28396149, PubMed:37138087).
CC Responds to activation by environmental stress by phosphorylating a
CC number of transcription factors, primarily components of AP-1 such as
CC Jra and also the transcriptional repressor aop, and thus regulates
CC transcriptional activity (PubMed:9224720). Component of the immune
CC response activated by bacterial infection, and is involved in wound
CC healing and in dorsal closure, a morphogenetic movement during
CC embryogenesis (PubMed:8946915, PubMed:9224720, PubMed:10433922,
CC PubMed:11784101). Functions in the systematic response to wounding
CC acting downstream of the Hayan-phenoloxidase PPO1 cascade
CC (PubMed:22227521). During epidermal wound healing involved in cellular
CC polarization by inducing the translocation of sktl and mys/integrin
CC beta to the trailing edge (PubMed:31704968). Exhibits cytoprotective
CC activity in neuronal cells in response to wounding to the integument
CC (PubMed:22227521). Controls the expression of a phosphatase, puckered,
CC at the edges of wounded epidermal tissue and in the dorsal epithelium
CC during dorsal closure (PubMed:10433922, PubMed:11784101). Regulates the
CC activity of SREBP in neurons and thereby the accumulation of lipids in
CC glia (PubMed:25594180). Plays a role in positively regulating the
CC expression of DIP2 independently of AP-1, thereby ensuring proper axon
CC guidance in mushroom bodies (PubMed:28396149). In enterocytes and
CC differentiating progenitors of the gut that are experiencing inorganic
CC phosphate (Pi) deficiency, activated by Cka to induce nearby progenitor
CC cells to proliferate and form new absorptive cells, probably helping
CC the organism to cope with the nutrient deficiency by maximizing
CC absorption of dietary Pi (PubMed:37138087).
CC {ECO:0000269|PubMed:10433922, ECO:0000269|PubMed:11784101,
CC ECO:0000269|PubMed:22227521, ECO:0000269|PubMed:25594180,
CC ECO:0000269|PubMed:28396149, ECO:0000269|PubMed:31704968,
CC ECO:0000269|PubMed:37138087, ECO:0000269|PubMed:8946915,
CC ECO:0000269|PubMed:9224720}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.24;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by threonine and tyrosine
CC phosphorylation by the dual specificity kinase, hep. Inhibited by dual
CC specificity phosphatase, puckered. {ECO:0000269|PubMed:10433922}.
CC -!- SUBUNIT: Interacts with MKP-4 (via tyrosine-protein phosphatase
CC domain); the interaction dephosphorylates bsk.
CC {ECO:0000269|PubMed:18456458}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18456458,
CC ECO:0000269|PubMed:25836674}. Cytoplasm {ECO:0000269|PubMed:18456458}.
CC -!- TISSUE SPECIFICITY: During gastrulation, expression is seen in cells
CC undergoing morphogenetic movements. By stage 9 of embryonic
CC development, expression is ubiquitous. At stages 12-14, expression
CC occurs in epidermis and central nervous system. At stage 15, expression
CC is restricted to ventral nerve cord, brain and some peripheral neurons.
CC In larvae, expression is seen in all imaginal disks, with highest
CC levels in wing and eye disks, and in the CNS. Adults express the
CC protein in fat body and hemocytes. {ECO:0000269|PubMed:8946915,
CC ECO:0000269|PubMed:8946916}.
CC -!- DEVELOPMENTAL STAGE: Expressed maternally and zygotically through to
CC adult (male and female). {ECO:0000269|PubMed:8946915}.
CC -!- INDUCTION: In neuronal cells by wounding of the integument (at protein
CC level) (PubMed:22227521). Activated by increased levels of reactive
CC oxygen species (ROS) (PubMed:25594180). {ECO:0000269|PubMed:22227521,
CC ECO:0000269|PubMed:25594180}.
CC -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC whose phosphorylation activates the MAP kinases.
CC -!- PTM: Dually phosphorylated on Thr-181 and Tyr-183, which activates the
CC enzyme. {ECO:0000269|PubMed:18456458}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in reduced levels
CC of DIP2. {ECO:0000269|PubMed:28396149}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. MAP kinase subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC47325.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U50965; AAB51187.1; -; Genomic_DNA.
DR EMBL; U50966; AAB51188.1; -; Genomic_DNA.
DR EMBL; U49180; AAB97094.1; -; mRNA.
DR EMBL; U49249; AAB48381.1; -; Genomic_DNA.
DR EMBL; U73196; AAC47325.1; ALT_FRAME; mRNA.
DR EMBL; AE014134; AAF52883.1; -; Genomic_DNA.
DR EMBL; AY122221; AAM52733.1; -; mRNA.
DR EMBL; AY070865; AAL48487.1; -; mRNA.
DR RefSeq; NP_001162930.1; NM_001169459.1.
DR RefSeq; NP_001162932.1; NM_001169461.3.
DR RefSeq; NP_723541.1; NM_164900.3.
DR PDB; 5AWM; X-ray; 1.79 A; A=1-372.
DR PDBsum; 5AWM; -.
DR AlphaFoldDB; P92208; -.
DR SMR; P92208; -.
DR BioGRID; 69288; 143.
DR DIP; DIP-17307N; -.
DR IntAct; P92208; 18.
DR STRING; 7227.FBpp0291573; -.
DR iPTMnet; P92208; -.
DR PaxDb; 7227-FBpp0079676; -.
DR DNASU; 44801; -.
DR EnsemblMetazoa; FBtr0080087; FBpp0079676; FBgn0000229.
DR EnsemblMetazoa; FBtr0300982; FBpp0290204; FBgn0000229.
DR EnsemblMetazoa; FBtr0302378; FBpp0291573; FBgn0000229.
DR GeneID; 44801; -.
DR KEGG; dme:Dmel_CG5680; -.
DR AGR; FB:FBgn0000229; -.
DR CTD; 44801; -.
DR FlyBase; FBgn0000229; bsk.
DR VEuPathDB; VectorBase:FBgn0000229; -.
DR eggNOG; KOG0665; Eukaryota.
DR GeneTree; ENSGT00940000169409; -.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; P92208; -.
DR OMA; QGHAFES; -.
DR OrthoDB; 158564at2759; -.
DR PhylomeDB; P92208; -.
DR BRENDA; 2.7.11.24; 1994.
DR Reactome; R-DME-193648; NRAGE signals death through JNK.
DR Reactome; R-DME-209397; Formation of the cytosolic BSK 'scaffolding complex'.
DR Reactome; R-DME-209409; Formation of the nuclear AP-1 transcription factor 'scaffolding complex'.
DR Reactome; R-DME-209425; Transcriptional activtion by AP-1 transcription factor.
DR Reactome; R-DME-209459; Imd pathway.
DR Reactome; R-DME-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-DME-2871796; FCERI mediated MAPK activation.
DR Reactome; R-DME-376172; DSCAM interactions.
DR Reactome; R-DME-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
DR Reactome; R-DME-450341; Activation of the AP-1 family of transcription factors.
DR Reactome; R-DME-9007892; Interleukin-38 signaling.
DR SignaLink; P92208; -.
DR BioGRID-ORCS; 44801; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 44801; -.
DR PRO; PR:P92208; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0000229; Expressed in eye disc (Drosophila) and 59 other cell types or tissues.
DR ExpressionAtlas; P92208; baseline and differential.
DR Genevisible; P92208; DM.
DR GO; GO:0030424; C:axon; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030425; C:dendrite; IDA:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004705; F:JUN kinase activity; IDA:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; IDA:FlyBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; TAS:Reactome.
DR GO; GO:0019731; P:antibacterial humoral response; IDA:FlyBase.
DR GO; GO:0048675; P:axon extension; IMP:FlyBase.
DR GO; GO:0007411; P:axon guidance; IDA:FlyBase.
DR GO; GO:0071243; P:cellular response to arsenic-containing substance; IDA:FlyBase.
DR GO; GO:0071276; P:cellular response to cadmium ion; IDA:FlyBase.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:FlyBase.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; IDA:FlyBase.
DR GO; GO:0046844; P:chorion micropyle formation; IMP:FlyBase.
DR GO; GO:0048674; P:collateral sprouting of injured axon; IMP:FlyBase.
DR GO; GO:0071907; P:determination of digestive tract left/right asymmetry; IGI:FlyBase.
DR GO; GO:0046843; P:dorsal appendage formation; IMP:FlyBase.
DR GO; GO:0007391; P:dorsal closure; IMP:FlyBase.
DR GO; GO:0007395; P:dorsal closure, spreading of leading edge cells; IMP:UniProtKB.
DR GO; GO:0048615; P:embryonic anterior midgut (ectodermal) morphogenesis; IGI:FlyBase.
DR GO; GO:0043652; P:engulfment of apoptotic cell; IMP:FlyBase.
DR GO; GO:0030707; P:follicle cell of egg chamber development; IMP:FlyBase.
DR GO; GO:0046529; P:imaginal disc fusion, thorax closure; IMP:FlyBase.
DR GO; GO:0048803; P:imaginal disc-derived male genitalia morphogenesis; IMP:FlyBase.
DR GO; GO:0007254; P:JNK cascade; IDA:UniProtKB.
DR GO; GO:0007258; P:JUN phosphorylation; IMP:FlyBase.
DR GO; GO:0007616; P:long-term memory; IGI:FlyBase.
DR GO; GO:0035006; P:melanization defense response; IMP:FlyBase.
DR GO; GO:0016319; P:mushroom body development; IMP:FlyBase.
DR GO; GO:0048666; P:neuron development; IMP:FlyBase.
DR GO; GO:0048812; P:neuron projection morphogenesis; IMP:FlyBase.
DR GO; GO:0061057; P:peptidoglycan recognition protein signaling pathway; IMP:FlyBase.
DR GO; GO:0010508; P:positive regulation of autophagy; IMP:FlyBase.
DR GO; GO:1903688; P:positive regulation of border follicle cell migration; IMP:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:1904801; P:positive regulation of neuron remodeling; IMP:FlyBase.
DR GO; GO:0043068; P:positive regulation of programmed cell death; IGI:FlyBase.
DR GO; GO:0140255; P:regulation of cellular response to phosphate starvation; IGI:UniProtKB.
DR GO; GO:0009408; P:response to heat; IMP:FlyBase.
DR GO; GO:0006979; P:response to oxidative stress; IMP:FlyBase.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IGI:FlyBase.
DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IDA:FlyBase.
DR GO; GO:0042060; P:wound healing; IDA:UniProtKB.
DR GO; GO:0035313; P:wound healing, spreading of epidermal cells; IMP:FlyBase.
DR CDD; cd07850; STKc_JNK; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003527; MAP_kinase_CS.
DR InterPro; IPR008351; MAPK_JNK.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24055; MITOGEN-ACTIVATED PROTEIN KINASE; 1.
DR PANTHER; PTHR24055:SF605; STRESS-ACTIVATED PROTEIN KINASE JNK; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR01772; JNKMAPKINASE.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS01351; MAPK; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Developmental protein; Kinase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..372
FT /note="Stress-activated protein kinase JNK"
FT /id="PRO_0000186271"
FT DOMAIN 24..320
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOTIF 181..183
FT /note="TXY"
FT ACT_SITE 149
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 31..36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 181
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18456458"
FT MOD_RES 183
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18456458"
FT MUTAGEN 225
FT /note="G->E: In BSK-1; defect in dorsal closure."
FT /evidence="ECO:0000269|PubMed:8946916"
FT MUTAGEN 316..372
FT /note="Missing: In BSK-2; defect in dorsal closure."
FT /evidence="ECO:0000269|PubMed:8946916"
FT CONFLICT 331..372
FT /note="APAPEPYDHSVDEREHTVEQWKELIYEEVMDYEAHNTNNRTR -> RPLRSH
FT MITAWTKGNTLWSSGRS (in Ref. 2; AAC47325)"
FT /evidence="ECO:0000305"
FT STRAND 8..13
FT /evidence="ECO:0007829|PDB:5AWM"
FT STRAND 16..21
FT /evidence="ECO:0007829|PDB:5AWM"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:5AWM"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:5AWM"
FT TURN 44..47
FT /evidence="ECO:0007829|PDB:5AWM"
FT STRAND 48..56
FT /evidence="ECO:0007829|PDB:5AWM"
FT HELIX 62..77
FT /evidence="ECO:0007829|PDB:5AWM"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:5AWM"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:5AWM"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:5AWM"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:5AWM"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:5AWM"
FT HELIX 113..118
FT /evidence="ECO:0007829|PDB:5AWM"
FT HELIX 123..142
FT /evidence="ECO:0007829|PDB:5AWM"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:5AWM"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:5AWM"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:5AWM"
FT HELIX 192..195
FT /evidence="ECO:0007829|PDB:5AWM"
FT HELIX 204..218
FT /evidence="ECO:0007829|PDB:5AWM"
FT HELIX 228..239
FT /evidence="ECO:0007829|PDB:5AWM"
FT HELIX 244..248
FT /evidence="ECO:0007829|PDB:5AWM"
FT HELIX 252..259
FT /evidence="ECO:0007829|PDB:5AWM"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:5AWM"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:5AWM"
FT HELIX 285..300
FT /evidence="ECO:0007829|PDB:5AWM"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:5AWM"
FT HELIX 311..316
FT /evidence="ECO:0007829|PDB:5AWM"
FT TURN 318..320
FT /evidence="ECO:0007829|PDB:5AWM"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:5AWM"
FT HELIX 326..329
FT /evidence="ECO:0007829|PDB:5AWM"
FT HELIX 348..361
FT /evidence="ECO:0007829|PDB:5AWM"
SQ SEQUENCE 372 AA; 43027 MW; 96662B278ABCCA19 CRC64;
MTTAQHQHYT VEVGDTNFTI HSRYINLRPI GSGAQGIVCA AYDTITQQNV AIKKLSRPFQ
NVTHAKRAYR EFKLMKLVNH KNIIGLLNAF TPQRNLEEFQ DVYLVMELMD ANLCQVIQMD
LDHDRMSYLL YQMLCGIKHL HSAGIIHRDL KPSNIVVKAD CTLKILDFGL ARTAGTTFMM
TPYVVTRYYR APEVILGMGY TENVDIWSVG CIMGEMIRGG VLFPGTDHID QWNKIIEQLG
TPSPSFMQRL QPTVRNYVEN RPRYTGYSFD RLFPDGLFPN DNNQNSRRKA SDARNLLSKM
LVIDPEQRIS VDEALKHEYI NVWYDAEEVD APAPEPYDHS VDEREHTVEQ WKELIYEEVM
DYEAHNTNNR TR
//
