IED Industry Enzyme Database

Detail Information for IndEnz0002015886
IED ID IndEnz0002015886
Enzyme Type ID protease015886
Protein Name Stress-activated protein kinase JNK
dJNK
EC 2.7.11.24
Protein basket
Gene Name bsk JNK CG5680
Organism Drosophila melanogaster (Fruit fly)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Diptera Brachycera Muscomorpha Eremoneura Cyclorrhapha Schizophora Acalyptratae Ephydroidea Drosophilidae (pomace flies) Drosophilinae Drosophilini Drosophila (fruit flies) Sophophora melanogaster group melanogaster subgroup Drosophila melanogaster (Fruit fly)
Enzyme Sequence MTTAQHQHYTVEVGDTNFTIHSRYINLRPIGSGAQGIVCAAYDTITQQNVAIKKLSRPFQNVTHAKRAYREFKLMKLVNHKNIIGLLNAFTPQRNLEEFQDVYLVMELMDANLCQVIQMDLDHDRMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKADCTLKILDFGLARTAGTTFMMTPYVVTRYYRAPEVILGMGYTENVDIWSVGCIMGEMIRGGVLFPGTDHIDQWNKIIEQLGTPSPSFMQRLQPTVRNYVENRPRYTGYSFDRLFPDGLFPNDNNQNSRRKASDARNLLSKMLVIDPEQRISVDEALKHEYINVWYDAEEVDAPAPEPYDHSVDEREHTVEQWKELIYEEVMDYEAHNTNNRTR
Enzyme Length 372
Uniprot Accession Number P92208
Absorption
Active Site ACT_SITE 149; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027"
Activity Regulation ACTIVITY REGULATION: Activated by threonine and tyrosine phosphorylation by the dual specificity kinase, hep. Inhibited by dual specificity phosphatase, puckered. {ECO:0000269|PubMed:10433922}.
Binding Site BINDING 53; /note=ATP; /evidence=ECO:0000255|PROSITE-ProRule:PRU00159
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.24;
DNA Binding
EC Number 2.7.11.24
Enzyme Function FUNCTION: Responds to activation by environmental stress by phosphorylating a number of transcription factors, primarily components of AP-1 such as Jra and also the transcriptional repressor aop, and thus regulates transcriptional activity (PubMed:9224720). Component of the immune response activated by bacterial infection, and is involved in wound healing and in dorsal closure, a morphogenetic movement during embryogenesis (PubMed:8946915, PubMed:9224720, PubMed:10433922, PubMed:11784101). Functions in the systematic response to wounding acting downstream of the Hayan-phenoloxidase PPO1 cascade (PubMed:22227521). Exhibits cytoprotective activity in neuronal cells in response to wounding to the integument (PubMed:22227521). Controls the expression of a phosphatase, puckered, at the edges of wounded epidermal tissue and in the dorsal epithelium during dorsal closure (PubMed:10433922, PubMed:11784101). Regulates the activity of SREBP in neurons and thereby the accumulation of lipids in glia (PubMed:25594180). Plays a role in positively regulating the expression of DIP2 independently of AP-1, thereby ensuring proper axon guidance in mushroom bodies (PubMed:28396149). {ECO:0000269|PubMed:10433922, ECO:0000269|PubMed:11784101, ECO:0000269|PubMed:22227521, ECO:0000269|PubMed:25594180, ECO:0000269|PubMed:28396149, ECO:0000269|PubMed:8946915, ECO:0000269|PubMed:9224720}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding NP_BIND 31..36; /note=ATP; /evidence=ECO:0000255|PROSITE-ProRule:PRU00159
Features Active site (1); Beta strand (11); Binding site (1); Chain (1); Domain (1); Frameshift (1); Helix (17); Modified residue (2); Motif (1); Mutagenesis (2); Nucleotide binding (1); Sequence conflict (1); Turn (3)
Keywords 3D-structure;ATP-binding;Cytoplasm;Developmental protein;Kinase;Nucleotide-binding;Nucleus;Phosphoprotein;Reference proteome;Serine/threonine-protein kinase;Transferase
Interact With
Induction INDUCTION: In neuronal cells by wounding of the integument (at protein level) (PubMed:22227521). Activated by increased levels of reactive oxygen species (ROS) (PubMed:25594180). {ECO:0000269|PubMed:22227521, ECO:0000269|PubMed:25594180}.
Subcellular Location SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18456458}. Cytoplasm {ECO:0000269|PubMed:18456458}.
Modified Residue MOD_RES 181; /note=Phosphothreonine; /evidence=ECO:0000269|PubMed:18456458; MOD_RES 183; /note=Phosphotyrosine; /evidence=ECO:0000269|PubMed:18456458
Post Translational Modification PTM: Dually phosphorylated on Thr-181 and Tyr-183, which activates the enzyme. {ECO:0000269|PubMed:18456458}.
Signal Peptide
Structure 3D X-ray crystallography (1)
Cross Reference PDB 5AWM;
Mapped Pubmed ID 10022918; 10026130; 10047521; 10047950; 10048301; 10085257; 10208418; 10322111; 10322485; 10323867; 10339422; 10399915; 10421564; 10427090; 10449347; 10449360; 10469646; 10471707; 10475855; 10502111; 10507837; 10556060; 10556061; 10557109; 10601009; 10617573; 10634792; 10656974; 10683140; 10744979; 10757786; 10801428; 10801879; 10878576; 10878822; 10903144; 10903184; 10903185; 10908587; 10924470; 10959830; 10985385; 11212302; 11283698; 11287182; 11316611; 11331897; 11402332; 11410534; 11439243; 11472834; 11489639; 11509232; 11543614; 11553345; 11702944; 11703923; 11703947; 11742539; 11825878; 11865058; 11868902; 11900973; 11912189; 11959832; 11976688; 12000787; 12012234; 12015117; 12015961; 12065414; 12091301; 12110163; 12135916; 12137730; 12147138; 12176339; 12198495; 12231350; 12231351; 12325120; 12350339; 12351623; 12354665; 12385750; 12413899; 12414186; 12415279; 12429700; 12453405; 12467587; 12470891; 12504027; 12508287; 12676357; 12728280; 12766944; 12874122; 12888007; 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Motif MOTIF 181..183; /note=TXY
Gene Encoded By
Mass 43,027
Kinetics
Metal Binding
Rhea ID RHEA:17989; RHEA:46608
Cross Reference Brenda 2.7.11.24;