UniProt functional annotation for P92208



	UniProt functional annotation for P92208

UniProt code: P92208.

Organism: Drosophila melanogaster (Fruit fly).

Taxonomy: Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora.

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 postively 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}.

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;

Cofactor: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};

Activity regulation: Activated by threonine and tyrosine phosphorylation by the dual specificity kinase, hep. Inhibited by dual specificity phosphatase, puckered. {ECO:0000269|PubMed:10433922}.

Subunit: Interacts with MKP-4 (via tyrosine-protein phosphatase domain); the interaction dephosphorylates bsk. {ECO:0000269|PubMed:18456458}.

Subcellular location: Nucleus {ECO:0000269|PubMed:18456458}. Cytoplasm {ECO:0000269|PubMed:18456458}.

Tissue specificity: During gastrulation, expression is seen in cells undergoing morphogenetic movements. By stage 9 of embryonic development, expression is ubiquitous. At stages 12-14, expression occurs in epidermis and central nervous system. At stage 15, expression is restricted to ventral nerve cord, brain and some peripheral neurons. In larvae, expression is seen in all imaginal disks, with highest levels in wing and eye disks, and in the CNS. Adults express the protein in fat body and hemocytes. {ECO:0000269|PubMed:8946915, ECO:0000269|PubMed:8946916}.

Developmental stage: Expressed maternally and zygotically through to adult (male and female). {ECO:0000269|PubMed:8946915}.

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}.

Domain: The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.

Ptm: Dually phosphorylated on Thr-181 and Tyr-183, which activates the enzyme. {ECO:0000269|PubMed:18456458}.

Disruption phenotype: RNAi-mediated knockdown results in reduced levels of DIP2. {ECO:0000269|PubMed:28396149}.

Similarity: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily. {ECO:0000305}.

Sequence caution: Sequence=AAC47325.1; Type=Frameshift; Evidence={ECO:0000305};

Annotations taken from UniProtKB at the EBI.


Organism:		Drosophila melanogaster (Fruit fly).
Taxonomy:		Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora.



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 postively 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}.


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;
Cofactor:		Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Activity regulation:		Activated by threonine and tyrosine phosphorylation by the dual specificity kinase, hep. Inhibited by dual specificity phosphatase, puckered. {ECO:0000269\|PubMed:10433922}.
Subunit:		Interacts with MKP-4 (via tyrosine-protein phosphatase domain); the interaction dephosphorylates bsk. {ECO:0000269\|PubMed:18456458}.
Subcellular location:		Nucleus {ECO:0000269\|PubMed:18456458}. Cytoplasm {ECO:0000269\|PubMed:18456458}.
Tissue specificity:		During gastrulation, expression is seen in cells undergoing morphogenetic movements. By stage 9 of embryonic development, expression is ubiquitous. At stages 12-14, expression occurs in epidermis and central nervous system. At stage 15, expression is restricted to ventral nerve cord, brain and some peripheral neurons. In larvae, expression is seen in all imaginal disks, with highest levels in wing and eye disks, and in the CNS. Adults express the protein in fat body and hemocytes. {ECO:0000269\|PubMed:8946915, ECO:0000269\|PubMed:8946916}.
Developmental stage:		Expressed maternally and zygotically through to adult (male and female). {ECO:0000269\|PubMed:8946915}.
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}.
Domain:		The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.
Ptm:		Dually phosphorylated on Thr-181 and Tyr-183, which activates the enzyme. {ECO:0000269\|PubMed:18456458}.
Disruption phenotype:		RNAi-mediated knockdown results in reduced levels of DIP2. {ECO:0000269\|PubMed:28396149}.
Similarity:		Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily. {ECO:0000305}.
Sequence caution:		Sequence=AAC47325.1; Type=Frameshift; Evidence={ECO:0000305};