ERKA_DROME
ID ERKA_DROME Reviewed; 376 AA.
AC P40417; A0A021WW06; A8Y4W1; A8Y4W2; Q7PL59; Q9W5M2; Q9W5M3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 3.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Mitogen-activated protein kinase ERK-A;
DE EC=2.7.11.24;
DE AltName: Full=Extracellular-regulated kinase A;
DE AltName: Full=Protein rolled;
GN Name=rl {ECO:0000303|PubMed:8157002, ECO:0000312|FlyBase:FBgn0003256};
GN Synonyms=ERKa {ECO:0000303|PubMed:1378625},
GN MAPK {ECO:0000303|PubMed:27552662};
GN ORFNames=CG12559 {ECO:0000312|FlyBase:FBgn0003256};
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 [MRNA] (ISOFORM C), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND PHOSPHORYLATION.
RC STRAIN=Oregon-R; TISSUE=Embryo, and Imaginal disk;
RX PubMed=1378625; DOI=10.1073/pnas.89.14.6295;
RA Biggs W.H. III, Zipursky S.L.;
RT "Primary structure, expression, and signal-dependent tyrosine
RT phosphorylation of a Drosophila homolog of extracellular signal-regulated
RT kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:6295-6299(1992).
RN [2]
RP ERRATUM OF PUBMED:1378625.
RA Biggs W.H. III, Zipursky S.L.;
RL Proc. Natl. Acad. Sci. U.S.A. 90:6377-6377(1993).
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] (ISOFORM C).
RC STRAIN=Berkeley; TISSUE=Embryo;
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.
RC STRAIN=Oregon-R;
RX PubMed=8157002; DOI=10.1002/j.1460-2075.1994.tb06426.x;
RA Biggs W.H. III, Zavitz K.H., Dickson B., van der Straten A., Brunner D.,
RA Hafen E., Zipursky S.L.;
RT "The Drosophila rolled locus encodes a MAP kinase required in the sevenless
RT signal transduction pathway.";
RL EMBO J. 13:1628-1635(1994).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-198 AND TYR-200, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19965758; DOI=10.1126/science.1176450;
RA Rewitz K.F., Yamanaka N., Gilbert L.I., O'Connor M.B.;
RT "The insect neuropeptide PTTH activates receptor tyrosine kinase torso to
RT initiate metamorphosis.";
RL Science 326:1403-1405(2009).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22140578; DOI=10.1371/journal.pone.0028349;
RA Geiger J.A., Carvalho L., Campos I., Santos A.C., Jacinto A.;
RT "Hole-in-one mutant phenotypes link EGFR/ERK signaling to epithelial tissue
RT repair in Drosophila.";
RL PLoS ONE 6:E28349-E28349(2011).
RN [10]
RP FUNCTION.
RX PubMed=27552662; DOI=10.1371/journal.pbio.1002539;
RA Ashton-Beaucage D., Lemieux C., Udell C.M., Sahmi M., Rochette S.,
RA Therrien M.;
RT "The Deubiquitinase USP47 Stabilizes MAPK by Counteracting the Function of
RT the N-end Rule ligase POE/UBR4 in Drosophila.";
RL PLoS Biol. 14:E1002539-E1002539(2016).
CC -!- FUNCTION: Serine/threonine kinase which acts as an essential component
CC of the MAP kinase signal transduction pathway to regulate
CC proliferation, differentiation and effect cell fate decisions in
CC various tissues (PubMed:8157002, PubMed:19965758, PubMed:22140578,
CC PubMed:27552662). Required downstream of phl/Raf in the sev/sevenless,
CC tor/torso, and EGF receptor homolog Egfr signal transduction pathways
CC (PubMed:8157002). Required for embryonic epithelial tissue repair
CC (PubMed:22140578). During larval development, mediates Ptth/tor
CC signaling leading to the production of ecdysone, a hormone required for
CC the initiation of metamorphosis (PubMed:19965758).
CC {ECO:0000269|PubMed:19965758, ECO:0000269|PubMed:22140578,
CC ECO:0000269|PubMed:27552662, ECO:0000269|PubMed:8157002}.
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 tyrosine and threonine
CC phosphorylation. {ECO:0000250}.
CC -!- INTERACTION:
CC P40417; Q9U1H0: cic; NbExp=3; IntAct=EBI-867790, EBI-98330;
CC P40417; Q24324: Dsor1; NbExp=2; IntAct=EBI-867790, EBI-671282;
CC P40417; Q9V393: krz; NbExp=12; IntAct=EBI-867790, EBI-100228;
CC P40417; Q24496: S6kII; NbExp=2; IntAct=EBI-867790, EBI-870498;
CC P40417; P32121: ARRB2; Xeno; NbExp=4; IntAct=EBI-867790, EBI-714559;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1378625}. Nucleus
CC {ECO:0000269|PubMed:1378625}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=C; Synonyms=D, E;
CC IsoId=P40417-3; Sequence=Displayed;
CC Name=H; Synonyms=F;
CC IsoId=P40417-1; Sequence=VSP_047792;
CC Name=G; Synonyms=B;
CC IsoId=P40417-2; Sequence=VSP_047793, VSP_047794;
CC -!- TISSUE SPECIFICITY: In third instar larvae, expressed in eye imaginal
CC disks. In adults, expressed in head and body.
CC {ECO:0000269|PubMed:1378625}.
CC -!- DEVELOPMENTAL STAGE: Embryos, larvae and adults.
CC {ECO:0000269|PubMed:1378625}.
CC -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC whose phosphorylation activates the MAP kinases.
CC -!- PTM: Dually phosphorylated on Thr-198 and Tyr-200, which activates the
CC enzyme (By similarity). Phosphorylated on tyrosine residue(s) in
CC response to insulin. {ECO:0000250, ECO:0000269|PubMed:1378625,
CC ECO:0000269|PubMed:18327897}.
CC -!- DISRUPTION PHENOTYPE: Embryonic wound healing defects
CC (PubMed:22140578). RNAi-mediated knockdown in the prothoracic gland
CC (PG) delays the onset of pupariation by prolonging the L3 larval stage
CC and increases adult weight (PubMed:19965758).
CC {ECO:0000269|PubMed:19965758, ECO:0000269|PubMed:22140578}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. MAP kinase subfamily. {ECO:0000305}.
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DR EMBL; M95124; AAA28677.1; -; mRNA.
DR EMBL; AE013599; EAA46310.2; -; Genomic_DNA.
DR EMBL; AE013599; EAA46311.2; -; Genomic_DNA.
DR EMBL; AE013599; EAA46312.4; -; Genomic_DNA.
DR EMBL; AE013599; EDP28106.2; -; Genomic_DNA.
DR EMBL; AE013599; EDP28107.1; -; Genomic_DNA.
DR EMBL; AE013599; EYR77323.1; -; Genomic_DNA.
DR EMBL; AY070996; AAL48618.1; -; mRNA.
DR PIR; A46036; A46036.
DR PIR; B46036; B46036.
DR RefSeq; NP_001015121.3; NM_001015121.3. [P40417-2]
DR RefSeq; NP_001015122.1; NM_001015122.3. [P40417-3]
DR RefSeq; NP_001015123.1; NM_001015123.3. [P40417-3]
DR RefSeq; NP_001104348.2; NM_001110878.4. [P40417-1]
DR RefSeq; NP_001104349.1; NM_001110879.2. [P40417-3]
DR RefSeq; NP_001287635.1; NM_001300706.2. [P40417-3]
DR AlphaFoldDB; P40417; -.
DR SMR; P40417; -.
DR BioGRID; 78013; 85.
DR DIP; DIP-17266N; -.
DR IntAct; P40417; 14.
DR MINT; P40417; -.
DR STRING; 7227.FBpp0112426; -.
DR iPTMnet; P40417; -.
DR PaxDb; P40417; -.
DR PRIDE; P40417; -.
DR DNASU; 3354888; -.
DR EnsemblMetazoa; FBtr0113700; FBpp0112423; FBgn0003256. [P40417-3]
DR EnsemblMetazoa; FBtr0113702; FBpp0112425; FBgn0003256. [P40417-3]
DR EnsemblMetazoa; FBtr0113703; FBpp0112426; FBgn0003256. [P40417-3]
DR EnsemblMetazoa; FBtr0329919; FBpp0302952; FBgn0003256. [P40417-2]
DR EnsemblMetazoa; FBtr0329920; FBpp0302953; FBgn0003256. [P40417-1]
DR EnsemblMetazoa; FBtr0345337; FBpp0311493; FBgn0003256. [P40417-3]
DR GeneID; 3354888; -.
DR KEGG; dme:Dmel_CG12559; -.
DR CTD; 3354888; -.
DR FlyBase; FBgn0003256; rl.
DR VEuPathDB; VectorBase:FBgn0003256; -.
DR eggNOG; KOG0660; Eukaryota.
DR GeneTree; ENSGT00940000156771; -.
DR InParanoid; P40417; -.
DR OMA; FINNHPY; -.
DR PhylomeDB; P40417; -.
DR BRENDA; 2.7.11.24; 1994.
DR Reactome; R-DME-110056; MAPK3 (ERK1) activation.
DR Reactome; R-DME-112409; RAF-independent MAPK1/3 activation.
DR Reactome; R-DME-112411; MAPK1 (ERK2) activation.
DR Reactome; R-DME-1181150; Signaling by NODAL.
DR Reactome; R-DME-1295596; Spry regulation of FGF signaling.
DR Reactome; R-DME-1502540; Signaling by Activin.
DR Reactome; R-DME-162658; Golgi Cisternae Pericentriolar Stack Reorganization.
DR Reactome; R-DME-170968; Frs2-mediated activation.
DR Reactome; R-DME-198753; ERK/MAPK targets.
DR Reactome; R-DME-202670; ERKs are inactivated.
DR Reactome; R-DME-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-DME-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR Reactome; R-DME-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-DME-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-DME-2559585; Oncogene Induced Senescence.
DR Reactome; R-DME-2871796; FCERI mediated MAPK activation.
DR Reactome; R-DME-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-DME-375165; NCAM signaling for neurite out-growth.
DR Reactome; R-DME-437239; Recycling pathway of L1.
DR Reactome; R-DME-445144; Signal transduction by L1.
DR Reactome; R-DME-450341; Activation of the AP-1 family of transcription factors.
DR Reactome; R-DME-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR Reactome; R-DME-5654726; Negative regulation of FGFR1 signaling.
DR Reactome; R-DME-5654733; Negative regulation of FGFR4 signaling.
DR Reactome; R-DME-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-DME-5673001; RAF/MAP kinase cascade.
DR Reactome; R-DME-5674135; MAP2K and MAPK activation.
DR Reactome; R-DME-5674499; Negative feedback regulation of MAPK pathway.
DR Reactome; R-DME-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR Reactome; R-DME-74749; Signal attenuation.
DR Reactome; R-DME-9634635; Estrogen-stimulated signaling through PRKCZ.
DR Reactome; R-DME-9634638; Estrogen-dependent nuclear events downstream of ESR-membrane signaling.
DR SignaLink; P40417; -.
DR BioGRID-ORCS; 3354888; 1 hit in 3 CRISPR screens.
DR ChiTaRS; rl; fly.
DR GenomeRNAi; 3354888; -.
DR PRO; PR:P40417; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0003256; Expressed in midgut and 17 other tissues.
DR ExpressionAtlas; P40417; baseline and differential.
DR Genevisible; P40417; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0031594; C:neuromuscular junction; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:FlyBase.
DR GO; GO:0004707; F:MAP kinase activity; IDA:FlyBase.
DR GO; GO:0019901; F:protein kinase binding; IPI:FlyBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:FlyBase.
DR GO; GO:0048149; P:behavioral response to ethanol; IMP:FlyBase.
DR GO; GO:0060446; P:branching involved in open tracheal system development; IDA:FlyBase.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
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:0034614; P:cellular response to reactive oxygen species; IDA:FlyBase.
DR GO; GO:0009267; P:cellular response to starvation; IMP:FlyBase.
DR GO; GO:0051607; P:defense response to virus; IMP:FlyBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
DR GO; GO:0046843; P:dorsal appendage formation; IEP:FlyBase.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IDA:FlyBase.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IDA:FlyBase.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IDA:FlyBase.
DR GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR GO; GO:0007474; P:imaginal disc-derived wing vein specification; IMP:FlyBase.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IDA:FlyBase.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0007479; P:leg disc proximal/distal pattern formation; IEP:FlyBase.
DR GO; GO:0035170; P:lymph gland crystal cell differentiation; IMP:FlyBase.
DR GO; GO:0035169; P:lymph gland plasmatocyte differentiation; IMP:FlyBase.
DR GO; GO:0000165; P:MAPK cascade; IMP:UniProtKB.
DR GO; GO:0007552; P:metamorphosis; IMP:FlyBase.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:FlyBase.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IMP:FlyBase.
DR GO; GO:0016242; P:negative regulation of macroautophagy; IMP:FlyBase.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:FlyBase.
DR GO; GO:0045793; P:positive regulation of cell size; IMP:FlyBase.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:FlyBase.
DR GO; GO:0046534; P:positive regulation of photoreceptor cell differentiation; IMP:FlyBase.
DR GO; GO:0090303; P:positive regulation of wound healing; IMP:FlyBase.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0007465; P:R7 cell fate commitment; IGI:FlyBase.
DR GO; GO:2000826; P:regulation of heart morphogenesis; IGI:FlyBase.
DR GO; GO:2001023; P:regulation of response to drug; IMP:FlyBase.
DR GO; GO:0045500; P:sevenless signaling pathway; IDA:FlyBase.
DR GO; GO:0007430; P:terminal branching, open tracheal system; IMP:FlyBase.
DR GO; GO:0007362; P:terminal region determination; IEP:FlyBase.
DR GO; GO:0008293; P:torso signaling pathway; IGI:FlyBase.
DR GO; GO:0035202; P:tracheal pit formation in open tracheal system; IEP:FlyBase.
DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IDA:FlyBase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003527; MAP_kinase_CS.
DR InterPro; IPR008349; MAPK_ERK1/2.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR01770; ERK1ERK2MAPK.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS01351; MAPK; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell cycle; Cytoplasm; Kinase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..376
FT /note="Mitogen-activated protein kinase ERK-A"
FT /id="PRO_0000186309"
FT DOMAIN 38..326
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOTIF 198..200
FT /note="TXY"
FT ACT_SITE 162
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 44..52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 198
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 200
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 1..110
FT /note="Missing (in isoform H)"
FT /evidence="ECO:0000305"
FT /id="VSP_047792"
FT VAR_SEQ 1..45
FT /note="Missing (in isoform G)"
FT /evidence="ECO:0000305"
FT /id="VSP_047793"
FT VAR_SEQ 46..53
FT /note="EGAYGMVV -> MESALVIR (in isoform G)"
FT /evidence="ECO:0000305"
FT /id="VSP_047794"
SQ SEQUENCE 376 AA; 43151 MW; 2642B3CBB0F234D2 CRC64;
MEEFNSSGSV VNGTGSTEVP QSNAEVIRGQ IFEVGPRYIK LAYIGEGAYG MVVSADDTLT
NQRVAIKKIS PFEHQTYCQR TLREITILTR FKHENIIDIR DILRVDSIDQ MRDVYIVQCL
METDLYKLLK TQRLSNDHIC YFLYQILRGL KYIHSANVLH RDLKPSNLLL NKTCDLKICD
FGLARIADPE HDHTGFLTEY VATRWYRAPE IMLNSKGYTK SIDIWSVGCI LAEMLSNRPI
FPGKHYLDQL NHILGVLGSP SRDDLECIIN EKARNYLESL PFKPNVPWAK LFPNADALAL
DLLGKMLTFN PHKRIPVEEA LAHPYLEQYY DPGDEPVAEV PFRINMENDD ISRDALKSLI
FEETLKFKER QPDNAP
