ID MK38B_DROME Reviewed; 365 AA. AC O61443; DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 27-MAR-2024, entry version 204. DE RecName: Full=Mitogen-activated protein kinase p38b {ECO:0000303|PubMed:9584193}; DE Short=MAP kinase p38b {ECO:0000303|PubMed:9584193}; DE Short=MAPK p38b {ECO:0000303|PubMed:9584193}; DE EC=2.7.11.24; GN Name=p38b {ECO:0000303|PubMed:9584193, GN ECO:0000312|FlyBase:FBgn0024846}; GN ORFNames=CG7393 {ECO:0000312|FlyBase:FBgn0024846}; 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], FUNCTION, AND ACTIVITY REGULATION. RC TISSUE=Embryo; RX PubMed=9584193; DOI=10.1128/mcb.18.6.3527; RA Han Z.S., Enslen H., Hu X., Meng X., Wu I.-H., Barrett T., Davis R.J., RA Ip Y.T.; RT "A conserved p38 mitogen-activated protein kinase pathway regulates RT Drosophila immunity gene expression."; RL Mol. Cell. Biol. 18:3527-3539(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION. RC TISSUE=Imaginal disk; RX PubMed=10022918; DOI=10.1128/mcb.19.3.2322; RA Adachi-Yamada T., Nakamura M., Irie K., Tomoyasu Y., Sano Y., Mori E., RA Goto S., Ueno N., Nishida Y., Matsumoto K.; RT "p38 mitogen-activated protein kinase can be involved in transforming RT growth factor beta superfamily signal transduction in Drosophila wing RT morphogenesis."; RL Mol. Cell. Biol. 19:2322-2329(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX PubMed=10471707; DOI=10.1093/genetics/153.1.179; RA Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T., RA Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., Harvey D.A., RA Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., Moshrefi A.R., RA Palazzolo M., Reese M.G., Spradling A.C., Tsang G., Wan K.H., Whitelaw K., RA Celniker S.E., Rubin G.M.; RT "An exploration of the sequence of a 2.9-Mb region of the genome of RT Drosophila melanogaster: the Adh region."; RL Genetics 153:179-219(1999). RN [4] 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 [5] 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, 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). CC -!- FUNCTION: Kinase involved in dpp signal transduction pathway in the CC process of wing morphogenesis when the levels of dpp are enhanced or CC inhibited. May down-regulate insect immunity gene expression after CC prolonged infection. {ECO:0000269|PubMed:10022918, CC ECO:0000269|PubMed:9584193}. 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 Mkk3. {ECO:0000269|PubMed:9584193}. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- TISSUE SPECIFICITY: At mid-embryogenesis, highest expression is seen in CC developing anterior and posterior midguts. Almost ubiquitous expression CC throughout all development. CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically in the CC embryo, expression seen in all developmental stages. CC -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues CC whose phosphorylation activates the MAP kinases. CC -!- PTM: Dually phosphorylated on Thr-183 and Tyr-185, which activates the CC enzyme. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr CC protein kinase family. MAP kinase subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF035548; AAC39032.1; -; mRNA. DR EMBL; AB006364; BAA35141.1; -; mRNA. DR EMBL; AE014134; AAF53326.1; -; Genomic_DNA. DR EMBL; AY058548; AAL13777.1; -; mRNA. DR RefSeq; NP_477361.1; NM_058013.5. DR AlphaFoldDB; O61443; -. DR SMR; O61443; -. DR BioGRID; 60814; 51. DR DIP; DIP-22779N; -. DR IntAct; O61443; 7. DR STRING; 7227.FBpp0080111; -. DR iPTMnet; O61443; -. DR PaxDb; 7227-FBpp0080111; -. DR DNASU; 34780; -. DR EnsemblMetazoa; FBtr0080534; FBpp0080111; FBgn0024846. DR GeneID; 34780; -. DR KEGG; dme:Dmel_CG7393; -. DR AGR; FB:FBgn0024846; -. DR CTD; 34780; -. DR FlyBase; FBgn0024846; p38b. DR VEuPathDB; VectorBase:FBgn0024846; -. DR eggNOG; KOG0660; Eukaryota. DR GeneTree; ENSGT00940000155325; -. DR HOGENOM; CLU_000288_181_1_1; -. DR InParanoid; O61443; -. DR OMA; NRYTDLN; -. DR OrthoDB; 158564at2759; -. DR PhylomeDB; O61443; -. DR BRENDA; 2.7.11.24; 1994. DR Reactome; R-DME-168638; NOD1/2 Signaling Pathway. DR Reactome; R-DME-171007; p38MAPK events. DR Reactome; R-DME-198753; ERK/MAPK targets. DR Reactome; R-DME-2559580; Oxidative Stress Induced Senescence. DR Reactome; R-DME-376172; DSCAM interactions. DR Reactome; R-DME-418592; ADP signalling through P2Y purinoceptor 1. DR Reactome; R-DME-432142; Platelet sensitization by LDL. DR Reactome; R-DME-4420097; VEGFA-VEGFR2 Pathway. DR Reactome; R-DME-450302; activated TAK1 mediates p38 MAPK activation. DR Reactome; R-DME-450341; Activation of the AP-1 family of transcription factors. DR Reactome; R-DME-525793; Myogenesis. DR Reactome; R-DME-5675221; Negative regulation of MAPK pathway. DR Reactome; R-DME-6798695; Neutrophil degranulation. DR SignaLink; O61443; -. DR BioGRID-ORCS; 34780; 0 hits in 3 CRISPR screens. DR ChiTaRS; p38b; fly. DR GenomeRNAi; 34780; -. DR PRO; PR:O61443; -. DR Proteomes; UP000000803; Chromosome 2L. DR Bgee; FBgn0024846; Expressed in adult Malpighian tubule (Drosophila) and 40 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004707; F:MAP 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; 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:0034614; P:cellular response to reactive oxygen species; IDA:FlyBase. DR GO; GO:0007623; P:circadian rhythm; IMP:FlyBase. DR GO; GO:0042742; P:defense response to bacterium; IMP:FlyBase. DR GO; GO:0050832; P:defense response to fungus; IMP:FlyBase. DR GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase. DR GO; GO:0003007; P:heart morphogenesis; IGI:FlyBase. DR GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IDA:UniProtKB. DR GO; GO:0006955; P:immune response; IMP:FlyBase. DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central. DR GO; GO:0000165; P:MAPK cascade; NAS:FlyBase. DR GO; GO:0035331; P:negative regulation of hippo signaling; IMP:FlyBase. DR GO; GO:0038066; P:p38MAPK cascade; IDA:FlyBase. DR GO; GO:0038001; P:paracrine signaling; IGI:FlyBase. DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IGI:FlyBase. DR GO; GO:0045793; P:positive regulation of cell size; IMP:FlyBase. DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:FlyBase. DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IGI:FlyBase. DR GO; GO:0006468; P:protein phosphorylation; IDA:FlyBase. DR GO; GO:0048082; P:regulation of adult chitin-containing cuticle pigmentation; IGI:FlyBase. DR GO; GO:0030510; P:regulation of BMP signaling pathway; IDA:UniProtKB. DR GO; GO:1900407; P:regulation of cellular response to oxidative stress; IMP:FlyBase. DR GO; GO:0045088; P:regulation of innate immune response; IDA:UniProtKB. DR GO; GO:2000331; P:regulation of terminal button organization; IMP:FlyBase. DR GO; GO:0009617; P:response to bacterium; IDA:FlyBase. DR GO; GO:0009408; P:response to heat; IMP:FlyBase. DR GO; GO:0042542; P:response to hydrogen peroxide; IMP:FlyBase. DR GO; GO:0009651; P:response to salt stress; IMP:FlyBase. DR GO; GO:0042594; P:response to starvation; IMP:FlyBase. DR CDD; cd07851; STKc_p38; 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; IPR008352; MAPK_p38-like. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR PANTHER; PTHR24055; MITOGEN-ACTIVATED PROTEIN KINASE; 1. DR PANTHER; PTHR24055:SF158; MITOGEN-ACTIVATED PROTEIN KINASE P38A-RELATED; 1. DR Pfam; PF00069; Pkinase; 1. DR PRINTS; PR01773; P38MAPKINASE. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS01351; MAPK; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR Genevisible; O61443; DM. PE 1: Evidence at protein level; KW ATP-binding; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; KW Reference proteome; Serine/threonine-protein kinase; Transferase. FT CHAIN 1..365 FT /note="Mitogen-activated protein kinase p38b" FT /id="PRO_0000186301" FT DOMAIN 24..311 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOTIF 183..185 FT /note="TXY" FT ACT_SITE 153 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 30..38 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 183 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 185 FT /note="Phosphotyrosine" FT /evidence="ECO:0000269|PubMed:18327897" SQ SEQUENCE 365 AA; 42098 MW; 3B3F217E467BAD53 CRC64; MSRKMAKFYK LDINRTEWEI PETYQNLQPV GQGAYGQVCK AVVRGTSTKV AIKKLARPFQ SAVHAKRTYR ELRLLKHMDH ENVIGLLDVF HPGQPADSLD QFQQVYMVTH LMDADLNNII RTQKLSDDHV QFLVYQILRG LKYIHSAGVI HRDLKPSNIA VNEDCELRIL DFGLARPAES EMTGYVATRW YRAPEIMLNW MHYNQTADIW SVGCIMAELL TGRTLFPGTD HIHQLNLIME VLGTPADEFM SRISSESARN YIRSLPVMPR RNFRDIFRGA NPLAIDLLEK MLELDADKRI TAEQALAHPY MEKYHDPTDE QTAALYDQSF EENELPVEKW REMVFSEVTA FKPTAAFAEL LPKEQ //