MK38B_DROME
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 03-AUG-2022, entry version 197.
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, 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}.
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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; O61443; -.
DR PRIDE; O61443; -.
DR DNASU; 34780; -.
DR EnsemblMetazoa; FBtr0080534; FBpp0080111; FBgn0024846.
DR GeneID; 34780; -.
DR KEGG; dme:Dmel_CG7393; -.
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; YTDLNPV; -.
DR OrthoDB; 683132at2759; -.
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 Reactome; R-DME-6804756; Regulation of TP53 Activity through Phosphorylation.
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 tissues.
DR Genevisible; O61443; DM.
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 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 Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR01773; P38MAPKINASE.
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.
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
