ID MAPK2_DROME Reviewed; 359 AA. AC P49071; Q9W480; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 07-JUN-2017, entry version 143. DE RecName: Full=MAP kinase-activated protein kinase 2; DE Short=MAPK-activated protein kinase 2; DE Short=MAPKAP kinase 2; DE Short=MAPKAPK-2; DE EC=2.7.11.1; GN Name=MAPk-Ak2; ORFNames=CG3086; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BIC-D(R26); TISSUE=Ovary; RX PubMed=7590268; DOI=10.1016/0378-1119(95)00279-F; RA Larochelle S., Suter B.; RT "The Drosophila melanogaster homolog of the mammalian MAPK-activated RT protein kinase-2 (MAPKAPK-2) lacks a proline-rich N-terminus."; RL Gene 163:209-214(1995). RN [2] 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., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA 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., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA 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., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., RA Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] 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., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). CC -!- FUNCTION: Its physiological substrate seems to be the small heat CC shock protein (HSP27/HSP25). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- PTM: Phosphorylated and activated by MAP kinase. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK CC Ser/Thr protein kinase family. {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; U20757; AAA86885.1; -; mRNA. DR EMBL; AE014298; AAG22408.1; -; Genomic_DNA. DR PIR; JC4297; JC4297. DR RefSeq; NP_001188547.1; NM_001201618.1. DR RefSeq; NP_001245536.1; NM_001258607.2. DR RefSeq; NP_524769.1; NM_080030.5. DR RefSeq; NP_788861.1; NM_176688.3. DR UniGene; Dm.1442; -. DR ProteinModelPortal; P49071; -. DR SMR; P49071; -. DR BioGrid; 69137; 3. DR DIP; DIP-21714N; -. DR IntAct; P49071; 4. DR MINT; MINT-760885; -. DR STRING; 7227.FBpp0070802; -. DR PaxDb; P49071; -. DR PRIDE; P49071; -. DR EnsemblMetazoa; FBtr0070837; FBpp0070802; FBgn0013987. DR EnsemblMetazoa; FBtr0070839; FBpp0070804; FBgn0013987. DR EnsemblMetazoa; FBtr0302940; FBpp0292066; FBgn0013987. DR EnsemblMetazoa; FBtr0308577; FBpp0300801; FBgn0013987. DR GeneID; 44573; -. DR KEGG; dme:Dmel_CG3086; -. DR CTD; 44573; -. DR FlyBase; FBgn0013987; MAPk-Ak2. DR eggNOG; KOG0604; Eukaryota. DR eggNOG; ENOG410XP8F; LUCA. DR GeneTree; ENSGT00830000128274; -. DR InParanoid; P49071; -. DR KO; K04443; -. DR OMA; CRHIVNI; -. DR OrthoDB; EOG091G14PL; -. DR PhylomeDB; P49071; -. DR BRENDA; 2.7.11.1; 1994. DR Reactome; R-DME-171007; p38MAPK events. DR Reactome; R-DME-199920; CREB phosphorylation. DR Reactome; R-DME-2559580; Oxidative Stress Induced Senescence. DR Reactome; R-DME-3371453; Regulation of HSF1-mediated heat shock response. DR Reactome; R-DME-4420097; VEGFA-VEGFR2 Pathway. DR Reactome; R-DME-450302; activated TAK1 mediates p38 MAPK activation. DR Reactome; R-DME-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA. DR SignaLink; P49071; -. DR GenomeRNAi; 44573; -. DR PRO; PR:P49071; -. DR Proteomes; UP000000803; Chromosome X. DR Bgee; FBgn0013987; -. DR Genevisible; P49071; DM. DR GO; GO:0005737; C:cytoplasm; ISS:FlyBase. DR GO; GO:0005634; C:nucleus; ISS:FlyBase. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0009931; F:calcium-dependent protein serine/threonine kinase activity; IBA:GO_Central. DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central. DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IBA:GO_Central. DR GO; GO:0004672; F:protein kinase activity; ISS:FlyBase. DR GO; GO:0004674; F:protein serine/threonine kinase activity; NAS:FlyBase. DR GO; GO:0004871; F:signal transducer activity; IBA:GO_Central. DR GO; GO:0007155; P:cell adhesion; IMP:FlyBase. DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central. DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central. DR GO; GO:0045793; P:positive regulation of cell size; IGI:FlyBase. DR GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central. DR GO; GO:0006468; P:protein phosphorylation; ISS:FlyBase. DR GO; GO:0008360; P:regulation of cell shape; IMP:FlyBase. DR GO; GO:0046328; P:regulation of JNK cascade; IGI:FlyBase. DR GO; GO:0009651; P:response to salt stress; IMP:FlyBase. DR Gene3D; 4.10.1170.10; -; 1. DR InterPro; IPR011009; Kinase-like_dom. DR InterPro; IPR027442; MAPKAPK_C. 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 SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 2: Evidence at transcript level; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase; KW Transferase. FT CHAIN 1 359 MAP kinase-activated protein kinase 2. FT /FTId=PRO_0000086291. FT DOMAIN 20 281 Protein kinase. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT NP_BIND 26 34 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT ACT_SITE 142 142 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU00159, ECO:0000255|PROSITE- FT ProRule:PRU10027}. FT BINDING 49 49 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. SQ SEQUENCE 359 AA; 41401 MW; 69C5F9A94D1511EC CRC64; MLSLQNQRQP KTTPLTDDYV TSNTVLGYGI NGKVVQCTHR RTQQNYALKV LLDSERARRE VDLHWRVSGC RYIVNIIDVY ENTFKDRKCL LVVMECMEGG ELFQRIQDKA DGAFTEREAA QIMHEICAAV DYLHSRDIAH RDLKPENLLY TTTQPNATLK LTDFGFAKET FTSYTLQTPC YTPYYVAPEV LGPEKYDKSC DIWSLGVVMY IIMCGFPPFY SNHGLAISPG MKNRIRTGQY DFPDPEWTNV SQAAKDLIKG MLNVDPSKRL RIQDVISNKW IAQYNAVPQT PLCTGRMLKE AEETWPEVQE EMTRSLATMR VDYDQMQIKA LDKSNNPLLT KRRKKIEEME LYMANATRN //