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MAP kinase-activated protein kinase 2 (MAPK-activated protein kinase 2) (MAPKAP kinase 2) (MAPKAPK-2) (EC 2.7.11.1)

 MAPK2_DROME             Reviewed;         359 AA.
P49071; Q9W480;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
25-OCT-2017, entry version 147.
RecName: Full=MAP kinase-activated protein kinase 2;
Short=MAPK-activated protein kinase 2;
Short=MAPKAP kinase 2;
Short=MAPKAPK-2;
EC=2.7.11.1;
Name=MAPk-Ak2; ORFNames=CG3086;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BIC-D(R26); TISSUE=Ovary;
PubMed=7590268; DOI=10.1016/0378-1119(95)00279-F;
Larochelle S., Suter B.;
"The Drosophila melanogaster homolog of the mammalian MAPK-activated
protein kinase-2 (MAPKAPK-2) lacks a proline-rich N-terminus.";
Gene 163:209-214(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
-!- FUNCTION: Its physiological substrate seems to be the small heat
shock protein (HSP27/HSP25). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- PTM: Phosphorylated and activated by MAP kinase. {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
Ser/Thr protein kinase family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; U20757; AAA86885.1; -; mRNA.
EMBL; AE014298; AAG22408.1; -; Genomic_DNA.
PIR; JC4297; JC4297.
RefSeq; NP_001188547.1; NM_001201618.1.
RefSeq; NP_001245536.1; NM_001258607.2.
RefSeq; NP_524769.1; NM_080030.5.
RefSeq; NP_788861.1; NM_176688.3.
UniGene; Dm.1442; -.
ProteinModelPortal; P49071; -.
SMR; P49071; -.
BioGrid; 69137; 6.
DIP; DIP-21714N; -.
IntAct; P49071; 4.
MINT; MINT-760885; -.
STRING; 7227.FBpp0070802; -.
PaxDb; P49071; -.
PRIDE; P49071; -.
EnsemblMetazoa; FBtr0070837; FBpp0070802; FBgn0013987.
EnsemblMetazoa; FBtr0070839; FBpp0070804; FBgn0013987.
EnsemblMetazoa; FBtr0302940; FBpp0292066; FBgn0013987.
EnsemblMetazoa; FBtr0308577; FBpp0300801; FBgn0013987.
GeneID; 44573; -.
KEGG; dme:Dmel_CG3086; -.
CTD; 44573; -.
FlyBase; FBgn0013987; MAPk-Ak2.
eggNOG; KOG0604; Eukaryota.
eggNOG; ENOG410XP8F; LUCA.
GeneTree; ENSGT00900000140876; -.
InParanoid; P49071; -.
KO; K04443; -.
OMA; CRHIVNI; -.
OrthoDB; EOG091G14PL; -.
PhylomeDB; P49071; -.
BRENDA; 2.7.11.1; 1994.
Reactome; R-DME-171007; p38MAPK events.
Reactome; R-DME-199920; CREB phosphorylation.
Reactome; R-DME-2559580; Oxidative Stress Induced Senescence.
Reactome; R-DME-3371453; Regulation of HSF1-mediated heat shock response.
Reactome; R-DME-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-DME-450302; activated TAK1 mediates p38 MAPK activation.
Reactome; R-DME-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
SignaLink; P49071; -.
GenomeRNAi; 44573; -.
PRO; PR:P49071; -.
Proteomes; UP000000803; Chromosome X.
Bgee; FBgn0013987; -.
Genevisible; P49071; DM.
GO; GO:0005737; C:cytoplasm; ISS:FlyBase.
GO; GO:0005634; C:nucleus; ISS:FlyBase.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0009931; F:calcium-dependent protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IBA:GO_Central.
GO; GO:0051019; F:mitogen-activated protein kinase binding; IBA:GO_Central.
GO; GO:0004672; F:protein kinase activity; ISS:FlyBase.
GO; GO:0004674; F:protein serine/threonine kinase activity; NAS:FlyBase.
GO; GO:0004871; F:signal transducer activity; IBA:GO_Central.
GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
GO; GO:0045793; P:positive regulation of cell size; IGI:FlyBase.
GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
GO; GO:0006468; P:protein phosphorylation; ISS:FlyBase.
GO; GO:0046328; P:regulation of JNK cascade; IGI:FlyBase.
GO; GO:0009651; P:response to salt stress; IMP:FlyBase.
Gene3D; 4.10.1170.10; -; 1.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR027442; MAPKAPK_C.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
2: Evidence at transcript level;
ATP-binding; Complete proteome; Kinase; Nucleotide-binding;
Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
Transferase.
CHAIN 1 359 MAP kinase-activated protein kinase 2.
/FTId=PRO_0000086291.
DOMAIN 20 281 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 26 34 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 142 142 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 49 49 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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


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