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O62618

- MK14A_DROME

UniProt

O62618 - MK14A_DROME

Protein

Mitogen-activated protein kinase 14A

Gene

Mpk2

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      Previous versions | rss
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    Functioni

    Kinase involved in a signal transduction pathway. May down-regulate insect immunity gene expression after prolonged infection.2 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.By similarity

    Enzyme regulationi

    Activated by threonine and tyrosine phosphorylation by Mkk3 in response to environmental stress.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei54 – 541ATPPROSITE-ProRule annotation
    Active sitei154 – 1541Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi31 – 399ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. MAP kinase activity Source: FlyBase
    3. protein serine/threonine kinase activity Source: FlyBase
    4. SAP kinase activity Source: FlyBase

    GO - Biological processi

    1. cellular response to arsenic-containing substance Source: FlyBase
    2. cellular response to cadmium ion Source: FlyBase
    3. cellular response to reactive oxygen species Source: FlyBase
    4. defense response to bacterium Source: FlyBase
    5. defense response to fungus Source: FlyBase
    6. determination of adult lifespan Source: FlyBase
    7. immune response Source: FlyBase
    8. MAPK cascade Source: FlyBase
    9. mucosal immune response Source: FlyBase
    10. negative regulation of antimicrobial humoral response Source: FlyBase
    11. positive regulation of cell size Source: FlyBase
    12. protein phosphorylation Source: FlyBase
    13. regulation of adult chitin-containing cuticle pigmentation Source: FlyBase
    14. regulation of cellular response to oxidative stress Source: FlyBase
    15. response to heat Source: FlyBase
    16. response to hydrogen peroxide Source: FlyBase
    17. response to osmotic stress Source: FlyBase
    18. response to oxidative stress Source: FlyBase
    19. response to starvation Source: FlyBase

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.24. 1994.
    ReactomeiREACT_180302. KSRP destabilizes mRNA.
    REACT_181712. Oxidative Stress Induced Senescence.
    REACT_203135. Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
    REACT_34513. DSCAM interactions.
    SignaLinkiO62618.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitogen-activated protein kinase 14A (EC:2.7.11.24)
    Short name:
    MAP kinase 14A
    Short name:
    MAPK 14A
    Alternative name(s):
    MAP kinase p38a
    Short name:
    D-p38a
    p38 MAPK
    Short name:
    Dp38
    Gene namesi
    Name:Mpk2
    Synonyms:p38a
    ORF Names:CG5475
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3R

    Organism-specific databases

    FlyBaseiFBgn0015765. Mpk2.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. nucleus Source: FlyBase

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 366366Mitogen-activated protein kinase 14APRO_0000186300Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei184 – 1841PhosphothreonineBy similarity
    Modified residuei186 – 1861Phosphotyrosine1 Publication

    Post-translational modificationi

    Dually phosphorylated on Thr-184 and Tyr-186, which activates the enzyme.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiO62618.
    PRIDEiO62618.

    Expressioni

    Developmental stagei

    Expressed both maternally and zygotically. Levels are highest at the preblastoderm stage but low levels are present throughout development.1 Publication

    Gene expression databases

    BgeeiO62618.

    Interactioni

    Protein-protein interaction databases

    BioGridi67799. 4 interactions.
    IntActiO62618. 2 interactions.
    MINTiMINT-4080391.
    STRINGi7227.FBpp0083966.

    Structurei

    3D structure databases

    ProteinModelPortaliO62618.
    SMRiO62618. Positions 9-356.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini25 – 312288Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi184 – 1863TXY

    Domaini

    The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00550000074271.
    InParanoidiO62618.
    KOiK04441.
    OMAiLNLIMEM.
    OrthoDBiEOG7PCJGV.
    PhylomeDBiO62618.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR003527. MAP_kinase_CS.
    IPR008352. MAPK_p38.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    PRINTSiPR01773. P38MAPKINASE.
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS01351. MAPK. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O62618-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSVSITKKFY KLDINRTEWE IPDIYQDLQP VGSGAYGQVS KAVVRGTNMH    50
    VAIKKLARPF QSAVHAKRTY RELRLLKHMD HENVIGLLDI FHPHPANGSL 100
    ENFQQVYLVT HLMDADLNNI IRMQHLSDDH VQFLVYQILR GLKYIHSAGV 150
    IHRDLKPSNI AVNEDCELRI LDFGLARPTE NEMTGYVATR WYRAPEIMLN 200
    WMHYDQTVDI WSVGCIMAEL ITRRTLFPGT DHIHQLNLIM EMLGTPPAEF 250
    LKKISSESAR SYIQSLPPMK GRSFKNVFKN ANPLAIDLLE KMLELDAEKR 300
    ITAEEALSHP YLEKYAEPSV EQTSPPYDHS FEDMDLPVDK WKELIYKEVT 350
    NFKPPPSYAQ VLKDVK 366
    Length:366
    Mass (Da):42,256
    Last modified:August 1, 1998 - v1
    Checksum:iB3592B869F97990E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti27 – 271D → G in AAB97138. (PubMed:9584193)Curated
    Sequence conflicti77 – 771K → R(PubMed:1378625)Curated
    Sequence conflicti80 – 801D → A in AAB97138. (PubMed:9584193)Curated
    Sequence conflicti108 – 1081L → LL(PubMed:1378625)Curated
    Sequence conflicti124 – 1241Q → QQ(PubMed:1378625)Curated
    Sequence conflicti149 – 1491Missing(PubMed:1378625)Curated
    Sequence conflicti163 – 1631N → NN(PubMed:1378625)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U86867 mRNA. Translation: AAB97138.1.
    AF035546 Genomic DNA. Translation: AAC39030.1.
    AF035547 mRNA. Translation: AAC39031.1.
    AE014297 Genomic DNA. Translation: AAF56244.1.
    AE014297 Genomic DNA. Translation: AAN13984.1.
    AY071670 mRNA. Translation: AAL49292.1.
    RefSeqiNP_001163711.1. NM_001170240.2.
    NP_477163.1. NM_057815.5.
    NP_732959.1. NM_170126.5.
    UniGeneiDm.2996.

    Genome annotation databases

    EnsemblMetazoaiFBtr0084580; FBpp0083965; FBgn0015765.
    FBtr0084581; FBpp0083966; FBgn0015765.
    FBtr0300572; FBpp0289799; FBgn0015765.
    GeneIDi42866.
    KEGGidme:Dmel_CG5475.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U86867 mRNA. Translation: AAB97138.1 .
    AF035546 Genomic DNA. Translation: AAC39030.1 .
    AF035547 mRNA. Translation: AAC39031.1 .
    AE014297 Genomic DNA. Translation: AAF56244.1 .
    AE014297 Genomic DNA. Translation: AAN13984.1 .
    AY071670 mRNA. Translation: AAL49292.1 .
    RefSeqi NP_001163711.1. NM_001170240.2.
    NP_477163.1. NM_057815.5.
    NP_732959.1. NM_170126.5.
    UniGenei Dm.2996.

    3D structure databases

    ProteinModelPortali O62618.
    SMRi O62618. Positions 9-356.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 67799. 4 interactions.
    IntActi O62618. 2 interactions.
    MINTi MINT-4080391.
    STRINGi 7227.FBpp0083966.

    Proteomic databases

    PaxDbi O62618.
    PRIDEi O62618.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0084580 ; FBpp0083965 ; FBgn0015765 .
    FBtr0084581 ; FBpp0083966 ; FBgn0015765 .
    FBtr0300572 ; FBpp0289799 ; FBgn0015765 .
    GeneIDi 42866.
    KEGGi dme:Dmel_CG5475.

    Organism-specific databases

    CTDi 42866.
    FlyBasei FBgn0015765. Mpk2.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00550000074271.
    InParanoidi O62618.
    KOi K04441.
    OMAi LNLIMEM.
    OrthoDBi EOG7PCJGV.
    PhylomeDBi O62618.

    Enzyme and pathway databases

    BRENDAi 2.7.11.24. 1994.
    Reactomei REACT_180302. KSRP destabilizes mRNA.
    REACT_181712. Oxidative Stress Induced Senescence.
    REACT_203135. Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
    REACT_34513. DSCAM interactions.
    SignaLinki O62618.

    Miscellaneous databases

    GenomeRNAii 42866.
    NextBioi 830992.

    Gene expression databases

    Bgeei O62618.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR003527. MAP_kinase_CS.
    IPR008352. MAPK_p38.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    PRINTSi PR01773. P38MAPKINASE.
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS01351. MAPK. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and characterization of a Drosophila p38 mitogen-activated protein kinase."
      Han S.-J., Choi K.-Y., Brey P.T., Lee W.-J.
      J. Biol. Chem. 273:369-374(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION AT TYR-186, FUNCTION, SUBCELLULAR LOCATION, ENZYME REGULATION.
      Tissue: Hemocyte.
    2. "A conserved p38 mitogen-activated protein kinase pathway regulates Drosophila immunity gene expression."
      Han Z.S., Enslen H., Hu X., Meng X., Wu I.-H., Barrett T., Davis R.J., Ip Y.T.
      Mol. Cell. Biol. 18:3527-3539(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, DEVELOPMENTAL STAGE, ENZYME REGULATION.
      Tissue: Embryo.
    3. "The genome sequence of Drosophila melanogaster."
      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.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    4. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Head.
    6. "Primary structure, expression, and signal-dependent tyrosine phosphorylation of a Drosophila homolog of extracellular signal-regulated kinase."
      Biggs W.H. III, Zipursky S.L.
      Proc. Natl. Acad. Sci. U.S.A. 89:6295-6299(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 38-188.
      Tissue: Imaginal disk.

    Entry informationi

    Entry nameiMK14A_DROME
    AccessioniPrimary (citable) accession number: O62618
    Secondary accession number(s): A4V3C0, O46216, Q9TXB4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 2, 2001
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 132 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3