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P92208

- JNK_DROME

UniProt

P92208 - JNK_DROME

Protein

Stress-activated protein kinase JNK

Gene

bsk

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 136 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
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    Functioni

    Responds to activation by environmental stress by phosphorylating a number of transcription factors, primarily components of AP-1 such as Jra and also the transcriptional repressor aop, and thus regulates transcriptional activity. Component of the immune response activated by bacterial infection, and is involved in wound healing and in dorsal closure, a morphogenetic movement during embryogenesis. Controls the expression of a phosphatase, puckered, at the edges of wounded epidermal tissue and in the dorsal epithelium during dorsal closure.4 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.By similarity

    Enzyme regulationi

    Activated by threonine and tyrosine phosphorylation by the dual specificity kinase, hep. Inhibited by dual specificity phosphatase, puckered.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei53 – 531ATPPROSITE-ProRule annotation
    Active sitei149 – 1491Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi31 – 366ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. antibacterial humoral response Source: FlyBase
    2. axon extension Source: FlyBase
    3. axon guidance Source: FlyBase
    4. border follicle cell migration Source: FlyBase
    5. cellular response to arsenic-containing substance Source: FlyBase
    6. cellular response to cadmium ion Source: FlyBase
    7. cellular response to oxidative stress Source: FlyBase
    8. cellular response to reactive oxygen species Source: FlyBase
    9. collateral sprouting of injured axon Source: FlyBase
    10. determination of digestive tract left/right asymmetry Source: FlyBase
    11. dorsal appendage formation Source: FlyBase
    12. dorsal closure Source: FlyBase
    13. embryonic anterior midgut (ectodermal) morphogenesis Source: FlyBase
    14. engulfment of apoptotic cell Source: FlyBase
    15. establishment of planar polarity Source: FlyBase
    16. imaginal disc-derived male genitalia morphogenesis Source: FlyBase
    17. imaginal disc fusion, thorax closure Source: FlyBase
    18. JNK cascade Source: UniProtKB
    19. JUN phosphorylation Source: FlyBase
    20. MAPK cascade Source: FlyBase
    21. melanization defense response Source: FlyBase
    22. micropyle formation Source: FlyBase
    23. negative regulation of JUN kinase activity Source: FlyBase
    24. neuron development Source: FlyBase
    25. neuron projection morphogenesis Source: FlyBase
    26. ovarian follicle cell development Source: FlyBase
    27. positive regulation of autophagy Source: FlyBase
    28. protein phosphorylation Source: FlyBase
    29. response to heat Source: FlyBase
    30. response to oxidative stress Source: FlyBase
    31. Wnt signaling pathway Source: FlyBase
    32. wound healing Source: UniProtKB
    33. wound healing, spreading of epidermal cells Source: FlyBase

    Keywords - Molecular functioni

    Developmental protein, Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.24. 1994.
    ReactomeiREACT_181694. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
    REACT_181712. Oxidative Stress Induced Senescence.
    REACT_202759. FCERI mediated MAPK activation.
    REACT_34513. DSCAM interactions.
    SignaLinkiP92208.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Stress-activated protein kinase JNK (EC:2.7.11.24)
    Short name:
    dJNK
    Alternative name(s):
    Protein basket
    Gene namesi
    Name:bsk
    Synonyms:JNK
    ORF Names:CG5680
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2L

    Organism-specific databases

    FlyBaseiFBgn0000229. bsk.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. axon Source: FlyBase
    2. cytoplasm Source: UniProtKB-SubCell
    3. dendrite Source: FlyBase

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi225 – 2251G → E in BSK-1; defect in dorsal closure. 1 Publication
    Mutagenesisi316 – 37257Missing in BSK-2; defect in dorsal closure. 1 PublicationAdd
    BLAST

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 372372Stress-activated protein kinase JNKPRO_0000186271Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei181 – 1811PhosphothreonineBy similarity
    Modified residuei183 – 1831PhosphotyrosineBy similarity

    Post-translational modificationi

    Dually phosphorylated on Thr-181 and Tyr-183, which activates the enzyme.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP92208.
    PRIDEiP92208.

    Expressioni

    Tissue specificityi

    During gastrulation, expression is seen in cells undergoing morphogenetic movements. By stage 9 of embryonic development, expression is ubiquitous. At stages 12-14, expression occurs in epidermis and central nervous system. At stage 15, expression is restricted to ventral nerve cord, brain and some peripheral neurons. In larvae, expression is seen in all imaginal disks, with highest levels in wing and eye disks, and in the CNS. Adults express the protein in fat body and hemocytes.2 Publications

    Developmental stagei

    Expressed maternally and zygotically through to adult (male and female).1 Publication

    Gene expression databases

    BgeeiP92208.

    Interactioni

    Protein-protein interaction databases

    BioGridi69288. 49 interactions.
    DIPiDIP-17307N.
    IntActiP92208. 18 interactions.
    MINTiMINT-337077.

    Structurei

    3D structure databases

    ProteinModelPortaliP92208.
    SMRiP92208. Positions 9-363.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini24 – 320297Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi181 – 1833TXY

    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.
    InParanoidiP92208.
    KOiK04440.
    OMAiEVMNFEE.
    OrthoDBiEOG7PCJGV.
    PhylomeDBiP92208.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR003527. MAP_kinase_CS.
    IPR008351. MAPK_JNK.
    IPR000719. Prot_kinase_dom.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    PRINTSiPR01772. JNKMAPKINASE.
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS01351. MAPK. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P92208-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTTAQHQHYT VEVGDTNFTI HSRYINLRPI GSGAQGIVCA AYDTITQQNV    50
    AIKKLSRPFQ NVTHAKRAYR EFKLMKLVNH KNIIGLLNAF TPQRNLEEFQ 100
    DVYLVMELMD ANLCQVIQMD LDHDRMSYLL YQMLCGIKHL HSAGIIHRDL 150
    KPSNIVVKAD CTLKILDFGL ARTAGTTFMM TPYVVTRYYR APEVILGMGY 200
    TENVDIWSVG CIMGEMIRGG VLFPGTDHID QWNKIIEQLG TPSPSFMQRL 250
    QPTVRNYVEN RPRYTGYSFD RLFPDGLFPN DNNQNSRRKA SDARNLLSKM 300
    LVIDPEQRIS VDEALKHEYI NVWYDAEEVD APAPEPYDHS VDEREHTVEQ 350
    WKELIYEEVM DYEAHNTNNR TR 372
    Length:372
    Mass (Da):43,027
    Last modified:May 1, 1997 - v1
    Checksum:i96662B278ABCCA19
    GO

    Sequence cautioni

    The sequence AAC47325.1 differs from that shown. Reason: Frameshift at position 331.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti331 – 37242APAPE…NNRTR → RPLRSHMITAWTKGNTLWSS GRS in AAC47325. (PubMed:8946916)CuratedAdd
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U50965 Genomic DNA. Translation: AAB51187.1.
    U50966 Genomic DNA. Translation: AAB51188.1.
    U49180 mRNA. Translation: AAB97094.1.
    U49249 Genomic DNA. Translation: AAB48381.1.
    U73196 mRNA. Translation: AAC47325.1. Frameshift.
    AE014134 Genomic DNA. Translation: AAF52883.1.
    AY122221 mRNA. Translation: AAM52733.1.
    AY070865 mRNA. Translation: AAL48487.1.
    RefSeqiNP_001162930.1. NM_001169459.1.
    NP_001162932.1. NM_001169461.2.
    NP_723541.1. NM_164900.3.
    UniGeneiDm.1448.

    Genome annotation databases

    EnsemblMetazoaiFBtr0080087; FBpp0079676; FBgn0000229.
    FBtr0300982; FBpp0290204; FBgn0000229.
    FBtr0302378; FBpp0291573; FBgn0000229.
    GeneIDi44801.
    KEGGidme:Dmel_CG5680.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U50965 Genomic DNA. Translation: AAB51187.1 .
    U50966 Genomic DNA. Translation: AAB51188.1 .
    U49180 mRNA. Translation: AAB97094.1 .
    U49249 Genomic DNA. Translation: AAB48381.1 .
    U73196 mRNA. Translation: AAC47325.1 . Frameshift.
    AE014134 Genomic DNA. Translation: AAF52883.1 .
    AY122221 mRNA. Translation: AAM52733.1 .
    AY070865 mRNA. Translation: AAL48487.1 .
    RefSeqi NP_001162930.1. NM_001169459.1.
    NP_001162932.1. NM_001169461.2.
    NP_723541.1. NM_164900.3.
    UniGenei Dm.1448.

    3D structure databases

    ProteinModelPortali P92208.
    SMRi P92208. Positions 9-363.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 69288. 49 interactions.
    DIPi DIP-17307N.
    IntActi P92208. 18 interactions.
    MINTi MINT-337077.

    Proteomic databases

    PaxDbi P92208.
    PRIDEi P92208.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0080087 ; FBpp0079676 ; FBgn0000229 .
    FBtr0300982 ; FBpp0290204 ; FBgn0000229 .
    FBtr0302378 ; FBpp0291573 ; FBgn0000229 .
    GeneIDi 44801.
    KEGGi dme:Dmel_CG5680.

    Organism-specific databases

    CTDi 44801.
    FlyBasei FBgn0000229. bsk.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00550000074271.
    InParanoidi P92208.
    KOi K04440.
    OMAi EVMNFEE.
    OrthoDBi EOG7PCJGV.
    PhylomeDBi P92208.

    Enzyme and pathway databases

    BRENDAi 2.7.11.24. 1994.
    Reactomei REACT_181694. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
    REACT_181712. Oxidative Stress Induced Senescence.
    REACT_202759. FCERI mediated MAPK activation.
    REACT_34513. DSCAM interactions.
    SignaLinki P92208.

    Miscellaneous databases

    GenomeRNAii 44801.
    NextBioi 837648.

    Gene expression databases

    Bgeei P92208.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR003527. MAP_kinase_CS.
    IPR008351. MAPK_JNK.
    IPR000719. Prot_kinase_dom.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    PRINTSi PR01772. JNKMAPKINASE.
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS01351. MAPK. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A JNK signal transduction pathway that mediates morphogenesis and an immune response in Drosophila."
      Sluss H.K., Han Z., Barrett T., Davis R.J., Ip Y.T.
      Genes Dev. 10:2745-2758(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
      Tissue: Embryo.
    2. "The Drosophila Jun-N-terminal kinase is required for cell morphogenesis but not for DJun-dependent cell fate specification in the eye."
      Riesgo-Escovar J.R., Jenni M., Fritz A., Hafen E.
      Genes Dev. 10:2759-2768(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS, TISSUE SPECIFICITY.
      Strain: Oregon-R.
      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: Embryo and Head.
    6. "Drosophila Jun kinase regulates expression of decapentaplegic via the ETS-domain protein Aop and the AP-1 transcription factor DJun during dorsal closure."
      Riesgo-Escovar J.R., Hafen E.
      Genes Dev. 11:1717-1727(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Thorax closure in Drosophila: involvement of Fos and the JNK pathway."
      Zeitlinger J., Bohmann D.
      Development 126:3947-3956(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION.
    8. "JNK signaling pathway is required for efficient wound healing in Drosophila."
      Raemet M., Lanot R., Zachary D., Manfruelli P.
      Dev. Biol. 241:145-156(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiJNK_DROME
    AccessioniPrimary (citable) accession number: P92208
    Secondary accession number(s): O01366, Q94542
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 30, 2003
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 136 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