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O61443

- MK14B_DROME

UniProt

O61443 - MK14B_DROME

Protein

Mitogen-activated protein kinase 14B

Gene

p38b

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 140 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      Previous versions | rss
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    Functioni

    Kinase involved in dpp signal transduction pathway in the process of wing morphogenesis when the levels of dpp are enhanced or inhibited. 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 Mkk3.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei53 – 531ATPPROSITE-ProRule annotation
    Active sitei153 – 1531Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi30 – 389ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. MAP kinase activity Source: FlyBase
    3. protein serine/threonine kinase activity Source: UniProtKB
    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. imaginal disc-derived wing morphogenesis Source: UniProtKB
    8. immune response Source: FlyBase
    9. MAPK cascade Source: FlyBase
    10. positive regulation of cell size Source: FlyBase
    11. positive regulation of multicellular organism growth Source: FlyBase
    12. positive regulation of protein phosphorylation Source: FlyBase
    13. protein phosphorylation Source: FlyBase
    14. regulation of adult chitin-containing cuticle pigmentation Source: FlyBase
    15. regulation of BMP signaling pathway Source: UniProtKB
    16. regulation of cellular response to oxidative stress Source: FlyBase
    17. regulation of innate immune response Source: UniProtKB
    18. regulation of terminal button organization Source: FlyBase
    19. response to bacterium Source: FlyBase
    20. response to heat Source: FlyBase
    21. response to hydrogen peroxide Source: FlyBase
    22. response to salt stress Source: FlyBase
    23. 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.
    SignaLinkiO61443.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitogen-activated protein kinase 14B (EC:2.7.11.24)
    Short name:
    MAP kinase 14B
    Short name:
    MAPK 14B
    Alternative name(s):
    MAP kinase p38b
    Short name:
    D-p38b
    Gene namesi
    Name:p38b
    ORF Names:CG7393
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2L

    Organism-specific databases

    FlyBaseiFBgn0024846. p38b.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 365365Mitogen-activated protein kinase 14BPRO_0000186301Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei183 – 1831Phosphothreonine1 Publication
    Modified residuei185 – 1851Phosphotyrosine1 Publication

    Post-translational modificationi

    Dually phosphorylated on Thr-183 and Tyr-185, which activates the enzyme.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiO61443.
    PRIDEiO61443.

    Expressioni

    Tissue specificityi

    At mid-embryogenesis, highest expression is seen in developing anterior and posterior midguts. Almost ubiquitous expression throughout all development.

    Developmental stagei

    Expressed both maternally and zygotically in the embryo, expression seen in all developmental stages.

    Gene expression databases

    BgeeiO61443.

    Interactioni

    Protein-protein interaction databases

    BioGridi60814. 12 interactions.
    DIPiDIP-22779N.
    IntActiO61443. 6 interactions.
    MINTiMINT-760858.
    STRINGi7227.FBpp0080111.

    Structurei

    3D structure databases

    ProteinModelPortaliO61443.
    SMRiO61443. Positions 8-353.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini24 – 311288Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi183 – 1853TXY

    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.
    InParanoidiO61443.
    KOiK04441.
    OMAiDIFRGAN.
    OrthoDBiEOG7PCJGV.
    PhylomeDBiO61443.

    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.

    O61443-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSRKMAKFYK LDINRTEWEI PETYQNLQPV GQGAYGQVCK AVVRGTSTKV    50
    AIKKLARPFQ SAVHAKRTYR ELRLLKHMDH ENVIGLLDVF HPGQPADSLD 100
    QFQQVYMVTH LMDADLNNII RTQKLSDDHV QFLVYQILRG LKYIHSAGVI 150
    HRDLKPSNIA VNEDCELRIL DFGLARPAES EMTGYVATRW YRAPEIMLNW 200
    MHYNQTADIW SVGCIMAELL TGRTLFPGTD HIHQLNLIME VLGTPADEFM 250
    SRISSESARN YIRSLPVMPR RNFRDIFRGA NPLAIDLLEK MLELDADKRI 300
    TAEQALAHPY MEKYHDPTDE QTAALYDQSF EENELPVEKW REMVFSEVTA 350
    FKPTAAFAEL LPKEQ 365
    Length:365
    Mass (Da):42,098
    Last modified:August 1, 1998 - v1
    Checksum:i3B3F217E467BAD53
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF035548 mRNA. Translation: AAC39032.1.
    AB006364 mRNA. Translation: BAA35141.1.
    AE014134 Genomic DNA. Translation: AAF53326.1.
    AY058548 mRNA. Translation: AAL13777.1.
    RefSeqiNP_477361.1. NM_058013.4.
    UniGeneiDm.2953.

    Genome annotation databases

    EnsemblMetazoaiFBtr0080534; FBpp0080111; FBgn0024846.
    GeneIDi34780.
    KEGGidme:Dmel_CG7393.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF035548 mRNA. Translation: AAC39032.1 .
    AB006364 mRNA. Translation: BAA35141.1 .
    AE014134 Genomic DNA. Translation: AAF53326.1 .
    AY058548 mRNA. Translation: AAL13777.1 .
    RefSeqi NP_477361.1. NM_058013.4.
    UniGenei Dm.2953.

    3D structure databases

    ProteinModelPortali O61443.
    SMRi O61443. Positions 8-353.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 60814. 12 interactions.
    DIPi DIP-22779N.
    IntActi O61443. 6 interactions.
    MINTi MINT-760858.
    STRINGi 7227.FBpp0080111.

    Proteomic databases

    PaxDbi O61443.
    PRIDEi O61443.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0080534 ; FBpp0080111 ; FBgn0024846 .
    GeneIDi 34780.
    KEGGi dme:Dmel_CG7393.

    Organism-specific databases

    CTDi 34780.
    FlyBasei FBgn0024846. p38b.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00550000074271.
    InParanoidi O61443.
    KOi K04441.
    OMAi DIFRGAN.
    OrthoDBi EOG7PCJGV.
    PhylomeDBi O61443.

    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 O61443.

    Miscellaneous databases

    ChiTaRSi p38b. drosophila.
    GenomeRNAii 34780.
    NextBioi 790183.

    Gene expression databases

    Bgeei O61443.

    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. "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 [MRNA], FUNCTION, ENZYME REGULATION.
      Tissue: Embryo.
    2. "p38 mitogen-activated protein kinase can be involved in transforming growth factor beta superfamily signal transduction in Drosophila wing morphogenesis."
      Adachi-Yamada T., Nakamura M., Irie K., Tomoyasu Y., Sano Y., Mori E., Goto S., Ueno N., Nishida Y., Matsumoto K.
      Mol. Cell. Biol. 19:2322-2329(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
      Tissue: Imaginal disk.
    3. "An exploration of the sequence of a 2.9-Mb region of the genome of Drosophila melanogaster: the Adh region."
      Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T., Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., Harvey D.A., Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., Moshrefi A.R.
      , Palazzolo M., Reese M.G., Spradling A.C., Tsang G., Wan K.H., Whitelaw K., Celniker S.E., Rubin G.M.
      Genetics 153:179-219(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    4. "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.
    5. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Embryo.
    7. "Phosphoproteome analysis of Drosophila melanogaster embryos."
      Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
      J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryo.

    Entry informationi

    Entry nameiMK14B_DROME
    AccessioniPrimary (citable) accession number: O61443
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 2, 2002
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 140 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