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P92208 (JNK_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Stress-activated protein kinase JNK

Short name=dJNK
EC=2.7.11.24
Alternative name(s):
Protein basket
Gene names
Name:bsk
Synonyms:JNK
ORF Names:CG5680
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length372 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.6 Ref.7 Ref.8

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium By similarity.

Enzyme regulation

Activated by threonine and tyrosine phosphorylation by the dual specificity kinase, hep. Inhibited by dual specificity phosphatase, puckered. Ref.7

Subcellular location

Cytoplasm By similarity.

Tissue specificity

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. Ref.1 Ref.2

Developmental stage

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

Domain

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

Post-translational modification

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

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily.

Contains 1 protein kinase domain.

Sequence caution

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

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Kinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processJNK cascade

Inferred from direct assay Ref.1. Source: UniProtKB

JUN phosphorylation

Inferred from mutant phenotype PubMed 11439243. Source: FlyBase

MAPK cascade

Non-traceable author statement PubMed 10878576. Source: FlyBase

Wnt signaling pathway

Non-traceable author statement PubMed 12231350. Source: FlyBase

antibacterial humoral response

Inferred from direct assay Ref.1. Source: FlyBase

axon extension

Inferred from mutant phenotype PubMed 17032066. Source: FlyBase

axon guidance

Inferred from mutant phenotype PubMed 18516287. Source: FlyBase

border follicle cell migration

Inferred from genetic interaction PubMed 17483425. Source: FlyBase

cellular response to arsenic-containing substance

Inferred from direct assay PubMed 16451733. Source: FlyBase

cellular response to cadmium ion

Inferred from direct assay PubMed 16451733. Source: FlyBase

cellular response to oxidative stress

Inferred from mutant phenotype PubMed 19540338. Source: FlyBase

cellular response to reactive oxygen species

Inferred from direct assay PubMed 16451733. Source: FlyBase

collateral sprouting of injured axon

Inferred from mutant phenotype PubMed 20921142. Source: FlyBase

determination of digestive tract left/right asymmetry

Inferred from genetic interaction PubMed 17915206. Source: FlyBase

dorsal appendage formation

Inferred from mutant phenotype PubMed 11543614. Source: FlyBase

dorsal closure

Inferred from genetic interaction Ref.6. Source: FlyBase

embryonic anterior midgut (ectodermal) morphogenesis

Inferred from genetic interaction PubMed 17915206. Source: FlyBase

engulfment of apoptotic cell

Inferred from mutant phenotype PubMed 22992958. Source: FlyBase

establishment of planar polarity

Non-traceable author statement PubMed 12414186. Source: FlyBase

imaginal disc fusion, thorax closure

Inferred from mutant phenotype PubMed 14585960. Source: FlyBase

imaginal disc-derived male genitalia morphogenesis

Inferred from mutant phenotype PubMed 21389055. Source: FlyBase

melanization defense response

Inferred from mutant phenotype PubMed 17356067. Source: FlyBase

micropyle formation

Inferred from mutant phenotype PubMed 11543614. Source: FlyBase

negative regulation of JUN kinase activity

Inferred from mutant phenotype PubMed 16150723. Source: FlyBase

neuron development

Inferred from mutant phenotype PubMed 20035736. Source: FlyBase

neuron projection morphogenesis

Inferred from mutant phenotype PubMed 20035736. Source: FlyBase

ovarian follicle cell development

Inferred from mutant phenotype PubMed 16542414. Source: FlyBase

positive regulation of autophagy

Inferred from mutant phenotype PubMed 19540338. Source: FlyBase

protein phosphorylation

Non-traceable author statement PubMed 10908587. Source: FlyBase

response to heat

Inferred from mutant phenotype PubMed 19627268. Source: FlyBase

response to oxidative stress

Inferred from mutant phenotype PubMed 19627268. Source: FlyBase

wound healing

Inferred from direct assay Ref.8. Source: UniProtKB

wound healing, spreading of epidermal cells

Inferred from mutant phenotype PubMed 15269788. Source: FlyBase

   Cellular_componentaxon

Inferred from direct assay PubMed 20035736. Source: FlyBase

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

dendrite

Inferred from direct assay PubMed 20035736. Source: FlyBase

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

JUN kinase activity

Inferred from direct assay Ref.1. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 11865058. Source: FlyBase

protein kinase activity

Inferred from direct assay Ref.6. Source: FlyBase

protein serine/threonine kinase activity

Non-traceable author statement PubMed 10908587. Source: FlyBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 372372Stress-activated protein kinase JNK
PRO_0000186271

Regions

Domain24 – 320297Protein kinase
Nucleotide binding31 – 366ATP By similarity
Motif181 – 1833TXY

Sites

Active site1491Proton acceptor By similarity
Binding site531ATP By similarity

Amino acid modifications

Modified residue1811Phosphothreonine By similarity
Modified residue1831Phosphotyrosine By similarity

Experimental info

Mutagenesis2251G → E in BSK-1; defect in dorsal closure.
Mutagenesis316 – 37257Missing in BSK-2; defect in dorsal closure.
Sequence conflict331 – 37242APAPE…NNRTR → RPLRSHMITAWTKGNTLWSS GRS in AAC47325. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P92208 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 96662B278ABCCA19

FASTA37243,027
        10         20         30         40         50         60 
MTTAQHQHYT VEVGDTNFTI HSRYINLRPI GSGAQGIVCA AYDTITQQNV AIKKLSRPFQ 

        70         80         90        100        110        120 
NVTHAKRAYR EFKLMKLVNH KNIIGLLNAF TPQRNLEEFQ DVYLVMELMD ANLCQVIQMD 

       130        140        150        160        170        180 
LDHDRMSYLL YQMLCGIKHL HSAGIIHRDL KPSNIVVKAD CTLKILDFGL ARTAGTTFMM 

       190        200        210        220        230        240 
TPYVVTRYYR APEVILGMGY TENVDIWSVG CIMGEMIRGG VLFPGTDHID QWNKIIEQLG 

       250        260        270        280        290        300 
TPSPSFMQRL QPTVRNYVEN RPRYTGYSFD RLFPDGLFPN DNNQNSRRKA SDARNLLSKM 

       310        320        330        340        350        360 
LVIDPEQRIS VDEALKHEYI NVWYDAEEVD APAPEPYDHS VDEREHTVEQ WKELIYEEVM 

       370 
DYEAHNTNNR TR 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
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. expand/collapse author list , 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.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[5]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001162930.1. NM_001169459.1.
NP_001162932.1. NM_001169461.2.
NP_723541.1. NM_164900.3.
UniGeneDm.1448.

3D structure databases

ProteinModelPortalP92208.
SMRP92208. Positions 9-363.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid69288. 49 interactions.
DIPDIP-17307N.
IntActP92208. 18 interactions.
MINTMINT-337077.

Proteomic databases

PaxDbP92208.
PRIDEP92208.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0080087; FBpp0079676; FBgn0000229.
FBtr0300982; FBpp0290204; FBgn0000229.
FBtr0302378; FBpp0291573; FBgn0000229.
GeneID44801.
KEGGdme:Dmel_CG5680.

Organism-specific databases

CTD44801.
FlyBaseFBgn0000229. bsk.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00550000074271.
InParanoidP92208.
KOK04440.
OMAEVMNFEE.
OrthoDBEOG7PCJGV.
PhylomeDBP92208.

Enzyme and pathway databases

BRENDA2.7.11.24. 1994.
SignaLinkP92208.

Gene expression databases

BgeeP92208.

Family and domain databases

InterProIPR011009. 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]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSPR01772. JNKMAPKINASE.
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS01351. MAPK. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi44801.
NextBio837648.

Entry information

Entry nameJNK_DROME
AccessionPrimary (citable) accession number: P92208
Secondary accession number(s): O01366, Q94542
Entry history
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: May 1, 1997
Last modified: July 9, 2014
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase