Reviewed, UniProtKB/Swiss-Prot P92208 (JNK_DROME)

Names and origin

Protein names

Recommended 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

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	372 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Developmental protein Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	JUN phosphorylation Inferred from mutant phenotype. Source: FlyBase Wnt receptor signaling pathway Non-traceable author statement. Source: FlyBase antibacterial humoral response Ref.1 Inferred from direct assay. Source: FlyBase axon extension Inferred from mutant phenotype. Source: FlyBase border follicle cell migration Inferred from genetic interaction. Source: FlyBase dorsal appendage formation Inferred from mutant phenotype. Source: FlyBase establishment of planar polarity Non-traceable author statement. Source: FlyBase imaginal disc fusion, thorax closure Inferred from mutant phenotype. Source: FlyBase initiation of dorsal closure Ref.2 Inferred from mutant phenotype. Source: FlyBase micropyle formation Inferred from mutant phenotype. Source: FlyBase negative regulation of JUN kinase activity Inferred from mutant phenotype. Source: FlyBase response to heat Inferred from mutant phenotype. Source: FlyBase response to oxidative stress Inferred from mutant phenotype. Source: FlyBase wound healing, spreading of epidermal cells Inferred from mutant phenotype. Source: FlyBase
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW JUN kinase activity Ref.1 Ref.2 Inferred from direct assay. Source: UniProtKB protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	Q8IMN1	1	EBI-74487,EBI-133392
Dhod	P32748	1	EBI-74487,EBI-139986
hep	Q23977	1	EBI-74487,EBI-74214
l(3)04053	Q9VNR6	1	EBI-74487,EBI-169083
Mapk8ip1	Q9WVI9	1	EBI-74487,EBI-74515	From a different organism.
spir	Q9U1K1	1	EBI-74487,EBI-91672
stv	Q9VU81	1	EBI-74487,EBI-179238

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 372	372	Stress-activated protein kinase JNK		PRO_0000186271
Regions
	Domain	24 – 320	297	Protein kinase
	Nucleotide binding	31 – 36	6	ATP By similarity
	Motif	181 – 183	3	TXY
Sites
	Active site	149	1	Proton acceptor By similarity
	Binding site	53	1	ATP By similarity
Amino acid modifications
	Modified residue	181	1	Phosphothreonine By similarity
	Modified residue	183	1	Phosphotyrosine By similarity
Experimental info
	Mutagenesis	225	1	G → E in BSK-1; defect in dorsal closure.
	Mutagenesis	316 – 372	57	Missing in BSK-2; defect in dorsal closure.
	Sequence conflict	331 – 372	42	APAPE…NNRTR → RPLRSHMITAWTKGNTLWSS GRS in AAC47325. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P92208-1 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: 96662B278ABCCA19	FASTA	372	43,027
	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

References

	« Hide 'large scale' referencesShow '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: 8946915] [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: 8946916] [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: 10731132] [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. , 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: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[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: 12537569] [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: 9224720] [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: 10433922] [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: 11784101] [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.
RefSeq	NP_001162930.1. NP_001162932.1. NP_723541.1.
3D structure databases
SMR	P92208. Positions 9-363.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-17307N.
IntAct	P92208. 32 interactions.
STRING	P92208.
Proteomic databases
PRIDE	P92208.
Genome annotation databases
Ensembl	FBtr0080087; FBpp0079676; FBgn0000229; Drosophila melanogaster. [Genome view]
GeneID	44801.
KEGG	dme:Dmel_CG5680.
NMPDR	fig|7227.3.peg.1745.
Organism-specific databases
CTD	44801.
FlyBase	FBgn0000229. bsk.
Phylogenomic databases
eggNOG	inNOG04873.
InParanoid	P92208.
OMA	EHNKLKX.
OrthoDB	EOG9JM7W5.
PhylomeDB	P92208.
Enzyme and pathway databases
BioCyc	DMEL-XXX-02:DMEL-XXX-02-008305-MONOMER.
BRENDA	2.7.11.24. 48.
Gene expression databases
ArrayExpress	P92208.
Bgee	P92208.
GermOnline	CG5680. Drosophila melanogaster.
Family and domain databases
InterPro	IPR008351. JNK_MAPK. IPR011009. Kinase-like_dom. IPR003527. MAP_kinase_CS. IPR000719. Prot_kinase_cat_dom. IPR017442. Se/Thr_prot_kinase-like_dom. IPR008271. Ser/Thr_prot_kinase_AS. IPR002290. Ser/Thr_prot_kinase_dom. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
PRINTS	PR01772. JNKMAPKINASE.
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	PS01351. MAPK. 1 hit. PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	837648.

Entry information

Entry name

JNK_DROME

Accession

Primary (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:	February 9, 2010
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project