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Protein

Stress-activated protein kinase JNK

Gene

bsk

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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 (PubMed:9224720). Component of the immune response activated by bacterial infection, and is involved in wound healing and in dorsal closure, a morphogenetic movement during embryogenesis (PubMed:8946915, PubMed:9224720, PubMed:10433922, PubMed:11784101). Functions in the systematic response to wounding acting downstream of the Hayan-phenoloxidase PPO1 cascade (PubMed:22227521). Exhibits cytoprotective activity in neuronal cells in response to wounding to the integument (PubMed:22227521). Controls the expression of a phosphatase, puckered, at the edges of wounded epidermal tissue and in the dorsal epithelium during dorsal closure (PubMed:10433922, PubMed:11784101).5 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Mg2+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)DescriptionActionsGraphical viewLength
Binding sitei53ATPPROSITE-ProRule annotation1
Active sitei149Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi31 – 36ATPPROSITE-ProRule annotation6

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • JUN kinase activity Source: UniProtKB
  • protein kinase activity Source: FlyBase
  • protein serine/threonine kinase activity Source: Reactome

GO - Biological processi

  • antibacterial humoral response Source: FlyBase
  • axon extension Source: FlyBase
  • axon guidance Source: FlyBase
  • border follicle cell migration Source: FlyBase
  • cellular response to arsenic-containing substance Source: FlyBase
  • cellular response to cadmium ion Source: FlyBase
  • cellular response to oxidative stress Source: FlyBase
  • cellular response to reactive oxygen species Source: FlyBase
  • collateral sprouting of injured axon Source: FlyBase
  • determination of digestive tract left/right asymmetry Source: FlyBase
  • dorsal appendage formation Source: FlyBase
  • dorsal closure Source: FlyBase
  • dorsal closure, spreading of leading edge cells Source: UniProtKB
  • embryonic anterior midgut (ectodermal) morphogenesis Source: FlyBase
  • engulfment of apoptotic cell Source: FlyBase
  • establishment of planar polarity Source: FlyBase
  • imaginal disc-derived male genitalia morphogenesis Source: FlyBase
  • imaginal disc fusion, thorax closure Source: FlyBase
  • JNK cascade Source: UniProtKB
  • JUN phosphorylation Source: FlyBase
  • long-term memory Source: FlyBase
  • MAPK cascade Source: FlyBase
  • melanization defense response Source: FlyBase
  • micropyle formation Source: FlyBase
  • mushroom body development Source: FlyBase
  • negative regulation of JUN kinase activity Source: FlyBase
  • neuron development Source: FlyBase
  • neuron projection morphogenesis Source: FlyBase
  • ovarian follicle cell development Source: FlyBase
  • positive regulation of autophagy Source: FlyBase
  • positive regulation of border follicle cell migration Source: UniProtKB
  • positive regulation of gene expression Source: UniProtKB
  • positive regulation of neuron remodeling Source: FlyBase
  • protein phosphorylation Source: FlyBase
  • regulation of gene expression Source: GO_Central
  • response to heat Source: FlyBase
  • response to oxidative stress Source: FlyBase
  • wound healing Source: UniProtKB
  • wound healing, spreading of epidermal cells Source: FlyBase

Keywordsi

Molecular functionDevelopmental protein, Kinase, Serine/threonine-protein kinase, Transferase
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.24 1994
ReactomeiR-DME-193648 NRAGE signals death through JNK
R-DME-209397 Formation of the cytosolic BSK 'scaffolding complex'
R-DME-209409 Formation of the nuclear AP-1 transcription factor 'scaffolding complex'
R-DME-209425 Transcriptional activtion by AP-1 transcription factor
R-DME-209478 Dephosphorylation of BSK
R-DME-2559580 Oxidative Stress Induced Senescence
R-DME-2871796 FCERI mediated MAPK activation
R-DME-450321 JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1
R-DME-450341 Activation of the AP-1 family of transcription factors
R-DME-9007892 Interleukin-38 signaling
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:bskImported
Synonyms:JNKImported
ORF Names:CG5680Imported
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0000229 bsk

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi225G → E in BSK-1; defect in dorsal closure. 1 Publication1
Mutagenesisi316 – 372Missing in BSK-2; defect in dorsal closure. 1 PublicationAdd BLAST57

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001862711 – 372Stress-activated protein kinase JNKAdd BLAST372

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei181Phosphothreonine1 Publication1
Modified residuei183Phosphotyrosine1 Publication1

Post-translational modificationi

Dually phosphorylated on Thr-181 and Tyr-183, which activates the enzyme.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP92208
PRIDEiP92208

PTM databases

iPTMnetiP92208

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

Inductioni

In neuronal cells by wounding of the integument (at protein level).1 Publication

Gene expression databases

BgeeiFBgn0000229
ExpressionAtlasiP92208 differential
GenevisibleiP92208 DM

Interactioni

Subunit structurei

Interacts with MKP-4 (via tyrosine-protein phosphatase domain); the interaction dephosphorylates bsk.1 Publication

Protein-protein interaction databases

BioGridi69288109 interactors.
DIPiDIP-17307N
IntActiP92208 32 interactors.
STRINGi7227.FBpp0079676

Structurei

Secondary structure

1372
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 13Combined sources6
Beta strandi16 – 21Combined sources6
Beta strandi24 – 29Combined sources6
Beta strandi38 – 43Combined sources6
Turni44 – 47Combined sources4
Beta strandi48 – 56Combined sources9
Helixi62 – 77Combined sources16
Beta strandi87 – 90Combined sources4
Beta strandi93 – 95Combined sources3
Turni96 – 98Combined sources3
Beta strandi101 – 107Combined sources7
Beta strandi110 – 112Combined sources3
Helixi113 – 118Combined sources6
Helixi123 – 142Combined sources20
Helixi152 – 154Combined sources3
Beta strandi155 – 157Combined sources3
Beta strandi163 – 165Combined sources3
Helixi192 – 195Combined sources4
Helixi204 – 218Combined sources15
Helixi228 – 239Combined sources12
Helixi244 – 248Combined sources5
Helixi252 – 259Combined sources8
Helixi269 – 272Combined sources4
Helixi275 – 277Combined sources3
Helixi285 – 300Combined sources16
Helixi305 – 307Combined sources3
Helixi311 – 316Combined sources6
Turni318 – 320Combined sources3
Helixi321 – 323Combined sources3
Helixi326 – 329Combined sources4
Helixi348 – 361Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5AWMX-ray1.79A1-372[»]
ProteinModelPortaliP92208
SMRiP92208
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini24 – 320Protein kinasePROSITE-ProRule annotationAdd BLAST297

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi181 – 183TXY3

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0665 Eukaryota
ENOG410XSHI LUCA
GeneTreeiENSGT00550000074271
InParanoidiP92208
KOiK04440
OMAiMSRHFLY
OrthoDBiEOG091G09G2
PhylomeDBiP92208

Family and domain databases

InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR003527 MAP_kinase_CS
IPR008351 MAPK_JNK
IPR000719 Prot_kinase_dom
IPR008271 Ser/Thr_kinase_AS
PfamiView protein in Pfam
PF00069 Pkinase, 1 hit
PRINTSiPR01772 JNKMAPKINASE
SMARTiView protein in SMART
SM00220 S_TKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS01351 MAPK, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

Sequencei

Sequence statusi: Complete.

P92208-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTAQHQHYT VEVGDTNFTI HSRYINLRPI GSGAQGIVCA AYDTITQQNV
60 70 80 90 100
AIKKLSRPFQ NVTHAKRAYR EFKLMKLVNH KNIIGLLNAF TPQRNLEEFQ
110 120 130 140 150
DVYLVMELMD ANLCQVIQMD LDHDRMSYLL YQMLCGIKHL HSAGIIHRDL
160 170 180 190 200
KPSNIVVKAD CTLKILDFGL ARTAGTTFMM TPYVVTRYYR APEVILGMGY
210 220 230 240 250
TENVDIWSVG CIMGEMIRGG VLFPGTDHID QWNKIIEQLG TPSPSFMQRL
260 270 280 290 300
QPTVRNYVEN RPRYTGYSFD RLFPDGLFPN DNNQNSRRKA SDARNLLSKM
310 320 330 340 350
LVIDPEQRIS VDEALKHEYI NVWYDAEEVD APAPEPYDHS VDEREHTVEQ
360 370
WKELIYEEVM DYEAHNTNNR TR
Length:372
Mass (Da):43,027
Last modified:May 1, 1997 - v1
Checksum:i96662B278ABCCA19
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti331 – 372APAPE…NNRTR → RPLRSHMITAWTKGNTLWSS GRS in AAC47325 (PubMed:8946916).CuratedAdd BLAST42

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_001169461.3
NP_723541.1, NM_164900.3
UniGeneiDm.1448

Genome annotation databases

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

Similar proteinsi

Entry informationi

Entry nameiJNK_DROME
AccessioniPrimary (citable) accession number: P92208
Secondary accession number(s): O01366, Q94542
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: May 1, 1997
Last modified: March 28, 2018
This is version 172 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome