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Entry version 187 (12 Aug 2020)
Sequence version 1 (01 May 1997)
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Protein

Stress-activated protein kinase JNK

Gene

bsk

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei53ATPPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei149Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi31 – 36ATPPROSITE-ProRule annotation6

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.11.24, 1994

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-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-209459, Imd pathway
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

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...
SignaLinki
P92208

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Stress-activated protein kinase JNK (EC:2.7.11.24)
Short name:
dJNK
Alternative name(s):
Protein basket
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:bskImported
Synonyms:JNKImported
ORF Names:CG5680Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiDrosophila melanogaster (Fruit fly)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri7227 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000803 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 2L

Organism-specific databases

Drosophila genome database

More...
FlyBasei
FBgn0000229, bsk

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi225G → E in BSK-1; defect in dorsal closure. 1 Publication1
Mutagenesisi316 – 372Missing in BSK-2; defect in dorsal closure. 1 PublicationAdd BLAST57

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001862711 – 372Stress-activated protein kinase JNKAdd BLAST372

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei181Phosphothreonine1 Publication1
Modified residuei183Phosphotyrosine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P92208

PRoteomics IDEntifications database

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PRIDEi
P92208

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P92208

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

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

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
FBgn0000229, Expressed in eye disc (Drosophila) and 63 other tissues

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P92208, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P92208, DM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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

1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
69288, 130 interactors

Database of interacting proteins

More...
DIPi
DIP-17307N

Protein interaction database and analysis system

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IntActi
P92208, 18 interactors

STRING: functional protein association networks

More...
STRINGi
7227.FBpp0079676

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1372
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P92208

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini24 – 320Protein kinasePROSITE-ProRule annotationAdd BLAST297

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi181 – 183TXY3

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0665, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000169409

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_000288_181_1_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P92208

KEGG Orthology (KO)

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KOi
K04440

Identification of Orthologs from Complete Genome Data

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OMAi
REFKLMN

Database of Orthologous Groups

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OrthoDBi
741207at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P92208

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011009, Kinase-like_dom_sf
IPR003527, MAP_kinase_CS
IPR008351, MAPK_JNK
IPR000719, Prot_kinase_dom
IPR008271, Ser/Thr_kinase_AS

Pfam protein domain database

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Pfami
View protein in Pfam
PF00069, Pkinase, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR01772, JNKMAPKINASE

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00220, S_TKc, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF56112, SSF56112, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01351, MAPK, 1 hit
PS50011, PROTEIN_KINASE_DOM, 1 hit
PS00108, PROTEIN_KINASE_ST, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i96662B278ABCCA19
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E1JHD6E1JHD6_DROME
Mitogen-activated protein kinase
bsk BSK, Bsk, D-JNK, D-junk, DBSK
372Annotation score:

Annotation score:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti331 – 372APAPE…NNRTR → RPLRSHMITAWTKGNTLWSS GRS in AAC47325 (PubMed:8946916).CuratedAdd BLAST42

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

NCBI Reference Sequences

More...
RefSeqi
NP_001162930.1, NM_001169459.1
NP_001162932.1, NM_001169461.3
NP_723541.1, NM_164900.3

Genome annotation databases

Ensembl metazoan genome annotation project

More...
EnsemblMetazoai
FBtr0080087; FBpp0079676; FBgn0000229
FBtr0300982; FBpp0290204; FBgn0000229
FBtr0302378; FBpp0291573; FBgn0000229

Database of genes from NCBI RefSeq genomes

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GeneIDi
44801

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
dme:Dmel_CG5680

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

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

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5AWMX-ray1.79A1-372[»]
SMRiP92208
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi69288, 130 interactors
DIPiDIP-17307N
IntActiP92208, 18 interactors
STRINGi7227.FBpp0079676

PTM databases

iPTMnetiP92208

Proteomic databases

PaxDbiP92208
PRIDEiP92208

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
44801
FlyBaseiFBgn0000229, bsk

Phylogenomic databases

eggNOGiKOG0665, Eukaryota
GeneTreeiENSGT00940000169409
HOGENOMiCLU_000288_181_1_1
InParanoidiP92208
KOiK04440
OMAiREFKLMN
OrthoDBi741207at2759
PhylomeDBiP92208

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-209459, Imd pathway
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

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

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BioGRID-ORCSi
44801, 0 hits in 5 CRISPR screens

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
44801

Protein Ontology

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PROi
PR:P92208

Gene expression databases

BgeeiFBgn0000229, Expressed in eye disc (Drosophila) and 63 other tissues
ExpressionAtlasiP92208, baseline and differential
GenevisibleiP92208, DM

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

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiJNK_DROME
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P92208
Secondary accession number(s): O01366, Q94542
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: May 1, 1997
Last modified: August 12, 2020
This is version 187 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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