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Protein

Stress-activated protein kinase jnk-1

Gene

jnk-1

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Serine/threonine-protein kinase which responds to activation by environmental stress by phosphorylating a number of transcription factors such as daf-16, and thus regulates transcriptional activity. By phosphorylating daf-16, plays a role in daf-16 nuclear translocation in intestinal cells in response to environmental stresses such as heat and oxidative stresses (PubMed:17894411). Downstream of jkk-1, may coordinate locomotion via type-D GABAergic motoneurons and regulates synaptic vesicle transport in conjunction with unc-16. Independently of jkk-1, may regulate some mechanosensory responses, such as response to touch (PubMed:11566876). Independently of jkk-1 and downstream of mek-1, plays a role in resistance to heavy metals, such as Cu2+ or Cd2+ (PubMed:11566876). Regulates germline cell apoptosis in response to heavy metals such as Cu2+ and arsenite (PubMed:18597494, PubMed:19497412). Downstream of jkk-1 but independently of mek-1, positively regulates lifespan (PubMed:15767565).6 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.4 Publications

Cofactori

Mg2+4 Publications

Enzyme regulationi

Activated by threonine and tyrosine phosphorylation by either of the dual specificity kinases, jkk-1 and mek-1.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei148 – 1481ATPPROSITE-ProRule annotation
Active sitei244 – 2441Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi126 – 1316ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • JUN kinase activity Source: WormBase
  • metal ion binding Source: UniProtKB-KW
  • protein kinase activity Source: WormBase
  • transcription factor binding Source: WormBase

GO - Biological processi

  • determination of adult lifespan Source: WormBase
  • hyperosmotic response Source: WormBase
  • JNK cascade Source: UniProtKB
  • JUN phosphorylation Source: WormBase
  • MAPK cascade Source: WormBase
  • negative regulation of axon regeneration Source: WormBase
  • protein phosphorylation Source: WormBase
  • response to heat Source: WormBase
  • vesicle transport along actin filament Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.24. 1045.
ReactomeiR-CEL-193648. NRAGE signals death through JNK.
R-CEL-2559580. Oxidative Stress Induced Senescence.
R-CEL-2871796. FCERI mediated MAPK activation.
R-CEL-450321. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
SignaLinkiQ8WQG9.

Names & Taxonomyi

Protein namesi
Recommended name:
Stress-activated protein kinase jnk-1 (EC:2.7.11.244 Publications)
Gene namesi
Name:jnk-1
ORF Names:B0478.1
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome IV

Organism-specific databases

WormBaseiB0478.1a; CE27574; WBGene00002178; jnk-1.
B0478.1b; CE30123; WBGene00002178; jnk-1.

Subcellular locationi

GO - Cellular componenti

  • axon Source: WormBase
  • cytoplasm Source: WormBase
  • neuronal cell body Source: WormBase
  • nucleus Source: WormBase
  • perikaryon Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi276 – 2761T → A: Abolishes phosphorylation. Loss of kinase activity; when associated with F-278. 2 Publications
Mutagenesisi278 – 2781Y → F: Abolishes phosphorylation. Loss of kinase activity; when associated with A-276. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 463463Stress-activated protein kinase jnk-1PRO_0000186270Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei276 – 2761Phosphothreonine3 Publications
Modified residuei278 – 2781Phosphotyrosine3 Publications

Post-translational modificationi

Dually phosphorylated on Thr-276 and Tyr-278, which activates the enzyme.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8WQG9.
PaxDbiQ8WQG9.
PRIDEiQ8WQG9.

PTM databases

iPTMnetiQ8WQG9.

Expressioni

Tissue specificityi

Expressed in most neurons, including nerve ring, head ganglions, dorsal and ventral nerve cords and tail ganglions (PubMed:10393177). The Thr-276/Tyr-278 phosphorylated form is present in the nerve ring upon heat exposure (PubMed:17894411).2 Publications

Developmental stagei

Isoform a and isoform b are expressed in embryo and in all larval stages.1 Publication

Interactioni

Subunit structurei

Binds to the scaffolding protein, unc-16. Unc-16 also binds other components of the JNK signaling pathway (PubMed:11738026). Interacts with daf-16 (PubMed:15767565).2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
JUNP054123EBI-321822,EBI-852823From a different organism.

GO - Molecular functioni

  • transcription factor binding Source: WormBase

Protein-protein interaction databases

BioGridi42580. 2 interactions.
DIPiDIP-26951N.
IntActiQ8WQG9. 4 interactions.
MINTiMINT-1087649.
STRINGi6239.B0478.1a.

Structurei

3D structure databases

ProteinModelPortaliQ8WQG9.
SMRiQ8WQG9. Positions 46-454.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini119 – 412294Protein kinasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi276 – 2783TXYCurated

Domaini

The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.2 Publications

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0665. Eukaryota.
ENOG410XSHI. LUCA.
GeneTreeiENSGT00550000074271.
HOGENOMiHOG000233024.
InParanoidiQ8WQG9.
KOiK04440.
OMAiIESVGNW.
PhylomeDBiQ8WQG9.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008351. MAPK_JNK.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR01772. JNKMAPKINASE.
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS01351. MAPK. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform a (identifier: Q8WQG9-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEERLSTTSS YPSHPGRSVE EDHNTLLASS SISSIIRGTR GHLNNFIESV
60 70 80 90 100
GNWLVPSSSG RDDDAVSLDS CQSVYSPVRH HINSGTGGGI LMEPSSIHVP
110 120 130 140 150
ENYYSVTIGE AQMVVLKRYQ NLRLIGSGAQ GIVCSAFDTV RNEQVAIKKL
160 170 180 190 200
SRPFQNVTHA KRAYRELKLM SLVNHKNIIG ILNCFTPQKK LDEFNDLYIV
210 220 230 240 250
MELMDANLCQ VIQMDLDHER LSYLLYQMLC GIRHLHSAGI IHRDLKPSNI
260 270 280 290 300
VVRSDCTLKI LDFGLARTAI EAFMMTPYVV TRYYRAPEVI LGMGYKENVD
310 320 330 340 350
VWSIGCIFGE LIRGRVLFPG GDHIDQWTRI IEQLGTPDRS FLERLQPTVR
360 370 380 390 400
NYVENRPRYQ ATPFEVLFSD NMFPMTADSS RLTGAQARDL LSRMLVIDPE
410 420 430 440 450
RRISVDDALR HPYVNVWFDE IEVYAPPPLP YDHNMDVEQN VDSWREHIFR
460
ELTDYARTHD IYS
Length:463
Mass (Da):52,885
Last modified:October 1, 2002 - v2
Checksum:iE12495B45B052BC7
GO
Isoform b (identifier: Q8WQG9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-91: Missing.

Show »
Length:372
Mass (Da):43,179
Checksum:iD923F874F36F9856
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 9191Missing in isoform b. CuratedVSP_050269Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB024085 mRNA. Translation: BAA82640.1.
FO080209 Genomic DNA. Translation: CCD62004.1.
FO080209 Genomic DNA. Translation: CCD62005.1.
PIRiT30031.
T37323.
RefSeqiNP_001021270.1. NM_001026099.3. [Q8WQG9-1]
NP_741434.2. NM_171371.4. [Q8WQG9-2]
UniGeneiCel.18197.

Genome annotation databases

EnsemblMetazoaiB0478.1a; B0478.1a; WBGene00002178. [Q8WQG9-1]
GeneIDi177460.
KEGGicel:CELE_B0478.1.
UCSCiB0478.1a. c. elegans. [Q8WQG9-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB024085 mRNA. Translation: BAA82640.1.
FO080209 Genomic DNA. Translation: CCD62004.1.
FO080209 Genomic DNA. Translation: CCD62005.1.
PIRiT30031.
T37323.
RefSeqiNP_001021270.1. NM_001026099.3. [Q8WQG9-1]
NP_741434.2. NM_171371.4. [Q8WQG9-2]
UniGeneiCel.18197.

3D structure databases

ProteinModelPortaliQ8WQG9.
SMRiQ8WQG9. Positions 46-454.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi42580. 2 interactions.
DIPiDIP-26951N.
IntActiQ8WQG9. 4 interactions.
MINTiMINT-1087649.
STRINGi6239.B0478.1a.

PTM databases

iPTMnetiQ8WQG9.

Proteomic databases

EPDiQ8WQG9.
PaxDbiQ8WQG9.
PRIDEiQ8WQG9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiB0478.1a; B0478.1a; WBGene00002178. [Q8WQG9-1]
GeneIDi177460.
KEGGicel:CELE_B0478.1.
UCSCiB0478.1a. c. elegans. [Q8WQG9-1]

Organism-specific databases

CTDi177460.
WormBaseiB0478.1a; CE27574; WBGene00002178; jnk-1.
B0478.1b; CE30123; WBGene00002178; jnk-1.

Phylogenomic databases

eggNOGiKOG0665. Eukaryota.
ENOG410XSHI. LUCA.
GeneTreeiENSGT00550000074271.
HOGENOMiHOG000233024.
InParanoidiQ8WQG9.
KOiK04440.
OMAiIESVGNW.
PhylomeDBiQ8WQG9.

Enzyme and pathway databases

BRENDAi2.7.11.24. 1045.
ReactomeiR-CEL-193648. NRAGE signals death through JNK.
R-CEL-2559580. Oxidative Stress Induced Senescence.
R-CEL-2871796. FCERI mediated MAPK activation.
R-CEL-450321. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
SignaLinkiQ8WQG9.

Miscellaneous databases

PROiQ8WQG9.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008351. MAPK_JNK.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR01772. JNKMAPKINASE.
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS01351. MAPK. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A Caenorhabditis elegans JNK signal transduction pathway regulates coordinated movement via type-D GABAergic motor neurons."
    Kawasaki M., Hisamoto N., Iino Y., Yamamoto M., Ninomiya-Tsuji J., Matsumoto K.
    EMBO J. 18:3604-3615(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  2. "jkk-1 and mek-1 regulate body movement coordination and response to heavy metals through jnk-1 in Caenorhabditis elegans."
    Villanueva A., Lozano J., Morales A., Lin X., Deng X., Hengartner M.O., Kolesnick R.N.
    EMBO J. 20:5114-5128(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, PHOSPHORYLATION AT THR-276 AND TYR-278, MUTAGENESIS OF THR-276 AND TYR-278.
  3. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ALTERNATIVE SPLICING.
    Strain: Bristol N2.
  4. "UNC-16, a JNK-signaling scaffold protein, regulates vesicle transport in C. elegans."
    Byrd D.T., Kawasaki M., Walcoff M., Hisamoto N., Matsumoto K., Jin Y.
    Neuron 32:787-800(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, INTERACTION WITH UNC-16.
  5. "JNK regulates lifespan in Caenorhabditis elegans by modulating nuclear translocation of forkhead transcription factor/DAF-16."
    Oh S.W., Mukhopadhyay A., Svrzikapa N., Jiang F., Davis R.J., Tissenbaum H.A.
    Proc. Natl. Acad. Sci. U.S.A. 102:4494-4499(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, INTERACTION WITH DAF-16, PHOSPHORYLATION AT THR-276 AND TYR-278, MUTAGENESIS OF THR-276 AND TYR-278.
  6. "Arsenite-induced germline apoptosis through a MAPK-dependent, p53-independent pathway in Caenorhabditis elegans."
    Pei B., Wang S., Guo X., Wang J., Yang G., Hang H., Wu L.
    Chem. Res. Toxicol. 21:1530-1535(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "The MAP kinase JNK-1 of Caenorhabditis elegans: location, activation, and influences over temperature-dependent insulin-like signaling, stress responses, and fitness."
    Wolf M., Nunes F., Henkel A., Heinick A., Paul R.J.
    J. Cell. Physiol. 214:721-729(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION AT THR-276 AND TYR-278.
  8. "Copper-induced germline apoptosis in Caenorhabditis elegans: the independent roles of DNA damage response signaling and the dependent roles of MAPK cascades."
    Wang S., Wu L., Wang Y., Luo X., Lu Y.
    Chem. Biol. Interact. 180:151-157(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiJNK1_CAEEL
AccessioniPrimary (citable) accession number: Q8WQG9
Secondary accession number(s): Q17507, Q9UAH2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: October 1, 2002
Last modified: June 8, 2016
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.