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Information on EC 2.7.11.24 - mitogen-activated protein kinase and Organism(s) Caenorhabditis elegans and UniProt Accession P39745
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2.7.11.24 mitogen-activated protein kinaseIUBMB Comments
Phosphorylation of specific tyrosine and threonine residues in the activation loop of this enzyme by EC 2.7.12.2, mitogen-activated protein kinase kinase (MAPKK) is necessary for enzyme activation. Once activated, the enzyme phosphorylates target substrates on serine or threonine residues followed by a proline . A distinguishing feature of all MAPKs is the conserved sequence Thr-Xaa-Tyr (TXY). Mitogen-activated protein kinase (MAPK) signal transduction pathways are among the most widespread mechanisms of cellular regulation. Mammalian MAPK pathways can be recruited by a wide variety of stimuli including hormones (e.g. insulin and growth hormone), mitogens (e.g. epidermal growth factor and platelet-derived growth factor), vasoactive peptides (e.g. angiotensin-II and endothelin), inflammatory cytokines of the tumour necrosis factor (TNF) family and environmental stresses such as osmotic shock, ionizing radiation and ischaemic injury.
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Word Map
- 2.7.11.24
- endothelial
- necrosis
- tnf
- agonist
- lipopolysaccharide
- 3-kinase
- pkc
- lps
- nf-kappab
- sirnas
- phosphatidylinositol
- caspase-3
- cardiac
- metastasis
-
lps-induced
- artery
- camp
- bcl-2
- monocyte
- chemokine
- collagen
- angiogenesis
- cox-2
- fibrosis
-
toll-like
- cyclins
-
neuroprotective
- melanoma
- stat3
- tnf-alpha
- prostaglandin
- c-fos
- phosphoinositide
- mtor
- cardiomyocytes
- factor-alpha
- osteoblast
-
dominant-negative
- creb
-
anti-apoptotic
- integrins
- cyclooxygenase-2
- angiotensin
- wortmannin
-
protein-coupled
- microglia
- mmp-9
- il-1beta
-
platelet-derived
- fak
- medicine
- drug development
- analysis
- pharmacology
The taxonomic range for the selected organisms is: Caenorhabditis elegans
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
+
a [protein]-(L-serine/L-threonine)
=
+
a [protein]-(L-serine/L-threonine) phosphate
Synonyms
mapk, p38, erk1/2, p38 mapk, mitogen-activated protein kinase, map kinase, extracellular signal-regulated kinase, p38 mitogen-activated protein kinase, p38mapk, p38 map kinase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C493C.10
cp38a
-
-
-
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cp38b
-
-
-
-
CSAID binding protein
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-
-
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CSBP
-
-
-
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Cytokine suppressive anti-inflammatory drug binding protein
-
-
-
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ERK5
-
-
-
-
kgb-1
MAP kinase
MAP kinase MXI2
-
-
-
-
MAP kinase p38 beta
-
-
-
-
MAP kinase p38 delta
-
-
-
-
MAP kinase p38 gamma
-
-
-
-
MAP kinase p38a
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-
-
-
MAP kinase p38alpha
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-
-
-
MAP kinase p38b
-
-
-
-
MAPK
mitogen-activated protein kinase
Mitogen-activated protein kinase p38 beta
-
-
-
-
Mitogen-activated protein kinase p38 delta
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-
-
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Mitogen-activated protein kinase p38 gamma
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-
-
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Mitogen-activated protein kinase p38a
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-
-
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Mitogen-activated protein kinase p38alpha
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-
-
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Mitogen-activated protein kinase p38b
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-
-
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p38b
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-
-
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SAPK2A
-
-
-
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stress-activated protein kinase 2a
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-
-
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MAPK
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-
-
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mitogen-activated protein kinase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:protein phosphotransferase (MAPKK-activated)
Phosphorylation of specific tyrosine and threonine residues in the activation loop of this enzyme by EC 2.7.12.2, mitogen-activated protein kinase kinase (MAPKK) is necessary for enzyme activation. Once activated, the enzyme phosphorylates target substrates on serine or threonine residues followed by a proline [6]. A distinguishing feature of all MAPKs is the conserved sequence Thr-Xaa-Tyr (TXY). Mitogen-activated protein kinase (MAPK) signal transduction pathways are among the most widespread mechanisms of cellular regulation. Mammalian MAPK pathways can be recruited by a wide variety of stimuli including hormones (e.g. insulin and growth hormone), mitogens (e.g. epidermal growth factor and platelet-derived growth factor), vasoactive peptides (e.g. angiotensin-II and endothelin), inflammatory cytokines of the tumour necrosis factor (TNF) family and environmental stresses such as osmotic shock, ionizing radiation and ischaemic injury.
CAS REGISTRY NUMBER
COMMENTARY
142243-02-5
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + GLH-1
ADP + phosphorylated GLH-1
-
-
-
?
additional information
?
-
enzyme is activated in response to a variety of cellular stresses and is involved in apoptosis in neurons
-
-
?
additional information
?
-
-
enzyme is activated in response to a variety of cellular stresses and is involved in apoptosis in neurons
-
-
?
additional information
?
-
UNC-16 may regulate the localization of vesicular cargo by integrating JNK signaling and kinesin-1 transport
-
-
?
additional information
?
-
-
UNC-16 may regulate the localization of vesicular cargo by integrating JNK signaling and kinesin-1 transport
-
-
?
additional information
?
-
-
promoting influence of JNK-1 on both nuclear DAF-16 translocations and DAF-16 target gene sod-3, encoding superoxide dismutase 3, expressions within peripheral, non-neuronal tissue, JNK-1 modulates the intestinal stress-induced translocation of DAF-16 from the cytosol into the cell nucleus. JNK-1 is controlled by the MAPK JKK-1 under heat stress
-
-
?
additional information
?
-
promoting influence of JNK-1 on both nuclear DAF-16 translocations and DAF-16 target gene sod-3, encoding superoxide dismutase 3, expressions within peripheral, non-neuronal tissue, JNK-1 modulates the intestinal stress-induced translocation of DAF-16 from the cytosol into the cell nucleus. JNK-1 is controlled by the MAPK JKK-1 under heat stress
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + GLH-1
ADP + phosphorylated GLH-1
-
-
-
?
additional information
?
-
enzyme is activated in response to a variety of cellular stresses and is involved in apoptosis in neurons
-
-
?
additional information
?
-
-
enzyme is activated in response to a variety of cellular stresses and is involved in apoptosis in neurons
-
-
?
additional information
?
-
UNC-16 may regulate the localization of vesicular cargo by integrating JNK signaling and kinesin-1 transport
-
-
?
additional information
?
-
-
UNC-16 may regulate the localization of vesicular cargo by integrating JNK signaling and kinesin-1 transport
-
-
?
additional information
?
-
-
promoting influence of JNK-1 on both nuclear DAF-16 translocations and DAF-16 target gene sod-3, encoding superoxide dismutase 3, expressions within peripheral, non-neuronal tissue, JNK-1 modulates the intestinal stress-induced translocation of DAF-16 from the cytosol into the cell nucleus. JNK-1 is controlled by the MAPK JKK-1 under heat stress
-
-
?
additional information
?
-
promoting influence of JNK-1 on both nuclear DAF-16 translocations and DAF-16 target gene sod-3, encoding superoxide dismutase 3, expressions within peripheral, non-neuronal tissue, JNK-1 modulates the intestinal stress-induced translocation of DAF-16 from the cytosol into the cell nucleus. JNK-1 is controlled by the MAPK JKK-1 under heat stress
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
arsenite
treatment of worms with arsenite, a toxic ROS-producing compound, induces a robust phosphorylation of PMK-1, induction of oxidative stress-responsive genes, and eventual lethality. Activation of PMK-1 following arsenite treatment is dependent on SEK-1 but independent of NSY-1, differing from the NSY-1/SEK-1/PMK-1 cascade used during infection and osmotic stress
additional information
-
JNK-1 is activated by phosphorylation, ambient temperature of 1-37°C specifically influences the activation/phosphorylation of the MAPkinase JNK-1
-
additional information
JNK-1 is activated by phosphorylation, ambient temperature of 1-37°C specifically influences the activation/phosphorylation of the MAPkinase JNK-1
-
additional information
-
C493C.10 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-5
-
additional information
C493C.10 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-5
-
additional information
C493C.10 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-5
-
additional information
C493C.10 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-5
-
additional information
C493C.10 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-5
-
additional information
C493C.10 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-5
-
additional information
C493C.10 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-5
-
additional information
-
jnk-1 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-4. Activation of JNK signaling occurs under conditions of heavy metal stress
-
additional information
jnk-1 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-4. Activation of JNK signaling occurs under conditions of heavy metal stress
-
additional information
jnk-1 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-4. Activation of JNK signaling occurs under conditions of heavy metal stress
-
additional information
jnk-1 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-4. Activation of JNK signaling occurs under conditions of heavy metal stress
-
additional information
jnk-1 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-4. Activation of JNK signaling occurs under conditions of heavy metal stress
-
additional information
jnk-1 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-4. Activation of JNK signaling occurs under conditions of heavy metal stress
-
additional information
jnk-1 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-4. Activation of JNK signaling occurs under conditions of heavy metal stress
-
additional information
-
kgb-1 is phosphorylated and activated by mitogen-activated protein kinase kinase jkk-1
-
additional information
kgb-1 is phosphorylated and activated by mitogen-activated protein kinase kinase jkk-1
-
additional information
kgb-1 is phosphorylated and activated by mitogen-activated protein kinase kinase jkk-1
-
additional information
kgb-1 is phosphorylated and activated by mitogen-activated protein kinase kinase jkk-1
-
additional information
kgb-1 is phosphorylated and activated by mitogen-activated protein kinase kinase jkk-1
-
additional information
kgb-1 is phosphorylated and activated by mitogen-activated protein kinase kinase jkk-1
-
additional information
kgb-1 is phosphorylated and activated by mitogen-activated protein kinase kinase jkk-1
-
additional information
-
kgb-2 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-3
-
additional information
kgb-2 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-3
-
additional information
kgb-2 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-3
-
additional information
kgb-2 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-3
-
additional information
kgb-2 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-3
-
additional information
kgb-2 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-3
-
additional information
kgb-2 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-3
-
additional information
-
pmk-1 is phosphorylated and activated by mitogen-activated protein kinase kinase mkk-4. Unique upstream components activating PMK-1 induce SKN-1 activation following toxin and bacterial exposure
-
additional information
pmk-1 is phosphorylated and activated by mitogen-activated protein kinase kinase mkk-4. Unique upstream components activating PMK-1 induce SKN-1 activation following toxin and bacterial exposure
-
additional information
pmk-1 is phosphorylated and activated by mitogen-activated protein kinase kinase mkk-4. Unique upstream components activating PMK-1 induce SKN-1 activation following toxin and bacterial exposure
-
additional information
pmk-1 is phosphorylated and activated by mitogen-activated protein kinase kinase mkk-4. Unique upstream components activating PMK-1 induce SKN-1 activation following toxin and bacterial exposure
-
additional information
pmk-1 is phosphorylated and activated by mitogen-activated protein kinase kinase mkk-4. Unique upstream components activating PMK-1 induce SKN-1 activation following toxin and bacterial exposure
-
additional information
pmk-1 is phosphorylated and activated by mitogen-activated protein kinase kinase mkk-4. Unique upstream components activating PMK-1 induce SKN-1 activation following toxin and bacterial exposure
-
additional information
pmk-1 is phosphorylated and activated by mitogen-activated protein kinase kinase mkk-4. Unique upstream components activating PMK-1 induce SKN-1 activation following toxin and bacterial exposure
-
additional information
-
pmk-2 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-1
-
additional information
pmk-2 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-1
-
additional information
pmk-2 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-1
-
additional information
pmk-2 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-1
-
additional information
pmk-2 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-1
-
additional information
pmk-2 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-1
-
additional information
pmk-2 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-1
-
additional information
-
pmk-3 is phosphorylated and activated by mitogen-activated protein kinase kinase mek-1
-
additional information
pmk-3 is phosphorylated and activated by mitogen-activated protein kinase kinase mek-1
-
additional information
pmk-3 is phosphorylated and activated by mitogen-activated protein kinase kinase mek-1
-
additional information
pmk-3 is phosphorylated and activated by mitogen-activated protein kinase kinase mek-1
-
additional information
pmk-3 is phosphorylated and activated by mitogen-activated protein kinase kinase mek-1
-
additional information
pmk-3 is phosphorylated and activated by mitogen-activated protein kinase kinase mek-1
-
additional information
pmk-3 is phosphorylated and activated by mitogen-activated protein kinase kinase mek-1
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 20
rise of degree of phosphorylation of isoforms JNK-1alpha and JNK-1beta
additional information
additional information
-
ambient temperature of 1-37°C specifically influences the activation/phosphorylation of the MAPkinase JNK-1
additional information
ambient temperature of 1-37°C specifically influences the activation/phosphorylation of the MAPkinase JNK-1
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1 - 37
degree of phosphorylation of isoforms JNK-1alpha and JNK-1beta increase with ambient temperature
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
the enzyme is expressed in neuronal tissue
additional information
-
the enzyme shows a broad tissue expression pattern
additional information
the enzyme shows a broad tissue expression pattern
additional information
the enzyme shows a broad tissue expression pattern
additional information
the enzyme shows a broad tissue expression pattern
additional information
the enzyme shows a broad tissue expression pattern
additional information
the enzyme shows a broad tissue expression pattern
additional information
the enzyme shows a broad tissue expression pattern
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
evolution
C493C.10 is an orthologue of mammalian JNK
evolution
jnk-1 is an orthologue of mammalian JNK
evolution
kgb-1 is an orthologue of mammalian JNK
evolution
kgb-2 is an orthologue of mammalian JNK. The JNK homologue KGB-2 shows 84% identity with KGB-1
evolution
pmk-1 is an orthologue of mammalian p38. The three pmk genes pmk1, pmk-2, and pmk-3, are encoded by a single polycistronic transcript (operon), precluding the generation of double mutants by traditional genetic crosses
evolution
pmk-2 is an orthologue of mammalian p38. The three pmk genes pmk1, pmk-2, and pmk-3, are encoded by a single polycistronic transcript (operon), precluding the generation of double mutants by traditional genetic crosses
evolution
pmk-3 is an orthologue of mammalian p38. The three pmk genes pmk1, pmk-2, and pmk-3, are encoded by a single polycistronic transcript (operon), precluding the generation of double mutants by traditional genetic crosses
malfunction
a kgb-1 null mutant, obtained by targeted deletion, shows extra germ cells, increased number of P granules, and temperature-sensitive sterility. RNAi-mediated knockdown of glh-1 in kgb-1 mutants partially rescues the P granule number and temperature-sensitive sterility. Null mutations in vhp-1 cause larval lethality, which can be suppressed by null mutations in mlk-1, mek-1, kgb-1, dlk-1, or pmk-3
malfunction
null mutations in vhp-1 cause larval lethality, which can be suppressed by null mutations in mlk-1, mek-1, kgb-1, dlk-1, or pmk-3. DLK-1/PMK-3 are identified to affect cilia length, via regulation of RAB-5 endosomes
malfunction
removing the 3'-UTR of pmk-2 causes its expression in the intestine, which is sufficient to rescue the Esp phenotype of pmk-1 mutants. The Esp mutant phenotype worms show enhanced susceptibility to Pseudomonas aeruginosa that causes an intestinal infection and eventual death of the worm
metabolism
distinct p38 and JNK MAPK cascades regulate a diverse class of normal biological processes during development and nervous system function
metabolism
the core MAPK signaling cassette consists of a MAPKKK/MAPKK/MAPK cascade, stress-activated MAPK components involved in non-stress-associated processes, overview
metabolism
the core MAPK signaling cassette consists of a MAPKKK/MAPKK/MAPK cascade, stress-activated MAPK components involved in non-stress-associated processes, overview. Distinct p38 and JNK MAPK cascades regulate a diverse class of normal biological processes during development and nervous system function
metabolism
the core MAPK signaling cassette consists of a MAPKKK/MAPKK/MAPK cascade, stress-activated MAPK components involved in non-stress-associated processes, overview. Distinct p38 and JNK MAPK cascades regulate a diverse class of normal biological processes during development and nervous system function. Functional redundancy of pmk-1 and pmk-2
metabolism
the core MAPK signaling cassette consists of a MAPKKK/MAPKK/MAPK cascade, stress-activated MAPK components involved in non-stress-associated processes, overview. Distinct p38 and JNK MAPK cascades regulate a diverse class of normal biological processes during development and nervous system function. The three kinases DLK-1/MKK-4/PMK-3 constitute a linear pathway. MAK-2 is the homologue of MAPKAPK2 (MK2), and acts downstream of PMK-3. The conserved pathway, the DLK-1/MKK-4/PMK-3 cascade, activation is necessary to initiate axonal regrowth. The cascade is tightly regulated by protein ubiquitination during synapse development
physiological function
activation of JNK signaling occurs under conditions of heavy metal stress. Olfactory memory in Caenorhabditis elegans allows for the association of cues with positive or negative experiences. The loss of these memories proceeds through the UNC-43/TIR-1/NSY-1/SEK-1/JNK-1 cascade
physiological function
PMK-3 acts during neuronal development. vhp-1 regulates MAP kinases in axon regeneration. svh-1 and svh-2 likely provide a layer of specificity in controlling the KGB-1/JNK pathway, independently of PMK-3 in axon injury response, crosstalk between the KGB-1 and PMK-3 cascades. The avoidance of high CO2 environments and pathogens is mediated by MOM-4/MKK-4/PMK-3 in the BAG neuron
physiological function
roles for KGB-2 are in excess carbon dioxide (hypercapnia)-induced fertility defects and a slight negative role in axon injury response
physiological function
the enzyme is involved in P granule formation in germ cell proliferation. KGB-1 can bind and phosphorylate GLH-1, which leads to degradation of phosphorylated GLH-1. KGB-1 activity negatively regulates GLH-1 and the steady state level of P granules to maintain fertility. vhp-1 regulates MAP kinases in axon regeneration. svh-1 and svh-2 likely provide a layer of specificity in controlling the KGB-1/JNK pathway, independently of PMK-3 in axon injury response, crosstalk between the KGB-1 and PMK-3 cascades. The aversive reaction to microbial exposure is mediated by a MLK-1/MEK-1(SEK-1)/KGB-1 pathway
physiological function
the NSY-1/SEK-1/PMK-1 and PMK-2 cascade acts during neuronal development to regulate AWC asymmetry. The activation of this cascade is regulated in part by calcium, via calmodulin kinase II, as well as the conserved protein TIR-1. PMK-1 and PMK-2 act redundantly downstream of TIR-1/NSY-1/SEK-1 to induce TPH-1 expression in the ADF neuron following exposure to bacteria. Genes pmk-1 and pmk-2 function redundantly during olfactory neuronal development
physiological function
the NSY-1/SEK-1/PMK-1 and PMK-2 cascade acts during neuronal development to regulate AWC asymmetry. The activation of this cascade is regulated in part by calcium, via calmodulin kinase II, as well as the conserved protein TIR-1. PMK-1 and PMK-2 act redundantly downstream of TIR-1/NSY-1/SEK-1 to induce TPH-1 expression in the ADF neuron following exposure to bacteria. Genes pmk-1 and pmk-2 function redundantly during olfactory neuronal development. Activation of PMK-1 following arsenite treatment is dependent on SEK-1 but independent of NSY-1, differing from the NSY-1/SEK-1/PMK-1 cascade used during infection and osmotic stress. Unique upstream components activating PMK-1 induce SKN-1 activation following toxin and bacterial exposure
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MPK1_CAEEL
444
0
50663
Swiss-Prot
other Location (Reliability: 3)
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoprotein
JNK-1 is activated by phosphorylation, ambient temperature of 1-37°C specifically influences the activation/phosphorylation of the MAPkinase JNK-1
phosphoprotein
C493C.10 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-5
phosphoprotein
jnk-1 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-4
phosphoprotein
kgb-1 is phosphorylated and activated by mitogen-activated protein kinase kinase jkk-1
phosphoprotein
kgb-2 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-3
phosphoprotein
pmk-1 is phosphorylated and activated by mitogen-activated protein kinase kinase mkk-4. Treatment of worms with arsenite, a toxic ROS-producing compound, induces a robust phosphorylation of PMK-1, induction of oxidative stress-responsive genes, and eventual lethality
phosphoprotein
pmk-2 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-1
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
transgenic jnk-1 deletion mutant, exhibits a reduced thermal tolerance and reproductive fitness at higher temperatures
additional information
transgenic jnk-1 deletion mutant, exhibits a reduced thermal tolerance and reproductive fitness at higher temperatures
additional information
-
construction of a JNK-1 deletion mutant expressing daf-16-GFP, the mutant exhibits a reduced thermal tolerance and reproductive fitness at higher temperatures compared to the wild-type enzyme, jnk-1 overexpression leads to enhanced translocation of DAF-16
additional information
construction of a JNK-1 deletion mutant expressing daf-16-GFP, the mutant exhibits a reduced thermal tolerance and reproductive fitness at higher temperatures compared to the wild-type enzyme, jnk-1 overexpression leads to enhanced translocation of DAF-16
additional information
-
a kgb-1 null mutant is obtained by targeted deletion
additional information
a kgb-1 null mutant is obtained by targeted deletion
additional information
a kgb-1 null mutant is obtained by targeted deletion
additional information
a kgb-1 null mutant is obtained by targeted deletion
additional information
a kgb-1 null mutant is obtained by targeted deletion
additional information
a kgb-1 null mutant is obtained by targeted deletion
additional information
a kgb-1 null mutant is obtained by targeted deletion
additional information
-
a strain with mutations in both pmk-1 and pmk-2 is serendipitously identified in a screen searching for suppressors of the pmk-1 loss of function phenotype following bacterial infection
additional information
a strain with mutations in both pmk-1 and pmk-2 is serendipitously identified in a screen searching for suppressors of the pmk-1 loss of function phenotype following bacterial infection
additional information
a strain with mutations in both pmk-1 and pmk-2 is serendipitously identified in a screen searching for suppressors of the pmk-1 loss of function phenotype following bacterial infection
additional information
a strain with mutations in both pmk-1 and pmk-2 is serendipitously identified in a screen searching for suppressors of the pmk-1 loss of function phenotype following bacterial infection
additional information
a strain with mutations in both pmk-1 and pmk-2 is serendipitously identified in a screen searching for suppressors of the pmk-1 loss of function phenotype following bacterial infection
additional information
a strain with mutations in both pmk-1 and pmk-2 is serendipitously identified in a screen searching for suppressors of the pmk-1 loss of function phenotype following bacterial infection
additional information
a strain with mutations in both pmk-1 and pmk-2 is serendipitously identified in a screen searching for suppressors of the pmk-1 loss of function phenotype following bacterial infection
additional information
-
a strain with mutations in both pmk-1 and pmk-2 is serendipitously identified in a screen searching for suppressors of the pmk-1 loss of function phenotype following bacterial infection. Removing the 3'-UTR of pmk-2 causes its expression in the intestine, which is sufficient to rescue the Esp phenotype of pmk-1 mutants
additional information
a strain with mutations in both pmk-1 and pmk-2 is serendipitously identified in a screen searching for suppressors of the pmk-1 loss of function phenotype following bacterial infection. Removing the 3'-UTR of pmk-2 causes its expression in the intestine, which is sufficient to rescue the Esp phenotype of pmk-1 mutants
additional information
a strain with mutations in both pmk-1 and pmk-2 is serendipitously identified in a screen searching for suppressors of the pmk-1 loss of function phenotype following bacterial infection. Removing the 3'-UTR of pmk-2 causes its expression in the intestine, which is sufficient to rescue the Esp phenotype of pmk-1 mutants
additional information
a strain with mutations in both pmk-1 and pmk-2 is serendipitously identified in a screen searching for suppressors of the pmk-1 loss of function phenotype following bacterial infection. Removing the 3'-UTR of pmk-2 causes its expression in the intestine, which is sufficient to rescue the Esp phenotype of pmk-1 mutants
additional information
a strain with mutations in both pmk-1 and pmk-2 is serendipitously identified in a screen searching for suppressors of the pmk-1 loss of function phenotype following bacterial infection. Removing the 3'-UTR of pmk-2 causes its expression in the intestine, which is sufficient to rescue the Esp phenotype of pmk-1 mutants
additional information
a strain with mutations in both pmk-1 and pmk-2 is serendipitously identified in a screen searching for suppressors of the pmk-1 loss of function phenotype following bacterial infection. Removing the 3'-UTR of pmk-2 causes its expression in the intestine, which is sufficient to rescue the Esp phenotype of pmk-1 mutants
additional information
a strain with mutations in both pmk-1 and pmk-2 is serendipitously identified in a screen searching for suppressors of the pmk-1 loss of function phenotype following bacterial infection. Removing the 3'-UTR of pmk-2 causes its expression in the intestine, which is sufficient to rescue the Esp phenotype of pmk-1 mutants
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
the use of 3'-UTR elements to regulate tissue-specific expression of pmk-2 provides a mechanism that endows context specificity to p38 paralogues
additional information
additional information
-
indirect interactions between neuronal MAPK and peripheral insulin-like signaling in response to environmental stimuli (temperature, H2O2)
additional information
indirect interactions between neuronal MAPK and peripheral insulin-like signaling in response to environmental stimuli (temperature, H2O2)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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Caenorhabditis elegans, Caenorhabditis elegans (H2KZI0), Caenorhabditis elegans (O44408), Caenorhabditis elegans (O44514), Caenorhabditis elegans (Q17446), Caenorhabditis elegans (Q8MXI4), Caenorhabditis elegans (Q8WQG9)
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