Page last updated: 2024-08-07 12:43:44

Receptor-interacting serine/threonine-protein kinase 2

A receptor-interacting serine/threonine-protein kinase 2 that is encoded in the genome of human. [PRO:DNx, UniProtKB:O43353]

Synonyms

EC 2.7.11.1;
CARD-containing interleukin-1 beta-converting enzyme-associated kinase;
CARD-containing IL-1 beta ICE-kinase;
RIP-like-interacting CLARP kinase;
Receptor-interacting protein 2;
RIP-2;
Tyrosine-protein kinase RIPK2;

Research

Bioassay Publications (19)

TimeframeStudies on this Protein(%)All Drugs %
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's6 (31.58)29.6817
2010's11 (57.89)24.3611
2020's2 (10.53)2.80

Compounds (244)

Drugs with Inhibition Measurements

DrugTaxonomyMeasurementAverage (mM)Bioassay(s)Publication(s)
1-NA-PP1Homo sapiens (human)IC500.120011
ag 1879Homo sapiens (human)IC500.019011
zm 336372Homo sapiens (human)IC50100.000011
staurosporineHomo sapiens (human)IC500.356022
birb 796Homo sapiens (human)IC5010.000011
sb 203580Homo sapiens (human)IC501.035978
sorafenibHomo sapiens (human)IC503.600011
Src Inhibitor-1Homo sapiens (human)IC500.026011
dasatinibHomo sapiens (human)IC500.109011
dasatinibHomo sapiens (human)Ki0.010011
1-tert-butyl-3-naphthalen-1-ylmethyl-1h-pyrazolo(3,4-d)pyrimidin-4-ylemineHomo sapiens (human)IC500.130011
pd 166285Homo sapiens (human)IC500.013011
sb-505124Homo sapiens (human)IC500.685011
ly-2157299Homo sapiens (human)IC500.044011
in 1130Homo sapiens (human)IC500.111011
ponatinibHomo sapiens (human)IC500.003822
dabrafenibHomo sapiens (human)IC500.077011
pf 3644022Homo sapiens (human)IC500.590010
ew-7197Homo sapiens (human)IC500.054011

Drugs with Activation Measurements

DrugTaxonomyMeasurementAverage (mM)Bioassay(s)Publication(s)
fasudilHomo sapiens (human)Kd30.000011
4-(4'-hydroxyphenyl)-amino-6,7-dimethoxyquinazolineHomo sapiens (human)Kd5.939011
sb 202190Homo sapiens (human)Kd0.250022
imatinibHomo sapiens (human)Kd16.666733
triciribine phosphateHomo sapiens (human)Kd30.000011
staurosporineHomo sapiens (human)Kd5.166733
picropodophyllinHomo sapiens (human)Kd30.000011
gefitinibHomo sapiens (human)Kd0.690844
lestaurtinibHomo sapiens (human)Kd10.426733
perifosineHomo sapiens (human)Kd30.000012
vatalanibHomo sapiens (human)Kd16.666733
ruboxistaurinHomo sapiens (human)Kd16.666733
canertinibHomo sapiens (human)Kd0.402344
birb 796Homo sapiens (human)Kd7.900022
cyc 202Homo sapiens (human)Kd20.000022
sb 203580Homo sapiens (human)Kd0.716033
enzastaurinHomo sapiens (human)Kd20.000022
erlotinibHomo sapiens (human)Kd3.300844
lapatinibHomo sapiens (human)Kd12.400033
sorafenibHomo sapiens (human)Kd7.360055
pd 173955Homo sapiens (human)Kd0.016011
s 1033Homo sapiens (human)Kd20.000022
xl147Homo sapiens (human)Kd30.000011
bms 387032Homo sapiens (human)Kd16.666733
sf 2370Homo sapiens (human)Kd0.526011
tandutinibHomo sapiens (human)Kd15.000044
vx-745Homo sapiens (human)Kd10.000022
dasatinibHomo sapiens (human)Kd0.027333
ha 1100Homo sapiens (human)Kd30.000011
7-epi-hydroxystaurosporineHomo sapiens (human)Kd30.000011
zd 6474Homo sapiens (human)Kd0.028644
4-(5-benzo(1,3)dioxol-5-yl-4-pyridin-2-yl-1h-imidazol-2-yl)benzamideHomo sapiens (human)Kd3.400011
imd 0354Homo sapiens (human)Kd30.000012
sirolimusHomo sapiens (human)Kd30.000011
alvocidibHomo sapiens (human)Kd16.666733
bosutinibHomo sapiens (human)Kd16.850022
orantinibHomo sapiens (human)Kd30.000011
su 11248Homo sapiens (human)Kd15.000044
palbociclibHomo sapiens (human)Kd30.000011
jnj-7706621Homo sapiens (human)Kd10.000011
vx680Homo sapiens (human)Kd16.666733
cyc 116Homo sapiens (human)Kd3.292011
everolimusHomo sapiens (human)Kd30.000012
ekb 569Homo sapiens (human)Kd20.000022
axitinibHomo sapiens (human)Kd19.950022
temsirolimusHomo sapiens (human)Kd30.000011
pd 184352Homo sapiens (human)Kd10.000011
on 01910Homo sapiens (human)Kd30.000011
av 412Homo sapiens (human)Kd30.000011
telatinibHomo sapiens (human)Kd30.000011
y-39983Homo sapiens (human)Kd30.000011
cp 547632Homo sapiens (human)Kd0.958011
bms345541Homo sapiens (human)Kd10.000011
lenvatinibHomo sapiens (human)Kd0.011011
pd 0325901Homo sapiens (human)Kd30.000011
midostaurinHomo sapiens (human)Kd15.000044
px-866Homo sapiens (human)Kd30.000011
ripasudilHomo sapiens (human)Kd30.000011
osi 930Homo sapiens (human)Kd30.000011
ki 20227Homo sapiens (human)Kd0.290011
scio-469Homo sapiens (human)Kd30.000011
cp 724714Homo sapiens (human)Kd20.000022
pi103Homo sapiens (human)Kd10.000022
hmn-214Homo sapiens (human)Kd30.000011
tivozanibHomo sapiens (human)Kd0.801011
hki 272Homo sapiens (human)Kd20.000022
tofacitinibHomo sapiens (human)Kd16.666733
n-(6-chloro-7-methoxy-9h-beta-carbolin-8-yl)-2-methylnicotinamideHomo sapiens (human)Kd10.000011
cediranibHomo sapiens (human)Kd15.049022
masitinibHomo sapiens (human)Kd20.000022
ly-2157299Homo sapiens (human)Kd0.038011
pazopanibHomo sapiens (human)Kd2.941733
azd 6244Homo sapiens (human)Kd20.000022
su 14813Homo sapiens (human)Kd16.666733
bibw 2992Homo sapiens (human)Kd16.350022
binimetinibHomo sapiens (human)Kd30.000011
sotrastaurinHomo sapiens (human)Kd30.000011
aee 788Homo sapiens (human)Kd30.000011
saracatinibHomo sapiens (human)Kd0.002011
vx 702Homo sapiens (human)Kd30.000011
crenolanibHomo sapiens (human)Kd1.312011
tg100-115Homo sapiens (human)Kd1.233522
cc 401Homo sapiens (human)Kd30.000011
bms 599626Homo sapiens (human)Kd30.000012
exel-7647Homo sapiens (human)Kd0.033011
volasertibHomo sapiens (human)Kd30.000011
pha 665752Homo sapiens (human)Kd10.000011
azd 7762Homo sapiens (human)Kd30.000011
regorafenibHomo sapiens (human)Kd0.767011
6-[[5-fluoro-2-(3,4,5-trimethoxyanilino)-4-pyrimidinyl]amino]-2,2-dimethyl-4H-pyrido[3,2-b][1,4]oxazin-3-oneHomo sapiens (human)Kd15.485022
brivanibHomo sapiens (human)Kd16.450022
mp470Homo sapiens (human)Kd30.000011
rgb 286638Homo sapiens (human)Kd30.000011
np 031112Homo sapiens (human)Kd30.000011
at 7519Homo sapiens (human)Kd20.000022
bms-690514Homo sapiens (human)Kd30.000011
bi 2536Homo sapiens (human)Kd20.000022
inno-406Homo sapiens (human)Kd1.469011
nvp-ast487Homo sapiens (human)Kd1.100022
kw 2449Homo sapiens (human)Kd16.850022
danusertibHomo sapiens (human)Kd30.000011
abt 869Homo sapiens (human)Kd16.666733
azd 8931Homo sapiens (human)Kd0.751011
arq 197Homo sapiens (human)Kd30.000011
azd 1152Homo sapiens (human)Kd1.850011
pf 00299804Homo sapiens (human)Kd0.988011
ridaforolimusHomo sapiens (human)Kd30.000011
ch 4987655Homo sapiens (human)Kd30.000011
6-(5-((cyclopropylamino)carbonyl)-3-fluoro-2-methylphenyl)-n-(2,2-dimethylprpyl)-3-pyridinecarboxamideHomo sapiens (human)Kd30.000012
cc-930Homo sapiens (human)Kd30.000011
gw 2580Homo sapiens (human)Kd10.000022
tak 285Homo sapiens (human)Kd30.000011
idelalisibHomo sapiens (human)Kd30.000012
crizotinibHomo sapiens (human)Kd15.450022
osi 906Homo sapiens (human)Kd1.364011
chir-265Homo sapiens (human)Kd10.633333
motesanibHomo sapiens (human)Kd16.433333
fostamatinibHomo sapiens (human)Kd30.000011
trametinibHomo sapiens (human)Kd30.000012
mln8054Homo sapiens (human)Kd16.666733
pf-562,271Homo sapiens (human)Kd30.000012
GDC-0879Homo sapiens (human)Kd2.500011
jnj-26483327Homo sapiens (human)Kd0.390011
ly2603618Homo sapiens (human)Kd30.000011
tg100801Homo sapiens (human)Kd0.192011
dactolisibHomo sapiens (human)Kd30.000011
bgt226Homo sapiens (human)Kd30.000011
gsk 461364Homo sapiens (human)Kd20.000022
azd 1152-hqpaHomo sapiens (human)Kd15.900034
nvp-tae684Homo sapiens (human)Kd9.600011
enmd 2076Homo sapiens (human)Kd30.000011
e 7050Homo sapiens (human)Kd0.097011
2-amino-8-ethyl-4-methyl-6-(1H-pyrazol-5-yl)-7-pyrido[2,3-d]pyrimidinoneHomo sapiens (human)Kd30.000011
tak-901Homo sapiens (human)Kd30.000011
gdc-0973Homo sapiens (human)Kd30.000011
buparlisibHomo sapiens (human)Kd30.000011
azd 1480Homo sapiens (human)Kd30.000011
azd8330Homo sapiens (human)Kd30.000011
pha 848125Homo sapiens (human)Kd30.000011
ro5126766Homo sapiens (human)Kd30.000011
fedratinibHomo sapiens (human)Kd18.050022
gsk690693Homo sapiens (human)Kd20.000022
14-methyl-20-oxa-5,7,14,26-tetraazatetracyclo(19.3.1.1(2,6).1(8,12))heptacosa-1(25),2(26),3,5,8(27),9,11,16,21,23-decaeneHomo sapiens (human)Kd30.000011
azd5438Homo sapiens (human)Kd30.000011
pf 04217903Homo sapiens (human)Kd30.000011
gdc 0941Homo sapiens (human)Kd20.000022
icotinibHomo sapiens (human)Kd2.627011
ph 797804Homo sapiens (human)Kd30.000011
kx-01Homo sapiens (human)Kd30.000011
plx 4720Homo sapiens (human)Kd0.430011
mk 5108Homo sapiens (human)Kd30.000011
cx 4945Homo sapiens (human)Kd30.000011
cudc 101Homo sapiens (human)Kd1.090011
arry-614Homo sapiens (human)Kd30.000011
tak 593Homo sapiens (human)Kd30.000011
mln 8237Homo sapiens (human)Kd30.000011
sgx 523Homo sapiens (human)Kd20.000022
bms 754807Homo sapiens (human)Kd30.000011
bms 777607Homo sapiens (human)Kd30.000011
sgi 1776Homo sapiens (human)Kd30.000011
pci 32765Homo sapiens (human)Kd0.057011
ponatinibHomo sapiens (human)Kd0.083011
amg 900Homo sapiens (human)Kd30.000011
mk-1775Homo sapiens (human)Kd30.000011
AMG-208Homo sapiens (human)Kd30.000011
quizartinibHomo sapiens (human)Kd14.233333
at13148Homo sapiens (human)Kd30.000011
tak 733Homo sapiens (human)Kd30.000011
mk 2206Homo sapiens (human)Kd30.000011
sns 314Homo sapiens (human)Kd30.000011
lucitanibHomo sapiens (human)Kd0.199011
pf-04691502Homo sapiens (human)Kd30.000011
n-(cyanomethyl)-4-(2-((4-(4-morpholinyl)phenyl)amino)-4-pyrimidinyl)benzamideHomo sapiens (human)Kd30.000011
dcc-2036Homo sapiens (human)Kd30.000011
cabozantinibHomo sapiens (human)Kd0.767011
defactinibHomo sapiens (human)Kd30.000011
ly2584702Homo sapiens (human)Kd30.000011
incb-018424Homo sapiens (human)Kd20.000022
poziotinibHomo sapiens (human)Kd0.048011
asp3026Homo sapiens (human)Kd30.000011
entrectinibHomo sapiens (human)Kd30.000012
pexidartinibHomo sapiens (human)Kd30.000011
TAK-580Homo sapiens (human)Kd30.000011
gsk 2126458Homo sapiens (human)Kd30.000011
emd1214063Homo sapiens (human)Kd30.000011
gsk 1838705aHomo sapiens (human)Kd10.000011
pf 3758309Homo sapiens (human)Kd30.000011
gdc 0980Homo sapiens (human)Kd30.000012
azd2014Homo sapiens (human)Kd30.000011
(5-(2,4-bis((3s)-3-methylmorpholin-4-yl)pyrido(2,3-d)pyrimidin-7-yl)-2-methoxyphenyl)methanolHomo sapiens (human)Kd30.000011
plx4032Homo sapiens (human)Kd0.427011
gsk 1363089Homo sapiens (human)Kd0.037522
arry-334543Homo sapiens (human)Kd0.810011
kin-193Homo sapiens (human)Kd30.000011
mk 2461Homo sapiens (human)Kd30.000011
bay 869766Homo sapiens (human)Kd30.000011
as 703026Homo sapiens (human)Kd30.000011
baricitinibHomo sapiens (human)Kd30.000011
dabrafenibHomo sapiens (human)Kd0.106011
pki 587Homo sapiens (human)Kd30.000011
n-(3-fluoro-4-((1-methyl-6-(1h-pyrazol-4-yl)-1h-indazol-5 yl)oxy)phenyl)-1-(4-fluorophenyl)-6-methyl-2-oxo-1,2-dihydropyridine-3-carboxamideHomo sapiens (human)Kd30.000011
ribociclibHomo sapiens (human)Kd30.000011
mk-8033Homo sapiens (human)Kd30.000011
pha 793887Homo sapiens (human)Kd30.000011
sb 1518Homo sapiens (human)Kd30.000011
abemaciclibHomo sapiens (human)Kd30.000011
mk-8776Homo sapiens (human)Kd30.000011
afuresertibHomo sapiens (human)Kd30.000011
gsk 1070916Homo sapiens (human)Kd0.611011
jnj38877605Homo sapiens (human)Kd30.000011
dinaciclibHomo sapiens (human)Kd30.000011
gilteritinibHomo sapiens (human)Kd0.482011
alectinibHomo sapiens (human)Kd30.000011
glpg0634Homo sapiens (human)Kd30.000011
encorafenibHomo sapiens (human)Kd0.323011
bms-911543Homo sapiens (human)Kd30.000011
gsk2141795Homo sapiens (human)Kd30.000011
azd8186Homo sapiens (human)Kd30.000011
byl719Homo sapiens (human)Kd30.000011
cep-32496Homo sapiens (human)Kd0.442011
rociletinibHomo sapiens (human)Kd30.000011
ceritinibHomo sapiens (human)Kd30.000011
azd1208Homo sapiens (human)Kd30.000011
vx-509Homo sapiens (human)Kd30.000011
debio 1347Homo sapiens (human)Kd30.000011
volitinibHomo sapiens (human)Kd30.000011
osimertinibHomo sapiens (human)Kd30.000011
at 9283Homo sapiens (human)Kd30.000011
otssp167Homo sapiens (human)Kd0.005011
chir 258Homo sapiens (human)Kd20.000034
osi 027Homo sapiens (human)Kd1.163011
nintedanibHomo sapiens (human)Kd23.333323
bay 80-6946Homo sapiens (human)Kd30.000011
pp242Homo sapiens (human)Kd0.077011

Enables

This protein enables 13 target(s):

TargetCategoryDefinition
protein serine/threonine kinase activitymolecular functionCatalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate, and ATP + protein threonine = ADP + protein threonine phosphate. [GOC:bf, MetaCyc:PROTEIN-KINASE-RXN, PMID:2956925]
non-membrane spanning protein tyrosine kinase activitymolecular functionCatalysis of the reaction: ATP + protein L-tyrosine = ADP + protein L-tyrosine phosphate by a non-membrane spanning protein. [EC:2.7.10.2]
signaling receptor bindingmolecular functionBinding to one or more specific sites on a receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function. [GOC:bf, GOC:ceb, ISBN:0198506732]
protein bindingmolecular functionBinding to a protein. [GOC:go_curators]
ATP bindingmolecular functionBinding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. [ISBN:0198506732]
LIM domain bindingmolecular functionBinding to a LIM domain (for Lin-11 Isl-1 Mec-3) of a protein, a domain with seven conserved cysteine residues and a histidine, that binds two zinc ions and acts as an interface for protein-protein interactions. [GOC:go_curators, Pfam:PF00412]
signaling adaptor activitymolecular functionThe binding activity of a molecule that brings together two or more molecules in a signaling pathway, permitting those molecules to function in a coordinated way. Adaptor molecules themselves do not have catalytic activity. [GOC:bf, PMID:19104498]
identical protein bindingmolecular functionBinding to an identical protein or proteins. [GOC:jl]
protein homodimerization activitymolecular functionBinding to an identical protein to form a homodimer. [GOC:jl]
CARD domain bindingmolecular functionBinding to a CARD (N-terminal caspase recruitment) domain, a protein-protein interaction domain that belongs to the death domain-fold superfamily. These protein molecule families are similar in structure with each consisting of six or seven anti-parallel alpha-helices that form highly specific homophilic interactions between signaling partners. CARD exists in the N-terminal prodomains of several caspases and in apoptosis-regulatory proteins and mediates the assembly of CARD-containing proteins that participate in activation or suppression of CARD carrying members of the caspase family. [PMID:12054670]
caspase bindingmolecular functionBinding to a caspase family protein. [GOC:dos, GOC:ha]
protein serine kinase activitymolecular functionCatalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate. [RHEA:17989]
JUN kinase kinase kinase activitymolecular functionCatalysis of the reaction: JNKK + ATP = JNKK phosphate + ADP. This reaction is the phosphorylation and activation of JUN kinase kinases (JNKKs). [GOC:bf]

Located In

This protein is located in 5 target(s):

TargetCategoryDefinition
cytoplasmcellular componentThe contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684]
endoplasmic reticulumcellular componentThe irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached). [ISBN:0198506732]
cytosolcellular componentThe part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. [GOC:hjd, GOC:jl]
cytoskeletoncellular componentA cellular structure that forms the internal framework of eukaryotic and prokaryotic cells. The cytoskeleton includes intermediate filaments, microfilaments, microtubules, the microtrabecular lattice, and other structures characterized by a polymeric filamentous nature and long-range order within the cell. The various elements of the cytoskeleton not only serve in the maintenance of cellular shape but also have roles in other cellular functions, including cellular movement, cell division, endocytosis, and movement of organelles. [GOC:mah, PMID:16959967, PMID:27419875]
vesiclecellular componentAny small, fluid-filled, spherical organelle enclosed by membrane. [GOC:mah, GOC:pz, GOC:vesicles]

Active In

This protein is active in 1 target(s):

TargetCategoryDefinition
plasma membranecellular componentThe membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. [ISBN:0716731363]

Part Of

This protein is part of 1 target(s):

TargetCategoryDefinition
protein-containing complexcellular componentA stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together. [GOC:dos, GOC:mah]

Involved In

This protein is involved in 58 target(s):

TargetCategoryDefinition
positive regulation of cytokine-mediated signaling pathwaybiological processAny process that activates or increases the frequency, rate or extent of a cytokine mediated signaling pathway. [GOC:hjd]
adaptive immune responsebiological processAn immune response mediated by cells expressing specific receptors for antigens produced through a somatic diversification process, and allowing for an enhanced secondary response to subsequent exposures to the same antigen (immunological memory). [GO_REF:0000022, GOC:add, ISBN:0781735149]
positive regulation of T-helper 1 type immune responsebiological processAny process that activates or increases the frequency, rate, or extent of a T-helper 1 type immune response. [GOC:add]
apoptotic processbiological processA programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died. [GOC:cjm, GOC:dhl, GOC:ecd, GOC:go_curators, GOC:mtg_apoptosis, GOC:tb, ISBN:0198506732, PMID:18846107, PMID:21494263]
inflammatory responsebiological processThe immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. [GO_REF:0000022, ISBN:0198506732]
signal transductionbiological processThe cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell. [GOC:go_curators, GOC:mtg_signaling_feb11]
canonical NF-kappaB signal transductionbiological processAn intracellular signaling cassette characterized by the I-kappaB-kinase (IKK)-dependent activation of NF-kappaB, also known as the canonical NF-kappaB signaling cascade. The cascade begins with activation of a trimeric IKK complex (consisting of catalytic kinase subunits IKKalpha and/or IKKbeta, and the regulatory scaffold protein NEMO) and ends with the regulation of transcription of target genes by NF-kappaB. In a resting state, NF-kappaB dimers are bound to I-kappaB proteins, sequestering NF-kappaB in the cytoplasm. Phosphorylation of I-kappaB targets I-kappaB for ubiquitination and proteasomal degradation, thus releasing the NF-kappaB dimers, which can translocate to the nucleus to bind DNA and regulate transcription. The canonical NF-kappaB pathway is mainly stimulated by proinflammatory cytokines such as IL-1beta, tumor necrosis factor (TNF)-alpha, antigen ligands, and toll-like receptors (TLRs). [GOC:bf, PMID:12773372, PMID:34659217]
JNK cascadebiological processA MAPK cascade containing at least the JNK (MAPK8) MAP kinase. It starts with the activation of JUN3K (a MAPK3K), which activates JNKK a MAP2K), which in turn activates JNK. The cascade can also contain an additional tier: the upstream MAP4K. The kinases in each tier phosphorylate and activate the kinases in the downstream tier. The JNK cascade is activated by stress signals, as well as by G protein-coupled receptors, growth factors, and cytokines, and results in cellular responses such as cell proliferation, cell differentiation, apoptosis and inflammation. [PMID:11790549, PMID:20811974, PMID:23125017]
positive regulation of peptidyl-threonine phosphorylationbiological processAny process that increases the frequency, rate or extent of peptidyl-threonine phosphorylation. Peptidyl-threonine phosphorylation is the phosphorylation of peptidyl-threonine to form peptidyl-O-phospho-L-threonine. [GOC:dph, GOC:tb]
cytokine-mediated signaling pathwaybiological processThe series of molecular signals initiated by the binding of a cytokine to a receptor on the surface of a cell, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:mah, GOC:signaling, PMID:19295629]
positive regulation of protein ubiquitinationbiological processAny process that activates or increases the frequency, rate or extent of the addition of ubiquitin groups to a protein. [GOC:mah]
lipopolysaccharide-mediated signaling pathwaybiological processThe series of molecular signals initiated by the binding of a lipopolysaccharide (LPS) to a receptor on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. Lipopolysaccharides are major components of the outer membrane of Gram-negative bacteria, making them prime targets for recognition by the immune system. [GOC:mah, GOC:signaling, PMID:15379975]
positive regulation of protein bindingbiological processAny process that activates or increases the frequency, rate or extent of protein binding. [GOC:mah]
positive regulation of chemokine productionbiological processAny process that activates or increases the frequency, rate, or extent of chemokine production. [GOC:mah]
positive regulation of interferon-alpha productionbiological processAny process that activates or increases the frequency, rate, or extent of interferon-alpha production. [GOC:mah, PMID:15546383]
positive regulation of interferon-beta productionbiological processAny process that activates or increases the frequency, rate, or extent of interferon-beta production. [GOC:mah, PMID:15546383]
positive regulation of type II interferon productionbiological processAny process that activates or increases the frequency, rate, or extent of interferon-gamma production. Interferon-gamma is also known as type II interferon. [GOC:add, GOC:mah, PMID:15546383]
positive regulation of interleukin-1 beta productionbiological processAny process that activates or increases the frequency, rate, or extent of interleukin-1 beta production. [GOC:mah]
positive regulation of interleukin-12 productionbiological processAny process that activates or increases the frequency, rate, or extent of interleukin-12 production. [GOC:mah]
positive regulation of interleukin-2 productionbiological processAny process that activates or increases the frequency, rate, or extent of interleukin-2 production. [GOC:mah]
positive regulation of interleukin-6 productionbiological processAny process that activates or increases the frequency, rate, or extent of interleukin-6 production. [GOC:mah]
positive regulation of tumor necrosis factor productionbiological processAny process that activates or increases the frequency, rate or extent of tumor necrosis factor production. [GO_REF:0000058, GOC:TermGenie, PMID:10891884, PMID:15560120]
positive regulation of stress-activated MAPK cascadebiological processAny process that activates or increases the frequency, rate or extent of signal transduction mediated by the stress-activated MAPK cascade. [GOC:mah]
immature T cell proliferation in thymusbiological processThe expansion of an immature T cell population by cell division in the thymus. [GOC:add, ISBN:0781735149]
positive regulation of immature T cell proliferation in thymusbiological processAny process that activates or increases the frequency, rate or extent of immature T cell proliferation in the thymus. [GOC:add, GOC:mah]
positive regulation of peptidyl-serine phosphorylationbiological processAny process that activates or increases the frequency, rate or extent of the phosphorylation of peptidyl-serine. [GOC:mah]
toll-like receptor 4 signaling pathwaybiological processThe series of molecular signals initiated by a ligand binding to toll-like receptor 4. [GOC:add, PMID:16551253, PMID:17328678]
CD4-positive, alpha-beta T cell proliferationbiological processThe expansion of a CD4-positive, alpha-beta T cell population by cell division. [CL:0000624, GOC:BHF]
defense response to bacteriumbiological processReactions triggered in response to the presence of a bacterium that act to protect the cell or organism. [GOC:jl]
positive regulation of apoptotic processbiological processAny process that activates or increases the frequency, rate or extent of cell death by apoptotic process. [GOC:jl, GOC:mtg_apoptosis]
response to exogenous dsRNAbiological processAny process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an exogenous double-stranded RNA stimulus. [GOC:go_curators]
innate immune responsebiological processInnate immune responses are defense responses mediated by germline encoded components that directly recognize components of potential pathogens. [GO_REF:0000022, GOC:add, GOC:ebc, GOC:mtg_sensu]
positive regulation of T-helper 1 cell differentiationbiological processAny process that activates or increases the frequency, rate or extent of T-helper 1 cell differentiation. [GOC:go_curators]
positive regulation of transcription by RNA polymerase IIbiological processAny process that activates or increases the frequency, rate or extent of transcription from an RNA polymerase II promoter. [GOC:go_curators, GOC:txnOH]
positive regulation of JNK cascadebiological processAny process that activates or increases the frequency, rate or extent of signal transduction mediated by the JNK cascade. [GOC:bf]
positive regulation of peptidyl-tyrosine phosphorylationbiological processAny process that activates or increases the frequency, rate or extent of the phosphorylation of peptidyl-tyrosine. [GOC:ai]
defense response to Gram-positive bacteriumbiological processReactions triggered in response to the presence of a Gram-positive bacterium that act to protect the cell or organism. [GOC:ai]
T cell receptor signaling pathwaybiological processThe series of molecular signals initiated by the cross-linking of an antigen receptor on a T cell. [GOC:add]
positive regulation of NF-kappaB transcription factor activitybiological processAny process that activates or increases the frequency, rate or extent of activity of the transcription factor NF-kappaB. [GOC:dph, GOC:tb, PMID:15087454, PMID:15170030]
protein homooligomerizationbiological processThe process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of identical component monomers. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer. [GOC:ai]
stress-activated MAPK cascadebiological processA MAPK cascade that starts with the activation of a stress-activated MAP kinase cascade. [GOC:ai, PMID:15936270]
positive regulation of macrophage cytokine productionbiological processAny process that increases the rate, frequency or extent of macrophage cytokine production. Macrophage cytokine production is the appearance of a chemokine due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. [GOC:dph, GOC:tb]
ERK1 and ERK2 cascadebiological processA MAPK cascade containing at least the ERK1 or ERK2 MAP kinases. It starts with the activation of a MAP3K, and the consecutive activation of a MPK2K and of ERK1 or ERK2. The cascade can also contain an additional tier: the upstream MAP4K. The kinases in each tier phosphorylate and activate the kinase in the downstream tier. The ERK1/ERK2 cascade is activated by mitogens, growth factors, G protein-coupled receptors, and results in cellular responses such as cell proliferation, cell differentiation and development. [PMID:20811974, PMID:23125017, PMID:28903453]
positive regulation of ERK1 and ERK2 cascadebiological processAny process that activates or increases the frequency, rate or extent of signal transduction mediated by the ERK1 and ERK2 cascade. [GOC:mah]
nucleotide-binding oligomerization domain containing 1 signaling pathwaybiological processThe series of molecular signals initiated by the binding of a ligand (such as a bacterial peptidoglycan) to a cytoplasmic nucleotide-binding oligomerization domain containing 1 (NOD1) protein receptor, and ending with regulation of a downstream cellular process. [GOC:add, PMID:17944960, PMID:18585455]
nucleotide-binding oligomerization domain containing 2 signaling pathwaybiological processThe series of molecular signals initiated by the binding of a ligand (such as a bacterial peptidoglycan) to a cytoplasmic nucleotide-binding oligomerization domain containing 2 (NOD2) protein receptor, and ending with regulation of a downstream cellular process. [GOC:add, PMID:17944960, PMID:18585455]
response to interleukin-1biological processAny process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an interleukin-1 stimulus. [GOC:BHF, GOC:mah]
response to interleukin-12biological processAny process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an interleukin-12 stimulus. [GOC:mah]
response to interleukin-18biological processAny process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an interleukin-18 stimulus. [GOC:mah]
cellular response to lipoteichoic acidbiological processAny process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a lipoteichoic acid stimulus; lipoteichoic acid is a major component of the cell wall of gram-positive bacteria and typically consists of a chain of glycerol-phosphate repeating units linked to a glycolipid anchor. [GOC:mah]
cellular response to peptidoglycanbiological processAny process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a peptidoglycan stimulus. Peptidoglycan is a bacterial cell wall macromolecule. [GOC:mah]
cellular response to muramyl dipeptidebiological processAny process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a muramyl dipeptide stimulus. Muramyl dipeptide is derived from peptidoglycan. [GOC:mah]
activation of cysteine-type endopeptidase activitybiological processAny process that initiates the activity of the inactive enzyme cysteine-type endopeptidase. [GOC:mtg_apoptosis, PMID:21726810]
xenophagybiological processThe selective degradation of intracellular pathogen or some part of an intracellular pathogen (e.g. viral capsid) by macroautophagy. [GOC:autophagy, GOC:pad, GOC:PARL, PMID:19802565, PMID:20159618, PMID:25497060]
positive regulation of protein K63-linked ubiquitinationbiological processAny process that activates or increases the frequency, rate or extent of protein K63-linked ubiquitination. [GOC:TermGenie, PMID:21931591]
positive regulation of xenophagybiological processAny process that activates or increases the frequency, rate or extent of xenophagy. [GO_REF:0000058, GOC:pad, GOC:PARL, GOC:TermGenie, PMID:21617041]
positive regulation of CD4-positive, alpha-beta T cell proliferationbiological processAny process that activates or increases the frequency, rate or extent of CD4-positive, alpha-beta T cell proliferation. [GOC:obol]
positive regulation of canonical NF-kappaB signal transductionbiological processAny process that activates or increases the frequency, rate or extent of a canonical NF-kappaB signaling cascade. [GOC:jl]