Ikbke
entrez
56489
canonical
uniprot
Q9R0T8
canonical
ensembl
ENSMUSG00000042349
resolver
ensp
ENSMUSP00000054126
resolver
ensp
ENSMUSP00000265008
resolver
ensp
ENSMUSP00000265011
resolver
ensp
ENSMUSP00000265013
resolver
ensp
ENSMUSP00000265014
resolver
enst
ENSMUST00000062108
resolver
genesymbol
Ikbke
resolver
genesymbol_syn
Ikke
resolver
genesymbol_syn
Ikki
resolver
uniprot
Q8C2I3
resolver
uniprot_entry
IKKE_MOUSE
resolver
uniprot_sec
Q8C2I3
resolver
activity_regulation
ACTIVITY REGULATION: Kinase activity is inhibited competitively by amlexanox. {ECO:0000269|PubMed:23396211}.
uniprot
proteins
amino_acid_sequence
MQSTTNYLWHTDDLLGQGATASVYKARNKKSGEVVAVKVFNSASYRRPPEVQVREFEVLRRLNHQNIVKLFAVEETGGSRQKVLIMEYCSSGSLLSVLEDPENTFGLSEEEFLVVLRCVVAGMNHLRENGIVHRDIKPGNIMRLVGEEGQSIYKLSDFGAARKLDDDEKFVSVYGTEEYLHPDMYERAVLRKPQQKAFGVTVDLWSIGVTLYHAATGSLPFIPFGGPRRNKEIMYRITTEKPAGAISGTQKQENGPLEWSYSLPITCRLSMGLQNQLVPILANILEVEEDKCWGFDQFFAETSDILQRTVIHVFSLPQAVLHHVYIHAHNTIAIFLEAVYEQTNVTPKHQEYLFEGHPCVLEPSLSAQHIAHTAASSPLTLFSMSSDTPKGLAFRDPALDVPKFVPKVDLQADYSTAKGVLGAGYQALWLARVLLDGQALMLRGLHWVLEVLQDTCQQTLEVTRTALLYLSSSLGTERFSSGAGMPDVQERKEATELRTRLQTLSEILSKCSHNVTETQRSLSCLGEELLKNRDQIHEDNKSIQKIQCCLDKMHFIYKQFKKSRMRPGLSYNEEQIHKLDKVNFSHLAKRLLQVFQEECVQTYQVSLVTHGKRMRQVQRAQNHLHLIGHSVATCNSEARGAQESLNKIFDQLLLDRASEQGAEVSPQPMAPHPGPDPKDLVFHMQELCNDMKLLAFDLQDNNRLIERLHRVPSAPDV
uniprot
proteins
ec_number
2.7.11.1
uniprot
proteins
ec_number
2.7.11.10
uniprot
proteins
function
FUNCTION: Serine/threonine kinase that plays an essential role in regulating inflammatory responses to viral infection, through the activation of the type I IFN, NF-kappa-B and STAT signaling (PubMed:15210742, PubMed:22171011). Also involved in TNFA and inflammatory cytokines, like Interleukin-1, signaling (By similarity). Following activation of viral RNA sensors, such as RIG-I-like receptors, associates with DDX3X and phosphorylates interferon regulatory factors (IRFs), IRF3 and IRF7, as well as DDX3X (By similarity). This activity allows subsequent homodimerization and nuclear translocation of the IRF3 leading to transcriptional activation of pro-inflammatory and antiviral genes including IFNB3 In order to establish such an antiviral state, IKBKE forms several different complexes whose composition depends on the type of cell and cellular stimuli (By similarity). Thus, several scaffolding molecules including IPS1/MAVS, TANK, AZI2/NAP1 or TBKBP1/SINTBAD can be recruited to the IKBKE-containing-complexes (By similarity). In addition, is also required for the induction of a subset of ISGs which displays antiviral activity, may be through the phosphorylation of STAT1 at 'Ser-708' (PubMed:17332413, PubMed:22065572). Phosphorylation of STAT1 at 'Ser-708' also seems to promote the assembly and DNA binding of ISGF3 (STAT1:STAT2:IRF9) complexes compared to GAF (STAT1:STAT1) complexes, in this way regulating the balance between type I and type II IFN responses (PubMed:17332413, PubMed:22065572). Activated by polyubiquitination in response to TNFA and interleukin-1, regulates the NF-kappa-B signaling pathway via the phosphorylation of CYLD, NFKBIA and p65/RELA (PubMed:10421793). Activates NF-kappa-B by mediating phosphorylation and inactivation of CYLD (By similarity). Phosphorylates inhibitors of NF-kappa-B, such as NFKBIA, thus leading to the dissociation of the inhibitor/NF-kappa-B complex and ultimately the degradation of the inhibitor (PubMed:10421793). Also activates NF-kappa-B signaling by mediating phosphorylation and activation of STING1 (PubMed:39262777). Protects cells against DNA damage-induced cell death (By similarity). Also plays an important role in energy balance regulation by sustaining a state of chronic, low-grade inflammation in obesity, wich leads to a negative impact on insulin sensitivity (PubMed:19737522, PubMed:23396211). Phosphorylates AKT1 (By similarity). {ECO:0000250|UniProtKB:Q14164, ECO:0000269|PubMed:10421793, ECO:0000269|PubMed:15210742, ECO:0000269|PubMed:17332413, ECO:0000269|PubMed:19737522, ECO:0000269|PubMed:22065572, ECO:0000269|PubMed:22171011, ECO:0000269|PubMed:23396211, ECO:0000269|PubMed:39262777}.
uniprot
proteins
mass_dalton
80953
uniprot
proteins
mutagenesis
MUTAGEN 38; /note="K->A: Dominant negative."; /evidence="ECO:0000269|PubMed:17332413
uniprot
proteins
post_translational_modification
PTM: Sumoylation by TOPORS upon DNA damage is required for protection of cells against DNA damage-induced cell death. Desumoylated by SENP1 (By similarity). {ECO:0000250}.; PTM: Autophosphorylated and phosphorylated by IKBKB/IKKB. Phosphorylation at Ser-172 is enhanced by the interaction with DDX3X. Phosphorylated at Thr-503 upon IFN activation. {ECO:0000269|PubMed:17332413}.; PTM: 'Lys-63'-linked polyubiquitinated at Lys-30 and Lys-403 by TRAF2:BIRC2 and TRAF2:BIRC3 complexes. Ubiquitination is induced by LPS, TNFA and interleukin-1 and required for full kinase activity and KF-kappa-B pathway activation (By similarity). {ECO:0000250}.
uniprot
proteins
protein_family
I-kappa-B kinase subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
Ser/Thr protein kinase family
uniprot
proteins
pubmed
10421793
uniprot
proteins
pubmed
15210742
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17332413
uniprot
proteins
pubmed
17568778
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
19737522
uniprot
proteins
pubmed
22065572
uniprot
proteins
pubmed
22171011
uniprot
proteins
pubmed
23396211
uniprot
proteins
pubmed
39262777
uniprot
proteins
sequence_length
717
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14164}. Nucleus {ECO:0000250|UniProtKB:Q14164}. Nucleus, PML body {ECO:0000250|UniProtKB:Q14164}. Note=Targeting to PML nuclear bodies upon DNA damage is TOPORS-dependent. Located diffusely throughout the cytoplasm but locates to punctate cytoplasmic bodies when coexpressed with TRIM6. {ECO:0000250|UniProtKB:Q14164}.
uniprot
proteins