Ikbkg
entrez
16151
canonical
uniprot
O88522
canonical
ensembl
ENSMUSG00000004221
resolver
ensp
ENSMUSP00000004330
resolver
ensp
ENSMUSP00000064017
resolver
ensp
ENSMUSP00000109762
resolver
ensp
ENSMUSP00000109763
resolver
ensp
ENSMUSP00000109764
resolver
ensp
ENSMUSP00000109765
resolver
ensp
ENSMUSP00000109768
resolver
ensp
ENSMUSP00000126770
resolver
ensp
ENSMUSP00000136573
resolver
ensp
ENSMUSP00000186779
resolver
ensp
ENSMUSP00000186783
resolver
ensp
ENSMUSP00000186784
resolver
ensp
ENSMUSP00000186789
resolver
enst
ENSMUST00000004330
resolver
enst
ENSMUST00000064407
resolver
enst
ENSMUST00000114127
resolver
enst
ENSMUST00000114128
resolver
enst
ENSMUST00000114129
resolver
enst
ENSMUST00000114130
resolver
enst
ENSMUST00000114133
resolver
enst
ENSMUST00000164101
resolver
enst
ENSMUST00000180230
resolver
genesymbol
Ikbkg
resolver
genesymbol_syn
Nemo
resolver
uniprot
E9Q2Y3
resolver
uniprot
F8WGW0
resolver
uniprot
J3QN32
resolver
uniprot
Q7TSS3
resolver
uniprot
Q8VC91
resolver
uniprot
Q924H4
resolver
uniprot_entry
E9Q2Y3_MOUSE
resolver
uniprot_entry
F8WGW0_MOUSE
resolver
uniprot_entry
J3QN32_MOUSE
resolver
uniprot_entry
NEMO_MOUSE
resolver
uniprot_entry
Q7TSS3_MOUSE
resolver
uniprot_entry
Q8VC91_MOUSE
resolver
uniprot_sec
Q924H4
resolver
amino_acid_sequence
MNKHPWKNQLSEMVQPSGGPAEDQDMLGEESSLGKPAMLHLPSEQGTPETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKGMQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLQREFNKLKVGCHESARIEDMRKRHVETPQPPLLPAPAHHSFHLALSNQRRSPPEEPPDFCCPKCQYQAPDMDTLQIHVMECIE
uniprot
proteins
function
FUNCTION: Regulatory subunit of the IKK core complex which phosphorylates inhibitors of NF-kappa-B thus leading to the dissociation of the inhibitor/NF-kappa-B complex and ultimately the degradation of the inhibitor (PubMed:9927690). Its binding to scaffolding polyubiquitin plays a key role in IKK activation by multiple signaling receptor pathways. Can recognize and bind both 'Lys-63'-linked and linear polyubiquitin upon cell stimulation, with a much higher affinity for linear polyubiquitin. Could be implicated in NF-kappa-B-mediated protection from cytokine toxicity. Essential for viral activation of IRF3. Involved in TLR3- and IFIH1-mediated antiviral innate response; this function requires 'Lys-27'-linked polyubiquitination (By similarity). {ECO:0000250|UniProtKB:Q9Y6K9, ECO:0000269|PubMed:9927690}.
uniprot
proteins
mass_dalton
47972
uniprot
proteins
mutagenesis
MUTAGEN 278; /note="K->R: Slight decrease in TRAF6-induced polyubiquitination."; /evidence="ECO:0000269|PubMed:17728323"; MUTAGEN 293; /note="V->A: Abolishes linear polyubiquitin-binding, impairs 'Lys-63'-linked polyubiquitin-binding and impairs NF-kappa-B activation; when associated with A-301 and A-302."; /evidence="ECO:0000269|PubMed:19303852"; MUTAGEN 301; /note="Y->A: Abolishes linear polyubiquitin-binding, impairs 'Lys-63'-linked polyubiquitin-binding and impairs NF-kappa-B activation; when associated with A-293 and A-302."; /evidence="ECO:0000269|PubMed:19303852"; MUTAGEN 302; /note="K->A: Abolishes linear polyubiquitin-binding, impairs 'Lys-63'-linked polyubiquitin-binding and impairs NF-kappa-B activation; when associated with A-293 and A-301."; /evidence="ECO:0000269|PubMed:19303852"; MUTAGEN 305; /note="F->A: Abolishes linear polyubiquitin-binding, impairs 'Lys-63'-linked polyubiquitin-binding and impairs of NF-kappa-B activation."; /evidence="ECO:0000269|PubMed:19303852"; MUTAGEN 309; /note="R->A: Abolishes linear polyubiquitin-binding, no effect on 'Lys-63'-linked polyubiquitin-binding and impairs NF-kappa-B activation; when associated with A-312 and A-313."; /evidence="ECO:0000269|PubMed:19303852"; MUTAGEN 312; /note="R->A: Abolishes linear polyubiquitin-binding, no effect on 'Lys-63'-linked polyubiquitin-binding and impairs NF-kappa-B activation; when associated with A-309 and A-313."; /evidence="ECO:0000269|PubMed:19303852"; MUTAGEN 313; /note="E->A: Impairs linear polyubiquitin-binding. Abolishes linear polyubiquitin-binding, no effect on 'Lys-63'-linked polyubiquitin-binding and impairs NF-kappa-B activation; when associated with A-309 and A-312. Abolishes linear polyubiquitin-binding; when associated with A-317 and A-320."; /evidence="ECO:0000269|PubMed:19303852"; MUTAGEN 314; /note="K->R: Slight decrease in TRAF6-induced polyubiquitination. Important decrease in TRAF6-induced polyubiquitination; when associated with R-318 and R-319."; /evidence="ECO:0000269|PubMed:17728323"; MUTAGEN 316; /note="V->P: Loss of interaction with TRAF6 and TRAF6-induced polyubiquitination."; /evidence="ECO:0000269|PubMed:17728323"; MUTAGEN 317; /note="E->A: Abolishes linear polyubiquitin-binding; when associated with A-313 and A-320."; /evidence="ECO:0000269|PubMed:19303852"; MUTAGEN 318; /note="K->R: Slight decrease in TRAF6-induced polyubiquitination. Decrease in TRAF6-induced polyubiquitination; when associated with R-319. Important decrease in TRAF6-induced polyubiquitination; when associated with R-314 and R-319."; /evidence="ECO:0000269|PubMed:17728323"; MUTAGEN 319; /note="K->R: Slight decrease in TRAF6-induced polyubiquitination. Decrease in TRAF6-induced polyubiquitination; when associated with R-318. Important decrease in TRAF6-induced polyubiquitination; when associated with R-314 and R-318."; /evidence="ECO:0000269|PubMed:17728323"; MUTAGEN 320; /note="E->A: Abolishes linear polyubiquitin-binding; when associated with A-313 and A-317."; /evidence="ECO:0000269|PubMed:19303852"; MUTAGEN 369; /note="S->A: Decreases phosphorylation and increases NF-kappa-B activity."; /evidence="ECO:0000269|PubMed:11971901"; MUTAGEN 375; /note="S->A: Decreases phosphorylation and increases NF-kappa-B activity."; /evidence="ECO:0000269|PubMed:11971901"; MUTAGEN 392; /note="K->R: 40% decrease in IL1-induced NF-kappa-B activation."; /evidence="ECO:0000269|PubMed:17728323
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-68 attenuates aminoterminal homodimerization. {ECO:0000250|UniProtKB:Q9Y6K9}.; PTM: Polyubiquitinated on Lys-278 via 'Lys-63'-linked ubiquitin; the ubiquitination is mediated downstream of NOD2 and RIPK2 and probably plays a role in signaling by facilitating interactions with ubiquitin domain-containing proteins and activates the NF-kappa-B pathway (By similarity). Polyubiquitinated on Lys-278 and Lys-302 through 'Lys-63'-linked ubiquitin; the ubiquitination is mediated by BCL10, MALT1 and TRAF6 and probably plays a role in signaling by facilitating interactions with ubiquitin domain-containing proteins and activates the NF-kappa-B pathway (By similarity). Monoubiquitinated on Lys-270 and Lys-302; promotes nuclear export (By similarity). Polyubiquitinated through 'Lys-27' by TRIM23; involved in antiviral innate and inflammatory responses (By similarity). Linear polyubiquitinated on Lys-111, Lys-143, Lys-226, Lys-246, Lys-270, Lys-278, Lys-285, Lys-295, Lys-302 and Lys-319; the head-to-tail polyubiquitination is mediated by the LUBAC complex and plays a key role in NF-kappa-B activation (By similarity). Deubiquitinated by USP10 in a TANK-dependent and -independent manner, leading to the negative regulation of NF-kappa-B signaling upon DNA damage (By similarity). Ubiquitinated at Lys-319 by MARCHF2 following bacterial and viral infection which leads to its degradation (By similarity). Polyubiquitinated via 'Lys-29'-linked ubiquitin; leading to lysosomal degradation (By similarity). {ECO:0000250|UniProtKB:Q9Y6K9}.; PTM: Sumoylated on Lys-270 and Lys-302 with SUMO1; the modification results in phosphorylation of Ser-85 by ATM leading to a replacement of the sumoylation by mono-ubiquitination on these residues. {ECO:0000250|UniProtKB:Q9Y6K9}.; PTM: Neddylated by TRIM40, resulting in stabilization of NFKBIA and down-regulation of NF-kappa-B activity. {ECO:0000250|UniProtKB:Q9Y6K9}.
uniprot
proteins
pubmed
11080499
uniprot
proteins
pubmed
11410370
uniprot
proteins
pubmed
11971901
uniprot
proteins
pubmed
12133833
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16684768
uniprot
proteins
pubmed
17728323
uniprot
proteins
pubmed
19303852
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
19854204
uniprot
proteins
pubmed
20622870
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
31519886
uniprot
proteins
pubmed
32935379
uniprot
proteins
pubmed
9657155
uniprot
proteins
pubmed
9891086
uniprot
proteins
pubmed
9927690
uniprot
proteins
sequence_length
412
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y6K9}. Nucleus {ECO:0000250|UniProtKB:Q9Y6K9}. Note=Sumoylated NEMO accumulates in the nucleus in response to genotoxic stress. {ECO:0000250|UniProtKB:Q9Y6K9}.
uniprot
proteins