IKBKG
entrez
8517
canonical
uniprot
Q9Y6K9
canonical
ensembl
ENSG00000269335
resolver
ensp
ENSP00000394934
resolver
ensp
ENSP00000471166
resolver
ensp
ENSP00000478616
resolver
ensp
ENSP00000479662
resolver
ensp
ENSP00000483825
resolver
ensp
ENSP00000484023
resolver
ensp
ENSP00000577193
resolver
ensp
ENSP00000577199
resolver
ensp
ENSP00000577200
resolver
ensp
ENSP00000577204
resolver
ensp
ENSP00000577206
resolver
ensp
ENSP00000577208
resolver
ensp
ENSP00000577210
resolver
ensp
ENSP00000638134
resolver
ensp
ENSP00000638137
resolver
enst
ENST00000617207
resolver
enst
ENST00000907134
resolver
enst
ENST00000907140
resolver
enst
ENST00000907141
resolver
enst
ENST00000907147
resolver
enst
ENST00000968075
resolver
enst
ENST00000968078
resolver
genesymbol
IKBKG
resolver
genesymbol_syn
FIP3
resolver
genesymbol_syn
NEMO
resolver
hgnc
HGNC:5961
resolver
uniprot
A0A087X1B1
resolver
uniprot
Q7LBY6
resolver
uniprot
Q7Z7F1
resolver
uniprot_entry
A0A087X1B1_HUMAN
resolver
uniprot_entry
NEMO_HUMAN
resolver
uniprot_sec
Q7LBY6
resolver
uniprot_sec
Q7Z7F1
resolver
amino_acid_sequence
MNRHLWKSQLCEMVQPSGGPAADQDVLGEESPLGKPAMLHLPSEQGAPETLQRCLEENQELRDAIRQSNQILRERCEELLHFQASQREEKEFLMCKFQEARKLVERLGLEKLDLKRQKEQALREVEHLKRCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHSVQVDQLRMQGQSVEAALRMERQAASEEKRKLAQLQVAYHQLFQEYDNHIKSSVVGSERKRGMQLEDLKQQLQQAEEALVAKQEVIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERQAREKLAEKKELLQEQLEQLQREYSKLKASCQESARIEDMRKRHVEVSQAPLPPAPAYLSSPLALPSQRRSPPEEPPDFCCPKCQYQAPDMDTLQIHVMECIE
uniprot
proteins
disease_involvement
DISEASE: Ectodermal dysplasia and immunodeficiency 1 (EDAID1) [MIM:300291]: A form of ectoderma dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. EDAID1 is an X-linked recessive disorder characterized by absence of sweat glands, sparse scalp hair, rare conical teeth and immunological abnormalities resulting in severe infectious diseases. Severely affected individuals may also show lymphedema, osteopetrosis, and, rarely, hematologic abnormalities. The phenotype is highly variable, and may be fatal in childhood. {ECO:0000269|PubMed:11047757, ECO:0000269|PubMed:11224521, ECO:0000269|PubMed:11242109, ECO:0000269|PubMed:12045264, ECO:0000269|PubMed:14651848, ECO:0000269|PubMed:15100680, ECO:0000269|PubMed:16547522, ECO:0000269|PubMed:19185524, ECO:0000269|PubMed:21606507}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Immunodeficiency 33 (IMD33) [MIM:300636]: An X-linked recessive disorder characterized by variably impaired immunologic function and early-onset recurrent infections, usually due to pneumococcus, H.influenzae, and atypical mycobacteria. Features of hypohidrotic ectodermal dysplasia are generally not present, although some patients may have conical teeth or hypodontia. {ECO:0000269|PubMed:15100680, ECO:0000269|PubMed:15356572, ECO:0000269|PubMed:16818673, ECO:0000269|PubMed:16950813, ECO:0000269|PubMed:19185524, ECO:0000269|PubMed:19854204}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.; DISEASE: Incontinentia pigmenti (IP) [MIM:308300]: A genodermatosis usually prenatally lethal in males. In affected females, it causes abnormalities of the skin, hair, eyes, nails, teeth, skeleton, heart, and central nervous system. The prominent skin signs occur in four classic cutaneous stages: perinatal inflammatory vesicles, verrucous patches, a distinctive pattern of hyperpigmentation and dermal scarring. {ECO:0000269|PubMed:10839543, ECO:0000269|PubMed:11590134, ECO:0000269|PubMed:15229184, ECO:0000269|PubMed:17728323, ECO:0000269|PubMed:19033441, ECO:0000269|PubMed:20434027, ECO:0000269|PubMed:24339369}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Autoinflammatory disease, systemic, X-linked (SAIDX) [MIM:301081]: An X-linked disorder characterized by systemic autoinflammation appearing in the first months of life. Clinical manifestations are variable, including lymphadenopathy, hepatosplenomegaly, fever, panniculitis, and nodular skin rash. Additional features may include inflammation of the optic nerve, intracranial hemorrhage, and lipodystrophy. {ECO:0000269|PubMed:31874111, ECO:0000269|PubMed:35289316}. Note=The disease is caused by variants affecting the gene represented in this entry.
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:14695475, PubMed:20724660, PubMed:21518757, PubMed:9751060). Its binding to scaffolding polyubiquitin plays a key role in IKK activation by multiple signaling receptor pathways (PubMed:16547522, PubMed:18287044, PubMed:19033441, PubMed:19185524, PubMed:21606507, PubMed:27777308, PubMed:33567255). Can recognize and bind both 'Lys-63'-linked and linear polyubiquitin upon cell stimulation, with a much higher affinity for linear polyubiquitin (PubMed:16547522, PubMed:18287044, PubMed:19033441, PubMed:19185524, PubMed:21606507, PubMed:27777308). Could be implicated in NF-kappa-B-mediated protection from cytokine toxicity. Essential for viral activation of IRF3 (PubMed:19854139). Involved in TLR3- and IFIH1-mediated antiviral innate response; this function requires 'Lys-27'-linked polyubiquitination (PubMed:20724660). {ECO:0000269|PubMed:14695475, ECO:0000269|PubMed:16547522, ECO:0000269|PubMed:18287044, ECO:0000269|PubMed:19033441, ECO:0000269|PubMed:19185524, ECO:0000269|PubMed:19854139, ECO:0000269|PubMed:20724660, ECO:0000269|PubMed:21518757, ECO:0000269|PubMed:21606507, ECO:0000269|PubMed:27777308, ECO:0000269|PubMed:33567255, ECO:0000269|PubMed:9751060}.; FUNCTION: (Microbial infection) Also considered to be a mediator for HTLV-1 Tax oncoprotein activation of NF-kappa-B. {ECO:0000269|PubMed:10364167, ECO:0000269|PubMed:11064457}.
uniprot
proteins
mass_dalton
48198
uniprot
proteins
mutagenesis
MUTAGEN 68; /note="S->A: Increases formation of homodimers."; /evidence="ECO:0000269|PubMed:17977820"; MUTAGEN 68; /note="S->E: Abolishes interaction with IKBKB; abolishes TNF induced NF-kappa-B activity."; /evidence="ECO:0000269|PubMed:17977820"; MUTAGEN 85; /note="S->A: Decreases ubiquitination and abolishes nuclear export."; /evidence="ECO:0000269|PubMed:16497931"; MUTAGEN 115; /note="K->R: No change in the ubiquitination level; when associated with R-399."; /evidence="ECO:0000269|PubMed:15620648"; MUTAGEN 224; /note="K->R: No change in the ubiquitination level; when associated with R-399."; /evidence="ECO:0000269|PubMed:15620648"; MUTAGEN 277; /note="K->A: Partial abolition of sumoylation. Abolishes sumoylation and IKK activation; when associated with A-309."; /evidence="ECO:0000269|PubMed:14651848"; MUTAGEN 285; /note="K->R: Decreased ability to activate NF-kappa-B. Important decrease in the ubiquitination level; when associated with R-399."; /evidence="ECO:0000269|PubMed:15620648, ECO:0000269|PubMed:17562858"; MUTAGEN 296; /note="E->A: No effet on oligomerization,impairs binding of 'Lys-63'-linked ubiuitin and linear tetra-ubiquitin, impairs TNF-induced NF-kappa-B activation."; /evidence="ECO:0000269|PubMed:19854204"; MUTAGEN 300; /note="V->D: Greatly impairs tandem ubiquitin binding."; /evidence="ECO:0000269|PubMed:19185524"; MUTAGEN 301; /note="L->A: Impairs tandem ubiquitin binding."; /evidence="ECO:0000269|PubMed:19185524"; MUTAGEN 302; /note="K->R: No effect on MARCH2F-mediated K48-linked ubiquitination."; /evidence="ECO:0000269|PubMed:32935379"; MUTAGEN 304; /note="Q->A: Complete loss of cleavage by HAV protease 3c."; /evidence="ECO:0000269|PubMed:24920812"; MUTAGEN 304; /note="Q->A: Impairs tandem ubiquitin binding."; /evidence="ECO:0000269|PubMed:19185524"; MUTAGEN 307; /note="I->N: Greatly impairs tandem ubiquitin binding."; /evidence="ECO:0000269|PubMed:19185524"; MUTAGEN 308; /note="Y->A: Greatly impairs tandem ubiquitin binding."; /evidence="ECO:0000269|PubMed:19185524"; MUTAGEN 309; /note="K->A: Partial abolition of sumoylation. Abolishes sumoylation and IKK activation; when associated with A-277. No effect on MARCH2F-mediated K48-linked ubiquitination."; /evidence="ECO:0000269|PubMed:14651848, ECO:0000269|PubMed:32935379"; MUTAGEN 312; /note="F->A: Greatly impairs tandem ubiquitin binding,impairs oligomerization, impairs TNF-induced NF-kappa-B activation."; /evidence="ECO:0000269|PubMed:19185524, ECO:0000269|PubMed:19854204"; MUTAGEN 312; /note="F->W: MNo effet on oligomerization, preferentially binds tri-ubiquitin chains ('Lys-48' or 'Lys-63'-linked)."; /evidence="ECO:0000269|PubMed:19185524, ECO:0000269|PubMed:19854204"; MUTAGEN 312; /note="F->Y: Impairs tandem ubiquitin binding."; /evidence="ECO:0000269|PubMed:19185524, ECO:0000269|PubMed:19854204"; MUTAGEN 313; /note="Q->A: Impairs tandem ubiquitin binding."; /evidence="ECO:0000269|PubMed:19185524"; MUTAGEN 315; /note="E->Q: Greatly impairs tandem ubiquitin binding."; /evidence="ECO:0000269|PubMed:19854204"; MUTAGEN 317; /note="Q->A,W: Greatly impairs tandem ubiquitin binding."; /evidence="ECO:0000269|PubMed:19185524"; MUTAGEN 321; /note="K->R: No effect on MARCH2F-mediated K48-linked ubiquitination."; /evidence="ECO:0000269|PubMed:32935379"; MUTAGEN 323; /note="A->D: Greatly impairs tandem ubiquitin binding."; /evidence="ECO:0000269|PubMed:19854204"; MUTAGEN 325; /note="K->R: No effect on MARCH2F-mediated K48-linked ubiquitination."; /evidence="ECO:0000269|PubMed:32935379"; MUTAGEN 326; /note="K->R: Abolishes MARCH2F-mediated K48-linked ubiquitination and subsequent suppression of antiviral and antibacterial innate immune response."; /evidence="ECO:0000269|PubMed:32935379"; MUTAGEN 329; /note="L->A: Impairs oligomerization, impairs binding of 'Lys-63'-linked ubiuitin, impairs TNF-induced NF-kappa-B activation; when associated with A-336."; /evidence="ECO:0000269|PubMed:16547522, ECO:0000269|PubMed:19854204"; MUTAGEN 329; /note="L->P: Abolished ubiquitin-binding."; /evidence="ECO:0000269|PubMed:16547522, ECO:0000269|PubMed:18287044, ECO:0000269|PubMed:19854204"; MUTAGEN 336; /note="L->A: Impairs oligomerization, impairs binding of 'Lys-63'-linked ubiuitin, impairs TNF-induced NF-kappa-B activation; when associated with A-329."; /evidence="ECO:0000269|PubMed:19854204"; MUTAGEN 342; /note="K->R: No effect on MARCH2F-mediated K48-linked ubiquitination."; /evidence="ECO:0000269|PubMed:32935379"; MUTAGEN 344; /note="K->R: No effect on MARCH2F-mediated K48-linked ubiquitination."; /evidence="ECO:0000269|PubMed:32935379"; MUTAGEN 358; /note="K->R: No effect on MARCH2F-mediated K48-linked ubiquitination."; /evidence="ECO:0000269|PubMed:32935379"; MUTAGEN 399; /note="K->R: Abolishes BCL10-mediated but not RIPK2-mediated ubiquitination. Important decrease in the ubiquitination level; when associated with R-285. No change in the ubiquitination level; when associated with R-115 or R-224."; /evidence="ECO:0000269|PubMed:14695475, ECO:0000269|PubMed:15620648"; MUTAGEN 414; /note="V->S: Abolishes binding to polyubiquitin."; /evidence="ECO:0000269|PubMed:19033441"; MUTAGEN 415; /note="M->S: Impairs binding to polyubiquitin."; /evidence="ECO:0000269|PubMed:19033441
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-68 attenuates aminoterminal homodimerization. {ECO:0000269|PubMed:17977820}.; PTM: Polyubiquitinated on Lys-285 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 (PubMed:15620648, PubMed:17562858, PubMed:19136968). Polyubiquitinated on Lys-285 and Lys-399 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 (PubMed:14695475, PubMed:17562858, PubMed:19136968). Monoubiquitinated on Lys-277 and Lys-309; promotes nuclear export (PubMed:14651848). Polyubiquitinated through 'Lys-27' by TRIM23; involved in antiviral innate and inflammatory responses (PubMed:20724660). Linear polyubiquitinated on Lys-111, Lys-143, Lys-226, Lys-246, Lys-264, Lys-277, Lys-285, Lys-292, Lys-302, Lys-309 and Lys-326; the head-to-tail polyubiquitination is mediated by the LUBAC complex and plays a key role in NF-kappa-B activation (PubMed:21455181). Deubiquitinated by USP10 in a TANK-dependent and -independent manner, leading to the negative regulation of NF-kappa-B signaling upon DNA damage (PubMed:25861989). Ubiquitinated at Lys-326 by MARCHF2 following bacterial and viral infection which leads to its degradation (PubMed:32935379). Polyubiquitinated via 'Lys-29'-linked ubiquitin; leading to lysosomal degradation (PubMed:21518757). {ECO:0000269|PubMed:14651848, ECO:0000269|PubMed:14695475, ECO:0000269|PubMed:15620648, ECO:0000269|PubMed:17562858, ECO:0000269|PubMed:19136968, ECO:0000269|PubMed:20724660, ECO:0000269|PubMed:21455181, ECO:0000269|PubMed:21518757, ECO:0000269|PubMed:25861989, ECO:0000269|PubMed:32935379}.; PTM: Sumoylated on Lys-277 and Lys-309 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:0000269|PubMed:14651848, ECO:0000269|PubMed:16497931, ECO:0000269|PubMed:19136968, ECO:0000269|PubMed:20010814, ECO:0000269|PubMed:21455181}.; PTM: Neddylated by TRIM40, resulting in stabilization of NFKBIA and down-regulation of NF-kappa-B activity. {ECO:0000269|PubMed:21474709}.; PTM: (Microbial infection) Cleaved by hepatitis A virus (HAV) protease 3C allowing the virus to disrupt the host innate immune signaling. {ECO:0000269|PubMed:24920812}.; PTM: (Microbial infection) Deubiquitinated by Epstein-Barr virus BPLF1 on both 'Lys-48' and 'Lys-63'-linked ubiquitin chains; leading to NF-kappa-B signaling inhibition. {ECO:0000269|PubMed:24586164}.; PTM: (Microbial infection) Polyubiquitinated on Lys-309 and Lys-321 via 'Lys-27'-linked ubiquitin by Shigella flexneri E3 ubiquitin-protein ligase ipah9.8, leading to its degradation by the proteasome. {ECO:0000269|PubMed:20010814}.; PTM: (Microbial infection) Polyubiquitination through 'Lys-63' is interrupted by interaction with SARS coronavirus-2/SARS-CoV-2 virus protein ORF9B which inhibits the NF-kappa-B pathway. {ECO:0000269|PubMed:33567255}.
uniprot
proteins
pubmed
10087442
uniprot
proteins
pubmed
10364167
uniprot
proteins
pubmed
10839543
uniprot
proteins
pubmed
10944468
uniprot
proteins
pubmed
11047757
uniprot
proteins
pubmed
11064457
uniprot
proteins
pubmed
11080499
uniprot
proteins
pubmed
11224521
uniprot
proteins
pubmed
11242109
uniprot
proteins
pubmed
11389905
uniprot
proteins
pubmed
11418127
uniprot
proteins
pubmed
11590134
uniprot
proteins
pubmed
11971985
uniprot
proteins
pubmed
12045264
uniprot
proteins
pubmed
12133833
uniprot
proteins
pubmed
12612076
uniprot
proteins
pubmed
12657630
uniprot
proteins
pubmed
12917691
uniprot
proteins
pubmed
14651848
uniprot
proteins
pubmed
14695475
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14754897
uniprot
proteins
pubmed
15100680
uniprot
proteins
pubmed
15125833
uniprot
proteins
pubmed
15229184
uniprot
proteins
pubmed
15356572
uniprot
proteins
pubmed
15456791
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15620648
uniprot
proteins
pubmed
15772651
uniprot
proteins
pubmed
16360037
uniprot
proteins
pubmed
16497931
uniprot
proteins
pubmed
16547522
uniprot
proteins
pubmed
16818673
uniprot
proteins
pubmed
16950813
uniprot
proteins
pubmed
17135271
uniprot
proteins
pubmed
17562858
uniprot
proteins
pubmed
17728323
uniprot
proteins
pubmed
17977820
uniprot
proteins
pubmed
18079694
uniprot
proteins
pubmed
18164680
uniprot
proteins
pubmed
18287044
uniprot
proteins
pubmed
18313693
uniprot
proteins
pubmed
18462684
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19033441
uniprot
proteins
pubmed
19136968
uniprot
proteins
pubmed
19185524
uniprot
proteins
pubmed
19854139
uniprot
proteins
pubmed
19854204
uniprot
proteins
pubmed
20010814
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20434027
uniprot
proteins
pubmed
20724660
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21455173
uniprot
proteins
pubmed
21455180
uniprot
proteins
pubmed
21455181
uniprot
proteins
pubmed
21474709
uniprot
proteins
pubmed
21518757
uniprot
proteins
pubmed
21606507
uniprot
proteins
pubmed
22099304
uniprot
proteins
pubmed
22672233
uniprot
proteins
pubmed
23453969
uniprot
proteins
pubmed
24012789
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24339369
uniprot
proteins
pubmed
24586164
uniprot
proteins
pubmed
24920812
uniprot
proteins
pubmed
25152375
uniprot
proteins
pubmed
25861989
uniprot
proteins
pubmed
26296658
uniprot
proteins
pubmed
26334375
uniprot
proteins
pubmed
27695001
uniprot
proteins
pubmed
27777308
uniprot
proteins
pubmed
28490597
uniprot
proteins
pubmed
31874111
uniprot
proteins
pubmed
32935379
uniprot
proteins
pubmed
33567255
uniprot
proteins
pubmed
35289316
uniprot
proteins
pubmed
9751060
uniprot
proteins
pubmed
9891086
uniprot
proteins
pubmed
9927690
uniprot
proteins
sequence_length
419
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14651848, ECO:0000269|PubMed:24586164}. Nucleus {ECO:0000269|PubMed:14651848}. Note=Sumoylated NEMO accumulates in the nucleus in response to genotoxic stress. {ECO:0000269|PubMed:14651848}.
uniprot
proteins