Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9Y6K9

- NEMO_HUMAN

UniProt

Q9Y6K9 - NEMO_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

NF-kappa-B essential modulator

Gene

IKBKG

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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. Its binding to scaffolding polyubiquitin seems to play a role in IKK activation by multiple signaling receptor pathways. However, the specific type of polyubiquitin recognized upon cell stimulation (either 'Lys-63'-linked or linear polyubiquitin) and its functional importance is reported conflictingly. Also considered to be a mediator for TAX activation of NF-kappa-B. 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.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri396 – 41722C2HC-typeAdd
BLAST

GO - Molecular functioni

  1. linear polyubiquitin binding Source: ParkinsonsUK-UCL
  2. metal ion binding Source: UniProtKB-KW
  3. protein domain specific binding Source: UniProtKB
  4. protein heterodimerization activity Source: UniProtKB
  5. protein homodimerization activity Source: UniProtKB
  6. signal transducer activity Source: ProtInc
  7. ubiquitin protein ligase binding Source: ParkinsonsUK-UCL

GO - Biological processi

  1. activation of MAPK activity Source: Reactome
  2. activation of NF-kappaB-inducing kinase activity Source: Ensembl
  3. apoptotic process Source: ProtInc
  4. B cell homeostasis Source: Ensembl
  5. cellular response to DNA damage stimulus Source: UniProtKB
  6. Fc-epsilon receptor signaling pathway Source: Reactome
  7. I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  8. immune response Source: ProtInc
  9. inflammatory response Source: UniProtKB
  10. innate immune response Source: UniProtKB
  11. JNK cascade Source: Reactome
  12. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
  13. MyD88-independent toll-like receptor signaling pathway Source: Reactome
  14. negative regulation of neuron death Source: ParkinsonsUK-UCL
  15. nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway Source: Reactome
  16. nucleotide-binding oligomerization domain containing signaling pathway Source: Reactome
  17. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: MGI
  18. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  19. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  20. positive regulation of type I interferon production Source: Reactome
  21. response to virus Source: UniProtKB
  22. stress-activated MAPK cascade Source: Reactome
  23. T cell receptor signaling pathway Source: UniProtKB
  24. toll-like receptor 10 signaling pathway Source: Reactome
  25. toll-like receptor 2 signaling pathway Source: Reactome
  26. toll-like receptor 3 signaling pathway Source: Reactome
  27. toll-like receptor 4 signaling pathway Source: Reactome
  28. toll-like receptor 5 signaling pathway Source: Reactome
  29. toll-like receptor 9 signaling pathway Source: Reactome
  30. toll-like receptor signaling pathway Source: Reactome
  31. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
  32. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
  33. transcription, DNA-templated Source: UniProtKB-KW
  34. TRIF-dependent toll-like receptor signaling pathway Source: Reactome
  35. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_118563. RIP-mediated NFkB activation via ZBP1.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_12555. Downstream TCR signaling.
REACT_163994. FCERI mediated NF-kB activation.
REACT_21281. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
REACT_21368. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
REACT_21399. activated TAK1 mediates p38 MAPK activation.
REACT_22442. Interleukin-1 signaling.
REACT_24918. IRAK1 recruits IKK complex.
REACT_24969. TRAF6 mediated NF-kB activation.
REACT_25039. NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
REACT_25354. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
REACT_25374. IKK complex recruitment mediated by RIP1.
REACT_75776. NOD1/2 Signaling Pathway.
SABIO-RKQ9Y6K9.

Names & Taxonomyi

Protein namesi
Recommended name:
NF-kappa-B essential modulator
Short name:
NEMO
Alternative name(s):
FIP-3
IkB kinase-associated protein 1
Short name:
IKKAP1
Inhibitor of nuclear factor kappa-B kinase subunit gamma
Short name:
I-kappa-B kinase subunit gamma
Short name:
IKK-gamma
Short name:
IKKG
Short name:
IkB kinase subunit gamma
NF-kappa-B essential modifier
Gene namesi
Name:IKBKG
Synonyms:FIP3, NEMO
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:5961. IKBKG.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication
Note: Sumoylated NEMO accumulates in the nucleus in response to genotoxic stress.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. IkappaB kinase complex Source: UniProtKB
  4. intracellular Source: LIFEdb
  5. nucleus Source: UniProtKB
  6. ubiquitin ligase complex Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Ectodermal dysplasia, anhidrotic, with immunodeficiency X-linked (EDAID) [MIM:300291]: A form of ectoderma dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. Characterized by absence of sweat glands, sparse scalp hair, rare conical teeth and immunological abnormalities resulting in severe infectious diseases.5 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti153 – 1531L → R in EDAID. 2 Publications
VAR_026495
Natural varianti175 – 1751R → P in EDAID. 1 Publication
Corresponds to variant rs179363868 [ dbSNP | Ensembl ].
VAR_011320
Natural varianti227 – 2271L → P in EDAID. 1 Publication
Corresponds to variant rs179363869 [ dbSNP | Ensembl ].
VAR_011321
Natural varianti288 – 2881A → G in EDAID. 1 Publication
VAR_011322
Natural varianti311 – 3111D → N in EDAID; abolishes binding to polyubiquitin ('K63'-linked and linear) and greatly impairs tandem ubiquitin binding. 1 Publication
Corresponds to variant rs179363867 [ dbSNP | Ensembl ].
VAR_011323
Natural varianti406 – 4061D → V in EDAID. 1 Publication
VAR_011324
Natural varianti417 – 4171C → F in EDAID. 2 Publications
Corresponds to variant rs137853326 [ dbSNP | Ensembl ].
VAR_011325
Natural varianti417 – 4171C → R in EDAID; loss of sumoylation. 5 Publications
VAR_011326
Ectodermal dysplasia, anhidrotic, with immunodeficiency, osteopetrosis and lymphedema (OLEDAID) [MIM:300301]: A form of ectoderma dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. Characterized by the association of anhidrotic ectodermal dysplasia with severe immunodeficiency, osteopetrosis and lymphedema.
Note: The disease is caused by mutations affecting the gene represented in this entry.
Immunodeficiency, NEMO-related, without anhidrotic ectodermal dysplasia (NEMOID) [MIM:300584]: Patients manifest immunodeficiency not associated with other abnormalities, and resulting in increased susceptibility to infections. Patients suffer from multiple episodes of infectious diseases.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti417 – 4171C → Y in NEMOID. 1 Publication
Corresponds to variant rs137853326 [ dbSNP | Ensembl ].
VAR_026496
Immunodeficiency 33 (IMD33) [MIM:300636]: A X-linked recessive form of Mendelian susceptibility to mycobacterial disease, a rare condition characterized by predisposition to illness caused by moderately virulent mycobacterial species, such as Bacillus Calmette-Guerin (BCG) vaccine, environmental non-tuberculous mycobacteria, and by the more virulent Mycobacterium tuberculosis. Other microorganisms rarely cause severe clinical disease in individuals with susceptibility to mycobacterial infections, with the exception of Salmonella which infects less than 50% of these individuals.1 Publication
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti315 – 3151E → A in IMD33; greatly impairs tandem ubiquitin binding. 1 Publication
VAR_031959
Natural varianti319 – 3191R → Q in IMD33; impairs tandem ubiquitin binding. 1 Publication
VAR_031960
Recurrent isolated invasive pneumococcal disease 2 (IPD2) [MIM:300640]: Recurrent invasive pneumococcal disease (IPD) is defined as two episodes of IPD occurring at least 1 month apart, whether caused by the same or different serotypes or strains. Recurrent IPD occurs in at least 2% of patients in most series, making IPD the most important known risk factor for subsequent IPD.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti173 – 1731R → G in IPD2. 1 Publication
Corresponds to variant rs179363866 [ dbSNP | Ensembl ].
VAR_031958
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.4 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti57 – 571E → K in IP; shows the same luciferase activity as the control. 2 Publications
Corresponds to variant rs148695964 [ dbSNP | Ensembl ].
VAR_026491
Natural varianti90 – 901Missing in IP; only 46.3% of the activation obtained with the wild-type protein. 1 Publication
VAR_026492
Natural varianti123 – 1231R → W in IP; shows the same luciferase activity as the control. 1 Publication
Corresponds to variant rs179363895 [ dbSNP | Ensembl ].
VAR_026494
Natural varianti173 – 1731R → G in IPD2. 1 Publication
Corresponds to variant rs179363866 [ dbSNP | Ensembl ].
VAR_031958
Natural varianti323 – 3231A → P in IP; diminishes interaction with TRAF6 and polyubiquitination, greatly impairs tandem ubiquitin binding. 1 Publication
Corresponds to variant rs179363865 [ dbSNP | Ensembl ].
VAR_042666
Natural varianti407 – 4071M → V in IP; impairs binding to ubiquitin. 2 Publications
VAR_009182

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi68 – 681S → A: Increases formation of homodimers. 1 Publication
Mutagenesisi68 – 681S → E: Abolishes interaction with IKBKB; abolishes TNF-alpha induced NF-kappa-B activity. 1 Publication
Mutagenesisi85 – 851S → A: Decreases ubiquitination and abolishes nuclear export. 1 Publication
Mutagenesisi115 – 1151K → R: No change in the ubiquitination level; when associated with R-399. 1 Publication
Mutagenesisi224 – 2241K → R: No change in the ubiquitination level; when associated with R-399. 1 Publication
Mutagenesisi277 – 2771K → A: Partial abolition of sumoylation. Abolishes sumoylation and IKK activation; when associated with A-309. 1 Publication
Mutagenesisi285 – 2851K → R: Important decrease in the ubiquitination level; when associated with R-399. 1 Publication
Mutagenesisi296 – 2961E → A: No effet on oligomerization,impairs binding of 'Lys-63'-linked ubiuitin and linear tetra-ubiquitin, impairs TNF-induced NF-kappa-B activation. 1 Publication
Mutagenesisi300 – 3001V → D: Greatly impairs tandem ubiquitin binding. 1 Publication
Mutagenesisi301 – 3011L → A: Impairs tandem ubiquitin binding. 1 Publication
Mutagenesisi304 – 3041Q → A: Impairs tandem ubiquitin binding. 1 Publication
Mutagenesisi307 – 3071I → N: Greatly impairs tandem ubiquitin binding. 1 Publication
Mutagenesisi308 – 3081Y → A: Greatly impairs tandem ubiquitin binding. 1 Publication
Mutagenesisi309 – 3091K → A: Partial abolition of sumoylation. Abolishes sumoylation and IKK activation; when associated with A-277. 1 Publication
Mutagenesisi312 – 3121F → A: Greatly impairs tandem ubiquitin binding,impairs oligomerization, impairs TNF-induced NF-kappa-B activation. 2 Publications
Mutagenesisi312 – 3121F → W: MNo effet on oligomerization, preferentially binds tri-ubiquitin chains ('Lys-48' or 'Lys-63'-linked). 2 Publications
Mutagenesisi312 – 3121F → Y: Impairs tandem ubiquitin binding. 2 Publications
Mutagenesisi313 – 3131Q → A: Impairs tandem ubiquitin binding. 1 Publication
Mutagenesisi315 – 3151E → A: Impairs oligomerization, impairs binding of 'Lys-63'-linked ubiuitin and linear tetra-ubiquitin, impairs TNF-induced NF-kappa-B activation. 1 Publication
Mutagenesisi315 – 3151E → Q: Greatly impairs tandem ubiquitin binding. 1 Publication
Mutagenesisi317 – 3171Q → A or W: Greatly impairs tandem ubiquitin binding. 1 Publication
Mutagenesisi323 – 3231A → D: Greatly impairs tandem ubiquitin binding. 1 Publication
Mutagenesisi323 – 3231A → P: Impairs oligomerization, greatly impairs binding of 'Lys-63'-linked ubiuitin, and linear tetra-ubiquitin, impairs TNF-induced NF-kappa-B activation. 1 Publication
Mutagenesisi329 – 3291L → A: Impairs oligomerization, impairs binding of 'Lys-63'-linked ubiuitin, impairs TNF-induced NF-kappa-B activation; when associated with A-336. 2 Publications
Mutagenesisi329 – 3291L → P: Abolishes binding to polyubiquitin. 2 Publications
Mutagenesisi336 – 3361L → A: Impairs oligomerization, impairs binding of 'Lys-63'-linked ubiuitin, impairs TNF-induced NF-kappa-B activation; when associated with A-329. 1 Publication
Mutagenesisi399 – 3991K → 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. 2 Publications
Mutagenesisi414 – 4141V → S: Abolishes binding to polyubiquitin. 1 Publication
Mutagenesisi415 – 4151M → S: Impairs binding to polyubiquitin. 1 Publication

Keywords - Diseasei

Disease mutation, Ectodermal dysplasia, Osteopetrosis

Organism-specific databases

MIMi300291. phenotype.
300301. phenotype.
300584. phenotype.
300636. phenotype.
300640. phenotype.
308300. phenotype.
Orphaneti69088. Anhidrotic ectodermal dysplasia - immunodeficiency - osteopetrosis - lymphedema.
98813. Hypohidrotic ectodermal dysplasia with immunodeficiency.
464. Incontinentia pigmenti.
319612. X-linked mendelian susceptibility to mycobacterial diseases due to IKBKG deficiency.
PharmGKBiPA29777.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 419419NF-kappa-B essential modulatorPRO_0000096782Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei31 – 311Phosphoserine; by IKKB1 Publication
Modified residuei43 – 431Phosphoserine; by IKKB1 Publication
Disulfide bondi54 – 54Interchain1 Publication
Modified residuei68 – 681Phosphoserine1 Publication
Modified residuei85 – 851Phosphoserine; by ATM1 Publication
Cross-linki111 – 111Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki139 – 139Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki143 – 143Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki226 – 226Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki246 – 246Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki264 – 264Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki277 – 277Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Cross-linki277 – 277Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate2 Publications
Cross-linki283 – 283Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki285 – 285Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)3 Publications
Cross-linki292 – 292Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki302 – 302Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki309 – 309Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Cross-linki309 – 309Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate4 Publications
Cross-linki321 – 321Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki325 – 325Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki326 – 326Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Disulfide bondi347 – 347Interchain1 Publication
Modified residuei376 – 3761Phosphoserine; by IKKB1 Publication
Modified residuei387 – 3871Phosphoserine1 Publication
Cross-linki399 – 399Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Post-translational modificationi

Phosphorylation at Ser-68 attenuates aminoterminal homodimerization.1 Publication
Polyubiquitinated on Lys-285 through 'Lys-63'; the ubiquitination is mediated by 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. Polyubiquitinated on Lys-399 through 'Lys-63'; 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. Monoubiquitinated on Lys-277 and Lys-309; promotes nuclear export. Polyubiquitinated through 'Lys-27' by TRIM23; involved in antiviral innate and inflammatory responses. 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. 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.6 Publications
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.5 Publications
Neddylated by TRIM40, resulting in stabilization of NFKBIA and down-regulation of NF-kappa-B activity.1 Publication

Keywords - PTMi

Disulfide bond, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9Y6K9.
PaxDbiQ9Y6K9.
PRIDEiQ9Y6K9.

PTM databases

PhosphoSiteiQ9Y6K9.

Expressioni

Tissue specificityi

Heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.

Gene expression databases

BgeeiQ9Y6K9.
CleanExiHS_IKBKG.
GenevestigatoriQ9Y6K9.

Organism-specific databases

HPAiCAB010373.
HPA000426.

Interactioni

Subunit structurei

Homodimer; disulfide-linked. Component of the I-kappa-B-kinase (IKK) core complex consisting of CHUK, IKBKB and IKBKG; probably four alpha/CHUK-beta/IKBKB dimers are associated with four gamma/IKBKG subunits. The IKK core complex seems to associate with regulatory or adapter proteins to form a IKK-signalosome holo-complex. The IKK complex associates with TERF2IP/RAP1, leading to promote IKK-mediated phosphorylation of RELA/p65. Part of a complex composed of NCOA2, NCOA3, CHUK/IKKA, IKBKB, IKBKG and CREBBP. Interacts with COPS3, CYLD, NALP2, TRPC4AP and LRDD. Interacts with ATM; the complex is exported from the nucleus. Interacts with TRAF6. Interacts with HTLV-1 Tax oncoprotein; the interaction activates IKBKG. Interacts with IKBKE. Interacts with TANK; the interaction is enhanced by IKBKE and TBK1. Part of a ternary complex consisting of TANK, IKBKB and IKBKG. Interacts with ZFAND5. Interacts with RIPK2. Interacts with TNIP1 and TNFAIP3; TNIP1 facilitates the TNFAIP3-mediated de-ubiquitination of IKBKG. Interacts with TNFAIP3; the interaction is induced by TNF stimulation and by polyubiquitin. Binds polyubiquitin; the interaction is mediated by two domains; reports about the binding to 'Lys-63'-linked and/or linear polyubiquitin, respective binding affinities and stoichiometry are conflicting. Interacts with Shigella flexneri ipah9.8; the interaction promotes TNIP1-dependent 'Lys-27'-linked polyubiquitination of IKBKG which perturbs NF-kappa-B activation during bacterial infection. Interacts with NLRP10.21 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ADAP2Q9NPF82EBI-81279,EBI-718895
ANXA1P040836EBI-81279,EBI-354007
ARL6IP4Q66PJ32EBI-81279,EBI-2683099
ATMQ133154EBI-81279,EBI-495465
ATRQ135352EBI-81279,EBI-968983
CALB1P059373EBI-81279,EBI-4286943
CDC37Q165434EBI-81279,EBI-295634
CDK2P249414EBI-81279,EBI-375096
CHUKO1511120EBI-81279,EBI-81249
COPS3Q9UNS22EBI-81279,EBI-350590
FLT3P368882EBI-81279,EBI-3946257
GIT2Q141616EBI-81279,EBI-1046878
HSP90AA1P079003EBI-81279,EBI-296047
HSP90AB1P082382EBI-81279,EBI-352572
IKBKBO1492025EBI-81279,EBI-81266
ipaH9.8Q8VSC38EBI-81279,EBI-6125799From a different organism.
KRT18P057833EBI-81279,EBI-297888
KRT8P057872EBI-81279,EBI-297852
MALT1Q9UDY82EBI-81279,EBI-1047372
MYCP011063EBI-81279,EBI-447544
NFKBIAP259635EBI-81279,EBI-307386
PPP2CAP677754EBI-81279,EBI-712311
RBCK1Q9BYM84EBI-81279,EBI-2340624
RIPK1Q135467EBI-81279,EBI-358507
RNF7Q9UBF63EBI-81279,EBI-398632
RUSC1Q9BVN2-24EBI-81279,EBI-6257338
SENP2Q9HC623EBI-81279,EBI-714881
SHARPINQ9H0F64EBI-81279,EBI-3942966
SQSTM1Q135012EBI-81279,EBI-307104
SRCP129313EBI-81279,EBI-621482
SUMO1P631653EBI-81279,EBI-80140
SYT1P215793EBI-81279,EBI-524909
TBK1Q9UHD22EBI-81279,EBI-356402
TNFP013752EBI-81279,EBI-359977
TNFAIP3P215804EBI-81279,EBI-527670
TNIP1Q150254EBI-81279,EBI-357849
TNIP2Q8NFZ56EBI-81279,EBI-359372
UBCP0CG484EBI-81279,EBI-3390054
ZC3H12AQ5D1E82EBI-81279,EBI-747793

Protein-protein interaction databases

BioGridi114089. 293 interactions.
DIPiDIP-27528N.
IntActiQ9Y6K9. 171 interactions.
MINTiMINT-128245.
STRINGi9606.ENSP00000358622.

Structurei

Secondary structure

1
419
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi50 – 10859Combined sources
Turni194 – 1963Combined sources
Helixi197 – 24953Combined sources
Helixi260 – 2689Combined sources
Helixi271 – 29525Combined sources
Helixi297 – 34145Combined sources
Beta strandi394 – 3963Combined sources
Beta strandi403 – 4064Combined sources
Helixi407 – 41610Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JVXNMR-A394-419[»]
2JVYNMR-A394-419[»]
3BRTX-ray2.25B/D44-111[»]
3BRVX-ray2.20B/D44-111[»]
3CL3X-ray3.20D/E150-272[»]
3FX0X-ray3.20A/B246-337[»]
4BWNX-ray2.27A/B258-344[»]
ProteinModelPortaliQ9Y6K9.
SMRiQ9Y6K9. Positions 49-109, 193-251, 263-333, 394-419.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y6K9.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni44 – 11168Interaction with CHUK/IKBKBAdd
BLAST
Regioni150 – 257108Interaction with TANKAdd
BLAST
Regioni242 – 350109Ubiquitin-binding (UBD)Add
BLAST
Regioni246 – 365120Self-associationAdd
BLAST
Regioni251 – 419169Required for interaction with TNFAIP3Add
BLAST
Regioni322 – 34322Leucine-zipperSequence AnalysisAdd
BLAST
Regioni382 – 41938Interaction with CYLDAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili49 – 356308Sequence AnalysisAdd
BLAST

Domaini

The leucine-zipper domain and the C2HC-type zinc-finger are essential for polyubiquitin binding and for the activation of IRF3.2 Publications

Sequence similaritiesi

Contains 1 C2HC-type zinc finger.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri396 – 41722C2HC-typeAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiNOG138369.
GeneTreeiENSGT00530000063808.
HOGENOMiHOG000293233.
HOVERGENiHBG000417.
InParanoidiQ9Y6K9.
KOiK07210.
OMAiPETFQRC.
PhylomeDBiQ9Y6K9.
TreeFamiTF326608.

Family and domain databases

InterProiIPR021063. NEMO_N.
[Graphical view]
PfamiPF11577. NEMO. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9Y6K9-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MNRHLWKSQL CEMVQPSGGP AADQDVLGEE SPLGKPAMLH LPSEQGAPET
60 70 80 90 100
LQRCLEENQE LRDAIRQSNQ ILRERCEELL HFQASQREEK EFLMCKFQEA
110 120 130 140 150
RKLVERLGLE KLDLKRQKEQ ALREVEHLKR CQQQMAEDKA SVKAQVTSLL
160 170 180 190 200
GELQESQSRL EAATKECQAL EGRARAASEQ ARQLESEREA LQQQHSVQVD
210 220 230 240 250
QLRMQGQSVE AALRMERQAA SEEKRKLAQL QVAYHQLFQE YDNHIKSSVV
260 270 280 290 300
GSERKRGMQL EDLKQQLQQA EEALVAKQEV IDKLKEEAEQ HKIVMETVPV
310 320 330 340 350
LKAQADIYKA DFQAERQARE KLAEKKELLQ EQLEQLQREY SKLKASCQES
360 370 380 390 400
ARIEDMRKRH VEVSQAPLPP APAYLSSPLA LPSQRRSPPE EPPDFCCPKC
410
QYQAPDMDTL QIHVMECIE
Length:419
Mass (Da):48,198
Last modified:May 30, 2000 - v2
Checksum:i322D1037881447FF
GO
Isoform 2 (identifier: Q9Y6K9-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MALVIQVGKLRPREVRTPQTINPSLFPSLPVKLSSIIEVPSGGERCCSRRTLVYKARAFWKGAPLPCWM

Show »
Length:487
Mass (Da):55,787
Checksum:i7A39E991E0013A73
GO
Isoform 3 (identifier: Q9Y6K9-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     174-224: Missing.
     257-304: Missing.

Show »
Length:320
Mass (Da):36,953
Checksum:i3BEF2487C4446725
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti341 – 3411S → R in AAD12183. (PubMed:9927690)Curated
Sequence conflicti387 – 3871S → R in AAD12183. (PubMed:9927690)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti57 – 571E → K in IP; shows the same luciferase activity as the control. 2 Publications
Corresponds to variant rs148695964 [ dbSNP | Ensembl ].
VAR_026491
Natural varianti90 – 901Missing in IP; only 46.3% of the activation obtained with the wild-type protein. 1 Publication
VAR_026492
Natural varianti113 – 1131D → N.1 Publication
Corresponds to variant rs179363896 [ dbSNP | Ensembl ].
VAR_026493
Natural varianti123 – 1231R → W in IP; shows the same luciferase activity as the control. 1 Publication
Corresponds to variant rs179363895 [ dbSNP | Ensembl ].
VAR_026494
Natural varianti153 – 1531L → R in EDAID. 2 Publications
VAR_026495
Natural varianti173 – 1731R → G in IPD2. 1 Publication
Corresponds to variant rs179363866 [ dbSNP | Ensembl ].
VAR_031958
Natural varianti175 – 1751R → P in EDAID. 1 Publication
Corresponds to variant rs179363868 [ dbSNP | Ensembl ].
VAR_011320
Natural varianti227 – 2271L → P in EDAID. 1 Publication
Corresponds to variant rs179363869 [ dbSNP | Ensembl ].
VAR_011321
Natural varianti288 – 2881A → G in EDAID. 1 Publication
VAR_011322
Natural varianti311 – 3111D → N in EDAID; abolishes binding to polyubiquitin ('K63'-linked and linear) and greatly impairs tandem ubiquitin binding. 1 Publication
Corresponds to variant rs179363867 [ dbSNP | Ensembl ].
VAR_011323
Natural varianti315 – 3151E → A in IMD33; greatly impairs tandem ubiquitin binding. 1 Publication
VAR_031959
Natural varianti319 – 3191R → Q in IMD33; impairs tandem ubiquitin binding. 1 Publication
VAR_031960
Natural varianti323 – 3231A → P in IP; diminishes interaction with TRAF6 and polyubiquitination, greatly impairs tandem ubiquitin binding. 1 Publication
Corresponds to variant rs179363865 [ dbSNP | Ensembl ].
VAR_042666
Natural varianti406 – 4061D → V in EDAID. 1 Publication
VAR_011324
Natural varianti407 – 4071M → V in IP; impairs binding to ubiquitin. 2 Publications
VAR_009182
Natural varianti417 – 4171C → F in EDAID. 2 Publications
Corresponds to variant rs137853326 [ dbSNP | Ensembl ].
VAR_011325
Natural varianti417 – 4171C → R in EDAID; loss of sumoylation. 5 Publications
VAR_011326
Natural varianti417 – 4171C → Y in NEMOID. 1 Publication
Corresponds to variant rs137853326 [ dbSNP | Ensembl ].
VAR_026496

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MALVIQVGKLRPREVRTPQT INPSLFPSLPVKLSSIIEVP SGGERCCSRRTLVYKARAFW KGAPLPCWM in isoform 2. 1 PublicationVSP_041000
Alternative sequencei174 – 22451Missing in isoform 3. 1 PublicationVSP_041001Add
BLAST
Alternative sequencei257 – 30448Missing in isoform 3. 1 PublicationVSP_041002Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF062089 mRNA. Translation: AAD12183.1.
AF091453 mRNA. Translation: AAD38081.1.
AF074382 mRNA. Translation: AAC36330.1.
AJ271718 Genomic DNA. Translation: CAB93146.1.
AF261086 mRNA. Translation: AAF99679.1.
AY114157 mRNA. Translation: AAM44073.1.
AK000593 mRNA. No translation available.
BT019621 mRNA. Translation: AAV38427.1.
AF277315 Genomic DNA. Translation: AAL27012.1.
BC000299 mRNA. Translation: AAH00299.1.
BC012114 mRNA. Translation: AAH12114.1.
BC046922 mRNA. Translation: AAH46922.1.
BC050612 mRNA. Translation: AAH50612.1.
CCDSiCCDS14757.1. [Q9Y6K9-1]
CCDS48196.1. [Q9Y6K9-2]
CCDS48197.1. [Q9Y6K9-3]
RefSeqiNP_001093326.2. NM_001099856.3. [Q9Y6K9-2]
NP_001093327.1. NM_001099857.2. [Q9Y6K9-1]
NP_001138727.1. NM_001145255.2. [Q9Y6K9-3]
NP_003630.1. NM_003639.4. [Q9Y6K9-1]
XP_005274820.1. XM_005274763.2. [Q9Y6K9-1]
UniGeneiHs.43505.

Genome annotation databases

EnsembliENST00000594239; ENSP00000471166; ENSG00000269335. [Q9Y6K9-1]
ENST00000611071; ENSP00000479662; ENSG00000269335. [Q9Y6K9-1]
ENST00000611176; ENSP00000478616; ENSG00000269335. [Q9Y6K9-3]
ENST00000618670; ENSP00000483825; ENSG00000269335. [Q9Y6K9-2]
GeneIDi8517.
KEGGihsa:8517.
UCSCiuc004fmb.4. human. [Q9Y6K9-1]
uc011mzr.2. human. [Q9Y6K9-2]
uc011mzs.2. human. [Q9Y6K9-3]

Polymorphism databases

DMDMi6685695.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

IKBKGbase

IKBKG mutation db

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF062089 mRNA. Translation: AAD12183.1 .
AF091453 mRNA. Translation: AAD38081.1 .
AF074382 mRNA. Translation: AAC36330.1 .
AJ271718 Genomic DNA. Translation: CAB93146.1 .
AF261086 mRNA. Translation: AAF99679.1 .
AY114157 mRNA. Translation: AAM44073.1 .
AK000593 mRNA. No translation available.
BT019621 mRNA. Translation: AAV38427.1 .
AF277315 Genomic DNA. Translation: AAL27012.1 .
BC000299 mRNA. Translation: AAH00299.1 .
BC012114 mRNA. Translation: AAH12114.1 .
BC046922 mRNA. Translation: AAH46922.1 .
BC050612 mRNA. Translation: AAH50612.1 .
CCDSi CCDS14757.1. [Q9Y6K9-1 ]
CCDS48196.1. [Q9Y6K9-2 ]
CCDS48197.1. [Q9Y6K9-3 ]
RefSeqi NP_001093326.2. NM_001099856.3. [Q9Y6K9-2 ]
NP_001093327.1. NM_001099857.2. [Q9Y6K9-1 ]
NP_001138727.1. NM_001145255.2. [Q9Y6K9-3 ]
NP_003630.1. NM_003639.4. [Q9Y6K9-1 ]
XP_005274820.1. XM_005274763.2. [Q9Y6K9-1 ]
UniGenei Hs.43505.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2JVX NMR - A 394-419 [» ]
2JVY NMR - A 394-419 [» ]
3BRT X-ray 2.25 B/D 44-111 [» ]
3BRV X-ray 2.20 B/D 44-111 [» ]
3CL3 X-ray 3.20 D/E 150-272 [» ]
3FX0 X-ray 3.20 A/B 246-337 [» ]
4BWN X-ray 2.27 A/B 258-344 [» ]
ProteinModelPortali Q9Y6K9.
SMRi Q9Y6K9. Positions 49-109, 193-251, 263-333, 394-419.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114089. 293 interactions.
DIPi DIP-27528N.
IntActi Q9Y6K9. 171 interactions.
MINTi MINT-128245.
STRINGi 9606.ENSP00000358622.

Chemistry

BindingDBi Q9Y6K9.
ChEMBLi CHEMBL2111328.

PTM databases

PhosphoSitei Q9Y6K9.

Polymorphism databases

DMDMi 6685695.

Proteomic databases

MaxQBi Q9Y6K9.
PaxDbi Q9Y6K9.
PRIDEi Q9Y6K9.

Protocols and materials databases

DNASUi 8517.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000594239 ; ENSP00000471166 ; ENSG00000269335 . [Q9Y6K9-1 ]
ENST00000611071 ; ENSP00000479662 ; ENSG00000269335 . [Q9Y6K9-1 ]
ENST00000611176 ; ENSP00000478616 ; ENSG00000269335 . [Q9Y6K9-3 ]
ENST00000618670 ; ENSP00000483825 ; ENSG00000269335 . [Q9Y6K9-2 ]
GeneIDi 8517.
KEGGi hsa:8517.
UCSCi uc004fmb.4. human. [Q9Y6K9-1 ]
uc011mzr.2. human. [Q9Y6K9-2 ]
uc011mzs.2. human. [Q9Y6K9-3 ]

Organism-specific databases

CTDi 8517.
GeneCardsi GC0XP153769.
GeneReviewsi IKBKG.
H-InvDB HIX0203333.
HGNCi HGNC:5961. IKBKG.
HPAi CAB010373.
HPA000426.
MIMi 300248. gene.
300291. phenotype.
300301. phenotype.
300584. phenotype.
300636. phenotype.
300640. phenotype.
308300. phenotype.
neXtProti NX_Q9Y6K9.
Orphaneti 69088. Anhidrotic ectodermal dysplasia - immunodeficiency - osteopetrosis - lymphedema.
98813. Hypohidrotic ectodermal dysplasia with immunodeficiency.
464. Incontinentia pigmenti.
319612. X-linked mendelian susceptibility to mycobacterial diseases due to IKBKG deficiency.
PharmGKBi PA29777.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG138369.
GeneTreei ENSGT00530000063808.
HOGENOMi HOG000293233.
HOVERGENi HBG000417.
InParanoidi Q9Y6K9.
KOi K07210.
OMAi PETFQRC.
PhylomeDBi Q9Y6K9.
TreeFami TF326608.

Enzyme and pathway databases

Reactomei REACT_118563. RIP-mediated NFkB activation via ZBP1.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_12555. Downstream TCR signaling.
REACT_163994. FCERI mediated NF-kB activation.
REACT_21281. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
REACT_21368. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
REACT_21399. activated TAK1 mediates p38 MAPK activation.
REACT_22442. Interleukin-1 signaling.
REACT_24918. IRAK1 recruits IKK complex.
REACT_24969. TRAF6 mediated NF-kB activation.
REACT_25039. NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
REACT_25354. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
REACT_25374. IKK complex recruitment mediated by RIP1.
REACT_75776. NOD1/2 Signaling Pathway.
SABIO-RK Q9Y6K9.

Miscellaneous databases

ChiTaRSi IKBKG. human.
EvolutionaryTracei Q9Y6K9.
GeneWikii IKBKG.
GenomeRNAii 8517.
NextBioi 31882.
PROi Q9Y6K9.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y6K9.
CleanExi HS_IKBKG.
Genevestigatori Q9Y6K9.

Family and domain databases

InterProi IPR021063. NEMO_N.
[Graphical view ]
Pfami PF11577. NEMO. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a cell protein (FIP-3) as a modulator of NF-kappaB activity and as a target of an adenovirus inhibitor of tumor necrosis factor alpha-induced apoptosis."
    Li Y., Kang J., Friedman J., Tarassishin L., Ye J., Kovalenko A., Wallach D., Horwitz M.S.
    Proc. Natl. Acad. Sci. U.S.A. 96:1042-1047(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Isolation of full-length cDNA and chromosomal localization of human NF-kappaB modulator NEMO to Xq28."
    Jin D.-Y., Jeang K.-T.
    J. Biomed. Sci. 6:115-120(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Mammary cancer.
  3. "IKK-gamma is an essential regulatory subunit of the IkappaB kinase complex."
    Rothwarf D.M., Zandi E., Natoli G., Karin M.
    Nature 395:297-300(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
    Tissue: Cervix carcinoma.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT IP VAL-407.
  5. "cDNA cloning by amplification of circularized first strand cDNAs reveals non-IRE-regulated iron-responsive mRNAs."
    Ye Z., Connor J.R.
    Biochem. Biophys. Res. Commun. 275:223-227(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Astrocytoma.
  6. "Ikbkg gene modulates the herpes virus susceptibility in mice."
    Perelygin A.A., Perelygina L.M.
    Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  7. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
  8. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  9. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lung, Placenta and Skin.
  11. "IkappaB kinase (IKK)-associated protein 1, a common component of the heterogeneous IKK complex."
    Mercurio F., Murray B.W., Shevchenko A., Bennett B.L., Young D.B., Li J.W., Pascual G., Motiwala A., Zhu H., Mann M., Manning A.M.
    Mol. Cell. Biol. 19:1526-1538(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 51-419 (ISOFORM 1), PROTEIN SEQUENCE OF 144-159.
    Tissue: Cervix carcinoma.
  12. "Role of adapter function in oncoprotein-mediated activation of NF-kappaB: human T-cell leukemia virus type I Tax interacts directly with IkappaB kinase gamma."
    Jin D.-Y., Giordano V., Kibler K.V., Nakano H., Jeang K.-T.
    J. Biol. Chem. 274:17402-17405(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HTLV-1 TAX-1.
  13. "Activation of IKKalpha and IKKbeta through their fusion with HTLV-I tax protein."
    Xiao G., Sun S.C.
    Oncogene 19:5198-5203(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HTLV-1 TAX-1.
  14. "Functional redundancy of the zinc fingers of A20 for inhibition of NF-kappaB activation and protein-protein interactions."
    Klinkenberg M., Van Huffel S., Heyninck K., Beyaert R.
    FEBS Lett. 498:93-97(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TNFAIP3.
  15. "CSN3 interacts with IKKgamma and inhibits TNF- but not IL-1-induced NF-kappaB activation."
    Hong X., Xu L.-G., Li X., Zhai Z., Shu H.-B.
    FEBS Lett. 499:133-136(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH COPS3.
  16. "Role of ikkgamma/nemo in assembly of the IkappaB kinase complex."
    Li X.-H., Fang X., Gaynor R.B.
    J. Biol. Chem. 276:4494-4500(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT OF THE IKK COMPLEX.
  17. "Association of the adaptor TANK with the I kappa B kinase (IKK) regulator NEMO connects IKK complexes with IKK epsilon and TBK1 kinases."
    Chariot A., Leonardi A., Muller J., Bonif M., Brown K., Siebenlist U.
    J. Biol. Chem. 277:37029-37036(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TANK AND IKBKB.
  18. "Regulation of SRC-3 (pCIP/ACTR/AIB-1/RAC-3/TRAM-1) coactivator activity by I kappa B kinase."
    Wu R.-C., Qin J., Hashimoto Y., Wong J., Xu J., Tsai S.Y., Tsai M.-J., O'Malley B.W.
    Mol. Cell. Biol. 22:3549-3561(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT OF A COMPLEX CONTAINING CREBBP; NCOA2; NCOA3; IKKA AND IKKB.
  19. "Sequential modification of NEMO/IKKgamma by SUMO-1 and ubiquitin mediates NF-kappaB activation by genotoxic stress."
    Huang T.T., Wuerzberger-Davis S.M., Wu Z.H., Miyamoto S.
    Cell 115:565-576(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-277 AND LYS-309, UBIQUITINATION AT LYS-277 AND LYS-309, MUTAGENESIS OF LYS-277 AND LYS-309, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT EDAID ARG-417.
  20. "In vivo identification of inducible phosphoacceptors in the IKKgamma/NEMO subunit of human IkappaB kinase."
    Carter R.S., Pennington K.N., Ungurait B.J., Ballard D.W.
    J. Biol. Chem. 278:19642-19648(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-31; SER-43 AND SER-376.
  21. "Tetrameric oligomerization of IkappaB kinase gamma (IKKgamma) is obligatory for IKK complex activity and NF-kappaB activation."
    Tegethoff S., Behlke J., Scheidereit C.
    Mol. Cell. Biol. 23:2029-2041(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SELF-ASSOCIATION, COMPOSITION OF THE IKK COMPLEX.
  22. "The tumour suppressor CYLD negatively regulates NF-kappaB signalling by deubiquitination."
    Kovalenko A., Chable-Bessia C., Cantarella G., Israeel A., Wallach D., Courtois G.
    Nature 424:801-805(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CYLD.
  23. "The Crohn's disease protein, NOD2, requires RIP2 in order to induce ubiquitinylation of a novel site on NEMO."
    Abbott D.W., Wilkins A., Asara J.M., Cantley L.C.
    Curr. Biol. 14:2217-2227(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION AT LYS-285, MUTAGENESIS OF LYS-115; LYS-224; LYS-285 AND LYS-399.
  24. "ZNF216 is an A20-like and IkappaB kinase gamma-interacting inhibitor of NFkappaB activation."
    Huang J., Teng L., Li L., Liu T., Li L., Chen D., Xu L.-G., Zhai Z., Shu H.-B.
    J. Biol. Chem. 279:16847-16853(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ZFAND5.
  25. "PAN1/NALP2/PYPAF2, an inducible inflammatory mediator that regulates NF-kappaB and caspase-1 activation in macrophages."
    Bruey J.-M., Bruey-Sedano N., Newman R., Chandler S., Stehlik C., Reed J.C.
    J. Biol. Chem. 279:51897-51907(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NALP2.
  26. "The TRAF6 ubiquitin ligase and TAK1 kinase mediate IKK activation by BCL10 and MALT1 in T lymphocytes."
    Sun L., Deng L., Ea C.-K., Xia Z.-P., Chen Z.J.
    Mol. Cell 14:289-301(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION.
  27. "Bcl10 activates the NF-kappaB pathway through ubiquitination of NEMO."
    Zhou H., Wertz I., O'Rourke K., Ultsch M., Seshagiri S., Eby M., Xiao W., Dixit V.M.
    Nature 427:167-171(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, UBIQUITINATION AT LYS-399, MUTAGENESIS OF LYS-399.
  28. "PIDD mediates NF-kappaB activation in response to DNA damage."
    Janssens S., Tinel A., Lippens S., Tschopp J.
    Cell 123:1079-1092(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LRDD.
  29. "Sensing of Lys 63-linked polyubiquitination by NEMO is a key event in NF-kappaB activation."
    Wu C.J., Conze D.B., Li T., Srinivasula S.M., Ashwell J.D.
    Nat. Cell Biol. 8:398-406(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITIN-BINDING, MUTAGENESIS OF LEU-329, CHARACTERIZATION OF VARIANT EDAID ASN-311.
  30. Erratum
    Wu C.J., Conze D.B., Li T., Srinivasula S.M., Ashwell J.D.
    Nat. Cell Biol. 8:424-424(2006)
  31. "Molecular linkage between the kinase ATM and NF-kappaB signaling in response to genotoxic stimuli."
    Wu Z.H., Shi Y., Tibbetts R.S., Miyamoto S.
    Science 311:1141-1146(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ATM, PHOSPHORYLATION AT SER-85, MUTAGENESIS OF SER-85.
  32. "Site-specific Lys-63-linked tumor necrosis factor receptor-associated factor 6 auto-ubiquitination is a critical determinant of I kappa B kinase activation."
    Lamothe B., Besse A., Campos A.D., Webster W.K., Wu H., Darnay B.G.
    J. Biol. Chem. 282:4102-4112(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION.
  33. "Intermolecular disulfide bond formation in the NEMO dimer requires Cys54 and Cys347."
    Herscovitch M., Comb W., Ennis T., Coleman K., Yong S., Armstead B., Kalaitzidis D., Chandani S., Gilmore T.D.
    Biochem. Biophys. Res. Commun. 367:103-108(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, DISULFIDE BONDS.
  34. "A critical role of RICK/RIP2 polyubiquitination in Nod-induced NF-kappaB activation."
    Hasegawa M., Fujimoto Y., Lucas P.C., Nakano H., Fukase K., Nunez G., Inohara N.
    EMBO J. 27:373-383(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RIPK2.
  35. "Phosphorylation of serine 68 in the IkappaB kinase (IKK)-binding domain of NEMO interferes with the structure of the IKK complex and tumor necrosis factor-alpha-induced NF-kappaB activity."
    Palkowitsch L., Leidner J., Ghosh S., Marienfeld R.B.
    J. Biol. Chem. 283:76-86(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IKBKB, PHOSPHORYLATION AT SER-68, MUTAGENESIS OF SER-68.
  36. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  37. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  38. "The zinc finger of NEMO is a functional ubiquitin-binding domain."
    Cordier F., Grubisha O., Traincard F., Veron M., Delepierre M., Agou F.
    J. Biol. Chem. 284:2902-2907(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITIN-BINDING, MUTAGENESIS OF VAL-414 AND MET-415, CHARACTERIZATION OF VARIANT IP VAL-407.
  39. "Key role of Ubc5 and lysine-63 polyubiquitination in viral activation of IRF3."
    Zeng W., Xu M., Liu S., Sun L., Chen Z.J.
    Mol. Cell 36:315-325(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DOMAIN LEUCINE-ZIPPER AND C2HC-TYPE ZINC-FINGER.
  40. Cited for: UBIQUITINATION AT LYS-285 AND LYS-309.
  41. "DARPin-assisted crystallography of the CC2-LZ domain of NEMO reveals a coupling between dimerization and ubiquitin binding."
    Grubisha O., Kaminska M., Duquerroy S., Fontan E., Cordier F., Haouz A., Raynal B., Chiaravalli J., Delepierre M., Israel A., Veron M., Agou F.
    J. Mol. Biol. 395:89-104(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF GLU-296; PHE-312; GLU-315; ALA-323; LEU-329 AND LEU-336.
  42. "A bacterial E3 ubiquitin ligase IpaH9.8 targets NEMO/IKKgamma to dampen the host NF-kappaB-mediated inflammatory response."
    Ashida H., Kim M., Schmidt-Supprian M., Ma A., Ogawa M., Sasakawa C.
    Nat. Cell Biol. 12:66-73(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SHIGELLA FLEXNERI IPAH9.8, UBIQUITINATION AT LYS-309 AND LYS-321.
  43. "Polyubiquitin conjugation to NEMO by tripartite motif protein 23 (TRIM23) is critical in antiviral defense."
    Arimoto K., Funami K., Saeki Y., Tanaka K., Okawa K., Takeuchi O., Akira S., Murakami Y., Shimotohno K.
    Proc. Natl. Acad. Sci. U.S.A. 107:15856-15861(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, UBIQUITINATION.
  44. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  45. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  46. "TRIM40 promotes neddylation of IKKgamma and is downregulated in gastrointestinal cancers."
    Noguchi K., Okumura F., Takahashi N., Kataoka A., Kamiyama T., Todo S., Hatakeyama S.
    Carcinogenesis 32:995-1004(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NEDDYLATION BY TRIM40.
  47. Cited for: UBIQUITIN-BINDING, CHARACTERIZATION OF VARIANT EDAID ASN-311.
  48. "Direct, noncatalytic mechanism of IKK inhibition by A20."
    Skaug B., Chen J., Du F., He J., Ma A., Chen Z.J.
    Mol. Cell 44:559-571(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TNFAIP3.
  49. Cited for: UBIQUITINATION BY THE LUBAC COMPLEX.
  50. "SHARPIN is a component of the NF-kappaB-activating linear ubiquitin chain assembly complex."
    Tokunaga F., Nakagawa T., Nakahara M., Saeki Y., Taniguchi M., Sakata S., Tanaka K., Nakano H., Iwai K.
    Nature 471:633-636(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION BY THE LUBAC COMPLEX.
  51. Cited for: UBIQUITINATION AT LYS-277; LYS-285; LYS-309; LYS-326; LYS-111; LYS-143; LYS-226; LYS-246; LYS-264; LYS-292 AND LYS-302 BY THE LUBAC COMPLEX, UBIQUITINATION AT LYS-139 AND LYS-283.
  52. Cited for: INTERACTION WITH NLRP10.
  53. "IKKepsilon-mediated tumorigenesis requires K63-linked polyubiquitination by a cIAP1/cIAP2/TRAF2 E3 ubiquitin ligase complex."
    Zhou A.Y., Shen R.R., Kim E., Lock Y.J., Xu M., Chen Z.J., Hahn W.C.
    Cell Rep. 3:724-733(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IKBKE.
  54. "Identifying post-translational modifications of NEMO by tandem mass spectrometry after high affinity purification."
    Jackson S.S., Coughlin E.E., Coon J.J., Miyamoto S.
    Protein Expr. Purif. 92:48-53(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-387.
  55. "Solution structure of NEMO zinc finger and impact of an anhidrotic ectodermal dysplasia with immunodeficiency-related point mutation."
    Cordier F., Vinolo E., Veron M., Delepierre M., Agou F.
    J. Mol. Biol. 377:1419-1432(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 394-419 OF WILD-TYPE AND MUTANT PHE-417, DOMAIN ZINC-FINGER.
  56. "Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site."
    Rushe M., Silvian L., Bixler S., Chen L.L., Cheung A., Bowes S., Cuervo H., Berkowitz S., Zheng T., Guckian K., Pellegrini M., Lugovskoy A.
    Structure 16:798-808(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 44-111 IN COMPLEX WITH CHUK AND IKBKB, SUBUNIT.
  57. Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 246-337, UBIQUITIN-BINDING, MUTAGENESIS OF VAL-300; LEU-301; GLN-304; ILE-307; TYR-308; PHE-312; GLN-313 AND GLN-317, CHARACTERIZATION OF VARIANT EDAID ASN-311, CHARACTERIZATION OF VARIANT IMD33 ALA-315, CHARACTERIZATION OF VARIANTS GLN-319 AND IP PRO-323.
  58. "A novel X-linked disorder of immune deficiency and hypohidrotic ectodermal dysplasia is allelic to incontinentia pigmenti and due to mutations in IKK-gamma (NEMO)."
    Zonana J., Elder M.E., Schneider L.C., Orlow S.J., Moss C., Golabi M., Shapira S.K., Farndon P.A., Wara D.W., Emmal S.A., Ferguson B.M.
    Am. J. Hum. Genet. 67:1555-1562(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS EDAID ARG-417 AND PHE-417.
  59. "A recurrent deletion in the ubiquitously expressed NEMO (IKK-gamma) gene accounts for the vast majority of incontinentia pigmenti mutations."
    Aradhya S., Woffendin H., Jakins T., Bardaro T., Esposito T., Smahi A., Shaw C., Levy M., Munnich A., D'Urso M., Lewis R.A., Kenwrick S., Nelson D.L.
    Hum. Mol. Genet. 10:2171-2179(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS IP LYS-57 AND VAL-407.
  60. Cited for: VARIANTS EDAID PRO-175; PRO-227; GLY-288; ASN-311; ARG-417 AND PHE-417.
  61. "Specific missense mutations in NEMO result in hyper-IgM syndrome with hypohydrotic ectodermal dysplasia."
    Jain A., Ma C.A., Liu S., Brown M., Cohen J., Strober W.
    Nat. Immunol. 2:223-228(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS EDAID VAL-406 AND ARG-417.
  62. Cited for: VARIANTS EDAID ARG-153 AND ARG-417.
  63. "Molecular analysis of the genetic defect in a large cohort of IP patients and identification of novel NEMO mutations interfering with NF-kappaB activation."
    Fusco F., Bardaro T., Fimiani G., Mercadante V., Miano M.G., Falco G., Israeel A., Courtois G., D'Urso M., Ursini M.V.
    Hum. Mol. Genet. 13:1763-1773(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS IP LYS-57; LYS-90 DEL AND TRP-123, VARIANT ASN-113, CHARACTERIZATION OF VARIANTS IP LYS-57; LYS-90 DEL AND TRP-123, CHARACTERIZATION OF VARIANT ASN-113.
  64. "The presentation and natural history of immunodeficiency caused by nuclear factor kappaB essential modulator mutation."
    Orange J.S., Jain A., Ballas Z.K., Schneider L.C., Geha R.S., Bonilla F.A.
    J. Allergy Clin. Immunol. 113:725-733(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS EDAID ARG-153 AND ARG-417, VARIANT NEMOID TYR-417.
  65. "Human nuclear factor kappa B essential modulator mutation can result in immunodeficiency without ectodermal dysplasia."
    Orange J.S., Levy O., Brodeur S.R., Krzewski K., Roy R.M., Niemela J.E., Fleisher T.A., Bonilla F.A., Geha R.S.
    J. Allergy Clin. Immunol. 114:650-656(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN NEMOID.
  66. Cited for: VARIANTS IMD33 ALA-315 AND GLN-319.
  67. "Identification of TRAF6-dependent NEMO polyubiquitination sites through analysis of a new NEMO mutation causing incontinentia pigmenti."
    Sebban-Benin H., Pescatore A., Fusco F., Pascuale V., Gautheron J., Yamaoka S., Moncla A., Ursini M.V., Courtois G.
    Hum. Mol. Genet. 16:2805-2815(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT IP PRO-323, CHARACTERIZATION OF VARIANT IP PRO-323, INTERACTION WITH TRAF6.
  68. "IRAK4 and NEMO mutations in otherwise healthy children with recurrent invasive pneumococcal disease."
    Ku C.-L., Picard C., Erdos M., Jeurissen A., Bustamante J., Puel A., von Bernuth H., Filipe-Santos O., Chang H.-H., Lawrence T., Raes M., Marodi L., Bossuyt X., Casanova J.-L.
    J. Med. Genet. 44:16-23(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT IPD2 GLY-173.

Entry informationi

Entry nameiNEMO_HUMAN
AccessioniPrimary (citable) accession number: Q9Y6K9
Secondary accession number(s): Q7LBY6, Q7Z7F1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: November 26, 2014
This is version 165 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3