Q9Y6K9 (NEMO_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 134.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | 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 names |
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| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 419 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| 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. 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 By similarity. Essential for viral activation of IRF3. Ref.26 Ref.34 |
| Subunit structure | 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 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. Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.21 Ref.23 Ref.24 Ref.27 Ref.28 Ref.30 Ref.31 Ref.32 Ref.41 Ref.51 |
| Subcellular location | Cytoplasm. Nucleus. Note: Sumoylated NEMO accumulates in the nucleus in response to genotoxic stress. Ref.18 |
| Tissue specificity | Heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. |
| Domain | The leucine-zipper domain and the C2HC-type zinc-finger are essential for polyubiquitin binding and for the activation of IRF3. Ref.34 Ref.40 |
| Post-translational modification | Phosphorylation at Ser-68 attenuates aminoterminal homodimerization. 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. 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. Sumoylated on Lys-277 and Lys-309 by SUMO1; the modification results in phosphorylation of Ser-85 by ATM leading to a replacement of the sumoylation by mono-ubiquitination on these residues. Ref.18 |
| Involvement in disease | Defects in IKBKG are the cause of ectodermal dysplasia anhidrotic with immunodeficiency X-linked (EDAID) [MIM:300291]; also known as hypohidrotic ectodermal dysplasia with immunodeficiency (HED-ID). Is 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. Ref.18 Ref.42 Ref.44 Ref.45 Ref.46 Ref.48 Defects in IKBKG are the cause of ectodermal dysplasia anhidrotic with immunodeficiency-osteopetrosis-lymphedema (OLEDAID) [MIM:300301]. Defects in IKBKG are a cause of immunodeficiency NEMO-related without anhidrotic ectodermal dysplasia (NEMOID) [MIM:300584]; also called immunodeficiency without anhidrotic ectodermal dysplasia, isolated immunodeficiency or pure immunodeficiency. Patients manifest immunodeficiency not associated with other abnormalities, and resulting in increased infection susceptibility. Patients suffer from multiple episodes of infectious diseases. Ref.48 Ref.49 Defects in IKBKG are the cause of susceptibility to X-linked familial atypical micobacteriosis type 1 (AMCBX1) [MIM:300636]; also known as X-linked disseminated atypical mycobacterial infection type 1 or X-linked susceptibility to mycobacterial disease type 1. AMCBX1 is the X-linked recessive form of mendelian susceptibility to mycobacterial disease (MSMD). MSMD is a congenital syndrome resulting in predisposition to clinical disease caused by weakly virulent mycobacterial species, such as bacillus Calmette-Guerin vaccines and non-tuberculous, environmental mycobacteria. Patients are also susceptible to the more virulent species Mycobacterium tuberculosis. Ref.50 Defects in IKBKG are the cause of recurrent isolated invasive pneumococcal disease type 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. Ref.52 Defects in IKBKG are the cause of incontinentia pigmenti (IP) [MIM:308300]; formerly designed familial incontinentia pigmenti type II (IP2). IP is 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. Ref.4 Ref.43 Ref.47 Ref.51 Ref.52 |
| Sequence similarities | Contains 1 C2HC-type zinc finger. |
Ontologies
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| ANXA1 | P04083 | 6 | EBI-81279,EBI-354007 | |
| CHUK | O15111 | 9 | EBI-81279,EBI-81249 | |
| COPS3 | Q9UNS2 | 2 | EBI-81279,EBI-350590 | |
| GIT2 | Q14161 | 6 | EBI-81279,EBI-1046878 | |
| IKBKB | O14920 | 6 | EBI-81279,EBI-81266 | |
| KRT18 | P05783 | 3 | EBI-81279,EBI-297888 | |
| KRT8 | P05787 | 2 | EBI-81279,EBI-297852 | |
| RIPK1 | Q13546 | 6 | EBI-81279,EBI-358507 | |
| SRC | P12931 | 3 | EBI-81279,EBI-621482 | |
| TNFAIP3 | P21580 | 2 | EBI-81279,EBI-527670 | |
| TNIP2 | Q8NFZ5 | 6 | EBI-81279,EBI-359372 |
Alternative products
| This entry describes 3 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q9Y6K9-1) 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. | ||||||
| Isoform 2 (identifier: Q9Y6K9-2) The sequence of this isoform differs from the canonical sequence as follows: 1-1: M → MALVIQVGKLRPREVRTPQTINPSLFPSLPVKLSSIIEVPSGGERCCSRRTLVYKARAFWKGAPLPCWM | ||||||
| Isoform 3 (identifier: Q9Y6K9-3) The sequence of this isoform differs from the canonical sequence as follows: 174-224: Missing. 257-304: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||
Molecule processing | ||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 419 | 419 | NF-kappa-B essential modulator | PRO_0000096782 | ||||||||||
Regions | ||||||||||||||
| Domain | 322 – 343 | 22 | Leucine-zipper Potential | |||||||||||
| Zinc finger | 396 – 417 | 22 | C2HC-type | |||||||||||
| Region | 44 – 111 | 68 | Interaction with CHUK/IKBKB | |||||||||||
| Region | 150 – 257 | 108 | Interaction with TANK | |||||||||||
| Region | 246 – 365 | 120 | Self-association | |||||||||||
| Region | 382 – 419 | 38 | Interaction with CYLD | |||||||||||
| Coiled coil | 49 – 356 | 308 | Potential | |||||||||||
Amino acid modifications | ||||||||||||||
| Modified residue | 31 | 1 | Phosphoserine; by IKKB Ref.19 | |||||||||||
| Modified residue | 43 | 1 | Phosphoserine; by IKKB Ref.19 | |||||||||||
| Modified residue | 68 | 1 | Phosphoserine Ref.32 | |||||||||||
| Modified residue | 85 | 1 | Phosphoserine; by ATM Ref.28 | |||||||||||
| Modified residue | 374 | 1 | Phosphotyrosine Ref.35 | |||||||||||
| Modified residue | 376 | 1 | Phosphoserine; by IKKB Ref.19 | |||||||||||
| Modified residue | 377 | 1 | Phosphoserine Ref.33 | |||||||||||
| Modified residue | 387 | 1 | Phosphoserine Ref.33 Ref.35 | |||||||||||
| Disulfide bond | 54 | Interchain Ref.30 | ||||||||||||
| Disulfide bond | 347 | Interchain Ref.30 | ||||||||||||
| Cross-link | 111 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.39 | ||||||||||||
| Cross-link | 139 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.39 | ||||||||||||
| Cross-link | 143 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.39 | ||||||||||||
| Cross-link | 226 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.39 | ||||||||||||
| Cross-link | 246 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.39 | ||||||||||||
| Cross-link | 264 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.39 | ||||||||||||
| Cross-link | 277 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate Ref.18 Ref.39 | ||||||||||||
| Cross-link | 277 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate | ||||||||||||
| Cross-link | 283 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.39 | ||||||||||||
| Cross-link | 285 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.22 Ref.36 Ref.39 | ||||||||||||
| Cross-link | 292 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.39 | ||||||||||||
| Cross-link | 302 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.39 | ||||||||||||
| Cross-link | 309 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate Ref.18 Ref.36 Ref.39 | ||||||||||||
| Cross-link | 309 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate | ||||||||||||
| Cross-link | 321 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity | ||||||||||||
| Cross-link | 325 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity | ||||||||||||
| Cross-link | 326 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity | ||||||||||||
| Cross-link | 399 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.26 | ||||||||||||
Natural variations | ||||||||||||||
| Alternative sequence | 1 | 1 | M → MALVIQVGKLRPREVRTPQT INPSLFPSLPVKLSSIIEVP SGGERCCSRRTLVYKARAFW KGAPLPCWM in isoform 2. | VSP_041000 | ||||||||||
| Alternative sequence | 174 – 224 | 51 | Missing in isoform 3. | VSP_041001 | ||||||||||
| Alternative sequence | 257 – 304 | 48 | Missing in isoform 3. | VSP_041002 | ||||||||||
| Natural variant | 57 | 1 | E → K in IP; shows the same luciferase activity as the control. Ref.43 Ref.47 Corresponds to variant rs148695964 [ dbSNP | Ensembl ]. | VAR_026491 | ||||||||||
| Natural variant | 90 | 1 | Missing in IP; only 46.3% of the activation obtained with the wild-type protein. | VAR_026492 | ||||||||||
| Natural variant | 113 | 1 | D → N. Ref.47 Corresponds to variant rs179363896 [ dbSNP | Ensembl ]. | VAR_026493 | ||||||||||
| Natural variant | 123 | 1 | R → W in IP; shows the same luciferase activity as the control. Ref.47 Corresponds to variant rs179363895 [ dbSNP | Ensembl ]. | VAR_026494 | ||||||||||
| Natural variant | 153 | 1 | L → R in EDAID. Ref.46 Ref.48 | VAR_026495 | ||||||||||
| Natural variant | 173 | 1 | R → G in IPD2. Ref.52 Corresponds to variant rs179363866 [ dbSNP | Ensembl ]. | VAR_031958 | ||||||||||
| Natural variant | 175 | 1 | R → P in EDAID. Ref.44 Corresponds to variant rs179363868 [ dbSNP | Ensembl ]. | VAR_011320 | ||||||||||
| Natural variant | 227 | 1 | L → P in EDAID. Ref.44 Corresponds to variant rs179363869 [ dbSNP | Ensembl ]. | VAR_011321 | ||||||||||
| Natural variant | 288 | 1 | A → G in EDAID. Ref.44 | VAR_011322 | ||||||||||
| Natural variant | 311 | 1 | D → N in EDAID. Ref.44 Corresponds to variant rs179363867 [ dbSNP | Ensembl ]. | VAR_011323 | ||||||||||
| Natural variant | 315 | 1 | E → A in AMCBX1. Ref.50 | VAR_031959 | ||||||||||
| Natural variant | 319 | 1 | R → Q in AMCBX1. Ref.50 | VAR_031960 | ||||||||||
| Natural variant | 323 | 1 | A → P in IP; diminishes interaction with TRAF6 and polyubiquitination. Ref.51 Corresponds to variant rs179363865 [ dbSNP | Ensembl ]. | VAR_042666 | ||||||||||
| Natural variant | 406 | 1 | D → V in EDAID. Ref.45 | VAR_011324 | ||||||||||
| Natural variant | 407 | 1 | M → V in IP. Ref.4 Ref.43 | VAR_009182 | ||||||||||
| Natural variant | 417 | 1 | C → F in EDAID. Ref.40 Ref.42 Ref.44 Corresponds to variant rs137853326 [ dbSNP | Ensembl ]. | VAR_011325 | ||||||||||
| Natural variant | 417 | 1 | C → R in EDAID; loss of sumoylation. Ref.18 Ref.42 Ref.44 Ref.45 Ref.46 Ref.48 | VAR_011326 | ||||||||||
| Natural variant | 417 | 1 | C → Y in NEMOID. Ref.48 Corresponds to variant rs137853326 [ dbSNP | Ensembl ]. | VAR_026496 | ||||||||||
Experimental info | ||||||||||||||
| Mutagenesis | 68 | 1 | S → A: Increases formation of homodimers. Ref.32 | |||||||||||
| Mutagenesis | 68 | 1 | S → E: Abolishes interaction with IKBKB; abolishes TNF-alpha induced NF-kappa-B activity. Ref.32 | |||||||||||
| Mutagenesis | 85 | 1 | S → A: Decreases ubiquitination and abolishes nuclear export. Ref.28 | |||||||||||
| Mutagenesis | 115 | 1 | K → R: No change in the ubiquitination level; when associated with R-399. Ref.22 | |||||||||||
| Mutagenesis | 224 | 1 | K → R: No change in the ubiquitination level; when associated with R-399. Ref.22 | |||||||||||
| Mutagenesis | 277 | 1 | K → A: Partial abolition of sumoylation. Abolishes sumoylation and IKK activation; when associated with A-309. Ref.18 | |||||||||||
| Mutagenesis | 285 | 1 | K → R: Important decrease in the ubiquitination level; when associated with R-399. Ref.22 | |||||||||||
| Mutagenesis | 309 | 1 | K → A: Partial abolition of sumoylation. Abolishes sumoylation and IKK activation; when associated with A-277. Ref.18 | |||||||||||
| Mutagenesis | 399 | 1 | 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. Ref.22 Ref.26 | |||||||||||
| Sequence conflict | 341 | 1 | S → R in AAD12183. Ref.1 | |||||||||||
| Sequence conflict | 387 | 1 | S → R in AAD12183. Ref.1 | |||||||||||
Secondary structure | ||||||||||||||
Helix Strand Turn | ||||||||||||||
| Helix | 50 – 108 | 59 | ||||||||||||
| Turn | 194 – 196 | 3 | ||||||||||||
| Helix | 197 – 249 | 53 | ||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [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: 9927690] [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: 10087442] [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: 9751060] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE. Tissue: Cervix carcinoma. |
| [4] | "Genomic rearrangement in NEMO impairs NF-kappaB activation and is a cause of incontinentia pigmenti." Smahi A., Courtois G., Vabres P., Yamaoka S., Heuertz S., Munnich A., Israel A., Heiss N.S., Klauck S.M., Kioschis P., Wiemann S., Poustka A., Esposito T., Bardaro T., Gianfrancesco F., Ciccodicola A., D'Urso M., Woffendin H. Nelson D.L.Nature 405:466-472(2000) [PubMed: 10839543] [Abstract] 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: 10944468] [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. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [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. Bentley D.R.Nature 434:325-337(2005) [PubMed: 15772651] [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: 15489334] [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: 9891086] [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: 10364167] [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: 11064457] [Abstract] Cited for: INTERACTION WITH HTLV-1 TAX-1. |
| [14] | "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: 11418127] [Abstract] Cited for: INTERACTION WITH COPS3. |
| [15] | "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: 11080499] [Abstract] Cited for: SUBUNIT OF THE IKK COMPLEX. |
| [16] | "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: 12133833] [Abstract] Cited for: INTERACTION WITH TANK AND IKBKB. |
| [17] | "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: 11971985] [Abstract] Cited for: SUBUNIT OF A COMPLEX CONTAINING CREBBP; NCOA2; NCOA3; IKKA AND IKKB. |
| [18] | "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: 14651848] [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. |
| [19] | "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: 12657630] [Abstract] Cited for: PHOSPHORYLATION AT SER-31; SER-43 AND SER-376. |
| [20] | "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: 12612076] [Abstract] Cited for: SELF-ASSOCIATION, COMPOSITION OF THE IKK COMPLEX. |
| [21] | "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: 12917691] [Abstract] Cited for: INTERACTION WITH CYLD. |
| [22] | "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: 15620648] [Abstract] Cited for: UBIQUITINATION AT LYS-285, MUTAGENESIS OF LYS-115; LYS-224; LYS-285 AND LYS-399. |
| [23] | "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: 14754897] [Abstract] Cited for: INTERACTION WITH ZFAND5. |
| [24] | "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: 15456791] [Abstract] Cited for: INTERACTION WITH NALP2. |
| [25] | "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: 15125833] [Abstract] Cited for: UBIQUITINATION. |
| [26] | "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: 14695475] [Abstract] Cited for: FUNCTION, UBIQUITINATION AT LYS-399, MUTAGENESIS OF LYS-399. |
| [27] | "PIDD mediates NF-kappaB activation in response to DNA damage." Janssens S., Tinel A., Lippens S., Tschopp J. Cell 123:1079-1092(2005) [PubMed: 16360037] [Abstract] Cited for: INTERACTION WITH LRDD. |
| [28] | "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: 16497931] [Abstract] Cited for: INTERACTION WITH ATM, PHOSPHORYLATION AT SER-85, MUTAGENESIS OF SER-85. |
| [29] | "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: 17135271] [Abstract] Cited for: UBIQUITINATION. |
| [30] | "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: 18164680] [Abstract] Cited for: SUBUNIT, DISULFIDE BONDS. |
| [31] | "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: 18079694] [Abstract] Cited for: INTERACTION WITH RIPK2. |
| [32] | "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: 17977820] [Abstract] Cited for: INTERACTION WITH IKBKB, PHOSPHORYLATION AT SER-68, MUTAGENESIS OF SER-68. |
| [33] | "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377 AND SER-387, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [34] | "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: 19854139] [Abstract] Cited for: FUNCTION, DOMAIN LEUCINE-ZIPPER AND C2HC-TYPE ZINC-FINGER. |
| [35] | "Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-374 AND SER-387, MASS SPECTROMETRY. |
| [36] | "Involvement of linear polyubiquitylation of NEMO in NF-kappaB activation." Tokunaga F., Sakata S., Saeki Y., Satomi Y., Kirisako T., Kamei K., Nakagawa T., Kato M., Murata S., Yamaoka S., Yamamoto M., Akira S., Takao T., Tanaka K., Iwai K. Nat. Cell Biol. 11:123-132(2009) [PubMed: 19136968] [Abstract] Cited for: UBIQUITINATION AT LYS-285 AND LYS-309. |
| [37] | "Linear ubiquitination prevents inflammation and regulates immune signalling." Gerlach B., Cordier S.M., Schmukle A.C., Emmerich C.H., Rieser E., Haas T.L., Webb A.I., Rickard J.A., Anderton H., Wong W.W., Nachbur U., Gangoda L., Warnken U., Purcell A.W., Silke J., Walczak H. Nature 471:591-596(2011) [PubMed: 21455173] [Abstract] Cited for: UBIQUITINATION BY THE LUBAC COMPLEX. |
| [38] | "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: 21455180] [Abstract] Cited for: UBIQUITINATION BY THE LUBAC COMPLEX. |
| [39] | "SHARPIN forms a linear ubiquitin ligase complex regulating NF-kappaB activity and apoptosis." Ikeda F., Deribe Y.L., Skanland S.S., Stieglitz B., Grabbe C., Franz-Wachtel M., van Wijk S.J., Goswami P., Nagy V., Terzic J., Tokunaga F., Androulidaki A., Nakagawa T., Pasparakis M., Iwai K., Sundberg J.P., Schaefer L., Rittinger K., Macek B., Dikic I. Nature 471:637-641(2011) [PubMed: 21455181] [Abstract] 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. |
| [40] | "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: 18313693] [Abstract] Cited for: STRUCTURE BY NMR OF 394-419 OF WILD-TYPE AND MUTANT PHE-417, DOMAIN ZINC FINGER. |
| [41] | "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: 18462684] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 44-111 IN COMPLEX WITH CHUK AND IKBKB, SUBUNIT. |
| [42] | "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: 11047757] [Abstract] Cited for: VARIANTS EDAID ARG-417 AND PHE-417. |
| [43] | "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: 11590134] [Abstract] Cited for: VARIANTS IP LYS-57 AND VAL-407. |
| [44] | "X-linked anhidrotic ectodermal dysplasia with immunodeficiency is caused by impaired NF-kappa B signaling." Doeffinger R., Smahi A., Bessia C., Geissmann F., Feinberg J., Durandy A., Bodemer C., Kenwrick S.J., Dupuis-Girod S., Blanche S., Wood P., Rabia S.H., Headon D.J., Overbeek P.A., Le Deist F., Holland S.M., Belani K., Kumararatne D.S. Casanova J.-L.Nat. Genet. 27:277-285(2001) [PubMed: 11242109] [Abstract] Cited for: VARIANTS EDAID PRO-175; PRO-227; GLY-288; ASN-311; ARG-417 AND PHE-417. |
| [45] | "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: 11224521] [Abstract] Cited for: VARIANTS EDAID VAL-406 AND ARG-417. |
| [46] | "Deficient natural killer cell cytotoxicity in patients with IKK-gamma/NEMO mutations." Orange J.S., Brodeur S.R., Jain A., Bonilla F.A., Schneider L.C., Kretschmer R., Nurko S., Rasmussen W.L., Koehler J.R., Gellis S.E., Ferguson B.M., Strominger J.L., Zonana J., Ramesh N., Ballas Z.K., Geha R.S. J. Clin. Invest. 109:1501-1509(2002) [PubMed: 12045264] [Abstract] Cited for: VARIANTS EDAID ARG-153 AND ARG-417. |
| [47] | "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: 15229184] [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. |
| [48] | "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: 15100680] [Abstract] Cited for: VARIANTS EDAID ARG-153 AND ARG-417, VARIANT NEMOID TYR-417. |
| [49] | "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: 15356572] [Abstract] Cited for: INVOLVEMENT IN NEMOID. |
| [50] | "X-linked susceptibility to mycobacteria is caused by mutations in NEMO impairing CD40-dependent IL-12 production." Filipe-Santos O., Bustamante J., Haverkamp M.H., Vinolo E., Ku C.-L., Puel A., Frucht D.M., Christel K., von Bernuth H., Jouanguy E., Feinberg J., Durandy A., Senechal B., Chapgier A., Vogt G., de Beaucoudrey L., Fieschi C., Picard C. Casanova J.-L.J. Exp. Med. 203:1745-1759(2006) [PubMed: 16818673] [Abstract] Cited for: VARIANTS AMCBX1 ALA-315 AND GLN-319. |
| [51] | "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: 17728323] [Abstract] Cited for: VARIANT IP PRO-323, CHARACTERIZATION OF VARIANT IP PRO-323, INTERACTION WITH TRAF6. |
| [52] | "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: 16950813] [Abstract] Cited for: VARIANT IPD2 GLY-173. |
| + | Additional computationally mapped references. |
Web resources
| IKBKGbase IKBKG mutation db |
| GeneReviews |
Cross-references
Sequence databases | |||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | 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. | ||||||||||||||||||||||||||||||||||||||||||
| IPI | IPI00002411. IPI00641117. IPI00641409. | ||||||||||||||||||||||||||||||||||||||||||
| RefSeq | NP_001093326.2. NM_001099856.2. NP_001093327.1. NM_001099857.1. NP_001138727.1. NM_001145255.1. NP_003630.1. NM_003639.3. | ||||||||||||||||||||||||||||||||||||||||||
| UniGene | Hs.43505. | ||||||||||||||||||||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||||||||||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||||||||||||||||||||||||||||||||
| ProteinModelPortal | Q9Y6K9. | ||||||||||||||||||||||||||||||||||||||||||
| SMR | Q9Y6K9. Positions 49-109, 193-251, 263-333, 394-419. | ||||||||||||||||||||||||||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||||||||||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||||||||||||||||||||||||||
| DIP | DIP-27528N. | ||||||||||||||||||||||||||||||||||||||||||
| IntAct | Q9Y6K9. 47 interactions. | ||||||||||||||||||||||||||||||||||||||||||
| MINT | MINT-1133340. | ||||||||||||||||||||||||||||||||||||||||||
| STRING | Q9Y6K9. | ||||||||||||||||||||||||||||||||||||||||||
PTM databases | |||||||||||||||||||||||||||||||||||||||||||
| PhosphoSite | Q9Y6K9. | ||||||||||||||||||||||||||||||||||||||||||
Polymorphism databases | |||||||||||||||||||||||||||||||||||||||||||
| DMDM | 6685695. | ||||||||||||||||||||||||||||||||||||||||||
Proteomic databases | |||||||||||||||||||||||||||||||||||||||||||
| PRIDE | Q9Y6K9. | ||||||||||||||||||||||||||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||||||||||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||||||||||||||||||||||||||
Genome annotation databases | |||||||||||||||||||||||||||||||||||||||||||
| Ensembl | ENST00000369601; ENSP00000358614; ENSG00000073009. ENST00000369606; ENSP00000358619; ENSG00000073009. ENST00000369607; ENSP00000358620; ENSG00000073009. ENST00000369609; ENSP00000358622; ENSG00000073009. | ||||||||||||||||||||||||||||||||||||||||||
| GeneID | 8517. | ||||||||||||||||||||||||||||||||||||||||||
| KEGG | hsa:8517. | ||||||||||||||||||||||||||||||||||||||||||
| UCSC | uc004flz.1. human. | ||||||||||||||||||||||||||||||||||||||||||
Organism-specific databases | |||||||||||||||||||||||||||||||||||||||||||
| CTD | 8517. | ||||||||||||||||||||||||||||||||||||||||||
| GeneCards | GC0XP153769. | ||||||||||||||||||||||||||||||||||||||||||
| H-InvDB | HIX0017162. | ||||||||||||||||||||||||||||||||||||||||||
| HGNC | HGNC:5961. IKBKG. | ||||||||||||||||||||||||||||||||||||||||||
| HPA | CAB010373. HPA000426. | ||||||||||||||||||||||||||||||||||||||||||
| MIM | 300248. gene. 300291. phenotype. 300301. phenotype. 300584. phenotype. 300636. phenotype. 300640. phenotype. 308300. phenotype. | ||||||||||||||||||||||||||||||||||||||||||
| neXtProt | NX_Q9Y6K9. | ||||||||||||||||||||||||||||||||||||||||||
| Orphanet | 69088. Anhidrotic ectodermal dysplasia - immunodeficiency - osteopetrosis - lymphedema. 98813. Hypohidrotic ectodermal dysplasia with immunodeficiency. 464. Incontinentia pigmenti. 748. Mendelian susceptibility to atypical mycobacteria. | ||||||||||||||||||||||||||||||||||||||||||
| GenAtlas | Search... | ||||||||||||||||||||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||||||||||||||||||||
| GeneTree | ENSGT00530000063808. | ||||||||||||||||||||||||||||||||||||||||||
| HOVERGEN | HBG000417. | ||||||||||||||||||||||||||||||||||||||||||
| InParanoid | Q9Y6K9. | ||||||||||||||||||||||||||||||||||||||||||
| OMA | FQEYDNH. | ||||||||||||||||||||||||||||||||||||||||||
| PhylomeDB | Q9Y6K9. | ||||||||||||||||||||||||||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||||||||||||||||||||||||||
| Pathway_Interaction_DB | bcr_5pathway. BCR signaling pathway. nfkappabcanonicalpathway. Canonical NF-kappaB pathway. fcer1pathway. Fc-epsilon receptor I signaling in mast cells. il1pathway. IL1-mediated signaling events. p75ntrpathway. p75(NTR)-mediated signaling. tcrpathway. TCR signaling in naive CD4+ T cells. cd8tcrpathway. TCR signaling in naive CD8+ T cells. tnfpathway. TNF receptor signaling pathway. trail_pathway. TRAIL signaling pathway. | ||||||||||||||||||||||||||||||||||||||||||
| Reactome | REACT_6900. Immune System. | ||||||||||||||||||||||||||||||||||||||||||
Gene expression databases | |||||||||||||||||||||||||||||||||||||||||||
| ArrayExpress | Q9Y6K9. | ||||||||||||||||||||||||||||||||||||||||||
| Bgee | Q9Y6K9. | ||||||||||||||||||||||||||||||||||||||||||
| CleanEx | HS_IKBKG. | ||||||||||||||||||||||||||||||||||||||||||
| Genevestigator | Q9Y6K9. | ||||||||||||||||||||||||||||||||||||||||||
| GermOnline | ENSG00000073009. Homo sapiens. | ||||||||||||||||||||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||||||||||||||||||||
| InterPro | IPR021063. NEMO_N. [Graphical view] | ||||||||||||||||||||||||||||||||||||||||||
| KO | K07210. | ||||||||||||||||||||||||||||||||||||||||||
| Pfam | PF11577. NEMO. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||||||||||||||||||||
Other | |||||||||||||||||||||||||||||||||||||||||||
| NextBio | 31882. | ||||||||||||||||||||||||||||||||||||||||||
| SOURCE | Search... | ||||||||||||||||||||||||||||||||||||||||||
Entry information
| Entry name | NEMO_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q9Y6K9 Secondary accession number(s): Q7LBY6, Q7Z7F1 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any 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. | ||||||||
Relevant documents
| Human chromosome X Human chromosome X: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with