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Entry version 169 (08 May 2019)
Sequence version 2 (27 Jul 2011)
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Protein

NF-kappa-B essential modulator

Gene

Ikbkg

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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. 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. Involved in TLR3- and IFIH1-mediated antiviral innate response; this function requires 'Lys-27'-linked polyubiquitination.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri382 – 412CCHC NOA-typePROSITE-ProRule annotationAdd BLAST31

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processDNA damage, Transcription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-1169091 Activation of NF-kappaB in B cells
R-MMU-168638 NOD1/2 Signaling Pathway
R-MMU-1810476 RIP-mediated NFkB activation via ZBP1
R-MMU-202424 Downstream TCR signaling
R-MMU-2871837 FCERI mediated NF-kB activation
R-MMU-445989 TAK1 activates NFkB by phosphorylation and activation of IKKs complex
R-MMU-4755510 SUMOylation of immune response proteins
R-MMU-5357905 Regulation of TNFR1 signaling
R-MMU-5357956 TNFR1-induced NFkappaB signaling pathway
R-MMU-5607764 CLEC7A (Dectin-1) signaling
R-MMU-5684264 MAP3K8 (TPL2)-dependent MAPK1/3 activation
R-MMU-5689880 Ub-specific processing proteases
R-MMU-5689896 Ovarian tumor domain proteases
R-MMU-9020702 Interleukin-1 signaling
R-MMU-933542 TRAF6 mediated NF-kB activation
R-MMU-937039 IRAK1 recruits IKK complex
R-MMU-937041 IKK complex recruitment mediated by RIP1
R-MMU-975144 IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
NF-kappa-B essential modulator
Short name:
NEMO
Alternative name(s):
IkB kinase-associated protein 1
Short name:
IKKAP1
Short name:
mFIP-3
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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Ikbkg
Synonyms:Nemo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome X

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1338074 Ikbkg

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi278K → R: Slight decrease in TRAF6-induced polyubiquitination. 1 Publication1
Mutagenesisi293V → A: Abolishes linear polyubiquitin-binding, impairs 'Lys-63'-linked polyubiquitin-binding and impairs NF-kappa-B activation; when associated with A-301 and A-302. 1 Publication1
Mutagenesisi301Y → A: Abolishes linear polyubiquitin-binding, impairs 'Lys-63'-linked polyubiquitin-binding and impairs NF-kappa-B activation; when associated with A-293 and A-302. 1 Publication1
Mutagenesisi302K → A: Abolishes linear polyubiquitin-binding, impairs 'Lys-63'-linked polyubiquitin-binding and impairs NF-kappa-B activation; when associated with A-293 and A-301. 1 Publication1
Mutagenesisi305F → A: Abolishes linear polyubiquitin-binding, impairs 'Lys-63'-linked polyubiquitin-binding and impairs of NF-kappa-B activation. 1 Publication1
Mutagenesisi309R → A: Abolishes linear polyubiquitin-binding, no effect on 'Lys-63'-linked polyubiquitin-binding and impairs NF-kappa-B activation; when associated with A-312 and A-313. 1 Publication1
Mutagenesisi312R → A: Abolishes linear polyubiquitin-binding, no effect on 'Lys-63'-linked polyubiquitin-binding and impairs NF-kappa-B activation; when associated with A-309 and A-313. 1 Publication1
Mutagenesisi313E → A: Impairs linear polyubiquitin-binding. Abolishes linear polyubiquitin-binding, no effect on 'Lys-63'-linked polyubiquitin-binding and impairs NF-kappa-B activation; when associated with A-309 and A-312. Abolishes linear polyubiquitin-binding; when associated with A-317 and A-320. 1 Publication1
Mutagenesisi314K → R: Slight decrease in TRAF6-induced polyubiquitination. Important decrease in TRAF6-induced polyubiquitination; when associated with R-318 and R-319. 1 Publication1
Mutagenesisi316V → P: Loss of interaction with TRAF6 and TRAF6-induced polyubiquitination. 1 Publication1
Mutagenesisi317E → A: Abolishes linear polyubiquitin-binding; when associated with A-313 and A-320. 1 Publication1
Mutagenesisi318K → R: Slight decrease in TRAF6-induced polyubiquitination. Decrease in TRAF6-induced polyubiquitination; when associated with R-319. Important decrease in TRAF6-induced polyubiquitination; when associated with R-314 and R-319. 1 Publication1
Mutagenesisi319K → R: Slight decrease in TRAF6-induced polyubiquitination. Decrease in TRAF6-induced polyubiquitination; when associated with R-318. Important decrease in TRAF6-induced polyubiquitination; when associated with R-314 and R-318. 1 Publication1
Mutagenesisi320E → A: Abolishes linear polyubiquitin-binding; when associated with A-313 and A-317. 1 Publication1
Mutagenesisi369S → A: Decreases phosphorylation and increases NF-kappa-B activity. 1 Publication1
Mutagenesisi375S → A: Decreases phosphorylation and increases NF-kappa-B activity. 1 Publication1
Mutagenesisi392K → R: 40% decrease in IL1-induced NF-kappa-B activation. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000967831 – 412NF-kappa-B essential modulatorAdd BLAST412

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei31Phosphoserine; by IKKBBy similarity1
Modified residuei43Phosphoserine; by IKKBBy similarity1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi54InterchainBy similarity
Modified residuei68PhosphoserineBy similarity1
Modified residuei85Phosphoserine; by ATMBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki111Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki139Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki143Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki226Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki246Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki270Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki270Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Cross-linki276Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki278Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki285Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki295Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki302Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki302Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Cross-linki314Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki318Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki319Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Disulfide bondi340InterchainBy similarity
Modified residuei369Phosphoserine; by IKKB1 Publication1
Modified residuei380PhosphoserineCombined sources1
Cross-linki392Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylation at Ser-68 attenuates aminoterminal homodimerization.By similarity
Polyubiquitinated on Lys-278 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-392 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-270 and Lys-302; 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-270, Lys-278, Lys-285, Lys-295, Lys-302 and Lys-319; the head-to-tail polyubiquitination is mediated by the LUBAC complex and plays a key role in NF-kappa-B activation. Deubiquitinated by USP10 in a TANK-dependent and -independent manner, leading to the negative regulation of NF-kappa-B signaling upon DNA damage (By similarity).By similarity
Sumoylated on Lys-270 and Lys-302 with SUMO1; the modification results in phosphorylation of Ser-85 by ATM leading to a replacement of the sumoylation by mono-ubiquitination on these residues.By similarity
Neddylated by TRIM40, resulting in stabilization of NFKBIA and down-regulation of NF-kappa-B activity.By similarity

Keywords - PTMi

Disulfide bond, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
O88522

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
O88522

MaxQB - The MaxQuant DataBase

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MaxQBi
O88522

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
O88522

PRoteomics IDEntifications database

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PRIDEi
O88522

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
O88522

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
O88522

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000004221 Expressed in 289 organ(s), highest expression level in blood

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
O88522 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
O88522 MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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 PIDD1.

Interacts with ATM; the complex is exported from the nucleus.

Interacts with TRAF6.

Interacts with IKBKE.

Interacts with TANK; the interaction is enhanced by TBK1 and IKBKE.

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.

Interacts with NLRP10.

Interacts with TANK; this interaction increases in response to DNA damage (By similarity).

Interacts with USP10; this interaction increases in response to DNA damage (By similarity).

Interacts with ZC3H12A; this interaction increases in response to DNA damage (By similarity).

Interacts with TRIM29; this interaction induces IKBKG/NEMO ubiquitination and proteolytic degradation (By similarity).

Interacts with TRIM13; this interaction leads to IKBKG/NEMO ubiquitination (By similarity).

By similarity4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
200602, 47 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-3270 IkappaB kinase complex

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
O88522

Database of interacting proteins

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DIPi
DIP-29811N

Protein interaction database and analysis system

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IntActi
O88522, 20 interactors

Molecular INTeraction database

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MINTi
O88522

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000109762

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1412
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
O88522

Database of comparative protein structure models

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ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
O88522

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni44 – 111Interaction with CHUK/IKBKBBy similarityAdd BLAST68
Regioni150 – 250Interaction with TANK1 PublicationAdd BLAST101
Regioni242 – 343Ubiquitin-binding (UBD)Add BLAST102
Regioni246 – 358Self-associationBy similarityAdd BLAST113
Regioni249 – 412Required for interaction with TNFAIP3By similarityAdd BLAST164
Regioni250 – 339Linear polyubiquitin-binding, does not bind to 'Lys-63'-linked polyubiquitinAdd BLAST90
Regioni315 – 336Leucine-zipperSequence analysisAdd BLAST22
Regioni375 – 412Interaction with CYLDBy similarityAdd BLAST38

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili49 – 345Sequence analysisAdd BLAST297

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The leucine-zipper domain and the CCHC NOA-type zinc-finger are essential for polyubiquitin binding and for the activation of IRF3.By similarity

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri382 – 412CCHC NOA-typePROSITE-ProRule annotationAdd BLAST31

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG410IJBJ Eukaryota
ENOG410Y1FG LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00530000063808

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000293233

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O88522

KEGG Orthology (KO)

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KOi
K07210

TreeFam database of animal gene trees

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TreeFami
TF326608

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR032419 CC2-LZ_dom
IPR021063 NEMO_N
IPR034735 NEMO_ZF

Pfam protein domain database

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Pfami
View protein in Pfam
PF16516 CC2-LZ, 1 hit
PF11577 NEMO, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS51801 ZF_CCHC_NOA, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry has 1 described isoform and 10 potential isoforms that are computationally mapped.Show allAlign All

O88522-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNKHPWKNQL SEMVQPSGGP AEDQDMLGEE SSLGKPAMLH LPSEQGTPET
60 70 80 90 100
LQRCLEENQE LRDAIRQSNQ MLRERCEELL HFQVSQREEK EFLMCKFQEA
110 120 130 140 150
RKLVERLSLE KLDLRSQREQ ALKELEQLKK CQQQMAEDKA SVKAQVTSLL
160 170 180 190 200
GELQESQSRL EAATKDRQAL EGRIRAVSEQ VRQLESEREV LQQQHSVQVD
210 220 230 240 250
QLRMQNQSVE AALRMERQAA SEEKRKLAQL QAAYHQLFQD YDSHIKSSKG
260 270 280 290 300
MQLEDLRQQL QQAEEALVAK QELIDKLKEE AEQHKIVMET VPVLKAQADI
310 320 330 340 350
YKADFQAERH AREKLVEKKE YLQEQLEQLQ REFNKLKVGC HESARIEDMR
360 370 380 390 400
KRHVETPQPP LLPAPAHHSF HLALSNQRRS PPEEPPDFCC PKCQYQAPDM
410
DTLQIHVMEC IE
Length:412
Mass (Da):47,972
Last modified:July 27, 2011 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i66C693C857A2D5E6
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 10 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q7TSS3Q7TSS3_MOUSE
Inhibitor of kappaB kinase gamma
Ikbkg
430Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
Q8VC91Q8VC91_MOUSE
Ikbkg protein
Ikbkg mCG_21233
411Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A3KG40A3KG40_MOUSE
NF-kappa-B essential modulator
Ikbkg
228Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A3KG39A3KG39_MOUSE
NF-kappa-B essential modulator
Ikbkg
126Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A3KG41A3KG41_MOUSE
NF-kappa-B essential modulator
Ikbkg
249Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9Q2Y3E9Q2Y3_MOUSE
NF-kappa-B essential modulator
Ikbkg
424Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A3KG37A3KG37_MOUSE
NF-kappa-B essential modulator
Ikbkg
141Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A3KG44A3KG44_MOUSE
NF-kappa-B essential modulator
Ikbkg
190Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A3KG38A3KG38_MOUSE
NF-kappa-B essential modulator
Ikbkg
265Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
D3YYY3D3YYY3_MOUSE
NF-kappa-B essential modulator
Ikbkg
16Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti13M → T in AAC40153 (PubMed:9657155).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AF069542 mRNA Translation: AAC40153.1
AF326207 Genomic DNA Translation: AAK69186.1
AF513109 mRNA Translation: AAP47160.1
AK154095 mRNA Translation: BAE32372.1
AL669976 Genomic DNA No translation available.
CH466650 Genomic DNA Translation: EDL29810.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS41023.1

NCBI Reference Sequences

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RefSeqi
NP_001154895.1, NM_001161423.1
NP_034677.2, NM_010547.2
XP_006527913.1, XM_006527850.2
XP_006527914.1, XM_006527851.2
XP_006527915.1, XM_006527852.2
XP_011245829.1, XM_011247527.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000114127; ENSMUSP00000109762; ENSMUSG00000004221
ENSMUST00000114128; ENSMUSP00000109763; ENSMUSG00000004221
ENSMUST00000114133; ENSMUSP00000109768; ENSMUSG00000004221
ENSMUST00000164101; ENSMUSP00000126770; ENSMUSG00000004221

Database of genes from NCBI RefSeq genomes

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GeneIDi
16151

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:16151

UCSC genome browser

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UCSCi
uc009toz.2 mouse

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF069542 mRNA Translation: AAC40153.1
AF326207 Genomic DNA Translation: AAK69186.1
AF513109 mRNA Translation: AAP47160.1
AK154095 mRNA Translation: BAE32372.1
AL669976 Genomic DNA No translation available.
CH466650 Genomic DNA Translation: EDL29810.1
CCDSiCCDS41023.1
RefSeqiNP_001154895.1, NM_001161423.1
NP_034677.2, NM_010547.2
XP_006527913.1, XM_006527850.2
XP_006527914.1, XM_006527851.2
XP_006527915.1, XM_006527852.2
XP_011245829.1, XM_011247527.2

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2V4HX-ray2.90A/B251-337[»]
2ZVNX-ray3.00B/D/F/H253-337[»]
2ZVOX-ray2.90B/D250-339[»]
3F89X-ray2.80A/B250-339[»]
3JSVX-ray2.70C/D250-343[»]
4OWFX-ray2.00A/B250-339[»]
SMRiO88522
ModBaseiSearch...

Protein-protein interaction databases

BioGridi200602, 47 interactors
ComplexPortaliCPX-3270 IkappaB kinase complex
CORUMiO88522
DIPiDIP-29811N
IntActiO88522, 20 interactors
MINTiO88522
STRINGi10090.ENSMUSP00000109762

PTM databases

iPTMnetiO88522
PhosphoSitePlusiO88522

Proteomic databases

EPDiO88522
jPOSTiO88522
MaxQBiO88522
PaxDbiO88522
PRIDEiO88522

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000114127; ENSMUSP00000109762; ENSMUSG00000004221
ENSMUST00000114128; ENSMUSP00000109763; ENSMUSG00000004221
ENSMUST00000114133; ENSMUSP00000109768; ENSMUSG00000004221
ENSMUST00000164101; ENSMUSP00000126770; ENSMUSG00000004221
GeneIDi16151
KEGGimmu:16151
UCSCiuc009toz.2 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
8517
MGIiMGI:1338074 Ikbkg

Phylogenomic databases

eggNOGiENOG410IJBJ Eukaryota
ENOG410Y1FG LUCA
GeneTreeiENSGT00530000063808
HOGENOMiHOG000293233
InParanoidiO88522
KOiK07210
TreeFamiTF326608

Enzyme and pathway databases

ReactomeiR-MMU-1169091 Activation of NF-kappaB in B cells
R-MMU-168638 NOD1/2 Signaling Pathway
R-MMU-1810476 RIP-mediated NFkB activation via ZBP1
R-MMU-202424 Downstream TCR signaling
R-MMU-2871837 FCERI mediated NF-kB activation
R-MMU-445989 TAK1 activates NFkB by phosphorylation and activation of IKKs complex
R-MMU-4755510 SUMOylation of immune response proteins
R-MMU-5357905 Regulation of TNFR1 signaling
R-MMU-5357956 TNFR1-induced NFkappaB signaling pathway
R-MMU-5607764 CLEC7A (Dectin-1) signaling
R-MMU-5684264 MAP3K8 (TPL2)-dependent MAPK1/3 activation
R-MMU-5689880 Ub-specific processing proteases
R-MMU-5689896 Ovarian tumor domain proteases
R-MMU-9020702 Interleukin-1 signaling
R-MMU-933542 TRAF6 mediated NF-kB activation
R-MMU-937039 IRAK1 recruits IKK complex
R-MMU-937041 IKK complex recruitment mediated by RIP1
R-MMU-975144 IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation

Miscellaneous databases

EvolutionaryTraceiO88522

Protein Ontology

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PROi
PR:O88522

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000004221 Expressed in 289 organ(s), highest expression level in blood
ExpressionAtlasiO88522 baseline and differential
GenevisibleiO88522 MM

Family and domain databases

InterProiView protein in InterPro
IPR032419 CC2-LZ_dom
IPR021063 NEMO_N
IPR034735 NEMO_ZF
PfamiView protein in Pfam
PF16516 CC2-LZ, 1 hit
PF11577 NEMO, 1 hit
PROSITEiView protein in PROSITE
PS51801 ZF_CCHC_NOA, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiNEMO_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O88522
Secondary accession number(s): Q924H4
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 27, 2011
Last modified: May 8, 2019
This is version 169 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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