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Entry version 114 (08 May 2019)
Sequence version 1 (05 Jul 2004)
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Protein

NF-kappa-B essential modulator

Gene

Ikbkg

Organism
Rattus norvegicus (Rat)
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 transcript 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. Essential for viral activation of IRF3. Involved in TLR3- and IFIH1-mediated antiviral innate response; this function requires 'Lys-27'-linked polyubiquitination (By similarity).By similarity

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-RNO-1169091 Activation of NF-kappaB in B cells
R-RNO-168638 NOD1/2 Signaling Pathway
R-RNO-1810476 RIP-mediated NFkB activation via ZBP1
R-RNO-202424 Downstream TCR signaling
R-RNO-2871837 FCERI mediated NF-kB activation
R-RNO-445989 TAK1 activates NFkB by phosphorylation and activation of IKKs complex
R-RNO-4755510 SUMOylation of immune response proteins
R-RNO-5357905 Regulation of TNFR1 signaling
R-RNO-5357956 TNFR1-induced NFkappaB signaling pathway
R-RNO-5607764 CLEC7A (Dectin-1) signaling
R-RNO-5684264 MAP3K8 (TPL2)-dependent MAPK1/3 activation
R-RNO-5689880 Ub-specific processing proteases
R-RNO-5689896 Ovarian tumor domain proteases
R-RNO-9020702 Interleukin-1 signaling
R-RNO-933542 TRAF6 mediated NF-kB activation
R-RNO-937039 IRAK1 recruits IKK complex
R-RNO-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
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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<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
  • UP000002494 <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

Rat genome database

More...
RGDi
735223 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 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_00002691971 – 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)By similarity
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)By similarity
Cross-linki319Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Disulfide bondi340InterchainBy similarity
Modified residuei369Phosphoserine; by IKKBBy similarity1
Modified residuei380PhosphoserineBy similarity1
Cross-linki392Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

<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

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

More...
PaxDbi
Q6TMG5

PRoteomics IDEntifications database

More...
PRIDEi
Q6TMG5

PTM databases

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

More...
PhosphoSitePlusi
Q6TMG5

<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
ENSRNOG00000060936 Expressed in 9 organ(s), highest expression level in liver

<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 IKBKE and TBK1.

Part of a ternary complex consisting of TANK, IKBKB and IKBKG.

Interacts with ZFAND5.

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 similarity

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
259339, 1 interactor

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
Q6TMG5

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000053114

<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

3D structure databases

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

More...
SMRi
Q6TMG5

Database of comparative protein structure models

More...
ModBasei
Search...

<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 TANKBy similarityAdd BLAST101
Regioni242 – 343Ubiquitin-binding (UBD)Add BLAST102
Regioni246 – 358Self-associationBy similarityAdd BLAST113
Regioni249 – 412Required for interaction with TNFAIP3By similarityAdd BLAST164
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 – 343Sequence analysisAdd BLAST295

<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

More...
eggNOGi
ENOG410IJBJ Eukaryota
ENOG410Y1FG LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00530000063808

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000293233

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q6TMG5

KEGG Orthology (KO)

More...
KOi
K07210

Identification of Orthologs from Complete Genome Data

More...
OMAi
SLINNMR

Database of Orthologous Groups

More...
OrthoDBi
745047at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q6TMG5

Family and domain databases

Integrated resource of protein families, domains and functional sites

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

Pfam protein domain database

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

PROSITE; a protein domain and family database

More...
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>Sequencei

<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.

Q6TMG5-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSRHLWKNQL SEMVQPSGGP AEDQDMLGEE SSLGKPAMLH LPSEQGTPET
60 70 80 90 100
LQRCLEENQE LRDAIRQSNQ MLRERCEELL HFQVSQREEK EFLMCKFQEA
110 120 130 140 150
RKLVERLSLE KLDLRRQREQ ALEDLEHLKK CQQQMAEDKA SVKAQVTSLL
160 170 180 190 200
GELQESQSRL EAATKERQTL 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 AREKLVERKE LLQEQLEQLQ REFNKLKVGC HESARIEDMR
360 370 380 390 400
KRHVETSQPP LLPAPAHHSF HLALSNQRRS PPEEPPDFCC PKCQYQAPDM
410
DTLQIHVMEC IE
Length:412
Mass (Da):48,066
Last modified:July 5, 2004 - v1
<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:i6D5D96B08A4CCEC2
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AY392762 mRNA Translation: AAQ94056.1

NCBI Reference Sequences

More...
RefSeqi
NP_954534.1, NM_199103.1
XP_006229646.1, XM_006229584.3
XP_006229647.1, XM_006229585.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000078438; ENSRNOP00000075158; ENSRNOG00000060936

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
309295

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:309295

<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
AY392762 mRNA Translation: AAQ94056.1
RefSeqiNP_954534.1, NM_199103.1
XP_006229646.1, XM_006229584.3
XP_006229647.1, XM_006229585.3

3D structure databases

SMRiQ6TMG5
ModBaseiSearch...

Protein-protein interaction databases

BioGridi259339, 1 interactor
CORUMiQ6TMG5
STRINGi10116.ENSRNOP00000053114

PTM databases

PhosphoSitePlusiQ6TMG5

Proteomic databases

PaxDbiQ6TMG5
PRIDEiQ6TMG5

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000078438; ENSRNOP00000075158; ENSRNOG00000060936
GeneIDi309295
KEGGirno:309295

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
8517
RGDi735223 Ikbkg

Phylogenomic databases

eggNOGiENOG410IJBJ Eukaryota
ENOG410Y1FG LUCA
GeneTreeiENSGT00530000063808
HOGENOMiHOG000293233
InParanoidiQ6TMG5
KOiK07210
OMAiSLINNMR
OrthoDBi745047at2759
PhylomeDBiQ6TMG5

Enzyme and pathway databases

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

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q6TMG5

Gene expression databases

BgeeiENSRNOG00000060936 Expressed in 9 organ(s), highest expression level in liver

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

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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_RAT
<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: Q6TMG5
<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: December 12, 2006
Last sequence update: July 5, 2004
Last modified: May 8, 2019
This is version 114 of the entry and version 1 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

Complete proteome, Reference proteome
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