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Protein

Inhibitor of nuclear factor kappa-B kinase subunit beta

Gene

IKBKB

Organism
Homo sapiens (Human)
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

Serine kinase that plays an essential role in the NF-kappa-B signaling pathway which is activated by multiple stimuli such as inflammatory cytokines, bacterial or viral products, DNA damages or other cellular stresses. Acts as part of the canonical IKK complex in the conventional pathway of NF-kappa-B activation and phosphorylates inhibitors of NF-kappa-B on 2 critical serine residues. These modifications allow polyubiquitination of the inhibitors and subsequent degradation by the proteasome. In turn, free NF-kappa-B is translocated into the nucleus and activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis. In addition to the NF-kappa-B inhibitors, phosphorylates several other components of the signaling pathway including NEMO/IKBKG, NF-kappa-B subunits RELA and NFKB1, as well as IKK-related kinases TBK1 and IKBKE. IKK-related kinase phosphorylations may prevent the overproduction of inflammatory mediators since they exert a negative regulation on canonical IKKs. Phosphorylates FOXO3, mediating the TNF-dependent inactivation of this pro-apoptotic transcription factor. Also phosphorylates other substrates including NCOA3, BCL10 and IRS1. Within the nucleus, acts as an adapter protein for NFKBIA degradation in UV-induced NF-kappa-B activation.8 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei44ATPPROSITE-ProRule annotation1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei145Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi21 – 29ATPPROSITE-ProRule annotation9

<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

  • ATP binding Source: UniProtKB-KW
  • identical protein binding Source: IntAct
  • IkappaB kinase activity Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • protein kinase activity Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • protein serine/threonine kinase activity Source: UniProtKB
  • scaffold protein binding Source: MGI

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

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processHost-virus interaction
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

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BRENDAi
2.7.11.10 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-1169091 Activation of NF-kappaB in B cells
R-HSA-1236974 ER-Phagosome pathway
R-HSA-168638 NOD1/2 Signaling Pathway
R-HSA-168927 TICAM1, RIP1-mediated IKK complex recruitment
R-HSA-1810476 RIP-mediated NFkB activation via ZBP1
R-HSA-202424 Downstream TCR signaling
R-HSA-209543 p75NTR recruits signalling complexes
R-HSA-209560 NF-kB is activated and signals survival
R-HSA-2871837 FCERI mediated NF-kB activation
R-HSA-445989 TAK1 activates NFkB by phosphorylation and activation of IKKs complex
R-HSA-5357905 Regulation of TNFR1 signaling
R-HSA-5357956 TNFR1-induced NFkappaB signaling pathway
R-HSA-5602636 IKBKB deficiency causes SCID
R-HSA-5603027 IKBKG deficiency causes anhidrotic ectodermal dysplasia with immunodeficiency (EDA-ID) (via TLR)
R-HSA-5603029 IkBA variant leads to EDA-ID
R-HSA-5607764 CLEC7A (Dectin-1) signaling
R-HSA-5684264 MAP3K8 (TPL2)-dependent MAPK1/3 activation
R-HSA-9020702 Interleukin-1 signaling
R-HSA-933542 TRAF6 mediated NF-kB activation
R-HSA-933543 NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10
R-HSA-937039 IRAK1 recruits IKK complex
R-HSA-937041 IKK complex recruitment mediated by RIP1
R-HSA-975144 IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation

SABIO-RK: Biochemical Reaction Kinetics Database

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SABIO-RKi
O14920

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
O14920

SIGNOR Signaling Network Open Resource

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SIGNORi
O14920

<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:
Inhibitor of nuclear factor kappa-B kinase subunit beta (EC:2.7.11.10)
Short name:
I-kappa-B-kinase beta
Short name:
IKK-B
Short name:
IKK-beta
Short name:
IkBKB
Alternative name(s):
I-kappa-B kinase 2
Short name:
IKK2
Nuclear factor NF-kappa-B inhibitor kinase beta
Short name:
NFKBIKB
<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:IKBKB
Synonyms:IKKB
<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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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
  • UP000005640 <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 8

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000104365.13

Human Gene Nomenclature Database

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HGNCi
HGNC:5960 IKBKB

Online Mendelian Inheritance in Man (OMIM)

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MIMi
603258 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_O14920

<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; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Membrane, 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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Immunodeficiency 15 (IMD15)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive primary immunodeficiency disorder characterized by onset in infancy of life-threatening bacterial, fungal, and viral infections and failure to thrive. Laboratory studies show hypo- or agammaglobulinemia with relatively normal numbers of B and T-cells, and impaired differentiation and activation of immune cells.
See also OMIM:615592

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>Mutagenesisi44K → A: Loss of kinase activity and no effect on binding to NIK. 2 Publications1
Mutagenesisi163K → R: Monoubiquitinated; when associated with E-177 and E-181. 1 Publication1
Mutagenesisi177 – 181SLCTS → ALCTA: COmplete loss of TBK1-mediated phosphorylation. 1 Publication5
Mutagenesisi177S → A: Decrease of activity. 2 Publications1
Mutagenesisi177S → E: Full activation. Interaction with TRIM21 is enhanced; when associated with E-181. Monoubiquitinated; when associated with R-163 and E-181. Strongly promoted NF-kappa-B gene expression; when associated with E-181. 2 Publications1
Mutagenesisi181S → A: Decrease of activity. 2 Publications1
Mutagenesisi181S → E: Full activation. Interaction with TRIM21 is enhanced; when associated with E-177. Monoubiquitinated; when associated with R-163 and E-177. Strongly promoted NF-kappa-B gene expression; when associated with E-177. 2 Publications1
Mutagenesisi191P → A: Loss of hypoxic inducibility. 1 Publication1

Keywords - Diseasei

SCID

Organism-specific databases

DisGeNET

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DisGeNETi
3551

MalaCards human disease database

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MalaCardsi
IKBKB
MIMi615592 phenotype

Open Targets

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OpenTargetsi
ENSG00000104365

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
397787 Severe combined immunodeficiency due to IKK2 deficiency

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA29776

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL1991

Drug and drug target database

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DrugBanki
DB06151 Acetylcysteine
DB00945 Acetylsalicylic acid
DB01169 Arsenic trioxide
DB00995 Auranofin
DB00244 Mesalazine
DB05183 MLN0415
DB00795 Sulfasalazine

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
2039

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
IKBKB

<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_00000860131 – 756Inhibitor of nuclear factor kappa-B kinase subunit betaAdd BLAST756

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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-linki163Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
<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 residuei177Phosphoserine; by TBK1 and PKC/PRKCZ3 Publications1
Modified residuei179S-nitrosocysteine1 Publication1
Modified residuei180O-acetylthreonine; by Yersinia yopJ1 Publication1
Modified residuei181Phosphoserine; by TBK1, PKC/PRKCZ and PDPK14 Publications1
Modified residuei191Hydroxyproline1 Publication1
Modified residuei670Phosphoserine; by autocatalysis1 Publication1
Modified residuei672PhosphoserineCombined sources1 Publication1
Modified residuei675PhosphoserineCombined sources1
Modified residuei675Phosphoserine; by autocatalysisCombined sources1 Publication1
Modified residuei682Phosphoserine; by autocatalysis1 Publication1
Modified residuei689Phosphoserine; by autocatalysis1 Publication1
Modified residuei692Phosphoserine; by autocatalysis1 Publication1
Modified residuei695Phosphoserine; by autocatalysis1 Publication1
Modified residuei697Phosphoserine; by autocatalysis1 Publication1
Modified residuei705Phosphoserine; by autocatalysis1 Publication1
Modified residuei733Phosphoserine; by autocatalysis1 Publication1
Modified residuei740Phosphoserine; by autocatalysis1 Publication1
Modified residuei750Phosphoserine; by autocatalysis1 Publication1

<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

Upon cytokine stimulation, phosphorylated on Ser-177 and Ser-181 by MEKK1 and/or MAP3K14/NIK as well as TBK1 and PRKCZ; which enhances activity. Once activated, autophosphorylates on the C-terminal serine cluster; which decreases activity and prevents prolonged activation of the inflammatory response. Phosphorylated by the IKK-related kinases TBK1 and IKBKE, which is associated with reduced CHUK/IKKA and IKBKB activity and NF-kappa-B-dependent gene transcription. Dephosphorylated at Ser-177 and Ser-181 by PPM1A and PPM1B.4 Publications
(Microbial infection) Acetylation of Thr-180 by Yersinia yopJ prevents phosphorylation and activation, thus blocking the I-kappa-B pathway.2 Publications
Ubiquitinated. Monoubiquitination involves TRIM21 that leads to inhibition of Tax-induced NF-kappa-B signaling. According to PubMed:19675099, 'Ser-163' does not serve as a monoubiquitination site. According to PubMed:16267042, ubiquitination on 'Ser-163' modulates phosphorylation on C-terminal serine residues.2 Publications
(Microbial infection) Monoubiquitination by TRIM21 is disrupted by Yersinia yopJ.1 Publication
Hydroxylated by PHD1/EGLN2, loss of hydroxylation under hypoxic conditions results in activation of NF-kappa-B.1 Publication

Keywords - PTMi

Acetylation, Hydroxylation, Isopeptide bond, Phosphoprotein, S-nitrosylation, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
O14920

MaxQB - The MaxQuant DataBase

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MaxQBi
O14920

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

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PaxDbi
O14920

PeptideAtlas

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PeptideAtlasi
O14920

PRoteomics IDEntifications database

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PRIDEi
O14920

ProteomicsDB human proteome resource

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ProteomicsDBi
48297
48298 [O14920-2]
48299 [O14920-3]
48300 [O14920-4]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
O14920

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

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PhosphoSitePlusi
O14920

<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

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Highly expressed in heart, placenta, skeletal muscle, kidney, pancreas, spleen, thymus, prostate, testis and peripheral blood.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000104365 Expressed in 227 organ(s), highest expression level in spleen

CleanEx database of gene expression profiles

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CleanExi
HS_IKBKB

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
O14920 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
O14920 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB004447
HPA001249

<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

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 (PubMed:12612076). The IKK complex associates with TERF2IP/RAP1, leading to promote IKK-mediated phosphorylation of RELA/p65 (By similarity). Part of a complex composed of NCOA2, NCOA3, CHUK/IKKA, IKBKB, IKBKG and CREBBP (PubMed:11971985). Part of a 70-90 kDa complex at least consisting of CHUK/IKKA, IKBKB, NFKBIA, RELA, ELP1 and MAP3K14 (PubMed:9751059). Found in a membrane raft complex, at least composed of BCL10, CARD11, DPP4 and IKBKB (PubMed:17287217). Interacts with SQSTM1 through PRKCZ or PRKCI (PubMed:10356400). Forms an NGF-induced complex with IKBKB, PRKCI and TRAF6 (By similarity). May interact with MAVS/IPS1 (PubMed:16177806). Interacts with NALP2 (PubMed:15456791). Interacts with TICAM1 (PubMed:14739303). Interacts with FAF1; the interaction disrupts the IKK complex formation (PubMed:17684021). Interacts with ATM (PubMed:16497931). Part of a ternary complex consisting of TANK, IKBKB and IKBKG (PubMed:12133833). Interacts with NIBP; the interaction is direct (PubMed:15951441). Interacts with ARRB1 and ARRB2 (PubMed:15173580). Interacts with TRIM21 (PubMed:19675099). Interacts with NLRC5; prevents IKBKB phosphorylation and kinase activity (PubMed:20434986). Interacts with PDPK1 (PubMed:16207722). Interacts with EIF2AK2/PKR (PubMed:10848580). The phosphorylated form interacts with PPM1A and PPM1B (PubMed:18930133). Interacts with ZNF268 isoform 2; the interaction is further increased in a TNF-alpha-dependent manner (PubMed:23091055). Interacts with IKBKE (PubMed:23453969). Interacts with NAA10, leading to NAA10 degradation (PubMed:19716809). Interacts with FOXO3 (PubMed:15084260). Interacts with AKAP13 (PubMed:23090968). Interacts with IFIT5; the interaction synergizes the recruitment of IKK to MAP3K7 and enhances IKK phosphorylation (PubMed:26334375). Interacts with LRRC14; disrupts IKBKB-IKBKG interaction preventing I-kappa-B-kinase (IKK) core complex formation and leading to a decrease of IKBKB phosphorylation and NF-kappaB activation (PubMed:27426725).By similarity24 Publications
(Microbial infection) Interacts with Yersinia yopJ.1 Publication
(Microbial infection) Interacts with vaccinia virus protein B14.1 Publication

<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)

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BioGridi
109767, 146 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-3269 IkappaB kinase complex

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
O14920

Database of interacting proteins

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DIPi
DIP-27527N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
O14920

Protein interaction database and analysis system

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IntActi
O14920, 78 interactors

Molecular INTeraction database

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MINTi
O14920

STRING: functional protein association networks

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STRINGi
9606.ENSP00000430684

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
O14920

<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

1756
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
O14920

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

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SMRi
O14920

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
O14920

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini15 – 300Protein kinasePROSITE-ProRule annotationAdd BLAST286

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>Regioni458 – 479Leucine-zipperAdd BLAST22
Regioni737 – 742NEMO-binding6

<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 kinase domain is located in the N-terminal region. The leucine zipper is important to allow homo- and hetero-dimerization. At the C-terminal region is located the region responsible for the interaction with NEMO/IKBKG.1 Publication

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. I-kappa-B kinase subfamily.PROSITE-ProRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG4250 Eukaryota
ENOG410XRMU LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000153790

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000038048

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG018241

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
O14920

KEGG Orthology (KO)

More...
KOi
K07209

Identification of Orthologs from Complete Genome Data

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OMAi
WINEINI

Database of Orthologous Groups

More...
OrthoDBi
EOG091G02VC

Database for complete collections of gene phylogenies

More...
PhylomeDBi
O14920

TreeFam database of animal gene trees

More...
TreeFami
TF324269

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR022007 IKKbetaNEMObind
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR008271 Ser/Thr_kinase_AS
IPR029071 Ubiquitin-like_domsf
IPR000626 Ubiquitin_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF12179 IKKbetaNEMObind, 1 hit
PF00069 Pkinase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01239 IKKbetaNEMObind, 1 hit
SM00220 S_TKc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF54236 SSF54236, 1 hit
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (4+)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 describes 4 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 4 described isoforms and 8 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: O14920-1) [UniParc]FASTAAdd to basket

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

« Hide
        10         20         30         40         50
MSWSPSLTTQ TCGAWEMKER LGTGGFGNVI RWHNQETGEQ IAIKQCRQEL
60 70 80 90 100
SPRNRERWCL EIQIMRRLTH PNVVAARDVP EGMQNLAPND LPLLAMEYCQ
110 120 130 140 150
GGDLRKYLNQ FENCCGLREG AILTLLSDIA SALRYLHENR IIHRDLKPEN
160 170 180 190 200
IVLQQGEQRL IHKIIDLGYA KELDQGSLCT SFVGTLQYLA PELLEQQKYT
210 220 230 240 250
VTVDYWSFGT LAFECITGFR PFLPNWQPVQ WHSKVRQKSE VDIVVSEDLN
260 270 280 290 300
GTVKFSSSLP YPNNLNSVLA ERLEKWLQLM LMWHPRQRGT DPTYGPNGCF
310 320 330 340 350
KALDDILNLK LVHILNMVTG TIHTYPVTED ESLQSLKARI QQDTGIPEED
360 370 380 390 400
QELLQEAGLA LIPDKPATQC ISDGKLNEGH TLDMDLVFLF DNSKITYETQ
410 420 430 440 450
ISPRPQPESV SCILQEPKRN LAFFQLRKVW GQVWHSIQTL KEDCNRLQQG
460 470 480 490 500
QRAAMMNLLR NNSCLSKMKN SMASMSQQLK AKLDFFKTSI QIDLEKYSEQ
510 520 530 540 550
TEFGITSDKL LLAWREMEQA VELCGRENEV KLLVERMMAL QTDIVDLQRS
560 570 580 590 600
PMGRKQGGTL DDLEEQAREL YRRLREKPRD QRTEGDSQEM VRLLLQAIQS
610 620 630 640 650
FEKKVRVIYT QLSKTVVCKQ KALELLPKVE EVVSLMNEDE KTVVRLQEKR
660 670 680 690 700
QKELWNLLKI ACSKVRGPVS GSPDSMNASR LSQPGQLMSQ PSTASNSLPE
710 720 730 740 750
PAKKSEELVA EAHNLCTLLE NAIQDTVREQ DQSFTALDWS WLQTEEEEHS

CLEQAS
Length:756
Mass (Da):86,564
Last modified:January 1, 1998 - 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:iF9CADF671AE9E14E
GO
Isoform 2 (identifier: O14920-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: MSWSPSLTTQTCGAWEMKERLGTGGFGNVIRWHN → MFSGGCHSPGFGRPSPAFPAPGSPPPAPRPCR

Show »
Length:754
Mass (Da):85,945
Checksum:i9C31F5C1DC92661E
GO
Isoform 3 (identifier: O14920-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     231-256: WHSKVRQKSEVDIVVSEDLNGTVKFS → CVRMWPGTVAHSCNPSTLGGRGRWIS
     257-756: Missing.

Show »
Length:256
Mass (Da):29,236
Checksum:i8B4762DD49F4065A
GO
Isoform 4 (identifier: O14920-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-66: MSWSPSLTTQTCGAWEMKERLGTGGFGNVIRWHNQETGEQIAIKQCRQELSPRNRERWCLEIQIMR → MSSDGTI

Note: No experimental confirmation available.
Show »
Length:697
Mass (Da):79,509
Checksum:i21B61110941FE1D9
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 8 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G3V105G3V105_HUMAN
Inhibitor of kappa light polypeptid...
IKBKB hCG_17395
562Annotation 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>
E5RGW5E5RGW5_HUMAN
Inhibitor of nuclear factor kappa-B...
IKBKB
375Annotation 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>
J3KNS5J3KNS5_HUMAN
Inhibitor of nuclear factor kappa-B...
IKBKB
164Annotation 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>
E5RFT3E5RFT3_HUMAN
Inhibitor of nuclear factor kappa-B...
IKBKB
76Annotation 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>
E5RIW0E5RIW0_HUMAN
Inhibitor of nuclear factor kappa-B...
IKBKB
51Annotation 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>
E5RJH2E5RJH2_HUMAN
Inhibitor of nuclear factor kappa-B...
IKBKB
43Annotation 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>
E5RFG5E5RFG5_HUMAN
Inhibitor of nuclear factor kappa-B...
IKBKB
109Annotation 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>
E5RGA0E5RGA0_HUMAN
Inhibitor of nuclear factor kappa-B...
IKBKB
48Annotation 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 conflicti259L → S in BAG63942 (PubMed:14702039).Curated1
Sequence conflicti259L → S in BAH14789 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_035626360A → S in breast cancer samples; infiltrating ductal carcinoma; somatic mutation. 2 Publications1
Natural variantiVAR_040567369Q → R1 PublicationCorresponds to variant dbSNP:rs56411242Ensembl.1
Natural variantiVAR_040568526R → Q1 PublicationCorresponds to variant dbSNP:rs2272736EnsemblClinVar.1
Natural variantiVAR_021124554R → W1 PublicationCorresponds to variant dbSNP:rs17875749Ensembl.1
Natural variantiVAR_040569710A → T1 PublicationCorresponds to variant dbSNP:rs34309584Ensembl.1
Natural variantiVAR_040570734F → L1 PublicationCorresponds to variant dbSNP:rs56301637Ensembl.1
Natural variantiVAR_051628736A → T. Corresponds to variant dbSNP:rs17611716Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0434081 – 66MSWSP…IQIMR → MSSDGTI in isoform 4. 1 PublicationAdd BLAST66
Alternative sequenceiVSP_0418251 – 34MSWSP…IRWHN → MFSGGCHSPGFGRPSPAFPA PGSPPPAPRPCR in isoform 2. 1 PublicationAdd BLAST34
Alternative sequenceiVSP_041826231 – 256WHSKV…TVKFS → CVRMWPGTVAHSCNPSTLGG RGRWIS in isoform 3. 1 PublicationAdd BLAST26
Alternative sequenceiVSP_041827257 – 756Missing in isoform 3. 1 PublicationAdd BLAST500

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
AF029684 mRNA Translation: AAC51860.1
AF080158 mRNA Translation: AAD08997.1
AF031416 mRNA Translation: AAC64675.1
AK302723 mRNA Translation: BAG63942.1
AK303528 mRNA Translation: BAG64556.1
AK316418 mRNA Translation: BAH14789.1
AY663108 Genomic DNA Translation: AAT65965.1
AC083973 Genomic DNA No translation available.
BC006231 mRNA Translation: AAH06231.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS55228.1 [O14920-2]
CCDS56535.1 [O14920-4]
CCDS6128.1 [O14920-1]

NCBI Reference Sequences

More...
RefSeqi
NP_001177649.1, NM_001190720.2 [O14920-2]
NP_001229707.1, NM_001242778.1 [O14920-4]
NP_001547.1, NM_001556.2 [O14920-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.597664

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000416505; ENSP00000404920; ENSG00000104365 [O14920-4]
ENST00000520810; ENSP00000430684; ENSG00000104365 [O14920-1]
ENST00000520835; ENSP00000430868; ENSG00000104365 [O14920-2]
ENST00000649612; ENSP00000497383; ENSG00000104365 [O14920-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
3551

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:3551

UCSC genome browser

More...
UCSCi
uc003xow.3 human [O14920-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF029684 mRNA Translation: AAC51860.1
AF080158 mRNA Translation: AAD08997.1
AF031416 mRNA Translation: AAC64675.1
AK302723 mRNA Translation: BAG63942.1
AK303528 mRNA Translation: BAG64556.1
AK316418 mRNA Translation: BAH14789.1
AY663108 Genomic DNA Translation: AAT65965.1
AC083973 Genomic DNA No translation available.
BC006231 mRNA Translation: AAH06231.1
CCDSiCCDS55228.1 [O14920-2]
CCDS56535.1 [O14920-4]
CCDS6128.1 [O14920-1]
RefSeqiNP_001177649.1, NM_001190720.2 [O14920-2]
NP_001229707.1, NM_001242778.1 [O14920-4]
NP_001547.1, NM_001556.2 [O14920-1]
UniGeneiHs.597664

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3BRTX-ray2.25A/C701-730[»]
3BRVX-ray2.20A/C701-745[»]
4E3CX-ray3.98A/B/C/D/E/F11-669[»]
4KIKX-ray2.83A/B2-664[»]
ProteinModelPortaliO14920
SMRiO14920
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109767, 146 interactors
ComplexPortaliCPX-3269 IkappaB kinase complex
CORUMiO14920
DIPiDIP-27527N
ELMiO14920
IntActiO14920, 78 interactors
MINTiO14920
STRINGi9606.ENSP00000430684

Chemistry databases

BindingDBiO14920
ChEMBLiCHEMBL1991
DrugBankiDB06151 Acetylcysteine
DB00945 Acetylsalicylic acid
DB01169 Arsenic trioxide
DB00995 Auranofin
DB00244 Mesalazine
DB05183 MLN0415
DB00795 Sulfasalazine
GuidetoPHARMACOLOGYi2039

PTM databases

iPTMnetiO14920
PhosphoSitePlusiO14920

Polymorphism and mutation databases

BioMutaiIKBKB

Proteomic databases

EPDiO14920
MaxQBiO14920
PaxDbiO14920
PeptideAtlasiO14920
PRIDEiO14920
ProteomicsDBi48297
48298 [O14920-2]
48299 [O14920-3]
48300 [O14920-4]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
3551
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000416505; ENSP00000404920; ENSG00000104365 [O14920-4]
ENST00000520810; ENSP00000430684; ENSG00000104365 [O14920-1]
ENST00000520835; ENSP00000430868; ENSG00000104365 [O14920-2]
ENST00000649612; ENSP00000497383; ENSG00000104365 [O14920-1]
GeneIDi3551
KEGGihsa:3551
UCSCiuc003xow.3 human [O14920-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
3551
DisGeNETi3551
EuPathDBiHostDB:ENSG00000104365.13

GeneCards: human genes, protein and diseases

More...
GeneCardsi
IKBKB
HGNCiHGNC:5960 IKBKB
HPAiCAB004447
HPA001249
MalaCardsiIKBKB
MIMi603258 gene
615592 phenotype
neXtProtiNX_O14920
OpenTargetsiENSG00000104365
Orphaneti397787 Severe combined immunodeficiency due to IKK2 deficiency
PharmGKBiPA29776

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG4250 Eukaryota
ENOG410XRMU LUCA
GeneTreeiENSGT00940000153790
HOGENOMiHOG000038048
HOVERGENiHBG018241
InParanoidiO14920
KOiK07209
OMAiWINEINI
OrthoDBiEOG091G02VC
PhylomeDBiO14920
TreeFamiTF324269

Enzyme and pathway databases

BRENDAi2.7.11.10 2681
ReactomeiR-HSA-1169091 Activation of NF-kappaB in B cells
R-HSA-1236974 ER-Phagosome pathway
R-HSA-168638 NOD1/2 Signaling Pathway
R-HSA-168927 TICAM1, RIP1-mediated IKK complex recruitment
R-HSA-1810476 RIP-mediated NFkB activation via ZBP1
R-HSA-202424 Downstream TCR signaling
R-HSA-209543 p75NTR recruits signalling complexes
R-HSA-209560 NF-kB is activated and signals survival
R-HSA-2871837 FCERI mediated NF-kB activation
R-HSA-445989 TAK1 activates NFkB by phosphorylation and activation of IKKs complex
R-HSA-5357905 Regulation of TNFR1 signaling
R-HSA-5357956 TNFR1-induced NFkappaB signaling pathway
R-HSA-5602636 IKBKB deficiency causes SCID
R-HSA-5603027 IKBKG deficiency causes anhidrotic ectodermal dysplasia with immunodeficiency (EDA-ID) (via TLR)
R-HSA-5603029 IkBA variant leads to EDA-ID
R-HSA-5607764 CLEC7A (Dectin-1) signaling
R-HSA-5684264 MAP3K8 (TPL2)-dependent MAPK1/3 activation
R-HSA-9020702 Interleukin-1 signaling
R-HSA-933542 TRAF6 mediated NF-kB activation
R-HSA-933543 NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10
R-HSA-937039 IRAK1 recruits IKK complex
R-HSA-937041 IKK complex recruitment mediated by RIP1
R-HSA-975144 IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation
SABIO-RKiO14920
SignaLinkiO14920
SIGNORiO14920

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
IKBKB human
EvolutionaryTraceiO14920

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
IKK2

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
3551

Protein Ontology

More...
PROi
PR:O14920

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000104365 Expressed in 227 organ(s), highest expression level in spleen
CleanExiHS_IKBKB
ExpressionAtlasiO14920 baseline and differential
GenevisibleiO14920 HS

Family and domain databases

InterProiView protein in InterPro
IPR022007 IKKbetaNEMObind
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR008271 Ser/Thr_kinase_AS
IPR029071 Ubiquitin-like_domsf
IPR000626 Ubiquitin_dom
PfamiView protein in Pfam
PF12179 IKKbetaNEMObind, 1 hit
PF00069 Pkinase, 1 hit
SMARTiView protein in SMART
SM01239 IKKbetaNEMObind, 1 hit
SM00220 S_TKc, 1 hit
SUPFAMiSSF54236 SSF54236, 1 hit
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiIKKB_HUMAN
<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: O14920
Secondary accession number(s): B4DZ30, B4E0U4, O75327
<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: June 1, 2001
Last sequence update: January 1, 1998
Last modified: December 5, 2018
This is version 210 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
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<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. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  7. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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