IκBα

IκBα (nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor alpha; NFKBIA) is one member of a family of cellular proteins that function to inhibit the NF-κB transcription factor. IκBα inhibits NF-κB by masking the nuclear localization signals (NLS) of NF-κB proteins and keeping them sequestered in an inactive state in the cytoplasm.^[5] In addition, IκBα blocks the ability of NF-κB transcription factors to bind to DNA, which is required for NF-κB's proper functioning.^[6]

NFKBIA
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1IKN, 1NFI
Identifiers
Aliases	NFKBIA, IKBA, MAD-3, NFKBI, NFKB inhibitor alpha, EDAID2
External IDs	OMIM: 164008; MGI: 104741; HomoloGene: 7863; GeneCards: NFKBIA; OMA:NFKBIA - orthologs
Gene location (Human) Chr. Chromosome 14 (human)[1] Band 14q13.2 Start 35,401,513 bp[1] End 35,404,749 bp[1]
Gene location (Mouse) Chr. Chromosome 12 (mouse)[2] Band 12|12 C1 Start 55,536,195 bp[2] End 55,539,432 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in vena cava pericardium lower lobe of lung oocyte nipple saphenous vein mucosa of urinary bladder beta cell monocyte upper lobe of lung Top expressed in carotid body Paneth cell mesenteric lymph nodes ciliary body vestibular membrane of cochlear duct right lung lobe left lung lobe stroma of bone marrow tibiofemoral joint endothelial cell of lymphatic vessel More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transcription factor binding protein binding nuclear localization sequence binding identical protein binding enzyme binding ubiquitin protein ligase binding heat shock protein binding protein-containing complex binding NF-kappaB binding Cellular component cytoplasm I-kappaB/NF-kappaB complex plasma membrane nucleus cytosol intracellular anatomical structure protein-containing complex nucleoplasm Biological process response to muscle stretch positive regulation of protein metabolic process response to exogenous dsRNA cytoplasmic sequestering of transcription factor negative regulation of DNA binding cellular response to organic cyclic compound cytoplasmic sequestering of NF-kappaB response to muramyl dipeptide negative regulation of apoptotic process cellular response to cytokine stimulus positive regulation of transcription, DNA-templated response to lipopolysaccharide cellular response to cold regulation of cell population proliferation positive regulation of cholesterol efflux nucleotide-binding oligomerization domain containing 2 signaling pathway regulation of gene expression negative regulation of lipid storage viral process negative regulation of NF-kappaB transcription factor activity negative regulation of myeloid cell differentiation negative regulation of macrophage derived foam cell differentiation nucleotide-binding oligomerization domain containing 1 signaling pathway lipopolysaccharide-mediated signaling pathway negative regulation of Notch signaling pathway positive regulation of transcription by RNA polymerase II apoptotic process liver regeneration toll-like receptor 4 signaling pathway protein deubiquitination I-kappaB kinase/NF-kappaB signaling tumor necrosis factor-mediated signaling pathway positive regulation of inflammatory response cellular response to tumor necrosis factor interleukin-1-mediated signaling pathway regulation of NIK/NF-kappaB signaling protein import into nucleus Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 4792 18035 Ensembl ENSG00000100906 ENSMUSG00000021025 UniProt P25963 Q9Z1E3 RefSeq (mRNA) NM_020529 NM_010907 RefSeq (protein) NP_065390 NP_035037 Location (UCSC) Chr 14: 35.4 – 35.4 Mb Chr 12: 55.54 – 55.54 Mb PubMed search [3] [4]
Wikidata
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Disease linkage

The gene encoding the IκBα protein is mutated in some Hodgkin's lymphoma cells; such mutations inactivate the IκBα protein, thus causing NF-κB to be chronically active in the lymphoma tumor cells and this activity contributes to the malignant state of these tumor cells.^[7]

Interactions

IκBα has been shown to interact with:

• BTRC,^[8][9]
• C22orf25,^[10]
• CHUK,^{[11][12][13][14]}
• DYNLL1,^[15]
• G3BP2,^[16]
• Heterogeneous nuclear ribonucleoprotein A1,^[17]
• IKK2,^[11][12][18]
• NFKB1,^[17][19]
• P53,^[20]
• RELA,^{[9][11][17][19][21][22][23]}
• RPS6KA1,^[24]
• SUMO4,^[25] and
• Valosin-containing protein.^[26]