NFKBIA | ENSG00000100906 | NCBI 4792

Details for: NFKBIA

Gene ID: 4792

Symbol: NFKBIA

Ensembl ID: ENSG00000100906

Description: NFKB inhibitor alpha

Associated with

Activation of nf-kappab in b cells
(R-HSA-1169091)
Adaptive immune system
(R-HSA-1280218)
C-type lectin receptors (clrs)
(R-HSA-5621481)
Cellular responses to mechanical stimuli
(R-HSA-9855142)
Cellular responses to stimuli
(R-HSA-8953897)
Clec7a (dectin-1) signaling
(R-HSA-5607764)
Cytokine signaling in immune system
(R-HSA-1280215)
Cytosolic sensors of pathogen-associated dna
(R-HSA-1834949)
Ddx58/ifih1-mediated induction of interferon-alpha/beta
(R-HSA-168928)
Death receptor signaling
(R-HSA-73887)
Deubiquitination
(R-HSA-5688426)
Disease
(R-HSA-1643685)
Diseases associated with the tlr signaling cascade
(R-HSA-5602358)
Diseases of immune system
(R-HSA-5260271)
Downstream signaling events of b cell receptor (bcr)
(R-HSA-1168372)
Downstream tcr signaling
(R-HSA-202424)
Fc epsilon receptor (fceri) signaling
(R-HSA-2454202)
Fceri mediated nf-kb activation
(R-HSA-2871837)
Ikba variant leads to eda-id
(R-HSA-5603029)
Immune system
(R-HSA-168256)
Infectious disease
(R-HSA-5663205)
Innate immune system
(R-HSA-168249)
Interleukin-1 family signaling
(R-HSA-446652)
Interleukin-1 signaling
(R-HSA-9020702)
Metabolism of proteins
(R-HSA-392499)
Myd88 cascade initiated on plasma membrane
(R-HSA-975871)
Myd88 dependent cascade initiated on endosome
(R-HSA-975155)
Myd88-independent tlr4 cascade
(R-HSA-166166)
Myd88:mal(tirap) cascade initiated on plasma membrane
(R-HSA-166058)
Nf-kb is activated and signals survival
(R-HSA-209560)
P75 ntr receptor-mediated signalling
(R-HSA-193704)
P75ntr signals via nf-kb
(R-HSA-193639)
Post-translational protein modification
(R-HSA-597592)
Response of endothelial cells to shear stress
(R-HSA-9860931)
Rip-mediated nfkb activation via zbp1
(R-HSA-1810476)
Sars-cov-1 activates/modulates innate immune responses
(R-HSA-9692916)
Sars-cov-1 infection
(R-HSA-9678108)
Sars-cov-1-host interactions
(R-HSA-9692914)
Sars-cov infections
(R-HSA-9679506)
Signaling by interleukins
(R-HSA-449147)
Signaling by the b cell receptor (bcr)
(R-HSA-983705)
Signal transduction
(R-HSA-162582)
Sumo e3 ligases sumoylate target proteins
(R-HSA-3108232)
Sumoylation
(R-HSA-2990846)
Sumoylation of immune response proteins
(R-HSA-4755510)
Tak1-dependent ikk and nf-kappa-b activation
(R-HSA-445989)
Tcr signaling
(R-HSA-202403)
Toll-like receptor cascades
(R-HSA-168898)
Toll like receptor 2 (tlr2) cascade
(R-HSA-181438)
Toll like receptor 3 (tlr3) cascade
(R-HSA-168164)
Toll like receptor 4 (tlr4) cascade
(R-HSA-166016)
Toll like receptor 5 (tlr5) cascade
(R-HSA-168176)
Toll like receptor 7/8 (tlr7/8) cascade
(R-HSA-168181)
Toll like receptor 9 (tlr9) cascade
(R-HSA-168138)
Toll like receptor 10 (tlr10) cascade
(R-HSA-168142)
Toll like receptor tlr1:tlr2 cascade
(R-HSA-168179)
Toll like receptor tlr6:tlr2 cascade
(R-HSA-168188)
Traf6 mediated induction of nfkb and map kinases upon tlr7/8 or 9 activation
(R-HSA-975138)
Traf6 mediated nf-kb activation
(R-HSA-933542)
Trif (ticam1)-mediated tlr4 signaling
(R-HSA-937061)
Turbulent (oscillatory, disturbed) flow shear stress activates signaling by piezo1 and integrins in endothelial cells
(R-HSA-9860927)
Ub-specific processing proteases
(R-HSA-5689880)
Viral infection pathways
(R-HSA-9824446)
Zbp1(dai) mediated induction of type i ifns
(R-HSA-1606322)
B cell receptor signaling pathway
(GO:0050853)
Canonical nf-kappab signal transduction
(GO:0007249)
Cytoplasmic sequestering of nf-kappab
(GO:0007253)
Enzyme binding
(GO:0019899)
Identical protein binding
(GO:0042802)
Lipopolysaccharide-mediated signaling pathway
(GO:0031663)
Molecular sequestering activity
(GO:0140313)
Negative regulation of canonical nf-kappab signal transduction
(GO:0043124)
Negative regulation of lipid storage
(GO:0010888)
Negative regulation of macrophage derived foam cell differentiation
(GO:0010745)
Negative regulation of myeloid cell differentiation
(GO:0045638)
Negative regulation of nf-kappab transcription factor activity
(GO:0032088)
Negative regulation of notch signaling pathway
(GO:0045746)
Nf-kappab binding
(GO:0051059)
Non-canonical nf-kappab signal transduction
(GO:0038061)
Notch signaling pathway
(GO:0007219)
Nuclear localization sequence binding
(GO:0008139)
Positive regulation of cholesterol efflux
(GO:0010875)
Positive regulation of inflammatory response
(GO:0050729)
Positive regulation of transcription by rna polymerase ii
(GO:0045944)
Protein binding
(GO:0005515)
Protein import into nucleus
(GO:0006606)
Protein sequestering activity
(GO:0140311)
Regulation of cell population proliferation
(GO:0042127)
Response to exogenous dsrna
(GO:0043330)
Response to muramyl dipeptide
(GO:0032495)
Response to muscle stretch
(GO:0035994)
Toll-like receptor 4 signaling pathway
(GO:0034142)
Transcription regulator inhibitor activity
(GO:0140416)
Tumor necrosis factor-mediated signaling pathway
(GO:0033209)
Ubiquitin protein ligase binding
(GO:0031625)

Cells (max top 100)

(Cell Significance Index and respective Thresholds are uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

Cell Name: polychromatophilic erythroblast (CL0000550)
Fold Change: 589.8285
Cell Significance Index: -91.7500
Cell Name: hematopoietic oligopotent progenitor cell (CL0002032)
Fold Change: 323.9194
Cell Significance Index: -82.1600
Cell Name: mucosal type mast cell (CL0000485)
Fold Change: 249.3987
Cell Significance Index: -101.3200
Cell Name: smooth muscle fiber of ileum (CL1000278)
Fold Change: 224.3485
Cell Significance Index: -105.9200
Cell Name: peripheral blood mononuclear cell (CL2000001)
Fold Change: 218.8632
Cell Significance Index: -112.5800
Cell Name: ileal goblet cell (CL1000326)
Fold Change: 158.2660
Cell Significance Index: -106.2000
Cell Name: ciliated cell of the bronchus (CL0002332)
Fold Change: 110.3753
Cell Significance Index: -105.3800
Cell Name: orthochromatic erythroblast (CL0000552)
Fold Change: 76.6086
Cell Significance Index: -94.4600
Cell Name: CD8-alpha-beta-positive, alpha-beta intraepithelial T cell (CL0000796)
Fold Change: 31.1812
Cell Significance Index: -83.5300
Cell Name: CD8-positive, alpha-beta regulatory T cell (CL0000795)
Fold Change: 27.6840
Cell Significance Index: -85.0300
Cell Name: stromal cell of bone marrow (CL0010001)
Fold Change: 25.1872
Cell Significance Index: -99.3900
Cell Name: epidermal Langerhans cell (CL0002457)
Fold Change: 19.7022
Cell Significance Index: -43.1200
Cell Name: stem cell of epidermis (CL1000428)
Fold Change: 17.9303
Cell Significance Index: 53.3300
Cell Name: fibroblast of mammary gland (CL0002555)
Fold Change: 14.9939
Cell Significance Index: 429.8100
Cell Name: vascular lymphangioblast (CL0005022)
Fold Change: 12.6250
Cell Significance Index: 223.1000
Cell Name: prostate gland microvascular endothelial cell (CL2000059)
Fold Change: 12.4876
Cell Significance Index: 89.6900
Cell Name: hepatic pit cell (CL2000054)
Fold Change: 12.3820
Cell Significance Index: 33.1700
Cell Name: CD14-positive, CD16-negative classical monocyte (CL0002057)
Fold Change: 11.5757
Cell Significance Index: 213.9500
Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
Fold Change: 7.7692
Cell Significance Index: 365.1500
Cell Name: basal cell of prostate epithelium (CL0002341)
Fold Change: 5.7915
Cell Significance Index: 157.6400
Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
Fold Change: 5.3932
Cell Significance Index: 401.9500
Cell Name: pancreatic endocrine cell (CL0008024)
Fold Change: 5.1846
Cell Significance Index: 591.8200
Cell Name: lactocyte (CL0002325)
Fold Change: 4.8006
Cell Significance Index: 620.2100
Cell Name: lung endothelial cell (CL1001567)
Fold Change: 4.7517
Cell Significance Index: 247.5100
Cell Name: peg cell (CL4033014)
Fold Change: 3.8936
Cell Significance Index: 89.9600
Cell Name: skeletal muscle fibroblast (CL0011027)
Fold Change: 3.5791
Cell Significance Index: 24.2500
Cell Name: luminal hormone-sensing cell of mammary gland (CL4033058)
Fold Change: 3.5472
Cell Significance Index: 21.8300
Cell Name: hair follicular keratinocyte (CL2000092)
Fold Change: 3.2533
Cell Significance Index: 1438.3700
Cell Name: endothelial cell of venule (CL1000414)
Fold Change: 3.0765
Cell Significance Index: 34.9500
Cell Name: stromal cell of ovary (CL0002132)
Fold Change: 3.0692
Cell Significance Index: 421.4800
Cell Name: cell in vitro (CL0001034)
Fold Change: 2.8291
Cell Significance Index: 1545.0600
Cell Name: basal cell of urothelium (CL1000486)
Fold Change: 2.5310
Cell Significance Index: 311.2100
Cell Name: odontoblast (CL0000060)
Fold Change: 2.4773
Cell Significance Index: 317.5800
Cell Name: early pro-B cell (CL0002046)
Fold Change: 2.4362
Cell Significance Index: 157.1700
Cell Name: sebum secreting cell (CL0000317)
Fold Change: 2.3008
Cell Significance Index: 162.7200
Cell Name: intermediate cell of urothelium (CL4030055)
Fold Change: 2.1626
Cell Significance Index: 389.8400
Cell Name: bladder urothelial cell (CL1001428)
Fold Change: 1.3158
Cell Significance Index: 68.3500
Cell Name: monocyte-derived dendritic cell (CL0011031)
Fold Change: 1.2218
Cell Significance Index: 20.9900
Cell Name: epithelial cell of small intestine (CL0002254)
Fold Change: 1.1851
Cell Significance Index: 192.7400
Cell Name: colon goblet cell (CL0009039)
Fold Change: 1.0369
Cell Significance Index: 102.5700
Cell Name: acinar cell of salivary gland (CL0002623)
Fold Change: 0.9709
Cell Significance Index: 45.2700
Cell Name: fibroblast of dermis (CL0002551)
Fold Change: 0.8079
Cell Significance Index: 16.9100
Cell Name: placental villous trophoblast (CL2000060)
Fold Change: 0.6794
Cell Significance Index: 18.1400
Cell Name: tonsil germinal center B cell (CL2000006)
Fold Change: 0.5140
Cell Significance Index: 60.6200
Cell Name: granulosa cell (CL0000501)
Fold Change: 0.4081
Cell Significance Index: 10.7300
Cell Name: enteroendocrine cell of colon (CL0009042)
Fold Change: 0.3706
Cell Significance Index: 70.5200
Cell Name: enteroendocrine cell of small intestine (CL0009006)
Fold Change: 0.2904
Cell Significance Index: 7.2600
Cell Name: pulmonary alveolar epithelial cell (CL0000322)
Fold Change: 0.2759
Cell Significance Index: 208.8400
Cell Name: small intestine goblet cell (CL1000495)
Fold Change: 0.2009
Cell Significance Index: 7.0600
Cell Name: neutrophil progenitor cell (CL0000834)
Fold Change: 0.1875
Cell Significance Index: 5.0100
Cell Name: enterocyte of epithelium of large intestine (CL0002071)
Fold Change: 0.1721
Cell Significance Index: 7.8000
Cell Name: pancreatic acinar cell (CL0002064)
Fold Change: 0.0957
Cell Significance Index: 16.3400
Cell Name: kidney loop of Henle cortical thick ascending limb epithelial cell (CL1001109)
Fold Change: 0.0637
Cell Significance Index: 46.6800
Cell Name: pigmented epithelial cell (CL0000529)
Fold Change: 0.0546
Cell Significance Index: 102.7500
Cell Name: abnormal cell (CL0001061)
Fold Change: 0.0424
Cell Significance Index: 4.3300
Cell Name: neoplastic cell (CL0001063)
Fold Change: -0.0144
Cell Significance Index: -2.8500
Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
Fold Change: -0.0540
Cell Significance Index: -34.3100
Cell Name: anterior lens cell (CL0002223)
Fold Change: -0.0595
Cell Significance Index: -109.6700
Cell Name: secondary lens fiber (CL0002225)
Fold Change: -0.0654
Cell Significance Index: -88.9500
Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
Fold Change: -0.0665
Cell Significance Index: -13.3300
Cell Name: lens epithelial cell (CL0002224)
Fold Change: -0.0666
Cell Significance Index: -102.5400
Cell Name: pancreatic A cell (CL0000171)
Fold Change: -0.0685
Cell Significance Index: -50.7100
Cell Name: pancreatic PP cell (CL0002275)
Fold Change: -0.0881
Cell Significance Index: -55.0400
Cell Name: GABAergic interneuron (CL0011005)
Fold Change: -0.0967
Cell Significance Index: -66.8900
Cell Name: type B pancreatic cell (CL0000169)
Fold Change: -0.1206
Cell Significance Index: -68.0400
Cell Name: obsolete caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
Fold Change: -0.1328
Cell Significance Index: -47.6300
Cell Name: microfold cell of epithelium of small intestine (CL1000353)
Fold Change: -0.1408
Cell Significance Index: -9.7400
Cell Name: ciliary muscle cell (CL1000443)
Fold Change: -0.2029
Cell Significance Index: -92.0900
Cell Name: dopaminergic neuron (CL0000700)
Fold Change: -0.3239
Cell Significance Index: -93.2000
Cell Name: pancreatic D cell (CL0000173)
Fold Change: -0.3286
Cell Significance Index: -69.2100
Cell Name: perivascular cell (CL4033054)
Fold Change: -0.3530
Cell Significance Index: -1.6300
Cell Name: pigmented ciliary epithelial cell (CL0002303)
Fold Change: -0.4148
Cell Significance Index: -60.2900
Cell Name: fibro/adipogenic progenitor cell (CL0009099)
Fold Change: -0.4209
Cell Significance Index: -21.2700
Cell Name: mesenchymal cell (CL0008019)
Fold Change: -0.5019
Cell Significance Index: -8.4000
Cell Name: mesonephric nephron tubule epithelial cell (CL1000022)
Fold Change: -0.5053
Cell Significance Index: -17.5600
Cell Name: pancreatic ductal cell (CL0002079)
Fold Change: -0.5344
Cell Significance Index: -61.2300
Cell Name: endothelial cell of placenta (CL0009092)
Fold Change: -0.5478
Cell Significance Index: -3.3100
Cell Name: epithelial cell of stomach (CL0002178)
Fold Change: -0.6449
Cell Significance Index: -75.1600
Cell Name: neuron associated cell (CL0000095)
Fold Change: -0.7299
Cell Significance Index: -29.9100
Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
Fold Change: -0.8409
Cell Significance Index: -23.5000
Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
Fold Change: -0.8939
Cell Significance Index: -93.0800
Cell Name: kidney loop of Henle descending limb epithelial cell (CL1001021)
Fold Change: -0.8960
Cell Significance Index: -70.9600
Cell Name: cardiac muscle myoblast (CL0000513)
Fold Change: -0.9742
Cell Significance Index: -74.7600
Cell Name: paneth cell of epithelium of small intestine (CL1000343)
Fold Change: -0.9956
Cell Significance Index: -21.5700
Cell Name: pro-T cell (CL0000827)
Fold Change: -1.0913
Cell Significance Index: -27.8800
Cell Name: glycinergic neuron (CL1001509)
Fold Change: -1.2188
Cell Significance Index: -63.9900
Cell Name: CD4-positive, alpha-beta memory T cell, CD45RO-positive (CL0001204)
Fold Change: -1.2306
Cell Significance Index: -36.1400
Cell Name: type I muscle cell (CL0002211)
Fold Change: -1.2406
Cell Significance Index: -30.2700
Cell Name: eye photoreceptor cell (CL0000287)
Fold Change: -1.4039
Cell Significance Index: -88.4900
Cell Name: hippocampal granule cell (CL0001033)
Fold Change: -1.5232
Cell Significance Index: -102.4200
Cell Name: preadipocyte (CL0002334)
Fold Change: -1.5361
Cell Significance Index: -29.9800
Cell Name: theca cell (CL0000503)
Fold Change: -1.6017
Cell Significance Index: -9.4100
Cell Name: retinal progenitor cell (CL0002672)
Fold Change: -1.6435
Cell Significance Index: -92.2300
Cell Name: transit amplifying cell of colon (CL0009011)
Fold Change: -1.6954
Cell Significance Index: -54.3000
Cell Name: intestinal tuft cell (CL0019032)
Fold Change: -1.7157
Cell Significance Index: -105.1900
Cell Name: conjunctival epithelial cell (CL1000432)
Fold Change: -1.7422
Cell Significance Index: -23.7700
Cell Name: forebrain neuroblast (CL1000042)
Fold Change: -1.8211
Cell Significance Index: -111.9400
Cell Name: paneth cell of colon (CL0009009)
Fold Change: -1.9401
Cell Significance Index: -29.0700
Cell Name: interstitial cell of ovary (CL0002094)
Fold Change: -2.0770
Cell Significance Index: -26.6000
Cell Name: umbrella cell of urothelium (CL4030056)
Fold Change: -2.1040
Cell Significance Index: -19.3800

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.

**Key Characteristics:** 1. **Negative Regulation of NF-κB**: NFKBIA inhibits the activation of NF-κB, preventing its translocation to the nucleus and subsequent transcriptional activity. 2. **Cellular Localization**: NFKBIA is primarily localized to the cytoplasm, where it inhibits NF-κB activation. 3. **Signaling Pathways**: NFKBIA regulates various signaling pathways, including the Toll-like receptor (TLR) signaling cascade, the MyD88-dependent signaling pathway, and the NF-κB-inducing kinase (NIK) pathway. 4. **Cell Type-Specific Expression**: NFKBIA is significantly expressed in various immune cells, including B cells, macrophages, dendritic cells, and natural killer cells. **Pathways and Functions:** 1. **Adaptive Immune Response**: NFKBIA regulates the adaptive immune response by inhibiting NF-κB activation, which is essential for the activation of B cells, T cells, and dendritic cells. 2. **Innate Immune Response**: NFKBIA also regulates the innate immune response by inhibiting NF-κB activation, which is essential for the production of cytokines and chemokines. 3. **Apoptosis**: NFKBIA regulates apoptosis by inhibiting NF-κB activation, which is essential for the regulation of programmed cell death. 4. **Inflammation**: NFKBIA regulates inflammation by inhibiting NF-κB activation, which is essential for the production of pro-inflammatory cytokines and chemokines. 5. **Cell Survival**: NFKBIA regulates cell survival by inhibiting NF-κB activation, which is essential for the regulation of anti-apoptotic genes. **Clinical Significance:** 1. **Autoimmune Disorders**: Dysregulation of NFKBIA has been implicated in various autoimmune disorders, including rheumatoid arthritis, lupus, and multiple sclerosis. 2. **Cancer**: NFKBIA has been shown to be a tumor suppressor gene, and its dysregulation has been implicated in various types of cancer, including breast cancer and lung cancer. 3. **Infectious Diseases**: NFKBIA regulates the immune response to infectious diseases, including viral and bacterial infections. 4. **Inflammatory Disorders**: NFKBIA regulates the inflammatory response in various inflammatory disorders, including asthma and chronic obstructive pulmonary disease (COPD). In conclusion, NFKBIA plays a critical role in regulating immune responses by inhibiting NF-κB activation. Its dysregulation has been implicated in various diseases, including autoimmune disorders, cancer, and infectious diseases. Further research is needed to fully understand the mechanisms of NFKBIA regulation and its clinical significance.

Disclaimer: This summary is generated by an AI language model and may contain inaccuracies or hallucinations. However, it is cross-referenced with curated gene expression data from major biological sources. Please verify the information before use.

NF-kappa-B inhibitor alpha

Genular Protein ID: 3642661006

Symbol: IKBA_HUMAN

Name: NF-kappa-B inhibitor alpha

UniProtKB Accession Codes:

P25963 B2R8L6

Database IDs:

Citations:

PubMed ID: 1829648

Title: Characterization of an immediate-early gene induced in adherent monocytes that encodes I kappa B-like activity.

PubMed ID: 1829648

DOI: 10.1016/0092-8674(91)90022-q

PubMed ID: 10637284

Title: Clonal deleterious mutations in the IkappaB alpha gene in the malignant cells in Hodgkin's lymphoma.

PubMed ID: 10637284

DOI: 10.1084/jem.191.2.395

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 12508121

Title: The DNA sequence and analysis of human chromosome 14.

PubMed ID: 12508121

DOI: 10.1038/nature01348

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 1493333

Title: I kappa B/MAD-3 masks the nuclear localization signal of NF-kappa B p65 and requires the transactivation domain to inhibit NF-kappa B p65 DNA binding.

PubMed ID: 1493333

DOI: 10.1091/mbc.3.12.1339

PubMed ID: 7796813

Title: Phosphorylation of human I kappa B-alpha on serines 32 and 36 controls I kappa B-alpha proteolysis and NF-kappa B activation in response to diverse stimuli.

PubMed ID: 7796813

DOI: 10.1002/j.1460-2075.1995.tb07287.x

PubMed ID: 7628694

Title: Signal-induced site-specific phosphorylation targets I kappa B alpha to the ubiquitin-proteasome pathway.

PubMed ID: 7628694

DOI: 10.1101/gad.9.13.1586

PubMed ID: 7479976

Title: Signal-induced degradation of IkappaB alpha requires site-specific ubiquitination.

PubMed ID: 7479976

DOI: 10.1073/pnas.92.24.11259

PubMed ID: 7878466

Title: Control of I kappa B-alpha proteolysis by site-specific, signal-induced phosphorylation.

PubMed ID: 7878466

DOI: 10.1126/science.7878466

PubMed ID: 8797825

Title: Tyrosine phosphorylation of IkappaB-alpha activates NF-kappaB without proteolytic degradation of IkappaB-alpha.

PubMed ID: 8797825

DOI: 10.1016/s0092-8674(00)80153-1

PubMed ID: 8631829

Title: Role of IkappaBalpha ubiquitination in signal-induced activation of NFkappaB in vivo.

PubMed ID: 8631829

DOI: 10.1074/jbc.271.13.7844

PubMed ID: 8940099

Title: Site-specific tyrosine phosphorylation of IkappaBalpha negatively regulates its inducible phosphorylation and degradation.

PubMed ID: 8940099

DOI: 10.1074/jbc.271.49.31049

PubMed ID: 8622692

Title: Casein kinase II phosphorylates I kappa B alpha at S-283, S-289, S-293, and T-291 and is required for its degradation.

PubMed ID: 8622692

DOI: 10.1128/mcb.16.3.899

PubMed ID: 8657102

Title: Mapping of the inducible IkappaB phosphorylation sites that signal its ubiquitination and degradation.

PubMed ID: 8657102

DOI: 10.1128/mcb.16.4.1295

PubMed ID: 8657113

Title: Phosphorylation of IkappaBalpha in the C-terminal PEST domain by casein kinase II affects intrinsic protein stability.

PubMed ID: 8657113

DOI: 10.1128/mcb.16.4.1401

PubMed ID: 9566872

Title: Nuclear localization of IkappaB alpha is mediated by the second ankyrin repeat: the IkappaB alpha ankyrin repeats define a novel class of cis-acting nuclear import sequences.

PubMed ID: 9566872

DOI: 10.1128/mcb.18.5.2524

PubMed ID: 9751059

Title: IKAP is a scaffold protein of the IkappaB kinase complex.

PubMed ID: 9751059

DOI: 10.1038/26254

PubMed ID: 9701247

Title: A minimal glycine-alanine repeat prevents the interaction of ubiquitinated I kappaB alpha with the proteasome: a new mechanism for selective inhibition of proteolysis.

PubMed ID: 9701247

DOI: 10.1038/nm0898-939

PubMed ID: 10437795

Title: A complex containing betaTrCP recruits Cdc34 to catalyse ubiquitination of IkappaBalpha.

PubMed ID: 10437795

DOI: 10.1016/s0014-5793(99)00895-9

PubMed ID: 10329681

Title: Identification of the ubiquitin carrier proteins, E2s, involved in signal-induced conjugation and subsequent degradation of IkappaBalpha.

PubMed ID: 10329681

DOI: 10.1074/jbc.274.21.14823

PubMed ID: 10574930

Title: Immunosuppressant FK506 activates NF-kappaB through the proteasome-mediated degradation of IkappaBalpha. Requirement for Ikappabalpha n-terminal phosphorylation but not ubiquitination sites.

PubMed ID: 10574930

DOI: 10.1074/jbc.274.49.34657

PubMed ID: 10454581

Title: Direct association and nuclear import of the hepatitis B virus X protein with the NF-kappaB inhibitor IkappaBalpha.

PubMed ID: 10454581

DOI: 10.1128/mcb.19.9.6345

PubMed ID: 10644755

Title: Homodimer of two F-box proteins betaTrCP1 or betaTrCP2 binds to IkappaBalpha for signal-dependent ubiquitination.

PubMed ID: 10644755

DOI: 10.1074/jbc.275.4.2877

PubMed ID: 10882136

Title: IKK epsilon is part of a novel PMA-inducible IkappaB kinase complex.

PubMed ID: 10882136

DOI: 10.1016/s1097-2765(00)80445-1

PubMed ID: 10783893

Title: NAK is an IkappaB kinase-activating kinase.

PubMed ID: 10783893

DOI: 10.1038/35008109

PubMed ID: 10657303

Title: A subclass of Ras proteins that regulate the degradation of IkappaB.

PubMed ID: 10657303

DOI: 10.1126/science.287.5454.869

PubMed ID: 10655476

Title: A nuclear export signal in the N-terminal regulatory domain of IkappaBalpha controls cytoplasmic localization of inactive NF-kappaB/IkappaBalpha complexes.

PubMed ID: 10655476

DOI: 10.1073/pnas.97.3.1014

PubMed ID: 11124955

Title: SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting.

PubMed ID: 11124955

DOI: 10.1074/jbc.m009476200

PubMed ID: 20356841

Title: Thrombin and collagen induce a feedback inhibitory signaling pathway in platelets involving dissociation of the catalytic subunit of protein kinase A from an NFkappaB-IkappaB complex.

PubMed ID: 20356841

DOI: 10.1074/jbc.m109.077602

PubMed ID: 16648481

Title: Protein methyltransferase 2 inhibits NF-kappaB function and promotes apoptosis.

PubMed ID: 16648481

DOI: 10.1128/mcb.26.10.3864-3874.2006

PubMed ID: 17003112

Title: Posttranslational hydroxylation of ankyrin repeats in IkappaB proteins by the hypoxia-inducible factor (HIF) asparaginyl hydroxylase, factor inhibiting HIF (FIH).

PubMed ID: 17003112

DOI: 10.1073/pnas.0606877103

PubMed ID: 17956732

Title: RSUME, a small RWD-containing protein, enhances SUMO conjugation and stabilizes HIF-1alpha during hypoxia.

PubMed ID: 17956732

DOI: 10.1016/j.cell.2007.07.044

PubMed ID: 18577712

Title: The familial Mediterranean fever protein, pyrin, is cleaved by caspase-1 and activates NF-kappaB through its N-terminal fragment.

PubMed ID: 18577712

DOI: 10.1182/blood-2008-01-134932

PubMed ID: 20347421

Title: Priming and extending: a UbcH5/Cdc34 E2 handoff mechanism for polyubiquitination on a SCF substrate.

PubMed ID: 20347421

DOI: 10.1016/j.molcel.2010.02.025

PubMed ID: 20504922

Title: The cysteine protease domain of porcine reproductive and respiratory syndrome virus nonstructural protein 2 possesses deubiquitinating and interferon antagonism functions.

PubMed ID: 20504922

DOI: 10.1128/jvi.00217-10

PubMed ID: 23469069

Title: In silico structural and functional characterization of the RSUME splice variants.

PubMed ID: 23469069

DOI: 10.1371/journal.pone.0057795

PubMed ID: 23675531

Title: DDRGK1 regulates NF-kappaB activity by modulating IkappaBalpha stability.

PubMed ID: 23675531

DOI: 10.1371/journal.pone.0064231

PubMed ID: 36651806

Title: USP39 Regulates NF-kappaB-Mediated Inflammatory Responses through Deubiquitinating K48-Linked IkappaBalpha.

PubMed ID: 36651806

DOI: 10.4049/jimmunol.2200603

PubMed ID: 9865693

Title: Structure of an IkappaBalpha/NF-kappaB complex.

PubMed ID: 9865693

DOI: 10.1016/s0092-8674(00)81698-0

PubMed ID: 9865694

Title: The crystal structure of the IkappaBalpha/NF-kappaB complex reveals mechanisms of NF-kappaB inactivation.

PubMed ID: 9865694

DOI: 10.1016/s0092-8674(00)81699-2

PubMed ID: 14523047

Title: A hypermorphic IkappaBalpha mutation is associated with autosomal dominant anhidrotic ectodermal dysplasia and T cell immunodeficiency.

PubMed ID: 14523047

DOI: 10.1172/jci18714

PubMed ID: 18412279

Title: A novel mutation in NFKBIA/IKBA results in a degradation-resistant N-truncated protein and is associated with ectodermal dysplasia with immunodeficiency.

PubMed ID: 18412279

DOI: 10.1002/humu.20740

Sequence Information:

Length: 317
Mass: 35609
Checksum: 088B313226786395
Sequence:

MFQAAERPQE WAMEGPRDGL KKERLLDDRH DSGLDSMKDE EYEQMVKELQ EIRLEPQEVP 
RGSEPWKQQL TEDGDSFLHL AIIHEEKALT MEVIRQVKGD LAFLNFQNNL QQTPLHLAVI 
TNQPEIAEAL LGAGCDPELR DFRGNTPLHL ACEQGCLASV GVLTQSCTTP HLHSILKATN 
YNGHTCLHLA SIHGYLGIVE LLVSLGADVN AQEPCNGRTA LHLAVDLQNP DLVSLLLKCG 
ADVNRVTYQG YSPYQLTWGR PSTRIQQQLG QLTLENLQML PESEDEESYD TESEFTEFTE 
DELPYDDCVF GGQRLTL

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: NFKBIA

Associated with

Cells (max top 100)

Other Information

Characterization of an immediate-early gene induced in adherent monocytes that encodes I kappa B-like activity. PubMed ID: 1829648

Clonal deleterious mutations in the IkappaB alpha gene in the malignant cells in Hodgkin's lymphoma. PubMed ID: 10637284

Complete sequencing and characterization of 21,243 full-length human cDNAs. PubMed ID: 14702039

The DNA sequence and analysis of human chromosome 14. PubMed ID: 12508121

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

I kappa B/MAD-3 masks the nuclear localization signal of NF-kappa B p65 and requires the transactivation domain to inhibit NF-kappa B p65 DNA binding. PubMed ID: 1493333

Phosphorylation of human I kappa B-alpha on serines 32 and 36 controls I kappa B-alpha proteolysis and NF-kappa B activation in response to diverse stimuli. PubMed ID: 7796813

Signal-induced site-specific phosphorylation targets I kappa B alpha to the ubiquitin-proteasome pathway. PubMed ID: 7628694

Signal-induced degradation of IkappaB alpha requires site-specific ubiquitination. PubMed ID: 7479976

Control of I kappa B-alpha proteolysis by site-specific, signal-induced phosphorylation. PubMed ID: 7878466

Tyrosine phosphorylation of IkappaB-alpha activates NF-kappaB without proteolytic degradation of IkappaB-alpha. PubMed ID: 8797825

Role of IkappaBalpha ubiquitination in signal-induced activation of NFkappaB in vivo. PubMed ID: 8631829

Site-specific tyrosine phosphorylation of IkappaBalpha negatively regulates its inducible phosphorylation and degradation. PubMed ID: 8940099

Casein kinase II phosphorylates I kappa B alpha at S-283, S-289, S-293, and T-291 and is required for its degradation. PubMed ID: 8622692

Mapping of the inducible IkappaB phosphorylation sites that signal its ubiquitination and degradation. PubMed ID: 8657102

Phosphorylation of IkappaBalpha in the C-terminal PEST domain by casein kinase II affects intrinsic protein stability. PubMed ID: 8657113

Nuclear localization of IkappaB alpha is mediated by the second ankyrin repeat: the IkappaB alpha ankyrin repeats define a novel class of cis-acting nuclear import sequences. PubMed ID: 9566872

IKAP is a scaffold protein of the IkappaB kinase complex. PubMed ID: 9751059

A minimal glycine-alanine repeat prevents the interaction of ubiquitinated I kappaB alpha with the proteasome: a new mechanism for selective inhibition of proteolysis. PubMed ID: 9701247

A complex containing betaTrCP recruits Cdc34 to catalyse ubiquitination of IkappaBalpha. PubMed ID: 10437795

Identification of the ubiquitin carrier proteins, E2s, involved in signal-induced conjugation and subsequent degradation of IkappaBalpha. PubMed ID: 10329681

Immunosuppressant FK506 activates NF-kappaB through the proteasome-mediated degradation of IkappaBalpha. Requirement for Ikappabalpha n-terminal phosphorylation but not ubiquitination sites. PubMed ID: 10574930

Direct association and nuclear import of the hepatitis B virus X protein with the NF-kappaB inhibitor IkappaBalpha. PubMed ID: 10454581

Homodimer of two F-box proteins betaTrCP1 or betaTrCP2 binds to IkappaBalpha for signal-dependent ubiquitination. PubMed ID: 10644755

IKK epsilon is part of a novel PMA-inducible IkappaB kinase complex. PubMed ID: 10882136

NAK is an IkappaB kinase-activating kinase. PubMed ID: 10783893

A subclass of Ras proteins that regulate the degradation of IkappaB. PubMed ID: 10657303

A nuclear export signal in the N-terminal regulatory domain of IkappaBalpha controls cytoplasmic localization of inactive NF-kappaB/IkappaBalpha complexes. PubMed ID: 10655476

SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting. PubMed ID: 11124955

Thrombin and collagen induce a feedback inhibitory signaling pathway in platelets involving dissociation of the catalytic subunit of protein kinase A from an NFkappaB-IkappaB complex. PubMed ID: 20356841

Protein methyltransferase 2 inhibits NF-kappaB function and promotes apoptosis. PubMed ID: 16648481

Posttranslational hydroxylation of ankyrin repeats in IkappaB proteins by the hypoxia-inducible factor (HIF) asparaginyl hydroxylase, factor inhibiting HIF (FIH). PubMed ID: 17003112

RSUME, a small RWD-containing protein, enhances SUMO conjugation and stabilizes HIF-1alpha during hypoxia. PubMed ID: 17956732

The familial Mediterranean fever protein, pyrin, is cleaved by caspase-1 and activates NF-kappaB through its N-terminal fragment. PubMed ID: 18577712

Priming and extending: a UbcH5/Cdc34 E2 handoff mechanism for polyubiquitination on a SCF substrate. PubMed ID: 20347421

The cysteine protease domain of porcine reproductive and respiratory syndrome virus nonstructural protein 2 possesses deubiquitinating and interferon antagonism functions. PubMed ID: 20504922

In silico structural and functional characterization of the RSUME splice variants. PubMed ID: 23469069

DDRGK1 regulates NF-kappaB activity by modulating IkappaBalpha stability. PubMed ID: 23675531

USP39 Regulates NF-kappaB-Mediated Inflammatory Responses through Deubiquitinating K48-Linked IkappaBalpha. PubMed ID: 36651806

Structure of an IkappaBalpha/NF-kappaB complex. PubMed ID: 9865693

The crystal structure of the IkappaBalpha/NF-kappaB complex reveals mechanisms of NF-kappaB inactivation. PubMed ID: 9865694

A hypermorphic IkappaBalpha mutation is associated with autosomal dominant anhidrotic ectodermal dysplasia and T cell immunodeficiency. PubMed ID: 14523047

A novel mutation in NFKBIA/IKBA results in a degradation-resistant N-truncated protein and is associated with ectodermal dysplasia with immunodeficiency. PubMed ID: 18412279