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NFKBIE
Identifiers
Aliases	NFKBIE, IKBE, NFKB inhibitor epsilon
External IDs	OMIM: 604548; MGI: 1194908; HomoloGene: 36160; GeneCards: NFKBIE; OMA:NFKBIE - orthologs
Gene location (Human) Chr. Chromosome 6 (human) Band 6p21.1 Start 44,258,166 bp End 44,265,788 bp
Gene location (Mouse) Chr. Chromosome 17 (mouse) Band 17|17 B3 Start 45,866,629 bp End 45,874,095 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in gonad granulocyte spleen monocyte cartilage tissue appendix bone marrow cells lymph node testicle blood Top expressed in mesenteric lymph nodes spleen lumbar spinal ganglion granulocyte otic vesicle thymus subcutaneous adipose tissue blood saccule condyle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding Cellular component cytoplasm perinuclear region of cytoplasm Golgi apparatus fibrillar center nucleus cytosol Biological process cytoplasmic sequestering of transcription factor D-serine transport Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 4794 18037 Ensembl ENSG00000146232 ENSMUSG00000023947 UniProt O00221 O54910 RefSeq (mRNA) NM_004556 NM_008690 NM_001304956 RefSeq (protein) NP_004547 NP_001291885 NP_032716 Location (UCSC) Chr 6: 44.26 – 44.27 Mb Chr 17: 45.87 – 45.87 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor, epsilon, also known as NFKBIE, is a protein which in humans is encoded by the NFKBIE gene.

Function

NFKBIE protein expression is up-regulated following NF-κB activation and during myelopoiesis. NFKBIE is able to inhibit NF-κB-directed transactivation via cytoplasmic retention of REL proteins.

NFKB1 or NFKB2 is bound to REL, RELA, or RELB to form the NF-κB transcription factor complex. The NF-κB complex is inhibited by I-kappa-B proteins (NFKBIA or NFKBIB), which inactivate NF-kappa-B by trapping it in the cytoplasm. Phosphorylation of serine residues on the I-kappa-B proteins by kinases (IKBKA, or IKBKB) marks them for destruction via the ubiquitination pathway, thereby allowing activation of the NF-kappa-B complex. Activated NF-κB complex translocates into the nucleus and binds DNA at kappa-B-binding motifs such as 5-prime GGGRNNYYCC 3-prime or 5-prime HGGARNYYCC 3-prime (where H is A, C, or T; R is an A or G purine; and Y is a C or T pyrimidine). For some genes, activation requires NF-κB interaction with other transcription factors, such as STAT (see STAT6), AP-1 (JUN), and NFAT (see NFATC1).

Interactions

NFKBIE has been shown to interact with NFKB2, RELA, NFKB1 and REL.

References

1. ^ GRCh38: Ensembl release 89: ENSG00000146232 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000023947 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. ^ "Entrez Gene: NFKBIE nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor, epsilon".
6. ^ Whiteside ST, Epinat JC, Rice NR, Israël A (March 1997). "I kappa B epsilon, a novel member of the I kappa B family, controls RelA and cRel NF-kappa B activity". EMBO J. 16 (6): 1413–26. doi:10.1093/emboj/16.6.1413. PMC 1169738. PMID 9135156.
7. ^ Li, Z; Nabel G J (October 1997). "A new member of the I kappaB protein family, I kappaB epsilon, inhibits RelA (p65)-mediated NF-kappaB transcription". Mol. Cell. Biol. 17 (10). United States: 6184–90. doi:10.1128/mcb.17.10.6184. ISSN 0270-7306. PMC 232469. PMID 9315679.
8. Kumar, S; Gélinas C (October 1993). "I kappa B alpha-mediated inhibition of v-Rel DNA binding requires direct interaction with the RXXRXRXXC Rel/kappa B DNA-binding motif". Proc. Natl. Acad. Sci. U.S.A. 90 (19). United States: 8962–6. Bibcode:1993PNAS...90.8962K. doi:10.1073/pnas.90.19.8962. ISSN 0027-8424. PMC 47481. PMID 8415639.
9. Spiecker, M; Darius H; Liao J K (March 2000). "A functional role of I kappa B-epsilon in endothelial cell activation". J. Immunol. 164 (6). United States: 3316–22. doi:10.4049/jimmunol.164.6.3316. ISSN 0022-1767. PMID 10706725.

Further reading

• Hansen SK, Baeuerle PA, Blasi F (1994). "Purification, reconstitution, and I kappa B association of the c-Rel-p65 (RelA) complex, a strong activator of transcription". Mol. Cell. Biol. 14 (4): 2593–603. doi:10.1128/mcb.14.4.2593. PMC 358627. PMID 8139561.
• Kumar S, Gélinas C (1993). "I kappa B alpha-mediated inhibition of v-Rel DNA binding requires direct interaction with the RXXRXRXXC Rel/kappa B DNA-binding motif". Proc. Natl. Acad. Sci. U.S.A. 90 (19): 8962–6. Bibcode:1993PNAS...90.8962K. doi:10.1073/pnas.90.19.8962. PMC 47481. PMID 8415639.
• Whiteside ST, Epinat JC, Rice NR, Israël A (1997). "I kappa B epsilon, a novel member of the I kappa B family, controls RelA and cRel NF-kappa B activity". EMBO J. 16 (6): 1413–26. doi:10.1093/emboj/16.6.1413. PMC 1169738. PMID 9135156.
• Curristin SM, Bird KJ, Tubbs RJ, Ruddell A (1997). "VBP and RelA regulate avian leukosis virus long terminal repeat-enhanced transcription in B cells". J. Virol. 71 (8): 5972–81. doi:10.1128/JVI.71.8.5972-5981.1997. PMC 191853. PMID 9223487.
• Li Z, Nabel GJ (1997). "A new member of the I kappaB protein family, I kappaB epsilon, inhibits RelA (p65)-mediated NF-kappaB transcription". Mol. Cell. Biol. 17 (10): 6184–90. doi:10.1128/mcb.17.10.6184. PMC 232469. PMID 9315679.
• Spiecker M, Darius H, Liao JK (2000). "A functional role of I kappa B-epsilon in endothelial cell activation". J. Immunol. 164 (6): 3316–22. doi:10.4049/jimmunol.164.6.3316. PMID 10706725.
• Bourke E, Kennedy EJ, Moynagh PN (2001). "Loss of Ikappa B-beta is associated with prolonged NF-kappa B activity in human glial cells" (PDF). J. Biol. Chem. 275 (51): 39996–40002. doi:10.1074/jbc.M007693200. PMID 10998424. S2CID 56360025.
• Lee SH, Hannink M (2002). "Characterization of the nuclear import and export functions of Ikappa B(epsilon)". J. Biol. Chem. 277 (26): 23358–66. doi:10.1074/jbc.M111559200. PMID 11970947.
• Bruno ME, Borchers CH, Dial JM, et al. (2002). "Effects of TCDD upon IkappaB and IKK subunits localized in microsomes by proteomics". Arch. Biochem. Biophys. 406 (2): 153–64. doi:10.1016/S0003-9861(02)00452-6. PMID 12361703.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Emmerich F, Theurich S, Hummel M, et al. (2004). "Inactivating I kappa B epsilon mutations in Hodgkin/Reed-Sternberg cells". J. Pathol. 201 (3): 413–20. doi:10.1002/path.1454. PMID 14595753. S2CID 33577004.
• Bouwmeester T, Bauch A, Ruffner H, et al. (2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nat. Cell Biol. 6 (2): 97–105. doi:10.1038/ncb1086. PMID 14743216. S2CID 11683986.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
• Nasu-Nishimura Y, Hayashi T, Ohishi T, et al. (2006). "Role of the Rho GTPase-activating protein RICS in neurite outgrowth". Genes Cells. 11 (6): 607–14. doi:10.1111/j.1365-2443.2006.00966.x. PMID 16716191. S2CID 7935936.
• Stefansson B, Brautigan DL (2006). "Protein phosphatase 6 subunit with conserved Sit4-associated protein domain targets IkappaBepsilon". J. Biol. Chem. 281 (32): 22624–34. doi:10.1074/jbc.M601772200. PMID 16769727.
• Chapman SJ, Khor CC, Vannberg FO, et al. (2007). "IkappaB genetic polymorphisms and invasive pneumococcal disease". Am. J. Respir. Crit. Care Med. 176 (2): 181–7. doi:10.1164/rccm.200702-169OC. PMID 17463416.

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