Nuclear factor gene transcriptions: Difference between revisions

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==Leucine zippers==
==Leucine zippers==
 
{{main|Leucine zipper}}
Leucine zippers are a dimerization motif of the BZIP domain (bZIP) (Basic-region leucine zipper) class of [[eukaryotic]] [[transcription factor]]s.<ref name="Vinson et al.">{{cite journal | vauthors = Vinson CR, Sigler PB, McKnight SL | title = Scissors-grip model for DNA recognition by a family of leucine zipper proteins | journal = Science | volume = 246 | issue = 4932 | pages = 911–6 | date = November 1989 | pmid = 2683088 | doi = 10.1126/science.2683088 | bibcode = 1989Sci...246..911V }}</ref> The bZIP domain is 60 to 80 [[amino acid]]s in length with a highly conserved [[DNA]] binding basic region and a more diversified leucine zipper dimerization region.<ref name="Zhang et al., 2014">{{cite journal | vauthors = E ZG, Zhang YP, Zhou JH, Wang L | title = Mini review roles of the bZIP gene family in rice | journal = Genetics and Molecular Research | volume = 13 | issue = 2 | pages = 3025–36 | date = April 2014 | pmid = 24782137 | doi = 10.4238/2014.April.16.11 | doi-access = free }}</ref> The localization of the leucines are critical for the DNA binding to the proteins. Leucine zippers are present in both eukaryotic and prokaryotic regulatory proteins, but are mainly a feature of eukaryotes.
Leucine zippers are a dimerization motif of the BZIP domain (bZIP) (Basic-region leucine zipper) class of [[eukaryotic]] [[transcription factor]]s.<ref name="Vinson et al.">{{cite journal | vauthors = Vinson CR, Sigler PB, McKnight SL | title = Scissors-grip model for DNA recognition by a family of leucine zipper proteins | journal = Science | volume = 246 | issue = 4932 | pages = 911–6 | date = November 1989 | pmid = 2683088 | doi = 10.1126/science.2683088 | bibcode = 1989Sci...246..911V }}</ref> The bZIP domain is 60 to 80 [[amino acid]]s in length with a highly conserved [[DNA]] binding basic region and a more diversified leucine zipper dimerization region.<ref name="Zhang et al., 2014">{{cite journal | vauthors = E ZG, Zhang YP, Zhou JH, Wang L | title = Mini review roles of the bZIP gene family in rice | journal = Genetics and Molecular Research | volume = 13 | issue = 2 | pages = 3025–36 | date = April 2014 | pmid = 24782137 | doi = 10.4238/2014.April.16.11 | doi-access = free }}</ref> The localization of the leucines are critical for the DNA binding to the proteins. Leucine zippers are present in both eukaryotic and prokaryotic regulatory proteins, but are mainly a feature of eukaryotes.


Revision as of 05:42, 4 May 2020

Nuclear factor kappa-light-chain-enhancer of activated B cells (NF-κB) is a protein complex that controls transcription of DNA, cytokine production and cell survival. NF-κB is found in almost all animal cell types and is involved in cellular responses to stimuli such as stress, cytokines, free radicals, heavy metals, ultraviolet irradiation, oxidized LDL, and bacterial or viral antigens.[1][2][3][4][5] NF-κB plays a key role in regulating the immune response to infection. Incorrect regulation of NF-κB has been linked to cancer, inflammatory and autoimmune diseases, septic shock, viral infection, and improper immune development. NF-κB has also been implicated in processes of synaptic plasticity and memory.[6][7][8][9][10][11]

Hepatic nuclear factors

Main article: HNF gene transcriptions

Nuclear factor-B/Rel transcription factors

"The NF‐κB/Rel family of eukaryotic transcription factors controls many mammalian genes of significant biomedical importance, including genes encoding pro‐inflammatory cytokines, interferones, major histocompatibility complex (MHC) proteins, growth factors, cell adhesion molecules, but also viruses such as the human immunodeficiency virus (HIV) or Herpes (Baeuerle and Henkel, 1994; Thanos and Maniatis, 1995; Baeuerle and Baltimore, 1996; Baldwin, 1996; Chytil and Verdine, 1996)."[12]

Nuclear factor of activated T cells

Main article: Nuclear factor of activated T cell gene transcriptions (NFAT)

DNA binding sites

The "natural 11 bp 𝜿B binding site MHC H-2 [is 3'-CCCCTAAGGGG-5'] which is well ordered in our structure."[12]

Hepatic nuclear factors (HNFs) bind through their DNA-binding domain (DBD) to consensus elements (A/G/T)(A/T)(A/G)T(C/T)(A/C/G)AT(A/C/G/T)(A/G/T), resulting in gene transcription.[13]

Leucine zippers

Main article: Leucine zipper

Leucine zippers are a dimerization motif of the BZIP domain (bZIP) (Basic-region leucine zipper) class of eukaryotic transcription factors.[14] The bZIP domain is 60 to 80 amino acids in length with a highly conserved DNA binding basic region and a more diversified leucine zipper dimerization region.[15] The localization of the leucines are critical for the DNA binding to the proteins. Leucine zippers are present in both eukaryotic and prokaryotic regulatory proteins, but are mainly a feature of eukaryotes.

They can also be annotated simply as ZIPs, and ZIP-like motifs have been found in proteins other than transcription factors and are thought to be one of the general protein modules for protein–protein interactions.[16]

The bZIP interacts with DNA via basic, amine residues (see basic amino acids in (provided table (sort by pH)) of certain amino acids in the "basic" domain, such as lysines and arginines. These basic residues interact in the major groove of the DNA, forming sequence-specific interactions. The mechanism of transcriptional regulation by bZIP proteins has been studied in detail. Most bZIP proteins show high binding affinity for the ACGT motifs, which include CACGTG (G box), GACGTC (C box), TACGTA (A box), AACGTT (T box), and a GCN4 motif, namely TGA(G/C)TCA.[17][15][18] The bZIP heterodimers exist in a variety of eukaryotes and are more common in organisms with higher evolution complexity.[19] Heterodimeric bZIP proteins differ from homodimeric bZIP and from each other in protein-protein interaction affinity.[20] These heterodimers exhibit complex DNA binding specificity. When combined with a different partner, most of the bZIP pairs bind to DNA sequences that each individual partner prefers. In some cases, dimerization of different bZIP partners can change the DNA sequence that the pair targets in a manner that could not have been predicted based on the preferences of each partner alone. This suggests that, as heterodimers, bZIP transcription factors are able to change their preferences for which location they target in the DNA. The ability of bZIP domain forming dimers with different partners greatly expands the locations on the genome to which bZIP transcription factors can bind and from which they can regulate gene expression.[20]

A small number of bZIP factors such as OsOBF1 can also recognize palindromic sequences.[21] However, the others, including LIP19, OsZIP-2a, and OsZIP-2b, do not bind to DNA sequences. Instead, these bZIP proteins form heterodimers with other bZIPs to regulate transcriptional activities.[21][22]

Nuclear factor genes

Gene ID: 4783 is NFIL3 nuclear factor, interleukin 3 regulated on 9q22.31: "The protein encoded by this gene is a transcriptional regulator that binds as a homodimer to activating transcription factor (ATF) sites in many cellular and viral promoters. The encoded protein represses PER1 and PER2 expression and therefore plays a role in the regulation of circadian rhythm. Three transcript variants encoding the same protein have been found for this gene."[23]

  1. NP_001276928.1 nuclear factor interleukin-3-regulated protein: "Transcript Variant: This variant (1) represents the longest transcript. All three variants encode the same protein."[23] "NFIL3, also called E4 promoter-binding protein 4 (E4BP4), is a Basic leucine zipper (bZIP) transcription factor that was independently identified as a transactivator of the IL3 promoter in T-cells and as a transcriptional repressor that binds to a DNA sequence site in the adenovirus E4 promoter. Its expression levels are regulated by cytokines and it plays crucial functions in the immune system. It is required for the development of natural killer cells and CD8+ conventional dendritic cells. In B-cells, NFIL3 mediates immunoglobulin heavy chain class switching that is required for IgE production, thereby influencing allergic and pathogenic immune responses. It is also involved in the polarization of T helper responses. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription."[24]
  2. NP_001276929.1 nuclear factor interleukin-3-regulated protein: "Transcript Variant: This variant (2) differs in the 5' UTR compared to variant 1. All three variants encode the same protein."[23]
  3. NP_005375.2 nuclear factor interleukin-3-regulated protein: "Transcript Variant: This variant (3) differs in the 5' UTR compared to variant 1. All three variants encode the same protein."[23]

Gene ID: 4784 is NFIX nuclear factor I X aka CCAAT-box-binding transcription factor, TGGCA-binding protein, on 19p13.13: "The protein encoded by this gene is a transcription factor that binds the palindromic sequence 5'-TTGGCNNNNNGCCAA-3 in viral and cellular promoters. The encoded protein can also stimulate adenovirus replication in vitro. Three transcript variants encoding different isoforms have been found for this gene."[25]

  1. NP_001257972.1 nuclear factor 1 X-type isoform 1: "Transcript Variant: This variant (1) encodes the longest isoform (1)."[25]
  2. NP_001257973.1 nuclear factor 1 X-type isoform 3: "Transcript Variant: This variant (3) differs in the 5' UTR and coding sequence and lacks an alternate 3' exon compared to variant 1, that causes a frameshift. The resulting isoform (3) has shorter and distinct N- and C-termini compared to isoform 1."[25]
  3. NP_001352831.1 nuclear factor 1 X-type isoform 4 [variant 4].[25]
  4. NP_001352911.1 nuclear factor 1 X-type isoform 5 [variant 5].[25]
  5. NP_001352912.1 nuclear factor 1 X-type isoform 6 [variant 6].[25]
  6. NP_001352913.1 nuclear factor 1 X-type isoform 7 [variant 7].[25]
  7. NP_001352914.1 nuclear factor 1 X-type isoform 8 [variant 8].[25]
  8. NP_001365333.1 nuclear factor 1 X-type isoform 9 [variant 9].[25]
  9. NP_001365334.1 nuclear factor 1 X-type isoform 10 [variant 10].[25]
  10. NP_002492.2 nuclear factor 1 X-type isoform 2: "Transcript Variant: This variant (2) differs in the 5' UTR and coding sequence and lacks an alternate 3' exon compared to variant 1, that causes a frameshift. The resulting isoform (2) has shorter and distinct N- and C-termini compared to isoform 1."[25]

Gene ID: 4790 is NFKB1 nuclear factor kappa B subunit 1 on 4q24: "This gene encodes a 105 kD protein which can undergo cotranslational processing by the 26S proteasome to produce a 50 kD protein. The 105 kD protein is a Rel protein-specific transcription inhibitor and the 50 kD protein is a DNA binding subunit of the NF-kappa-B (NFKB) protein complex. NFKB is a transcription regulator that is activated by various intra- and extra-cellular stimuli such as cytokines, oxidant-free radicals, ultraviolet irradiation, and bacterial or viral products. Activated NFKB translocates into the nucleus and stimulates the expression of genes involved in a wide variety of biological functions. Inappropriate activation of NFKB has been associated with a number of inflammatory diseases while persistent inhibition of NFKB leads to inappropriate immune cell development or delayed cell growth. Alternative splicing results in multiple transcript variants encoding different isoforms, at least one of which is proteolytically processed."[26]

  1. NP_001158884.1 nuclear factor NF-kappa-B p105 subunit isoform 2 proprotein: "Transcript Variant: This variant (2) uses an alternate in-frame splice site in the 5' coding region compared to variant 1. The resulting isoform (2) has the same N- and C-termini but is 1 amino acid shorter than isoform 1. Variants 2 and 3 encode the same isoform (2)."[26]
  2. NP_001306155.1 nuclear factor NF-kappa-B p105 subunit isoform 2 proprotein: "Transcript Variant: This variant (3) differs in its 5' UTR and uses an alternate in-frame splice site in the 5' coding region compared to variant 1. The resulting isoform (2) has the same N- and C-termini but is 1 amino acid shorter than isoform 1. Variants 2 and 3 encode the same isoform (2)."[26]
  3. NP_003989.2 nuclear factor NF-kappa-B p105 subunit isoform 1: "Transcript Variant: This variant (1) represents the longest transcript and encodes the longer isoform (1). This isoform (1) may undergo proteolytic processing similar to that of isoform 2."[26]

Gene ID: 4791 is NFKB2 nuclear factor kappa B subunit 2 on 10q24.32: "This gene encodes a subunit of the transcription factor complex nuclear factor-kappa-B (NFkB). The NFkB complex is expressed in numerous cell types and functions as a central activator of genes involved in inflammation and immune function. The protein encoded by this gene can function as both a transcriptional activator or repressor depending on its dimerization partner. The p100 full-length protein is co-translationally processed into a p52 active form. Chromosomal rearrangements and translocations of this locus have been observed in B cell lymphomas, some of which may result in the formation of fusion proteins. There is a pseudogene for this gene on chromosome 18. Alternative splicing results in multiple transcript variants."[27]

  1. NP_001070962.1 nuclear factor NF-kappa-B p100 subunit isoform a: "Transcript Variant: This variant (1) encodes the longest isoform (a). Variants 1 and 5 both encode the same isoform (a)."[27]
  2. NP_001248332.1 nuclear factor NF-kappa-B p100 subunit isoform b: "Transcript Variant: This variant (4) differs in the 5' UTR and uses an alternate in-frame splice site in the 3' coding region, compared to variant 1. The encoded isoform (b) is shorter than isoform a. Variants 2, 3, and 4 encode the same isoform (b)."[27]
  3. NP_001275653.1 nuclear factor NF-kappa-B p100 subunit isoform b: "Transcript Variant: This variant (3) differs in the 5' UTR and uses an alternate in-frame splice site in the 3' coding region, compared to variant 1. The encoded isoform (b) is shorter than isoform a. Variants 2, 3, and 4 encode the same isoform (b)."[27]
  4. NP_001309863.1 nuclear factor NF-kappa-B p100 subunit isoform a: "Transcript Variant: This variant (5) and variant 1 both encode the same isoform (a)."[27]
  5. NP_001309864.1 nuclear factor NF-kappa-B p100 subunit isoform c [variant 6].[27]
  6. NP_002493.3 nuclear factor NF-kappa-B p100 subunit isoform b: "Transcript Variant: This variant (2) differs in the 5' UTR and uses an alternate in-frame splice site in the 3' coding region, compared to variant 1. The encoded isoform (b) is shorter than isoform a. Variants 2, 3, and 4 encode the same isoform (b)."[27]

Gene ID: 4792 is NFKBIA NFKB inhibitor alpha aka major histocompatibility complex enhancer-binding protein [mitotic arrest deficient 3] MAD3 on 14q13.2: "This gene encodes a member of the NF-kappa-B inhibitor family, which contain multiple ankrin repeat domains. The encoded protein interacts with REL dimers to inhibit NF-kappa-B/REL complexes which are involved in inflammatory responses. The encoded protein moves between the cytoplasm and the nucleus via a nuclear localization signal and CRM1-mediated nuclear export. Mutations in this gene have been found in ectodermal dysplasia anhidrotic with T-cell immunodeficiency autosomal dominant disease."[28]

Gene ID: 5970 is RELA RELA proto-oncogene, NF-kB subunit, aka NFKB3 on 11q13.1: "NF-kappa-B is a ubiquitous transcription factor involved in several biological processes. It is held in the cytoplasm in an inactive state by specific inhibitors. Upon degradation of the inhibitor, NF-kappa-B moves to the nucleus and activates transcription of specific genes. NF-kappa-B is composed of NFKB1 or NFKB2 bound to either REL, RELA, or RELB. The most abundant form of NF-kappa-B is NFKB1 complexed with the product of this gene, RELA. Four transcript variants encoding different isoforms have been found for this gene."[29]

  1. NP_001138610.1 transcription factor p65 isoform 2: "Transcript Variant: This variant (2) uses an alternate in-frame acceptor splice site at one of the coding exons compared to transcript variant 1. This results in a shorter isoform (2) missing a 3 aa segment compared to isoform 1."[29]
  2. NP_001230913.1 transcription factor p65 isoform 3: "Transcript Variant: This variant (3) uses an alternate in-frame splice site at the 5' end of the last exon compared to variant 1. The resulting isoform (3) lacks an alternate internal segment compared to isoform 1."[29]
  3. NP_001230914.1 transcription factor p65 isoform 4: "Transcript Variant: This variant (4) lacks an alternate internal in-frame segment in the last exon compared to variant 1. The resulting isoform (4) lacks an alternate internal segment compared to isoform 1."[29]
  4. NP_068810.3 transcription factor p65 isoform 1: "Transcript Variant: This variant (1) represents the predominant transcript and encodes the longer isoform (1)."[29]

See also

References

  1. ↑ Gilmore TD (October 2006). "Introduction to NF-kappaB: players, pathways, perspectives". Oncogene. 25 (51): 6680–4. doi:10.1038/sj.onc.1209954. PMID 17072321.
  2. ↑ Brasier AR (2006). "The NF-kappaB regulatory network". Cardiovascular Toxicology. 6 (2): 111–30. doi:10.1385/CT:6:2:111. PMID 17303919.
  3. ↑ Perkins ND (January 2007). "Integrating cell-signalling pathways with NF-kappaB and IKK function". Nature Reviews Molecular Cell Biology. 8 (1): 49–62. doi:10.1038/nrm2083. PMID 17183360.
  4. ↑ Gilmore TD (November 1999). "The Rel/NF-kappaB signal transduction pathway: introduction". Oncogene. 18 (49): 6842–4. doi:10.1038/sj.onc.1203237. PMID 10602459.
  5. ↑ Tian B, Brasier AR (2003). "Identification of a nuclear factor kappa B-dependent gene network". Recent Progress in Hormone Research. 58: 95–130. doi:10.1210/rp.58.1.95. PMID 12795416.
  6. ↑ Albensi BC, Mattson MP (February 2000). "Evidence for the involvement of TNF and NF-kappaB in hippocampal synaptic plasticity". Synapse. 35 (2): 151–9. doi:10.1002/(SICI)1098-2396(200002)35:2<151::AID-SYN8>3.0.CO;2-P. PMID 10611641.
  7. ↑ Meffert MK, Chang JM, Wiltgen BJ, Fanselow MS, Baltimore D (October 2003). "NF-kappa B functions in synaptic signaling and behavior". Nature Neuroscience. 6 (10): 1072–8. doi:10.1038/nn1110. PMID 12947408.
  8. ↑ Levenson JM, Choi S, Lee SY, Cao YA, Ahn HJ, Worley KC, Pizzi M, Liou HC, Sweatt JD (April 2004). "A bioinformatics analysis of memory consolidation reveals involvement of the transcription factor c-rel". The Journal of Neuroscience. 24 (16): 3933–43. doi:10.1523/JNEUROSCI.5646-03.2004. PMID 15102909.
  9. ↑ Freudenthal R, Locatelli F, Hermitte G, Maldonado H, Lafourcade C, Delorenzi A, Romano A (February 1998). "Kappa-B like DNA-binding activity is enhanced after spaced training that induces long-term memory in the crab Chasmagnathus". Neuroscience Letters. 242 (3): 143–6. doi:10.1016/S0304-3940(98)00059-7. PMID 9530926.
  10. ↑ Merlo E, Freudenthal R, Romano A (2002). "The IkappaB kinase inhibitor sulfasalazine impairs long-term memory in the crab Chasmagnathus". Neuroscience. 112 (1): 161–72. doi:10.1016/S0306-4522(02)00049-0. PMID 12044481.
  11. ↑ Park HJ, Youn HS (March 2013). "Mercury induces the expression of cyclooxygenase-2 and inducible nitric oxide synthase". Toxicology and Industrial Health. 29 (2): 169–74. doi:10.1177/0748233711427048. PMID 22080037.
  12. ↑ 12.0 12.1 Patrick Cramer, Christopher J. Larson, Gregory L. Verdine and Christoph W. Müller (1 December 1997). "Structure of the human NF‐κB p52 homodimer‐DNA complex at 2.1 Å resolution". The EMBO Journal. 16 (23): 7078–90. doi:10.1093/emboj/16.23.7078. Retrieved 3 May 2020.
  13. ↑ Cissi Gardmo and Agneta Mode (1 December 2006). "In vivo transfection of rat liver discloses binding sites conveying GH-dependent and female-specific gene expression". Journal of Molecular Endocrinology. 37 (3\): 433–441. doi:10.1677/jme.1.02116. Retrieved 2017-09-01.
  14. ↑ Vinson CR, Sigler PB, McKnight SL (November 1989). "Scissors-grip model for DNA recognition by a family of leucine zipper proteins". Science. 246 (4932): 911–6. Bibcode:1989Sci...246..911V. doi:10.1126/science.2683088. PMID 2683088.
  15. ↑ 15.0 15.1 E ZG, Zhang YP, Zhou JH, Wang L (April 2014). "Mini review roles of the bZIP gene family in rice". Genetics and Molecular Research. 13 (2): 3025–36. doi:10.4238/2014.April.16.11. PMID 24782137.
  16. ↑ Hakoshima, T. (2005). "Leucine Zippers". Encyclopedia of Life Sciences. doi:10.1038/npg.els.0005049. ISBN 0470016175.
  17. ↑ Landschulz WH, Johnson PF, McKnight SL (June 1988). "The leucine zipper: a hypothetical structure common to a new class of DNA binding proteins". Science. 240 (4860): 1759–64. Bibcode:1988Sci...240.1759L. doi:10.1126/science.3289117. PMID 3289117.
  18. ↑ Nijhawan A, Jain M, Tyagi AK, Khurana JP (February 2008). "Genomic survey and gene expression analysis of the basic leucine zipper transcription factor family in rice". Plant Physiology. 146 (2): 333–50. doi:10.1104/pp.107.112821. PMC 2245831. PMID 18065552.
  19. ↑ Reinke AW, Baek J, Ashenberg O, Keating AE (May 2013). "Networks of bZIP protein-protein interactions diversified over a billion years of evolution". Science. 340 (6133): 730–4. Bibcode:2013Sci...340..730R. doi:10.1126/science.1233465. PMC 4115154. PMID 23661758.
  20. ↑ 20.0 20.1 Rodríguez-Martínez JA, Reinke AW, Bhimsaria D, Keating AE, Ansari AZ (February 2017). "Combinatorial bZIP dimers display complex DNA-binding specificity landscapes". eLife. 6: e19272. doi:10.7554/eLife.19272. PMC 5349851. PMID 28186491.
  21. ↑ 21.0 21.1 Shimizu H, Sato K, Berberich T, Miyazaki A, Ozaki R, Imai R, Kusano T (October 2005). "LIP19, a basic region leucine zipper protein, is a Fos-like molecular switch in the cold signaling of rice plants". Plant & Cell Physiology. 46 (10): 1623–34. doi:10.1093/pcp/pci178. PMID 16051676.
  22. ↑ Nantel A, Quatrano RS (December 1996). "Characterization of three rice basic/leucine zipper factors, including two inhibitors of EmBP-1 DNA binding activity". The Journal of Biological Chemistry. 271 (49): 31296–305. doi:10.1074/jbc.271.49.31296. PMID 8940135.
  23. ↑ 23.0 23.1 23.2 23.3 RefSeq (February 2014). "NFIL3 nuclear factor, interleukin 3 regulated [ Homo sapiens (human) ]". 8600 Rockville Pike, Bethesda MD, 20894 USA: National Center for Biotechnology Information, U.S. National Library of Medicine. Retrieved 3 May 2020.
  24. ↑ cd14694 (2 March 2014). "Conserved Protein Domain Family bZIP_NFIL3". 8600 Rockville Pike, Bethesda MD, 20894 USA: National Center for Biotechnology Information, U.S. National Library of Medicine. Retrieved 3 May 2020.
  25. ↑ 25.00 25.01 25.02 25.03 25.04 25.05 25.06 25.07 25.08 25.09 25.10 RefSeq (August 2012). "NFIX nuclear factor I X [ Homo sapiens (human) ]". 8600 Rockville Pike, Bethesda MD, 20894 USA: National Center for Biotechnology Information, U.S. National Library of Medicine. Retrieved 3 May 2020.
  26. ↑ 26.0 26.1 26.2 26.3 RefSeq (February 2016). "NFKB1 nuclear factor kappa B subunit 1 [ Homo sapiens (human) ]". 8600 Rockville Pike, Bethesda MD, 20894 USA: National Center for Biotechnology Information, U.S. National Library of Medicine. Retrieved 3 May 2020.
  27. ↑ 27.0 27.1 27.2 27.3 27.4 27.5 27.6 RefSeq (December 2013). "NFKB2 nuclear factor kappa B subunit 2 [ Homo sapiens (human) ]". 8600 Rockville Pike, Bethesda MD, 20894 USA: National Center for Biotechnology Information, U.S. National Library of Medicine. Retrieved 3 May 2020.
  28. ↑ RefSeq (August 2011). "NFKBIA NFKB inhibitor alpha [ Homo sapiens (human) ]". 8600 Rockville Pike, Bethesda MD, 20894 USA: National Center for Biotechnology Information, U.S. National Library of Medicine. Retrieved 28 March 2020.
  29. ↑ 29.0 29.1 29.2 29.3 29.4 RefSeq (September 2011). "RELA RELA proto-oncogene, NF-kB subunit [ Homo sapiens (human) ]". 8600 Rockville Pike, Bethesda MD, 20894 USA: National Center for Biotechnology Information, U.S. National Library of Medicine. Retrieved 3 May 2020.

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