The NFkB activation domain is 14-amino-acid-long variant of the 9aaTAD
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14110%2F23%3A00130376" target="_blank" >RIV/00216224:14110/23:00130376 - isvavai.cz</a>
Result on the web
<a href="https://portlandpress.com/biochemj/article/doi/10.1042/BCJ20220605/232597/The-NFkB-activation-domain-is-14-amino-acid-long" target="_blank" >https://portlandpress.com/biochemj/article/doi/10.1042/BCJ20220605/232597/The-NFkB-activation-domain-is-14-amino-acid-long</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1042/BCJ20220605" target="_blank" >10.1042/BCJ20220605</a>
Alternative languages
Result language
angličtina
Original language name
The NFkB activation domain is 14-amino-acid-long variant of the 9aaTAD
Original language description
The nine-amino-acid TransActivation Domains (9aaTAD) was identified in numerous transcription factors including Gal4, p53, E2A, MLL, c-Myc, N-Myc, and also in SP, KLF and SOX families. Most of the 9aaTAD domains interact with the KIX domain of transcription mediators MED15 and CBP to activate transcription. The NFkB activation domain occupied the same position on the KIX domain as the 9aaTADs of MLL, E2A and p53. Binding of the KIX domain is established by the two-point interaction involving 9aaTAD positions p3-4 and p6-7. The NFkB primary binding region (position p3-4) is almost identical to MLL and E2A, but secondary NFkB binding region differs by the position and engages the distal NFkB region p10-11. Thus, the NFkB activation domain is 5 amino acids longer than the other 9aaTADs. The NFkB activation domain includes an additional region, which we called the Omichinski Insert extending activation domain length to 14 amino acids. By deletion, we demonstrated that Omichinski Insert is an entirely non-essential part of NFkB activation domain. In summary, we recognized the NFkB activation domain as prolonged 9aaTAD conserved in evolution from humans to amphibians.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
30102 - Immunology
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2023
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
The Biochemical journal
ISSN
0264-6021
e-ISSN
1470-8728
Volume of the periodical
480
Issue of the periodical within the volume
5
Country of publishing house
GB - UNITED KINGDOM
Number of pages
10
Pages from-to
297-306
UT code for WoS article
000950074500001
EID of the result in the Scopus database
2-s2.0-85150001300