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RELA

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For other uses, see RELA Corps.
V-rel reticuloendotheliosis viral oncogene homolog A (avian)

PDB rendering based on 1bft.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols RELA; NFKB3; p65
External IDs OMIM: 164014 MGI: 103290 HomoloGene: 32064 ChEMBL: 5533 GeneCards: RELA Gene
RNA expression pattern
PBB GE RELA 201783 s at tn.png
PBB GE RELA 209878 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 5970 19697
Ensembl ENSG00000173039 ENSMUSG00000024927
UniProt Q04206 Q04207
RefSeq (mRNA) NM_001145138 NM_009045
RefSeq (protein) NP_001138610 NP_033071
Location (UCSC) Chr 11:
65.42 – 65.43 Mb		 Chr 19:
5.64 – 5.65 Mb
PubMed search [1] [2]
This box:

Transcription factor p65 is a protein that in humans is encoded by the RELA gene.[1]

Contents

[edit] Function

NFKB1 (MIM 164011) or NFKB2 is bound to REL , RELA (this gene), or RELB to form the NF-κB complex. The p50 (NFKB1)/p65 (RELA) heterodimer is the most abundant form of NF-κB. The NF-κB complex is inhibited by IκB (NFKBIA, or NFKBIB), which inactivates NF-κB 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-κB 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).[2]

[edit] Interactions

RELA has been shown to interact with:


[edit] References

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  34. ^ Gu Y, Xu You Cheng, Wu Ru Feng, Nwariaku Fiemu E, Souza Rhonda F, Flores Sonia C, Terada Lance S (May 2003). "p47phox participates in activation of RelA in endothelial cells". J. Biol. Chem. 278 (19): 17210–7. doi:10.1074/jbc.M210314200. PMID 12618429. 
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  43. ^ Caldenhoven E, Liden J, Wissink S, Van de Stolpe A, Raaijmakers J, Koenderman L, Okret S, Gustafsson J A, Van der Saag P T (April 1995). "Negative cross-talk between RelA and the glucocorticoid receptor: a possible mechanism for the antiinflammatory action of glucocorticoids". Mol. Endocrinol. 9 (4): 401–12. doi:10.1210/me.9.4.401. PMID 7659084. 
  44. ^ Espinosa Lí, Inglés-Esteve Julia, Robert-Moreno Alex, Bigas Anna (February 2003). "IkappaBalpha and p65 regulate the cytoplasmic shuttling of nuclear corepressors: cross-talk between Notch and NFkappaB pathways". Mol. Biol. Cell 14 (2): 491–502. doi:10.1091/mbc.E02-07-0404. PMC 149987. PMID 12589049. 
  45. ^ Lee SK, Kim J H, Lee Y C, Cheong J, Lee J W (April 2000). "Silencing mediator of retinoic acid and thyroid hormone receptors, as a novel transcriptional corepressor molecule of activating protein-1, nuclear factor-kappaB, and serum response factor". J. Biol. Chem. 275 (17): 12470–4. doi:10.1074/jbc.275.17.12470. PMID 10777532. 
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  47. ^ van Heel DA, Udalova Irina A, De Silva Arjuna P, McGovern Dermot P, Kinouchi Yoshitaka, Hull Jeremy, Lench Nicholas J, Cardon Lon R, Carey Alisoun H, Jewell Derek P, Kwiatkowski Dominic (May 2002). "Inflammatory bowel disease is associated with a TNF polymorphism that affects an interaction between the OCT1 and NF(-kappa)B transcription factors". Hum. Mol. Genet. 11 (11): 1281–9. doi:10.1093/hmg/11.11.1281. PMID 12019209. 
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  49. ^ Takada N, Sanda Takaomi, Okamoto Hiroshi, Yang Jian-Ping, Asamitsu Kaori, Sarol Lilen, Kimura Genjiro, Uranishi Hiroaki, Tetsuka Toshifumi, Okamoto Takashi (August 2002). "RelA-associated inhibitor blocks transcription of human immunodeficiency virus type 1 by inhibiting NF-kappaB and Sp1 actions". J. Virol. 76 (16): 8019–30. doi:10.1128/JVI.76.16.8019-8030.2002. PMC 155123. PMID 12134007. 
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  60. ^ Schmitz ML, Stelzer G, Altmann H, Meisterernst M, Baeuerle P A (March 1995). "Interaction of the COOH-terminal transactivation domain of p65 NF-kappa B with TATA-binding protein, transcription factor IIB, and coactivators". J. Biol. Chem. 270 (13): 7219–26. doi:10.1074/jbc.270.13.7219. PMID 7706261. 
  61. ^ Wu M, Xu Liang-Guo, Zhai Zhonghe, Shu Hong-Bing (July 2003). "SINK is a p65-interacting negative regulator of NF-kappaB-dependent transcription". J. Biol. Chem. 278 (29): 27072–9. doi:10.1074/jbc.M209814200. PMID 12736262. 

[edit] Further reading

  • Baldwin AS (1996). "The NF-kappa B and I kappa B proteins: new discoveries and insights.". Annu. Rev. Immunol. 14: 649–83. doi:10.1146/annurev.immunol.14.1.649. PMID 8717528. 
  • Bottex-Gauthier C, Pollet S, Favier A, Vidal DR (2002). "[The Rel/NF-kappa-B transcription factors: complex role in cell regulation]". Pathol. Biol. 50 (3): 204–11. PMID 11980335. 
  • Garg A, Aggarwal BB (2002). "Nuclear transcription factor-kappaB as a target for cancer drug development.". Leukemia 16 (6): 1053–68. doi:10.1038/sj.leu.2402482. PMID 12040437. 
  • Clarke R, Liu MC, Bouker KB, et al. (2003). "Antiestrogen resistance in breast cancer and the role of estrogen receptor signaling.". Oncogene 22 (47): 7316–39. doi:10.1038/sj.onc.1206937. PMID 14576841. 

[edit] External links

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