REL

Protein-coding gene in the species Homo sapiens
REL
Identifiers
AliasesREL, C-Rel, REL proto-oncogene, NF-kB subunit, HIVEN86A, IMD92
External IDsOMIM: 164910 MGI: 97897 HomoloGene: 2182 GeneCards: REL
Gene location (Human)
Chromosome 2 (human)
Chr.Chromosome 2 (human)[1]
Chromosome 2 (human)
Genomic location for REL
Genomic location for REL
Band2p16.1Start60,881,521 bp[1]
End60,931,612 bp[1]
Gene location (Mouse)
Chromosome 11 (mouse)
Chr.Chromosome 11 (mouse)[2]
Chromosome 11 (mouse)
Genomic location for REL
Genomic location for REL
Band11 A3.2|11 14.36 cMStart23,686,847 bp[2]
End23,720,970 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • bone marrow

  • secondary oocyte

  • bone marrow cells

  • monocyte

  • mucosa of urinary bladder

  • human penis

  • superficial temporal artery

  • appendix

  • nipple

  • lower lobe of lung
Top expressed in
  • blood

  • spleen

  • conjunctival fornix

  • bone marrow

  • secondary oocyte

  • cumulus cell

  • epidermis

  • subcutaneous adipose tissue

  • cornea

  • hair follicle
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • RNA polymerase II cis-regulatory region sequence-specific DNA binding
  • DNA binding
  • sequence-specific DNA binding
  • chromatin binding
  • DNA-binding transcription activator activity, RNA polymerase II-specific
  • protein binding
  • DNA-binding transcription factor activity
  • DNA-binding transcription factor activity, RNA polymerase II-specific
  • RNA polymerase II transcription regulatory region sequence-specific DNA binding
Cellular component
  • cytoplasm
  • cytosol
  • I-kappaB/NF-kappaB complex
  • transcription regulator complex
  • nucleoplasm
  • nucleus
Biological process
  • response to cytokine
  • regulation of transcription, DNA-templated
  • negative regulation of transcription by RNA polymerase II
  • negative regulation of interferon-beta production
  • negative regulation of gene expression
  • transcription, DNA-templated
  • positive regulation of transcription, DNA-templated
  • NIK/NF-kappaB signaling
  • positive regulation of I-kappaB kinase/NF-kappaB signaling
  • innate immune response
  • inflammatory response
  • positive regulation of transcription by RNA polymerase II
  • negative regulation of neuron death
  • I-kappaB kinase/NF-kappaB signaling
  • transcription by RNA polymerase II
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

5966

19696

Ensembl

ENSG00000162924

ENSMUSG00000020275

UniProt

Q04864

P15307

RefSeq (mRNA)

NM_001291746
NM_002908

NM_009044

RefSeq (protein)

NP_001278675
NP_002899

NP_033070

Location (UCSC)Chr 2: 60.88 – 60.93 MbChr 11: 23.69 – 23.72 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

The proto-oncogene c-Rel is a protein that in humans is encoded by the REL gene.[5] The c-Rel protein is a member of the NF-κB family of transcription factors and contains a Rel homology domain (RHD) at its N-terminus and two C-terminal transactivation domains. c-Rel is a myeloid checkpoint protein that can be targeted for treating cancer.[6] c-Rel has an important role in B-cell survival and proliferation. The REL gene is amplified or mutated in several human B-cell lymphomas, including diffuse large B-cell lymphoma and Hodgkin's lymphoma.[7]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000162924 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000020275 – 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. ^ Ruben SM, Klement JF, Coleman TA, Maher M, Chen CH, Rosen CA (Jun 1992). "I-Rel: a novel rel-related protein that inhibits NF-kappa B transcriptional activity". Genes Dev. 6 (5): 745–60. doi:10.1101/gad.6.5.745. PMID 1577270.
  6. ^ Li T, Li X, Chen YH (May 2020). "c-Rel is a myeloid checkpoint for cancer immunotherapy". Nature Cancer. 1 (5): 507–517. doi:10.1038/s43018-020-0061-3. PMC 7808269. PMID 33458695.
  7. ^ Gilmore TD, Kalaitzidis D, Liang MC, Starczynowski DT (March 2004). "The c-Rel transcription factor and B-cell proliferation: a deal with the devil". Oncogene. 23 (13): 2275–86. doi:10.1038/sj.onc.1207410. PMID 14755244.

Further reading

  • Rayet B, Gélinas C (2000). "Aberrant rel/nfkb genes and activity in human cancer". Oncogene. 18 (49): 6938–47. doi:10.1038/sj.onc.1203221. PMID 10602468.
  • Kunsch C, Ruben SM, Rosen CA (1992). "Selection of optimal kappa B/Rel DNA-binding motifs: interaction of both subunits of NF-kappa B with DNA is required for transcriptional activation". Mol. Cell. Biol. 12 (10): 4412–21. doi:10.1128/mcb.12.10.4412. PMC 360365. PMID 1406630.
  • Neumann M, Tsapos K, Scheppler JA, et al. (1992). "Identification of complex formation between two intracellular tyrosine kinase substrates: human c-Rel and the p105 precursor of p50 NF-kappa B.". Oncogene. 7 (11): 2095–104. PMID 1437141.
  • Kochel T, Rice NR (1992). "v-rel- and c-rel-protein complexes bind to the NF-kappa B site in vitro". Oncogene. 7 (3): 567–72. PMID 1549370.
  • Kumar S, Rabson AB, Gélinas C (1992). "The RxxRxRxxC motif conserved in all Rel/kappa B proteins is essential for the DNA-binding activity and redox regulation of the v-Rel oncoprotein". Mol. Cell. Biol. 12 (7): 3094–106. doi:10.1128/mcb.12.7.3094. PMC 364524. PMID 1620118.
  • Lu D, Thompson JD, Gorski GK, et al. (1991). "Alterations at the rel locus in human lymphoma". Oncogene. 6 (7): 1235–41. PMID 1650444.
  • Muchardt C, Seeler JS, Nirula A, et al. (1992). "Regulation of human immunodeficiency virus enhancer function by PRDII-BF1 and c-rel gene products". J. Virol. 66 (1): 244–50. doi:10.1128/JVI.66.1.244-250.1992. PMC 238281. PMID 1727488.
  • Hansen SK, Nerlov C, Zabel U, et al. (1992). "A novel complex between the p65 subunit of NF-kappa B and c-Rel binds to a DNA element involved in the phorbol ester induction of the human urokinase gene". EMBO J. 11 (1): 205–13. doi:10.1002/j.1460-2075.1992.tb05043.x. PMC 556441. PMID 1740106.
  • Davis N, Ghosh S, Simmons DL, et al. (1991). "Rel-associated pp40: an inhibitor of the rel family of transcription factors". Science. 253 (5025): 1268–71. Bibcode:1991Sci...253.1268D. doi:10.1126/science.1891714. PMID 1891714.
  • Lim MY, Davis N, Zhang JY, Bose HR (1990). "The v-rel oncogene product is complexed with cellular proteins including its proto-oncogene product and heat shock protein 70". Virology. 175 (1): 149–60. doi:10.1016/0042-6822(90)90195-W. PMID 2155506.
  • Brownell E, Mittereder N, Rice NR (1989). "A human rel proto-oncogene cDNA containing an Alu fragment as a potential coding exon". Oncogene. 4 (7): 935–42. PMID 2666912.
  • Brownell E, O'Brien SJ, Nash WG, Rice N (1986). "Genetic characterization of human c-rel sequences". Mol. Cell. Biol. 5 (10): 2826–31. doi:10.1128/mcb.5.10.2826. PMC 367021. PMID 3016517.
  • Brownell E, Kozak CA, Fowle JR, et al. (1986). "Comparative genetic mapping of cellular rel sequences in man, mouse, and the domestic cat". Am. J. Hum. Genet. 39 (2): 194–202. PMC 1683919. PMID 3529946.
  • John S, Reeves RB, Lin JX, et al. (1995). "Regulation of cell-type-specific interleukin-2 receptor alpha-chain gene expression: potential role of physical interactions between Elf-1, HMG-I(Y), and NF-kappa B family proteins". Mol. Cell. Biol. 15 (3): 1786–96. doi:10.1128/mcb.15.3.1786. PMC 230403. PMID 7862168.
  • Xu X, Gélinas C (1995). "The v-Rel oncoprotein complexes with new Rel- and RelA-related proteins in transformed cells". Virology. 207 (2): 362–8. doi:10.1006/viro.1995.1095. PMID 7886940.
  • Mackman N (1994). "Protease inhibitors block lipopolysaccharide induction of tissue factor gene expression in human monocytic cells by preventing activation of c-Rel/p65 heterodimers". J. Biol. Chem. 269 (42): 26363–7. doi:10.1016/S0021-9258(18)47202-X. PMID 7929355.
  • Sif S, Gilmore TD (1994). "Interaction of the v-Rel oncoprotein with cellular transcription factor Sp1". J. Virol. 68 (11): 7131–8. doi:10.1128/JVI.68.11.7131-7138.1994. PMC 237152. PMID 7933095.
  • 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.
  • Beg AA, Baldwin AS (1994). "Activation of multiple NF-kappa B/Rel DNA-binding complexes by tumor necrosis factor". Oncogene. 9 (5): 1487–92. PMID 8152812.

External links

  • v
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  • e
(1) Basic domains
(1.1) Basic leucine zipper (bZIP)
(1.2) Basic helix-loop-helix (bHLH)
Group A
Group B
Group C
bHLH-PAS
Group D
Group E
Group F
bHLH-COE
(1.3) bHLH-ZIP
(1.4) NF-1
(1.5) RF-X
(1.6) Basic helix-span-helix (bHSH)
(2) Zinc finger DNA-binding domains
(2.1) Nuclear receptor (Cys4)
subfamily 1
subfamily 2
subfamily 3
subfamily 4
subfamily 5
subfamily 6
subfamily 0
(2.2) Other Cys4
(2.3) Cys2His2
(2.4) Cys6
(2.5) Alternating composition
(2.6) WRKY
(3) Helix-turn-helix domains
(3.1) Homeodomain
Antennapedia
ANTP class
protoHOX
Hox-like
metaHOX
NK-like
other
(3.2) Paired box
(3.3) Fork head / winged helix
(3.4) Heat shock factors
(3.5) Tryptophan clusters
(3.6) TEA domain
  • transcriptional enhancer factor
(4) β-Scaffold factors with minor groove contacts
(4.1) Rel homology region
(4.2) STAT
(4.3) p53-like
(4.4) MADS box
(4.6) TATA-binding proteins
(4.7) High-mobility group
(4.9) Grainyhead
(4.10) Cold-shock domain
(4.11) Runt
(0) Other transcription factors
(0.2) HMGI(Y)
(0.3) Pocket domain
(0.5) AP-2/EREBP-related factors
(0.6) Miscellaneous
see also transcription factor/coregulator deficiencies


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