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GeneQ18031107· pop 5· linked from 812 articles

Also known as regulatory factor X2

DNA-binding protein RFX2 is a protein that in humans is encoded by the RFX2 gene.

Gene data

RFX2
Name
regulatory factor X2
Type
protein-coding
Position
5,993,164–6,199,572 (−)
RefSeq RNA
NM_000635.4, NM_134433.3, XM_017027107.2, XM_047439196.1, XM_047439197.1
RefSeq protein
NP_000626.2, NP_602309.1, XP_016882596.1, XP_047295152.1, XP_047295153.1

This gene is a member of the regulatory factor X gene family, which encodes transcription factors that contain a highly-conserved winged helix DNA binding domain. The protein encoded by this gene is structurally related to regulatory factors X1, X3, X4, and X5. It is a transcriptional activator that can bind DNA as a monomer or as a heterodimer with other RFX family members. This protein can bind to cis elements in the promoter of the IL-5 receptor alpha gene. Two transcript variants encoding different isoforms have been described for this gene, and both variants utilize alternative polyadenylation sites. [provided by RefSeq, Jul 2008].

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Gene · Ensembl

regulatory factor X2

Symbol
RFX2
Biotype
Protein coding
Organism
Homo sapiens
Location
19:5,993,164-6,199,572
Strand
Reverse (−)
Assembly
GRCh38
View on Ensembl →

via Ensembl · EMBL-EBI

Wikidata facts

Show 5 more facts
HomoloGene ID
30980
genomic end
6199583
genomic start
5993175
cytogenetic location
19p13.3
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DNA-binding protein RFX2 is a protein that in humans is encoded by the RFX2 gene.

This gene is a member of the regulatory factor X gene family, which encodes transcription factors that contain a highly-conserved winged helix DNA binding domain. The protein encoded by this gene is structurally related to regulatory factors X1, X3, X4, and X5. It is a transcriptional activator that can bind DNA as a monomer or as a heterodimer with other RFX family members. This protein can bind to cis elements in the promoter of the IL-5 receptor alpha gene. Two transcript variants encoding different isoforms have been described for this gene, and both variants utilize alternative polyadenylation sites.

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