SFPQ: Regulation of Gene Expression During Splicing and Alternative Splitting

Target Name: SFPQ

NCBI ID: G6421

SFPQ

SFPQ: Regulation of Gene Expression During Splicing and Alternative Splitting

SFPQ (Polypyrimidine tract-binding protein-associated-splicing factor) is a protein that is expressed in various tissues and cells throughout the body. It is a non-coding RNA molecule that plays a critical role in the regulation of gene expression during the splicing process. SFPQ is associated with the poly(A)/poly(T) exon in RNA splicing and is known as the splicing factor-1 (SF1).

SFPQ is a member of the SFP/ASF family of proteins, which are known for their ability to interact with splicing factors and enhance the efficiency of splicing. SFPQ has been shown to interact with several splicing factors, including SFP2, SFP3, and SFP4. These interactions can enhance the formation of higher-order RNA structures, such as exons and introns, which can increase the efficiency of splicing and result in the production of more accurate transcripts.

SFPQ is also known as PAP-1 (poly(A)/poly(T) exon-binding protein 1). PAP-1 is a protein that is expressed in various tissues and cells throughout the body, including the brain, heart, and tests. It is a 21-kDa protein that is composed of two distinct domains: an N-terminal transmembrane domain and a C-terminal non-membrane domain. The N-terminal domain is responsible for the protein's cytoplasmic localization, while the C- terminal domain is involved in the protein's interactions with other cellular components.

SFPQ has been shown to play a critical role in the regulation of gene expression during splicing. It has been shown to interact with splicing factors and enhance the formation of higher-order RNA structures, which can increase the efficiency of splicing and result in the production of more accurate transcripts.

SFPQ is also involved in the regulation of alternative splicing (AS) events, which are a type of splicing that occurs when an exon is not included in the final RNA product. AS events can result in the production of different RNA species with different protein sequences . SFPQ has been shown to interact with the ASF2 protein, which is a known AS-specific splicing factor. This interaction may play a role in the regulation of AS events.

SFPQ is also involved in the regulation of gene expression during translation, which is the process by which RNA molecules are translated into proteins. SFPQ has been shown to interact with the protein translation factor eIF4F, which is involved in the regulation of protein translation. This interaction may play a role in the regulation of gene expression during translation.

SFPQ has also been shown to play a role in the regulation of cell apoptosis, which is the process by which cells die or are terminated. SFPQ has also been shown to interact with the protein Bcl-2, which is involved in the regulation of cell apoptosis. . This interaction may play a role in the regulation of cell apoptosis.

SFPQ is also involved in the regulation of stem cell proliferation and self-renewal. SFPQ has been shown to interact with the protein p53, which is involved in the regulation of stem cell proliferation and self-renewal. This interaction may play a role in the regulation of stem cell proliferation and self-renewal.

SFPQ has also been shown to play a role in the regulation of tissue repair and regeneration. SFPQ has been shown to interact with the protein transforming growth factor-beta (TGF-beta), which is involved in the regulation of tissue repair and regeneration. This interaction may play a role in the regulation of tissue repair and regeneration.

SFPQ is also involved in the regulation of the immune response. SFPQ has been shown to interact with the protein

Protein Name: Splicing Factor Proline And Glutamine Rich

Functions: DNA- and RNA binding protein, involved in several nuclear processes. Essential pre-mRNA splicing factor required early in spliceosome formation and for splicing catalytic step II, probably as a heteromer with NONO. Binds to pre-mRNA in spliceosome C complex, and specifically binds to intronic polypyrimidine tracts. Involved in regulation of signal-induced alternative splicing. During splicing of PTPRC/CD45, a phosphorylated form is sequestered by THRAP3 from the pre-mRNA in resting T-cells; T-cell activation and subsequent reduced phosphorylation is proposed to lead to release from THRAP3 allowing binding to pre-mRNA splicing regulatotry elements which represses exon inclusion. Interacts with U5 snRNA, probably by binding to a purine-rich sequence located on the 3' side of U5 snRNA stem 1b. May be involved in a pre-mRNA coupled splicing and polyadenylation process as component of a snRNP-free complex with SNRPA/U1A. The SFPQ-NONO heteromer associated with MATR3 may play a role in nuclear retention of defective RNAs. SFPQ may be involved in homologous DNA pairing; in vitro, promotes the invasion of ssDNA between a duplex DNA and produces a D-loop formation. The SFPQ-NONO heteromer may be involved in DNA unwinding by modulating the function of topoisomerase I/TOP1; in vitro, stimulates dissociation of TOP1 from DNA after cleavage and enhances its jumping between separate DNA helices. The SFPQ-NONO heteromer binds DNA (PubMed:25765647). The SFPQ-NONO heteromer may be involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination and may stabilize paired DNA ends; in vitro, the complex strongly stimulates DNA end joining, binds directly to the DNA substrates and cooperates with the Ku70/G22P1-Ku80/XRCC5 (Ku) dimer to establish a functional preligation complex. SFPQ is involved in transcriptional regulation. Functions as transcriptional activator (PubMed:25765647). Transcriptional repression is mediated by an interaction of SFPQ with SIN3A and subsequent recruitment of histone deacetylases (HDACs). The SFPQ-NONO-NR5A1 complex binds to the CYP17 promoter and regulates basal and cAMP-dependent transcriptional activity. SFPQ isoform Long binds to the DNA binding domains (DBD) of nuclear hormone receptors, like RXRA and probably THRA, and acts as transcriptional corepressor in absence of hormone ligands. Binds the DNA sequence 5'-CTGAGTC-3' in the insulin-like growth factor response element (IGFRE) and inhibits IGF-I-stimulated transcriptional activity. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-BMAL1 heterodimer. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex through histone deacetylation (By similarity). Required for the assembly of nuclear speckles (PubMed:25765647). Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway (PubMed:28712728)

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