SFPQ

LOC654780
Identifiers
Aliases	POMP100PPP1R140PSFSFPQsplicing factor proline/glutamine-rich
External IDs	GeneCards:
Gene location (Human)
Chr.	Chromosome 16 (human)
End	84,197,053 bp
RNA expression pattern
	Top expressed in
	sperm; ; nipple; ; thymus; ; inferior ganglion of vagus nerve; ; renal medulla; ; pylorus; ; corpus callosum; ; cardia; ; superior surface of tongue; ; trachea;
	n/a
	More reference expression data
	; ; ; ;
	More reference expression data
Orthologs
	654780
	n/a
	ENSG00000250685
	n/a
	n ; a
	n/a
	NM_001039504
	n/a
	n/a
	n/a
	Wikidata
View/Edit Human

Last updated October 12, 2022

Splicing factor, proline- and glutamine-rich is a protein that in humans is encoded by the SFPQ gene.^[3]^[4]

Interactions

SFPQ has been shown to interact with PTBP1,^[3]^[5] NONO,^[6] CDC5L ^[7] and Ubiquitin C.^[8]

Related Research Articles

RNA splicing is a process in molecular biology where a newly-made precursor messenger RNA (pre-mRNA) transcript is transformed into a mature messenger RNA (mRNA). It works by removing all the introns and splicing back together exons. For nuclear-encoded genes, splicing occurs in the nucleus either during or immediately after transcription. For those eukaryotic genes that contain introns, splicing is usually needed to create an mRNA molecule that can be translated into protein. For many eukaryotic introns, splicing occurs in a series of reactions which are catalyzed by the spliceosome, a complex of small nuclear ribonucleoproteins (snRNPs). There exist self-splicing introns, that is, ribozymes that can catalyze their own excision from their parent RNA molecule. The process of transcription, splicing and translation is called gene expression, the central dogma of molecular biology.

Alternative splicing, or alternative RNA splicing, or differential splicing, is an alternative splicing process during gene expression that allows a single gene to code for multiple proteins. In this process, particular exons of a gene may be included within or excluded from the final, processed messenger RNA (mRNA) produced from that gene. This means the exons are joined in different combinations, leading to different (alternative) mRNA strands. Consequently, the proteins translated from alternatively spliced mRNAs will contain differences in their amino acid sequence and, often, in their biological functions.

A spliceosome is a large ribonucleoprotein (RNP) complex found primarily within the nucleus of eukaryotic cells. The spliceosome is assembled from small nuclear RNAs (snRNA) and numerous proteins. Small nuclear RNA (snRNA) molecules bind to specific proteins to form a small nuclear ribonucleoprotein complex, which in turn combines with other snRNPs to form a large ribonucleoprotein complex called a spliceosome. The spliceosome removes introns from a transcribed pre-mRNA, a type of primary transcript. This process is generally referred to as splicing. An analogy is a film editor, who selectively cuts out irrelevant or incorrect material from the initial film and sends the cleaned-up version to the director for the final cut.

Heterogeneous nuclear ribonucleoproteins (hnRNPs) are complexes of RNA and protein present in the cell nucleus during gene transcription and subsequent post-transcriptional modification of the newly synthesized RNA (pre-mRNA). The presence of the proteins bound to a pre-mRNA molecule serves as a signal that the pre-mRNA is not yet fully processed and therefore not ready for export to the cytoplasm. Since most mature RNA is exported from the nucleus relatively quickly, most RNA-binding protein in the nucleus exist as heterogeneous ribonucleoprotein particles. After splicing has occurred, the proteins remain bound to spliced introns and target them for degradation.

<span class="mw-page-title-main">Paraspeckle</span> Cell compartment found in the nucleuss interchromatin space

In cell biology, a paraspeckle is an irregularly shaped compartment of the cell, approximately 0.2-1 μm in size, found in the nucleus' interchromatin space. First documented in HeLa cells, where there are generally 10-30 per nucleus, Paraspeckles are now known to also exist in all human primary cells, transformed cell lines and tissue sections. Their name is derived from their distribution in the nucleus; the "para" is short for parallel and the "speckle" refers to the splicing speckles to which they are always in close proximity. Their function is still not fully understood, but they are thought to regulate gene expression by sequestrating proteins or mRNAs with inverted repeats in their 3′ UTRs.

Polypyrimidine tract-binding protein, also known as PTB or hnRNP I, is an RNA-binding protein. PTB functions mainly as a splicing regulator, although it is also involved in alternative 3' end processing, mRNA stability and RNA localization. Two 2020 studies have shown that depleting PTB mRNA in astrocytes can convert these astrocytes to functional neurons. These studies also show that such a treatment can be applied to the substantia nigra of mice models of Parkinson's disease in order to convert astrocytes to dopaminergic neurons and as a consequence restore motor function in these mice.

Splicing factor U2AF 65 kDa subunit is a protein that in humans is encoded by the U2AF2 gene.

Interleukin enhancer-binding factor 3 is a protein that in humans is encoded by the ILF3 gene.

Non-POU domain-containing octamer-binding protein (NonO) is a protein that in humans is encoded by the NONO gene.

The perinucleolar compartment (PNC) is a subnuclear body characterized by its location at the periphery of the nucleolus. The PNC participates in the patterned compartmentalization inside the nucleus to organize the specialized functions. It is almost exclusively found in oncogenic cells and enriched with RNA binding proteins as well as RNA polymerase III transcripts.

Transcription factor PU.1 is a protein that in humans is encoded by the SPI1 gene.

Splicing factor, arginine/serine-rich 3 is a protein that in humans is encoded by the SFRS3 gene.

U5 small nuclear ribonucleoprotein 200 kDa helicase is an enzyme that in humans is encoded by the SNRNP200 gene.

Heterogeneous nuclear ribonucleoprotein L is a protein that in humans is encoded by the HNRNPL gene.

Interleukin enhancer-binding factor 2 is a protein that in humans is encoded by the ILF2 gene.

Far upstream element-binding protein 2 is a protein that in humans is encoded by the KHSRP gene.

116 kDa U5 small nuclear ribonucleoprotein component is a protein that in humans is encoded by the EFTUD2 gene.

Splicing factor, arginine/serine-rich 12 is a protein that in humans is encoded by the SFRS12 gene.

Polypyrimidine tract-binding protein 1 is a protein that in humans is encoded by the PTBP1 gene.

Splicing factor proline and glutamine rich is a protein that in humans is encoded by the SFPQ gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000250685 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
1 2 Patton JG, Porro EB, Galceran J, Tempst P, Nadal-Ginard B (Mar 1993). "Cloning and characterization of PSF, a novel pre-mRNA splicing factor". Genes & Development. 7 (3): 393–406. doi: 10.1101/gad.7.3.393 . PMID 8449401.
↑ "Entrez Gene: SFPQ splicing factor proline/glutamine-rich (polypyrimidine tract binding protein associated)".
↑ Meissner M, Dechat T, Gerner C, Grimm R, Foisner R, Sauermann G (Jan 2000). "Differential nuclear localization and nuclear matrix association of the splicing factors PSF and PTB". Journal of Cellular Biochemistry. 76 (4): 559–66. doi:10.1002/(SICI)1097-4644(20000315)76:4<559::AID-JCB4>3.0.CO;2-U. PMID 10653975. S2CID 25669908.
↑ Peng R, Dye BT, Pérez I, Barnard DC, Thompson AB, Patton JG (Oct 2002). "PSF and p54nrb bind a conserved stem in U5 snRNA". RNA. 8 (10): 1334–47. doi:10.1017/S1355838202022070. PMC 1370341 . PMID 12403470.
↑ Ajuh P, Kuster B, Panov K, Zomerdijk JC, Mann M, Lamond AI (Dec 2000). "Functional analysis of the human CDC5L complex and identification of its components by mass spectrometry". The EMBO Journal. 19 (23): 6569–81. doi:10.1093/emboj/19.23.6569. PMC 305846 . PMID 11101529.
↑ Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (Sep 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. hdl: 11858/00-001M-0000-0010-8592-0 . PMID 16169070. S2CID 8235923.

Shav-Tal Y, Zipori D (Nov 2002). "PSF and p54(nrb)/NonO--multi-functional nuclear proteins". FEBS Letters. 531 (2): 109–14. doi: 10.1016/S0014-5793(02)03447-6 . PMID 12417296. S2CID 12485304.
Gower HJ, Moore SE, Dickson G, Elsom VL, Nayak R, Walsh FS (Apr 1989). "Cloning and characterization of a myoblast cell surface antigen defined by 24.1D5 monoclonal antibody". Development. 105 (4): 723–31. doi:10.1242/dev.105.4.723. PMID 2480877.
Gozani O, Patton JG, Reed R (Jul 1994). "A novel set of spliceosome-associated proteins and the essential splicing factor PSF bind stably to pre-mRNA prior to catalytic step II of the splicing reaction". The EMBO Journal. 13 (14): 3356–67. doi:10.1002/j.1460-2075.1994.tb06638.x. PMC 395233 . PMID 8045264.
Zhang WW, Zhang LX, Busch RK, Farrés J, Busch H (Feb 1993). "Purification and characterization of a DNA-binding heterodimer of 52 and 100 kDa from HeLa cells". The Biochemical Journal. 290 (1): 267–72. doi:10.1042/bj2900267. PMC 1132410 . PMID 8439294.
Clark J, Lu YJ, Sidhar SK, Parker C, Gill S, Smedley D, Hamoudi R, Linehan WM, Shipley J, Cooper CS (Oct 1997). "Fusion of splicing factor genes PSF and NonO (p54nrb) to the TFE3 gene in papillary renal cell carcinoma". Oncogene. 15 (18): 2233–9. doi: 10.1038/sj.onc.1201394 . PMID 9393982.
Teigelkamp S, Mundt C, Achsel T, Will CL, Lührmann R (Nov 1997). "The human U5 snRNP-specific 100-kD protein is an RS domain-containing, putative RNA helicase with significant homology to the yeast splicing factor Prp28p". RNA. 3 (11): 1313–26. PMC 1369570 . PMID 9409622.
Straub T, Grue P, Uhse A, Lisby M, Knudsen BR, Tange TO, Westergaard O, Boege F (Oct 1998). "The RNA-splicing factor PSF/p54 controls DNA-topoisomerase I activity by a direct interaction". The Journal of Biological Chemistry. 273 (41): 26261–4. doi: 10.1074/jbc.273.41.26261 . PMID 9756848.
Lutz CS, Cooke C, O'Connor JP, Kobayashi R, Alwine JC (Dec 1998). "The snRNP-free U1A (SF-A) complex(es): identification of the largest subunit as PSF, the polypyrimidine-tract binding protein-associated splicing factor". RNA. 4 (12): 1493–9. doi:10.1017/S1355838298981183. PMC 1369720 . PMID 9848648.
Meissner M, Dechat T, Gerner C, Grimm R, Foisner R, Sauermann G (Jan 2000). "Differential nuclear localization and nuclear matrix association of the splicing factors PSF and PTB". Journal of Cellular Biochemistry. 76 (4): 559–66. doi:10.1002/(SICI)1097-4644(20000315)76:4<559::AID-JCB4>3.0.CO;2-U. PMID 10653975. S2CID 25669908.
Urban RJ, Bodenburg Y, Kurosky A, Wood TG, Gasic S (Jun 2000). "Polypyrimidine tract-binding protein-associated splicing factor is a negative regulator of transcriptional activity of the porcine p450scc insulin-like growth factor response element". Molecular Endocrinology. 14 (6): 774–82. doi: 10.1210/mend.14.6.0485 . PMID 10847580.
Straub T, Knudsen BR, Boege F (Jun 2000). "PSF/p54(nrb) stimulates "jumping" of DNA topoisomerase I between separate DNA helices". Biochemistry. 39 (25): 7552–8. doi:10.1021/bi992898e. PMID 10858305.
Akhmedov AT, Lopez BS (Aug 2000). "Human 100-kDa homologous DNA-pairing protein is the splicing factor PSF and promotes DNA strand invasion". Nucleic Acids Research. 28 (16): 3022–30. doi:10.1093/nar/28.16.3022. PMC 108454 . PMID 10931916.
de Vries H, Rüegsegger U, Hübner W, Friedlein A, Langen H, Keller W (Nov 2000). "Human pre-mRNA cleavage factor II(m) contains homologs of yeast proteins and bridges two other cleavage factors". The EMBO Journal. 19 (21): 5895–904. doi:10.1093/emboj/19.21.5895. PMC 305781 . PMID 11060040.
Dye BT, Patton JG (Feb 2001). "An RNA recognition motif (RRM) is required for the localization of PTB-associated splicing factor (PSF) to subnuclear speckles". Experimental Cell Research. 263 (1): 131–44. doi:10.1006/excr.2000.5097. PMID 11161712.
Mathur M, Tucker PW, Samuels HH (Apr 2001). "PSF is a novel corepressor that mediates its effect through Sin3A and the DNA binding domain of nuclear hormone receptors". Molecular and Cellular Biology. 21 (7): 2298–311. doi:10.1128/MCB.21.7.2298-2311.2001. PMC 86864 . PMID 11259580.
Shav-Tal Y, Cohen M, Lapter S, Dye B, Patton JG, Vandekerckhove J, Zipori D (Aug 2001). "Nuclear relocalization of the pre-mRNA splicing factor PSF during apoptosis involves hyperphosphorylation, masking of antigenic epitopes, and changes in protein interactions". Molecular Biology of the Cell. 12 (8): 2328–40. doi:10.1091/mbc.12.8.2328. PMC 58597 . PMID 11514619.
Zhang Z, Carmichael GG (Aug 2001). "The fate of dsRNA in the nucleus: a p54(nrb)-containing complex mediates the nuclear retention of promiscuously A-to-I edited RNAs". Cell. 106 (4): 465–75. doi: 10.1016/S0092-8674(01)00466-4 . PMID 11525732. S2CID 18799711.
Andersen JS, Lyon CE, Fox AH, Leung AK, Lam YW, Steen H, Mann M, Lamond AI (Jan 2002). "Directed proteomic analysis of the human nucleolus". Current Biology. 12 (1): 1–11. doi: 10.1016/S0960-9822(01)00650-9 . PMID 11790298. S2CID 14132033.
Sewer MB, Nguyen VQ, Huang CJ, Tucker PW, Kagawa N, Waterman MR (Apr 2002). "Transcriptional activation of human CYP17 in H295R adrenocortical cells depends on complex formation among p54(nrb)/NonO, protein-associated splicing factor, and SF-1, a complex that also participates in repression of transcription". Endocrinology. 143 (4): 1280–90. doi: 10.1210/endo.143.4.8748 . PMID 11897684.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000250685 - Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid8449401-3] 1 2 Patton JG, Porro EB, Galceran J, Tempst P, Nadal-Ginard B (Mar 1993). "Cloning and characterization of PSF, a novel pre-mRNA splicing factor". Genes & Development. 7 (3): 393–406. doi: 10.1101/gad.7.3.393 . PMID 8449401.

[entrez-4] "Entrez Gene: SFPQ splicing factor proline/glutamine-rich (polypyrimidine tract binding protein associated)".

[pmid10653975-5] Meissner M, Dechat T, Gerner C, Grimm R, Foisner R, Sauermann G (Jan 2000). "Differential nuclear localization and nuclear matrix association of the splicing factors PSF and PTB". Journal of Cellular Biochemistry. 76 (4): 559–66. doi:10.1002/(SICI)1097-4644(20000315)76:4<559::AID-JCB4>3.0.CO;2-U. PMID 10653975. S2CID 25669908.

[pmid12403470-6] Peng R, Dye BT, Pérez I, Barnard DC, Thompson AB, Patton JG (Oct 2002). "PSF and p54nrb bind a conserved stem in U5 snRNA". RNA. 8 (10): 1334–47. doi:10.1017/S1355838202022070. PMC 1370341 . PMID 12403470.

[pmid11101529-7] Ajuh P, Kuster B, Panov K, Zomerdijk JC, Mann M, Lamond AI (Dec 2000). "Functional analysis of the human CDC5L complex and identification of its components by mass spectrometry". The EMBO Journal. 19 (23): 6569–81. doi:10.1093/emboj/19.23.6569. PMC 305846 . PMID 11101529.

[pmid16169070-8] Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (Sep 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. hdl: 11858/00-001M-0000-0010-8592-0 . PMID 16169070. S2CID 8235923.

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SFPQ

Contents

Interactions

Related Research Articles

References

Further reading