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SFPQ

  • Official Full Name

    splicing factor proline/glutamine-rich

  • Overview

    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 an heteromer with NONO. Binds to pre-mRNA in spliceosome C complex, and specifically binds to intronic polypyrimidine tracts. 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 may be involved in DNA nonhomologous 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. Transcriptional repression is probably mediated by an interaction of SFPQ with SIN3A and subsequent recruitment of histone deacetylases (HDACs). The SFPQ-NONO/SF-1 complex binds to the CYP17 promoter and regulates basal and cAMP-dependent transcriptional avtivity. 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.
  • Synonyms

    SFPQ; splicing factor proline/glutamine-rich; PSF; POMP100; splicing factor, proline- and glutamine-rich; hPOMp100; 100 kDa DNA-pairing protein; PTB-associated splicing factor; PTB-associated-splicing factor; DNA-binding p52/p100 complex, 100 kDa subunit; polypyrimidine tract binding protein associated; polypyrimidine tract-binding protein-associated splicing factor; polypyrimidine tract-binding protein-associated-splicing factor; splicing factor proline/glutamine rich (polypyrimidine tract binding protein associated); splicing factor proline/glutamine rich (polypyrimidine tract-binding protein-associated);

  • Recombinant Proteins
  • Cell & Tissue Lysates
  • Protein Pre-coupled Magnetic Beads
  • Human
  • Mouse
  • Zebrafish
  • E.coli
  • HEK293
  • HEK293T
  • Mammalian Cell
  • Mammalian cells
  • Wheat Germ
  • Flag
  • GST
  • His
  • His (Fc)
  • Avi
  • Myc
  • DDK
  • N/A
Species Cat.# Product name Source (Host) Tag Protein Length Price
Human SFPQ-856H Recombinant Human SFPQ protein, GST-tagged Wheat Germ GST
Human SFPQ-30711TH Recombinant Human SFPQ, His-tagged E.coli His
Human SFPQ-2617H Recombinant Human SFPQ, His-tagged E.coli His 1-300aa
Human SFPQ-1911HCL Recombinant Human SFPQ 293 Cell Lysate HEK293 N/A
Human SFPQ-789HFL Recombinant Full Length Human SFPQ Protein, C-Flag-tagged Mammalian cells Flag
Human SFPQ-1992H Recombinant Human SFPQ Protein, His (Fc)-Avi-tagged HEK293 His (Fc)-Avi
Human SFPQ-1992H-B Recombinant Human SFPQ Protein Pre-coupled Magnetic Beads HEK293
Mouse SFPQ-15007M Recombinant Mouse SFPQ Protein Mammalian Cell His
Mouse SFPQ-8083M Recombinant Mouse SFPQ Protein, His (Fc)-Avi-tagged HEK293 His (Fc)-Avi
Mouse Sfpq-5814M Recombinant Mouse Sfpq Protein, Myc/DDK-tagged HEK293T Myc/DDK
Mouse SFPQ-8083M-B Recombinant Mouse SFPQ Protein Pre-coupled Magnetic Beads HEK293
Zebrafish SFPQ-12471Z Recombinant Zebrafish SFPQ Mammalian Cell His
  • Involved Pathway
  • Protein Function
  • Interacting Protein
  • SFPQ Related Articles

SFPQ involved in several pathways and played different roles in them. We selected most pathways SFPQ participated on our site, such as mRNA processing, which may be useful for your reference. Also, other proteins which involved in the same pathway with SFPQ were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

Pathway Name Pathway Related Protein
mRNA processingNONO;CELF1;ADAM5;CD2BP2;EIF4E3;SF3B2;SNURF;PTBP1;CLASRP

SFPQ has several biochemical functions, for example, RNA polymerase II distal enhancer sequence-specific DNA binding, chromatin binding, core promoter binding. Some of the functions are cooperated with other proteins, some of the functions could acted by SFPQ itself. We selected most functions SFPQ had, and list some proteins which have the same functions with SFPQ. You can find most of the proteins on our site.

Function Related Protein
RNA polymerase II distal enhancer sequence-specific DNA bindingCDX1;ARX;MEOX2;SFPI1;NR2F6;NFKB1;SOX10;NFATC1;PROP1
chromatin bindingURI1;NR5A5;SSBP1;CDC45;PRKCBB;HMGB1;KDM5A;CENPB;WHSC1
core promoter bindingRB1;KLF4;AGO2;E2F3;MYBBP1A;PYDC3;HDAC2;NKX2-1;FOXP3
histone deacetylase bindingTOP2A;HDAC10;MEF2B;NR2C1;MECP2;TAL1;CRY1;RBBP4;SIX3
nucleotide bindingRBM15;MARF1;TTLL9;VDAC2;TUBA8L4;POLR2D;PHKG1A;OXSR1A;DCLK1A
poly(A) RNA bindingEDF1;DZIP3;MRPS11;DIMT1;MEX3B;RPL5B;RIMS1;HSPA9;DIEXF
protein bindingIPO4;SLC9A7;DCBLD2;COG3;GRAP;BANK1;PTPRZ1;VPS18;BCL2A1A
transcription regulatory region DNA bindingMTERFD3;JUND;AIRE;FOXI1;SALL2;HDAC1;FOXA3;CTCFL;MSX2
transcription regulatory region sequence-specific DNA bindingNFE2;NKX3;BAHD1;NFE2L2;EPAS1B;FOXJ1;NKX3-1;BTBD8;ATF3

SFPQ has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with SFPQ here. Most of them are supplied by our site. Hope this information will be useful for your research of SFPQ.

PTBP1; PTK6; SNRPA; THRAP3; RNF43

Chang, HH; Hu, HH; et al. Proteomic analyses and identification of arginine methylated proteins differentially recognized by autosera from anti-Sm positive SLE patients. JOURNAL OF BIOMEDICAL SCIENCE 20:-(2013).
Kurokawa, K; Tanahashi, T; et al. Role of miR-19b and its target mRNAs in 5-fluorouracil resistance in colon cancer cells. JOURNAL OF GASTROENTEROLOGY 47:883-895(2012).
  • Q&As
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