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Symbol SFPQ contributors: mct/pgu - updated : 23-01-2019
HGNC name splicing factor proline/glutamine-rich
HGNC id 10774
Location 1p34.3      Physical location : 35.649.202 - 35.658.743
Synonym name
  • splicing factor proline/glutamine rich (polypyrimidine tract binding protein associated)
  • PTB-associated splicing factor, spliceosome associated protein 102/68
  • 100 kDa DNA-pairing protein
  • polypyrimidine tract-binding protein-associated-splicing factor
  • PTB-associated splicing factor
  • Synonym symbol(s) PSF, SAP102/68, POMP100, PPP1R140
    TYPE functioning gene
    STRUCTURE 9.54 kb     10 Exon(s)
    Genomic sequence alignment details
    10 Kb 5' upstream gene genomic sequence study
    MAPPING cloned Y linked N status provisional
    TRANSCRIPTS type messenger
    identificationnb exonstypebpproduct
    ProteinkDaAAspecific expressionYearPubmed
    10 - 3073 - 707 - 2018 29530979
    Type ubiquitous
       expressed in (based on citations)
    SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
    Cardiovascularheart   highly
    Reproductivemale systemtestis  highly Homo sapiens
    Respiratoryrespiratory tractlarynx  highly
    SystemCellPubmedSpeciesStageRna symbol
    ReproductiveSertoli cell Homo sapiens
    cell lineage
    cell lines
    at STAGE
    Text in human embryonic stem cells (hESCs)
  • two consensus RNA-binding domains
  • an unusual N terminus rich in proline and glutamine residues
  • a DNA-binding domain
  • a protein phosphatase 1 (PP1) consensus binding RVXF motifs, playing an important role in controlling the multifunctional properties of NONO and SFPQ in the regulation of gene transcription
  • a coiled-coil interaction motif (ability to polymerize is essential for the cellular functions of SFPQ: disruptive mutation of the coiled-coil interaction motif results in SFPQ mislocalization, reduced formation of nuclear bodies, abrogated molecular interactions and deficient transcriptional regulation)
  • mono polymer heteromer , monomer , dimer , tetramer
    FAMILY DBHS (Drosophila melanogaster behavior, human splicing) family
    CATEGORY RNA associated , tumor suppressor
    SUBCELLULAR LOCALIZATION     intracellular
    intracellular,nucleus,nucleoplasm,nuclear bodies,nuclear speckles
    text nuclear, predominantly in nuclear matrix
    basic FUNCTION
  • late splicing factor, repressing the transcription of multiple oncogenic genes
  • acting as a progesterone receptor corepressor and contributing to the functional withdrawal of progesterone and the initiation of labor
  • repressor which interacts with SIN3A and mediates silencing through the recruitment of HDACs to the receptor DNA binding domains
  • with PSPC1 and NONO, may cooperatively regulate androgen receptor-mediated gene transcription
  • may have dual functions in homologous recombination and RNA processing
  • core paraspeckle protein
  • critical to the control of gene expression through the nuclear retention of RNA containing double-stranded RNA regions that have been subject to adenosine-to-inosine editing
  • have homologous recombination and non-homologous end joining related activities and also to bind and modulate the function of RAD51
  • SFPQ/NONO heterodimer was previously found to enhance DNA strand break rejoining
  • have multiple functions in RNA processing, transcription and DNA repair by mitotic recombination
  • may function as an activator for the meiosis-specific recombinase DMC1 in higher eukaryotes
  • involvement of NONO and SFPQ in DNA double-strand break repair (DSB) and radioresistance
  • important role of NONO, PSPC1, SFPQ within the circadian oscillator
  • overlapping or redundant roles of NONO, PSPC1, SFPQ as transcriptional cofactors at circadian clock-regulated genes
  • is an RNA-binding proteins (RBPs) that binds and regulates multiple mRNAs in dorsal root ganglion sensory neurons and thereby promotes neurotrophin-dependent axonal viability
  • acts in nuclei, cytoplasm and axons to regulate functionally related mRNAs essential for axon survival
  • plays an important role regulating proliferation and migration during the development of the cerebral cortex
  • SFPQ is targeted for proteolysis within the nucleus by viral proteinase 3CD/3C, and a fragment of SFPQ was shown to migrate to the cytoplasm at mid-to-late times of infection
  • SFPQ, a proline and glutamine rich splicing factor that participates in diverse molecular functions including paraspeckle formation, microRNA synthesis and transcription regulation, is known to regulate host innate immune response to viruses
  • CELLULAR PROCESS nucleotide, recombination
    nucleotide, transcription
    nucleotide, RNA splicing
    a component
  • spliceosome integrated in late splicing complex C in the spliceosome assembly process
  • component of a snRNP- free complex with SNRPA/U1A
  • part of complex consisiting of SFPQ, NONO and MATR3
  • SFPQ/NONO heterodimer
  • GTF2I, PARP1, and SFPQ proteins, each previously implicated in gene regulation, forms a complex controlling transcription of DYX1C1
    DNA binding
    RNA binding to intron polypyrimidine tracts
    small molecule
  • binding to PTBP1
  • interacting with PARK7 and NONO (binding partner in dopaminergic neuronal cells)
  • binding to GAGE6 promoter DNA
  • interacts with SNRPA/U1A
  • interacts with two FGFR1 fusion partners, ZNF198 and CPSF6, that are functionally related to the recurrent PDGFRalpha partner FIP1L1
  • interacting with RAD51, enhancing its-mediated homologous pairing and strand exchange at low RAD51 concentrations and inhibiting it at the optimal concentration
  • target of PTK6
  • HNRNPM interacts with SFPQ and NONO and co-localizes within defined nuclear structures
  • interact with the nuclear matrix protein Matrin 3 (MATR3), which we found to be a novel ATM target
  • interacting partner with the RAD51 paralogs, RAD51D, RAD51C and XRCC2
  • SFPQ interacts directly with RAD51 and deficiency of both proteins confers a severe loss of cell viability, indicating a synthetic lethal relationship
  • interaction between LMX1B and PSPC1 in a larger protein complex also containing SFPQ
  • NEAT1 plays an important role in the innate immune response through the transcriptional regulation of antiviral genes by the stimulus-responsive cooperative action of NEAT1 and SFPQ
  • interactions between FUS and proteins involved in neurodegenerative diseases and/or ubiquitin proteasome pathway, such as VCP, SFPQ, UBA1, and 26S proteosome non-ATPase regulatory subunit 12 (PSMD12)
  • although NONO and SFPQ are nuclear paraspeckle components, these proteins formed cytoplasmic granules with RBPMS in the neurites
  • THRAP3 interacts with dimeric SFPQ to block access of RNA to RRM2, thereby regulating the activity of SFPQ toward a broad set of splicing events in T cells
  • association of the multifunctional RNA-binding protein SFPQ to KDM1A during the development of the cerebral cortex
  • interactions between histone proteins and splicing factors such as RBFOX2, RBFOX3, and splicing factor proline and glutamine rich protein (SFPQ)
  • cell & other
    corresponding disease(s)
    Other morbid association(s)
    TypeGene ModificationChromosome rearrangementProtein expressionProtein Function
    tumoral   translocation    
    in papillary renal cell carcinoma in which is partnered with the TFE3 gene as a result of a translocation, t(X;1)(p11.2;p34)
    tumoral       loss of function
    deficiency of SFPQ alone also leads to sister chromatid cohesion defects and chromosome instability
    tumoral fusion      
    with ABL in t(1;9)(p34;q34) and B cell progenitor acute lymphoid leukemia
    Susceptibility to familial and sporadic amyotrophic lateral sclerosis (ALS)
    Variant & Polymorphism other
  • SFPQ intron retention (IR) and nuclear loss are molecular hallmarks of familial and sporadic ALS
  • Candidate gene
    Therapy target
  • Sfpq disruption caused neuronal apoptosis in developing mouse brains