Identification
HMDB Protein ID CDBP01698
Secondary Accession Numbers Not Available
Name Splicing factor, proline- and glutamine-rich
Description Not Available
Synonyms
  1. 100 kDa DNA-pairing protein
  2. DNA-binding p52/p100 complex, 100 kDa subunit
  3. PSF
  4. PTB-associated-splicing factor
  5. Polypyrimidine tract-binding protein-associated-splicing factor
  6. hPOMp100
Gene Name SFPQ
Protein Type Enzyme
Biological Properties
General Function Involved in nucleotide binding
Specific Function 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
GO Classification
Function
binding
nucleotide binding
nucleic acid binding
Cellular Location
  1. Nucleus matrix
Pathways
Gene Properties
Chromosome Location Chromosome:1
Locus 1p34.3
SNPs SFPQ
Gene Sequence
>2124 bp
ATGTCTCGGGATCGGTTCCGGAGTCGTGGCGGTGGCGGTGGTGGCTTCCACAGGCGTGGA
GGAGGCGGCGGCCGCGGCGGCCTCCACGACTTCCGTTCTCCGCCGCCCGGCATGGGCCTC
AATCAGAATCGCGGCCCCATGGGTCCTGGCCCGGGCCAGAGCGGCCCTAAGCCTCCGATC
CCGCCACCGCCTCCACACCAACAGCAGCAACAGCCACCACCGCAGCAGCCACCGCCGCAG
CAGCCGCCACCGCATCAGCCGCCGCCGCATCCACAGCCGCATCAGCAGCAGCAGCCGCCG
CCACCGCCGCAGGACTCTTCCAAGCCCGTCGTTGCTCAGGGACCCGGCCCCGCTCCCGGA
GTAGGCAGCGCACCACCAGCCTCCAGCTCGGCCCCGCCCGCCACTCCACCAACCTCGGGG
GCCCCGCCAGGGTCCGGGCCAGGCCCGACTCCGACCCCGCCGCCTGCAGTCACCTCGGCC
CCTCCCGGGGCGCCGCCACCCACCCCGCCAAGCAGCGGGGTCCCTACCACACCTCCTCAG
GCCGGAGGCCCGCCGCCTCCGCCCGCGGCAGTCCCGGGCCCGGGTCCAGGGCCTAAGCAG
GGCCCAGGTCCGGGTGGTCCCAAAGGCGGCAAAATGCCTGGCGGGCCGAAGCCAGGTGGC
GGCCCGGGCCTAAGTACGCCTGGCGGCCACCCCAAGCCGCCGCATCGAGGCGGCGGGGAG
CCCCGCGGGGGCCGCCAGCACCACCCGCCCTACCACCAGCAGCATCACCAGGGGCCCCCG
CCCGGCGGGCCCGGCGGCCGCAGCGAGGAGAAGATCTCGGACTCGGAGGGGTTTAAAGCC
AATTTGTCTCTCTTGAGGAGGCCTGGAGAGAAAACTTACACACAGCGATGTCGGTTGTTT
GTTGGGAATCTACCTGCTGATATCACGGAGGATGAATTCAAAAGACTATTTGCTAAATAT
GGAGAACCAGGAGAAGTTTTTATCAACAAAGGCAAAGGATTCGGATTTATTAAGCTTGAA
TCTAGAGCTTTGGCTGAAATTGCCAAAGCCGAACTGGATGATACACCCATGAGAGGTAGA
CAGCTTCGAGTTCGCTTTGCCACACATGCTGCTGCCCTTTCTGTTCGTAATCTTTCACCT
TATGTTTCCAATGAACTGTTGGAAGAAGCCTTTAGCCAATTTGGTCCTATTGAAAGGGCT
GTTGTAATAGTGGATGATCGTGGAAGATCTACAGGGAAAGGCATTGTTGAATTTGCTTCT
AAGCCAGCAGCAAGAAAGGCATTTGAACGATGCAGTGAAGGTGTTTTCTTACTGACGACA
ACTCCTCGTCCAGTCATTGTGGAACCACTTGAACAACTAGATGATGAAGATGGTCTTCCT
GAAAAACTTGCCCAGAAGAATCCAATGTATCAAAAGGAGAGAGAAACCCCTCCTCGTTTT
GCCCAGCATGGCACGTTTGAGTACGAATATTCTCAGCGATGGAAGTCTTTGGATGAAATG
GAAAAACAGCAAAGGGAACAAGTTGAAAAAAACATGAAAGATGCAAAAGACAAATTGGAA
AGTGAAATGGAAGATGCCTATCATGAACATCAGGCAAATCTTTTGCGCCAAGATCTGATG
AGACGACAGGAAGAATTAAGACGCATGGAAGAACTTCACAATCAAGAAATGCAGAAACGT
AAAGAAATGCAATTGAGGCAAGAGGAGGAACGACGTAGAAGAGAGGAAGAGATGATGATT
CGTCAACGTGAGATGGAAGAACAAATGAGGCGCCAAAGAGAGGAAAGTTACAGCCGAATG
GGCTACATGGATCCACGGGAAAGAGACATGCGAATGGGTGGCGGAGGAGCAATGAACATG
GGAGATCCCTATGGTTCAGGAGGCCAGAAATTTCCACCTCTAGGAGGTGGTGGTGGCATA
GGTTATGAAGCTAATCCTGGCGTTCCACCAGCAACCATGAGTGGTTCCATGATGGGAAGT
GACATGCGTACTGAGCGCTTTGGGCAGGGAGGTGCGGGGCCTGTGGGTGGACAGGGTCCT
AGAGGAATGGGGCCTGGAACTCCAGCAGGATATGGTAGAGGGAGAGAAGAGTACGAAGGC
CCAAACAAAAAACCCCGATTTTAG
Protein Properties
Number of Residues 707
Molecular Weight 76149.1
Theoretical pI 9.95
Pfam Domain Function
Signals
  • ["None"]
Transmembrane Regions
  • ["None"]
Protein Sequence
>Splicing factor, proline- and glutamine-rich
MSRDRFRSRGGGGGGFHRRGGGGGRGGLHDFRSPPPGMGLNQNRGPMGPGPGQSGPKPPI
PPPPPHQQQQQPPPQQPPPQQPPPHQPPPHPQPHQQQQPPPPPQDSSKPVVAQGPGPAPG
VGSAPPASSSAPPATPPTSGAPPGSGPGPTPTPPPAVTSAPPGAPPPTPPSSGVPTTPPQ
AGGPPPPPAAVPGPGPGPKQGPGPGGPKGGKMPGGPKPGGGPGLSTPGGHPKPPHRGGGE
PRGGRQHHPPYHQQHHQGPPPGGPGGRSEEKISDSEGFKANLSLLRRPGEKTYTQRCRLF
VGNLPADITEDEFKRLFAKYGEPGEVFINKGKGFGFIKLESRALAEIAKAELDDTPMRGR
QLRVRFATHAAALSVRNLSPYVSNELLEEAFSQFGPIERAVVIVDDRGRSTGKGIVEFAS
KPAARKAFERCSEGVFLLTTTPRPVIVEPLEQLDDEDGLPEKLAQKNPMYQKERETPPRF
AQHGTFEYEYSQRWKSLDEMEKQQREQVEKNMKDAKDKLESEMEDAYHEHQANLLRQDLM
RRQEELRRMEELHNQEMQKRKEMQLRQEEERRRREEEMMIRQREMEEQMRRQREESYSRM
GYMDPRERDMRMGGGGAMNMGDPYGSGGQKFPPLGGGGGIGYEANPGVPPATMSGSMMGS
DMRTERFGQGGAGPVGGQGPRGMGPGTPAGYGRGREEYEGPNKKPRF
GenBank ID Protein 55960496
UniProtKB/Swiss-Prot ID P23246
UniProtKB/Swiss-Prot Entry Name SFPQ_HUMAN
PDB IDs Not Available
GenBank Gene ID AL590434
GeneCard ID SFPQ
GenAtlas ID SFPQ
HGNC ID HGNC:10774
References
General References Not Available