CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018228
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Splicing factor, proline- and glutamine-rich 
Protein Synonyms/Alias
 DNA-binding p52/p100 complex, 100 kDa subunit; Polypyrimidine tract-binding protein-associated-splicing factor; PSF; PTB-associated-splicing factor 
Gene Name
 Sfpq 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
200GPGPGGPKGGKMPGGacetylation[1]
263PGPRTEEKISDSEGFubiquitination[2]
271ISDSEGFKANLSLLRubiquitination[2]
306DITEDEFKRLFAKYGacetylation[3]
311EFKRLFAKYGEPGEVacetylation[3]
311EFKRLFAKYGEPGEVubiquitination[2]
322PGEVFINKGKGFGFIacetylation[3]
322PGEVFINKGKGFGFIubiquitination[2]
324EVFINKGKGFGFIKLubiquitination[2]
330GKGFGFIKLESRALAacetylation[3]
330GKGFGFIKLESRALAubiquitination[2]
341RALAEIAKAELDDTPacetylation[3]
405DRGRSTGKGIVEFASubiquitination[2]
413GIVEFASKPAARKAFacetylation[3]
413GIVEFASKPAARKAFubiquitination[2]
458LPEKLAQKNPMYQKEubiquitination[2]
Reference
 [1] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [2] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [3] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441] 
Functional Description
 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 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-NR5A1 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 (By similarity). 
Sequence Annotation
 REPEAT 9 11 1.
 REPEAT 19 21 2.
 REPEAT 25 27 3.
 DOMAIN 289 361 RRM 1.
 DOMAIN 363 444 RRM 2.
 REGION 9 27 3 X 3 AA repeats of R-G-G.
 MOD_RES 7 7 Omega-N-methylated arginine (By
 MOD_RES 8 8 Phosphoserine; by MKNK2 (By similarity).
 MOD_RES 9 9 Omega-N-methylated arginine (By
 MOD_RES 19 19 Omega-N-methylated arginine (By
 MOD_RES 25 25 Omega-N-methylated arginine (By
 MOD_RES 33 33 Phosphoserine (By similarity).
 MOD_RES 265 265 Phosphoserine (By similarity).
 MOD_RES 275 275 Phosphoserine; by MKNK2 (By similarity).
 MOD_RES 285 285 Phosphotyrosine; by ALK (By similarity).
 MOD_RES 306 306 N6,N6-dimethyllysine (By similarity).
 MOD_RES 311 311 N6-acetyllysine (By similarity).
 MOD_RES 330 330 N6-acetyllysine (By similarity).
 MOD_RES 371 371 Phosphoserine (By similarity).
 MOD_RES 413 413 N6-acetyllysine (By similarity).
 MOD_RES 464 464 N6-acetyllysine (By similarity).
 MOD_RES 563 563 Dimethylated arginine (By similarity).
 MOD_RES 618 618 Phosphoserine (By similarity).
 MOD_RES 673 673 Omega-N-methylarginine (By similarity).
 MOD_RES 679 679 Phosphothreonine (By similarity).
 MOD_RES 685 685 Dimethylated arginine (By similarity).  
Keyword
 Acetylation; Activator; Complete proteome; Cytoplasm; Direct protein sequencing; DNA damage; DNA repair; DNA-binding; Methylation; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor; RNA-binding; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 699 AA 
Protein Sequence
MSRDRFRSRG GGGGGFHRRG GGGGRGGLHD FRSPPPGMGL NQNRGPMGPG PGGPKPPLPP 60
PPPHQQQQQP PPQQPPPQQP PPHQQPPPHQ PPHQQPPPPP QESKPVVPQG PGSAPGVSSA 120
PPPAVSAPPA NPPTTGAPPG PGPTPTPPPA VPSTAPGPPP PSTPSSGVST TPPQTGGPPP 180
PPAGGAGPGP KPGPGPGGPK GGKMPGGPKP GGGPGMGAPG GHPKPPHRGG GEPRGGRQHH 240
APYHQQHHQG PPPGGPGPRT EEKISDSEGF KANLSLLRRP GEKTYTQRCR LFVGNLPADI 300
TEDEFKRLFA KYGEPGEVFI NKGKGFGFIK LESRALAEIA KAELDDTPMR GRQLRVRFAT 360
HAAALSVRNL SPYVSNELLE EAFSQFGPIE RAVVIVDDRG RSTGKGIVEF ASKPAARKAF 420
ERCSEGVFLL TTTPRPVIVE PLEQLDDEDG LPEKLAQKNP MYQKERETPP RFAQHGTFEY 480
EYSQRWKSLD EMEKQQREQV EKNMKDAKDK LESEMEDAYH EHQANLLRQD LMRRQEELRR 540
MEELHSQEMQ KRKEMQLRQE EERRRREEEM MIRQREMEEQ MRRQREESYS RMGYMDPRER 600
DMRMGGGGTM NMGDPYGSGG QKFPPLGGGG GIGYEANPGV PPATMSGSMM GSDMRTERFG 660
QGGAGPVGGQ GPRGMGPGTP AGYGRGREEY EGPNKKPRF 699 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
 GO:0042382; C:paraspeckles; IEA:Compara.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0000380; P:alternative mRNA splicing, via spliceosome; IEA:Compara.
 GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Compara.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR012975; NOPS.
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom. 
Pfam
 PF08075; NOPS
 PF00076; RRM_1 
SMART
 SM00360; RRM 
PROSITE
 PS50102; RRM 
PRINTS