SFPQ_MOUSE - dbPTM
SFPQ_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SFPQ_MOUSE
UniProt AC Q8VIJ6
Protein Name Splicing factor, proline- and glutamine-rich
Gene Name Sfpq
Organism Mus musculus (Mouse).
Sequence Length 699
Subcellular Localization Nucleus speckle . Nucleus matrix . Cytoplasm . Predominantly in nuclear matrix.
Protein 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 binds DNA. The SFPQ-NONO heteromer may be involved in DNA non-homologous 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. Functions as transcriptional activator (By similarity). Transcriptional repression is 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 activity. 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). Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex through histone deacetylation. [PubMed: 21680841]
Protein Sequence MSRDRFRSRGGGGGGFHRRGGGGGRGGLHDFRSPPPGMGLNQNRGPMGPGPGGPKPPLPPPPPHQQQQQPPPQQPPPQQPPPHQQPPPHQPPHQQPPPPPQESKPVVPQGPGSAPGVSSAPPPAVSAPPANPPTTGAPPGPGPTPTPPPAVPSTAPGPPPPSTPSSGVSTTPPQTGGPPPPPAGGAGPGPKPGPGPGGPKGGKMPGGPKPGGGPGMGAPGGHPKPPHRGGGEPRGGRQHHAPYHQQHHQGPPPGGPGPRTEEKISDSEGFKANLSLLRRPGEKTYTQRCRLFVGNLPADITEDEFKRLFAKYGEPGEVFINKGKGFGFIKLESRALAEIAKAELDDTPMRGRQLRVRFATHAAALSVRNLSPYVSNELLEEAFSQFGPIERAVVIVDDRGRSTGKGIVEFASKPAARKAFERCSEGVFLLTTTPRPVIVEPLEQLDDEDGLPEKLAQKNPMYQKERETPPRFAQHGTFEYEYSQRWKSLDEMEKQQREQVEKNMKDAKDKLESEMEDAYHEHQANLLRQDLMRRQEELRRMEELHSQEMQKRKEMQLRQEEERRRREEEMMIRQREMEEQMRRQREESYSRMGYMDPRERDMRMGGGGTMNMGDPYGSGGQKFPPLGGGGGIGYEANPGVPPATMSGSMMGSDMRTERFGQGGAGPVGGQGPRGMGPGTPAGYGRGREEYEGPNKKPRF
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
7Dimethylation-MSRDRFRSRGGGGG
-CCHHHHHHCCCCCC		26.74-
7Methylation-MSRDRFRSRGGGGG
-CCHHHHHHCCCCCC		26.74136655
8PhosphorylationMSRDRFRSRGGGGGG
CCHHHHHHCCCCCCC		32.34-
9MethylationSRDRFRSRGGGGGGF
CHHHHHHCCCCCCCC		43.4424129315
9Asymmetric dimethylarginineSRDRFRSRGGGGGGF
CHHHHHHCCCCCCCC		43.44-
18MethylationGGGGGFHRRGGGGGR
CCCCCCCCCCCCCCC		36.3630988953
19MethylationGGGGFHRRGGGGGRG
CCCCCCCCCCCCCCC		39.2725056395
19DimethylationGGGGFHRRGGGGGRG
CCCCCCCCCCCCCCC		39.27-
25DimethylationRRGGGGGRGGLHDFR
CCCCCCCCCCCCCCC		39.00-
25MethylationRRGGGGGRGGLHDFR
CCCCCCCCCCCCCCC		39.0018960163
32DimethylationRGGLHDFRSPPPGMG
CCCCCCCCCCCCCCC		55.07-
32MethylationRGGLHDFRSPPPGMG
CCCCCCCCCCCCCCC		55.0730762951
33PhosphorylationGGLHDFRSPPPGMGL
CCCCCCCCCCCCCCC		41.5721659605
200AcetylationGPGPGGPKGGKMPGG
CCCCCCCCCCCCCCC		81.3123806337
228MethylationGHPKPPHRGGGEPRG
CCCCCCCCCCCCCCC		51.7524129315
234MethylationHRGGGEPRGGRQHHA
CCCCCCCCCCCCCCC		56.7624129315
237MethylationGGEPRGGRQHHAPYH
CCCCCCCCCCCCCCH		35.1724129315
263UbiquitinationPGPRTEEKISDSEGF
CCCCCHHHCCCCCCH		41.0822790023
265PhosphorylationPRTEEKISDSEGFKA
CCCHHHCCCCCCHHH		46.2627742792
267PhosphorylationTEEKISDSEGFKANL
CHHHCCCCCCHHHHH		32.5928833060
271UbiquitinationISDSEGFKANLSLLR
CCCCCCHHHHHHHHH		47.4222790023
275PhosphorylationEGFKANLSLLRRPGE
CCHHHHHHHHHCCCC		25.7627149854
285PhosphorylationRRPGEKTYTQRCRLF
HCCCCCCHHHCCEEE		16.37-
306"N6,N6-dimethyllysine"DITEDEFKRLFAKYG
CCCHHHHHHHHHHHC		46.25-
306MethylationDITEDEFKRLFAKYG
CCCHHHHHHHHHHHC		46.25-
306AcetylationDITEDEFKRLFAKYG
CCCHHHHHHHHHHHC		46.2522826441
311AcetylationEFKRLFAKYGEPGEV
HHHHHHHHHCCCCCE		46.5922826441
311UbiquitinationEFKRLFAKYGEPGEV
HHHHHHHHHCCCCCE		46.5922790023
312PhosphorylationFKRLFAKYGEPGEVF
HHHHHHHHCCCCCEE		24.24-
322AcetylationPGEVFINKGKGFGFI
CCCEEEECCCCCCEE		58.1222826441
322UbiquitinationPGEVFINKGKGFGFI
CCCEEEECCCCCCEE		58.1227667366
322MalonylationPGEVFINKGKGFGFI
CCCEEEECCCCCCEE		58.1226320211
324UbiquitinationEVFINKGKGFGFIKL
CEEEECCCCCCEEEE		53.3122790023
330UbiquitinationGKGFGFIKLESRALA
CCCCCEEEECHHHHH		43.8922790023
330AcetylationGKGFGFIKLESRALA
CCCCCEEEECHHHHH		43.8922826441
341AcetylationRALAEIAKAELDDTP
HHHHHHHHHHHCCCC		48.3222826441
347PhosphorylationAKAELDDTPMRGRQL
HHHHHCCCCCCCCHH		20.74-
352UbiquitinationDDTPMRGRQLRVRFA
CCCCCCCCHHHHHHH		23.2327667366
360PhosphorylationQLRVRFATHAAALSV
HHHHHHHHHHHHHHH		14.8825266776
366PhosphorylationATHAAALSVRNLSPY
HHHHHHHHHCCCCHH		17.8229176673
371PhosphorylationALSVRNLSPYVSNEL
HHHHCCCCHHCCHHH		20.1026643407
373PhosphorylationSVRNLSPYVSNELLE
HHCCCCHHCCHHHHH		17.0926745281
375PhosphorylationRNLSPYVSNELLEEA
CCCCHHCCHHHHHHH		20.8126643407
400UbiquitinationVVIVDDRGRSTGKGI
EEEECCCCCCCCCCH		34.5827667366
405UbiquitinationDRGRSTGKGIVEFAS
CCCCCCCCCHHHHCC		45.6222790023
411UbiquitinationGKGIVEFASKPAARK
CCCHHHHCCCHHHHH		11.7927667366
413MalonylationGIVEFASKPAARKAF
CHHHHCCCHHHHHHH		34.9326320211
413UbiquitinationGIVEFASKPAARKAF
CHHHHCCCHHHHHHH		34.9327667366
413AcetylationGIVEFASKPAARKAF
CHHHHCCCHHHHHHH		34.9322826441
458MalonylationLPEKLAQKNPMYQKE
CCHHHHHHCCCCHHH		58.3626320211
458UbiquitinationLPEKLAQKNPMYQKE
CCHHHHHHCCCCHHH		58.3627667366
464UbiquitinationQKNPMYQKERETPPR
HHCCCCHHHCCCCCC		41.0527667366
464AcetylationQKNPMYQKERETPPR
HHCCCCHHHCCCCCC		41.05-
468PhosphorylationMYQKERETPPRFAQH
CCHHHCCCCCCHHHC		44.8320139300
480PhosphorylationAQHGTFEYEYSQRWK
HHCCCCHHHHHHHHH		18.9022817900
488PhosphorylationEYSQRWKSLDEMEKQ
HHHHHHHCHHHHHHH		33.8121082442
502UbiquitinationQQREQVEKNMKDAKD
HHHHHHHHHHHHHHH		64.5827667366
508AcetylationEKNMKDAKDKLESEM
HHHHHHHHHHHHHHH		66.587712041
513PhosphorylationDAKDKLESEMEDAYH
HHHHHHHHHHHHHHH		53.3226525534
546PhosphorylationRRMEELHSQEMQKRK
HHHHHHHHHHHHHHH		40.2225338131
547UbiquitinationRMEELHSQEMQKRKE
HHHHHHHHHHHHHHH		39.1627667366
553UbiquitinationSQEMQKRKEMQLRQE
HHHHHHHHHHHHHHH		65.6527667366
563MethylationQLRQEEERRRREEEM
HHHHHHHHHHHHHHH		40.46-
588PhosphorylationMRRQREESYSRMGYM
HHHHHHHHHHHHCCC		24.5329514104
590PhosphorylationRQREESYSRMGYMDP
HHHHHHHHHHCCCCH		25.6829514104
609PhosphorylationMRMGGGGTMNMGDPY
CCCCCCCCCCCCCCC		14.5114729942
618PhosphorylationNMGDPYGSGGQKFPP
CCCCCCCCCCCCCCC		33.6325521595
644PhosphorylationNPGVPPATMSGSMMG
CCCCCCCCCCCCCCC		20.04-
673MethylationPVGGQGPRGMGPGTP
CCCCCCCCCCCCCCC		55.3324129315
675OxidationGGQGPRGMGPGTPAG
CCCCCCCCCCCCCCC		6.5517242355
679PhosphorylationPRGMGPGTPAGYGRG
CCCCCCCCCCCCCCC		17.0725521595
683PhosphorylationGPGTPAGYGRGREEY
CCCCCCCCCCCCCCC		13.0224759943
685MethylationGTPAGYGRGREEYEG
CCCCCCCCCCCCCCC		32.2924129315
687MethylationPAGYGRGREEYEGPN
CCCCCCCCCCCCCCC		32.0116187657
690PhosphorylationYGRGREEYEGPNKKP
CCCCCCCCCCCCCCC		22.7925159016
698MethylationEGPNKKPRF------
CCCCCCCCC------		59.8054558339
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
8SPhosphorylationKinaseMKNK2Q8CDB0
Uniprot
275SPhosphorylationKinaseMKNK2Q8CDB0
Uniprot
285YPhosphorylationKinaseALKP97793
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
679TPhosphorylation

17242355
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of SFPQ_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PER2_MOUSEPer2physical
21680841
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SFPQ_MOUSE

loading...

Related Literatures of Post-Translational Modification

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory