DAVID Bioinformatics
The Database for Annotation, Visualization and Integrated Discovery
DAVID Bioinformatics Resources 2008
National Institute of Allergy and Infectious Diseases (NIAID), NIH
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26731 splicing factor, arginine/serine-rich 1 (asf/sf2) Related Genes Mus musculus
SP_COMMENT PTM:Extensively phosphorylated on serine residues in the RS domain. This may regulate nucleocytoplasmic shuttling., domain:Both the RS domain and an RRM domain are required for nucleocytoplasmic shuttling., function:Plays a role in preventing exon skipping, ensuring the accuracy of splicing and regulating alternative splicing. Interacts with other spliceosomal components, via the RS domains, to form a bridge between the 5'- and 3'-splice site binding components, U1 snRNP and U2AF. Can stimulate binding of U1 snRNP to a 5'-splice site-containing pre-mRNA. Binds to purine-rich RNA sequences, either the octamer, 5'-RGAAGAAC-3' (r=A or G) or the decamers, AGGACAGAGC/AGGACGAAGC. Three copies of the octamer constitute a powerful splicing enhancer in vitro, the ASF/SF2 splicing enhancer (ASE) which can specifically activate ASE-dependent splicing (By similarity). Specifically regulates alternative splicing of cardiac isoforms of CAMK2D, LDB3/CYPHER and TNNT2/CTNT during heart remodeling at the juvenile to adult transition. The inappropriate accumulation of a neonatal and neuronal isoform of CAMKD2 in the adult heart results in aberrant calcium handling and defective excitation-contraction coupling in cardiomyocytes., similarity:Belongs to the splicing factor SR family., similarity:Contains 2 RRM (RNA recognition motif) domains., subcellular location:Cytoplasm (By similarity). Nucleus (By similarity). Nucleus speckle (By similarity). Note=Shuttles between the nucleus and the cytoplasm., subunit:Consists of two polypeptides of p32 and p33. In vitro, binds SFRS1 (ASF/SF2), SNRP70 and U2AF1 but not U2AF2. Binds SFRS12. Interacts with SAFB/SAFB1. Interacts with SRPK1. Interacts with PSIP1/LEDGF. Identified in the spliceosome C complex, at least composed of AQR, ASCC3L1, C19orf29, CDC40, CDC5L, CRNKL1, DDX23, DDX41, DDX48, DDX5, DGCR14, DHX35, DHX38, DHX8, EFTUD2, FRG1, GPATC1, HNRPA1, HNRPA2B1, HNRPA3, HNRPC, HNRPF, HNRPH1, HNRPK, HNRPM, HNRPR, HNRPU, KIAA1160, KIAA1604, LSM2, LSM3, MAGOH, MORG1, PABPC1, PLRG1, PNN, PPIE, PPIL1, PPIL3, PPWD1, PRPF19, PRPF4B, PRPF6, PRPF8, RALY, RBM22, RBM8A, RBMX, SART1, SF3A1, SF3A2, SF3A3, SF3B1, SF3B2, SF3B3, SFRS1, SKIV2L2, SNRPA1, SNRPB, SNRPB2, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, SNW1, SRRM1, SRRM2, SYF2, SYNCRIP, TFIP11, THOC4, U2AF1, WDR57, XAB2 and ZCCHC8.,
REFSEQ_PROTEIN NP_001071635, NP_775550, XP_001480947,
REFSEQ_MRNA NM_001078167, NM_173374, XM_001480897,
GENPEPT_ACCESSION AAH46773, AAH58627, BAC25546, BAC37367, BAE29641, CAI24416, CAI24417, EDL01863, EDL01864, EDL01865, Genomic_DNA, mRNA,
GENE_SYMBOL Sfrs1,
GENE_NAME Splicing factor, arginine/serine-rich 1, splicing factor, arginine/serine-rich 1 (ASF/SF2),
GENERIF_SUMMARY Disruption of an SF2/ASF-dependent exonic splicing enhancer in SMN2 causes spinal muscular atrophy in the absence of SMN1, Both hnRNP A1 and alternative splicing factor/splicing factor 2 contents rose in adenomas and during injury-induced hyperplasia compared to control lungs,
CHROMOSOME 11,
ENTREZ_GENE_ID 110809,
PIR_SUMMARY Plays a role in preventing exon skipping, ensuring the accuracy of splicing and regulating alternative splicing. Interacts with other spliceosomal components, via the RS domains, to form a bridge between the 5'- and 3'-splice site binding components, U1 snRNP and U2AF. Can stimulate binding of U1 snRNP to a 5'-splice site-containing pre-mRNA. Binds to purine-rich RNA sequences, either the octamer, 5'-RGAAGAAC-3' (r=A or G) or the decamers, AGGACAGAGC/AGGACGAAGC. Three copies of the octamer constitute a powerful splicing enhancer in vitro, the ASF/SF2 splicing enhancer (ASE) which can specifically activate ASE- dependent splicing (By similarity). Specifically regulates alternative splicing of cardiac isoforms of CAMK2D, LDB3/CYPHER and TNNT2/CTNT during heart remodeling at the juvenile to adult transition. The inappropriate accumulation of a neonatal and neuronal isoform of CAMKD2 in the adult heart results in aberrant calcium handling and defective excitation-contraction coupling in cardiomyocytes.,
UNIGENE Mm.391719, Mm.412737, Mm.457606, Mm.465221,
PIR_NREF_ID NF00500358, NF01174804, NF01284096,
UNIREF100_ID UniRef100_Q07955,
UNIPROT_ID Q3UCH2_MOUSE, SFRS1_MOUSE,
CYTOBAND 11 49.0 cM, 11 C,



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