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Symbol SRSF1 contributors: mct - updated : 11-02-2015
HGNC name serine/arginine-rich splicing factor 1
HGNC id 10780
Location 17q22      Physical location : 56.078.281 - 56.084.707
Synonym name
  • splicing factor, arginine/serine-rich 1
  • splicing factor, arginine/serine-rich 1 (splicing factor 2, alternate splicing factor)
  • alternative splicing factor/splicing factor II 5ASF/SF2)
  • pre-mRNA-splicing factor SF2, P33 subunit
  • Synonym symbol(s) ASF/SF2, ASF, SF2, SRp30a, SF2p33, MGC5228, ASF-1, SFRS1
    TYPE functioning gene
    STRUCTURE 6.43 kb     4 Exon(s)
    MAPPING cloned Y linked N status confirmed
    TRANSCRIPTS type messenger
    text isoform ASF-2 and isoform ASF-3 act as splicing repressors
    identificationnb exonstypebpproduct
    ProteinkDaAAspecific expressionYearPubmed
    4 - 5468 27.7 248 - 2007 17310252
    also called ASF-1
    - - - - 291 - 2007 17310252
    also called ASF-2
    3 - 5668 - 200 - 2007 17310252
    also called ASF-3
    Type ubiquitous
       expressed in (based on citations)
    SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
    Digestiveintestinesmall intestine  moderately
    Lymphoid/Immunelymph node   highly
     thymus   moderately
    Reproductivefemale systemuterus  moderately
     male systemtestis  moderately
    Urinarybladder   moderately
    SystemTissueTissue level 1Tissue level 2LevelPubmedSpeciesStageRna symbol
    Blood / hematopoieticbone marrow   
    cell lineage
    cell lines
    at STAGE
  • two N terminal RNP (RRM) motifs, which recognize a 7-nucleotide exonic splicing enhancer (ESE) motif on pre-mRNA, and RNA recognition motif 2 is necessary and sufficient for sumoylation enhancement
  • an RS domain with numerous repeats of serine-arginine dipeptides, required for the shuttling of SFRS1 and contributes to its nuclear localization
  • conjugated Other
    interspecies ortholog to murine Sfrs1
    homolog to drosophila SF2
    homolog to C. elegans rsp-31
  • splicing factor SR family
  • CATEGORY RNA associated , protooncogene
    SUBCELLULAR LOCALIZATION     intracellular
    intracellular,nucleus,nucleoplasm,nuclear bodies,nuclear speckles
  • ability to shuttle between the nucleus and the cytoplasm
  • basic FUNCTION
  • mediating protein-protein interaction within the intron during spliceosome assembly
  • independently binding to exonic enhancer sequences and recruiting components to adjacent introns for splice-site recognition and alternative splicing
  • playing a role in preventing exon skipping, ensuring the accuracy of splicing and regulating alternative splicing
  • can stimulate binding of U1 snRNP to a 5'-splice-site-containing pre-mRNA
  • preventing formation of mutagenic R loop structures by recruitment of ASF/SF2 to nascent transcripts by RNA polymerase II
  • is a shuttling protein and is involved in transcription, mRNA export, NMD, translation, and maintenance of genome stability
  • can act as an oncoprotein and is a potential target for cancer therapy
  • multifunctional RNA binding protein with roles in pre-mRNA splicing, mRNA export and mRNA translation
  • has the capacity to co-regulate the nuclear and cytoplasmic processing of specific mRNAs
  • with CUGBP1, SFRS3, act antagonistically to regulate insulin receptor alternative splicing and the relative ratios of SFRS1, SFRS3 to CUGBP1 in different cells determine the degree of exon inclusion
  • SR protein splicing factors, associated with interphase chromatin, and released from hyperphosphorylated mitotic chromosomes, but reassociate with chromatin late in M-phase
  • oncoprotein that functions in pre-mRNA splicing, with additional roles in other posttranscriptional and translational events
  • shuttling protein that shows predominant nuclear localization in the steady state
  • regulator of the sumoylation pathway, and acts as a cofactor stimulating SUMO conjugation
  • exerts its effect at least at two different levels: it interacts with UBE2I promoting the sumoylation of specific substrates and it regulates the SUMO E3 ligase activity of PIAS1
  • role of SRSF1 in RNA polymerase II-mediated transcription
  • SRSF1 along with MALAT1 could influence the recruitment of splicing factors to nuclear speckles
  • plays a separate, nonoverlapping role in organizing nuclear speckle components
  • might play a central role not only in the tumor cells, but also in the surrounding stroma
  • CELLULAR PROCESS nucleotide, transcription, maturation
    nucleotide, RNA splicing
    text mRNA
    a component
  • component of the E commitment complex in the spliceosome assembly process
  • interacting 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
  • extensively phosphorylated on serine residues in the RS domain
  • acetylation
    RNA binding to purine-rich RNA sequences, either the octamer, 5'-RGAAGAAC-3' (r>A or G) or the decamers, AGGACAGAGC/AGGACGAAGC
    small molecule
  • ELF5-binding proteins that could activate splicing of an enhancer-dependent splicing reporter through ELF5
  • MALAT1 influenced the speckle association of SRSF1 in a phosphorylation-independent manner
  • controls alternative splicing of the tumor suppressor BIN1 and the kinases MKNK2 and RPS6KB1
  • cooperation with the transcription factor PPAR-gamma for regulating UCP3 alternative splicing (alternative polyadenylation)
  • interacts with the SUMO E3 ligase PIAS1, regulating PIAS1-induced overall protein sumoylation
  • ZRSR2 physically interacts with U2AF2, as well as SRSF1 and SRSF2, with a distinct function from its homologue, U2AF1
  • RWDD3 and SRSF1 have been shown to positively regulate UBE2I activity, although with distinct molecular mechanisms
  • ARVCF interacts with different proteins involved in mRNA-processing: SRSF1 (SF2/ASF), DDX5, and HNRNPH2
  • upon T cell activation, SRSF1 becomes limiting, and its function in CD6 exon 5 splicing is countered by an increase in CD6 transcription, dependent on chromatin acetylation
  • RECQL5 helicase promotes TOP1 SUMOylation by facilitating the interaction between PIAS1, SRSF1 and TOP1
  • cell & other
    corresponding disease(s)
    Other morbid association(s)
    TypeGene ModificationChromosome rearrangementProtein expressionProtein Function
    constitutional     --over  
    in dorsolateral prefontal cortex of schizophrenic patient
    tumoral     --over  
    in lung and colon cancers
    tumoral   amplification    
    in some breast tumors
    tumoral     --low  
    in newly diagnosed acute myeloid leukemia
    constitutional     --low  
    results in the disorganization of nuclear speckle components
    Variant & Polymorphism
    Candidate gene
    Therapy target
    potential target for cancer therapy