Selected-GenAtlas references SOURCE GeneCards NCBI Gene Swiss-Prot Ensembl
HGNC UniGene Nucleotide OMIM UCSC
Home Page
Symbol SRSF2 contributors: mct/npt/pgu - updated : 09-06-2020
HGNC name serine/arginine-rich splicing factor 2
HGNC id 10783
Location 17q25.1      Physical location : 74.730.198 - 74.733.493
Synonym name
  • PR264, ribonucleoprotein 80
  • splicing factor 35
  • Synonym symbol(s) PR264, SC35, SC-35, SFRS2A, SRp30b, SFRS2
    TYPE functioning gene
    STRUCTURE 3.29 kb     2 Exon(s)
    MAPPING cloned Y linked N status confirmed
    TRANSCRIPTS type messenger
    identificationnb exonstypebpproduct
    ProteinkDaAAspecific expressionYearPubmed
    2 - 2922 - 221 - 2019 31295920
    3 - 1888 - 221 - 2019 31295920
    Type ubiquitous
       expressed in (based on citations)
    SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
    Cardiovascularheart   highly
    Digestiveintestinesmall intestine  highly
    Lymphoid/Immunespleen   highly
    Nervousbrain     Mus musculus
    Urinarybladder   highly
    SystemCellPubmedSpeciesStageRna symbol
    Nervousneuron Mus musculus
    Nervousoligodendrocyte Mus musculus
    Reproductivespermatid Homo sapiens
    cell lineage
    cell lines
    at STAGE
  • a N terminal RNP (RRM) motif
  • a C terminal RS domain, ribonucleoprotein 80
  • Ser-Rich Arg (SR) proteins family
  • CATEGORY RNA associated
    SUBCELLULAR LOCALIZATION     intracellular
    intracellular,nucleus,nucleoplasm,nuclear bodies,nuclear speckles
  • colocalized with SIR1 and RP9 in nuclear speckles
  • basic FUNCTION
  • alternative pre m-RNA splicing factor, 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
  • involved in the regulation of DNA stability and depletion of SRSF2 can lead to genomic instability
  • serine/arginine-rich protein belonging to the family of SR proteins that are crucial regulators of constitutive and alternative pre-mRNA splicing
  • did not affect tau transcription, but stabilized tau mRNA by binding to the SC35-like element of exon 10
  • new function of SRSF2 in the process of cellular senescence and CDKN1A is a key target of SRSF2 in this setting
  • SRSF2 is a cell cycle-regulated protein involved in entry and progression into S phase
  • new role of SRSF2 in the control of cell cycle progression suggesting functional link between SRSF2 and E2F1 proteins
  • SRSF2 is a unique SR protein that activates transcription in a position-dependent manner while three other SR proteins enhance translation in a position-independent fashion
  • intact SRSF2 is essential for the functional integrity of the hematopoietic system and that its mutations likely contribute to development of myelodysplastic syndromes
  • is an RNA-binding protein that plays important roles in splicing of mRNA precursors
  • SRSF2 governs splicing of multiple genes involved in the stress-induced cell death pathway in the liver
  • is a key regulator of RNA splicing dysregulation in cancer, with possible clinical implications as a candidate prognostic factor in patients with hepatocellular carcinoma (HCC)
  • SRSF2 mutations drive oncogenesis by activating a global program of aberrant alternative splicing in hematopoietic cells
  • SRSF2 and U2AF1 mutations have cell context-specific effects and that the generation of myeloid disease phenotype by mutations in the genes coding these two proteins likely involves different intracellular mechanisms
  • is a gene encoding critical spliceosomal proteins
  • SRSF2 facilitates exon exclusion by activating a cryptic 3'AG' and inhibiting downstream intron splicing
  • CELLULAR PROCESS nucleotide, RNA splicing
    text mRNA
    a component
  • of the E commitnent in the spliceosome assembly pattern
  • can form a complex with splicing factor SFRS2 and plays an important role in constitutive pre-mRNA splicing, alternative splicing, and transcriptional activation
    small molecule
  • ELF5-binding proteins that could activate splicing of an enhancer-dependent splicing reporter through ELF5
  • CIR1 interact with U2AF1 through the BA domain, with SRSF2 and SF2/ASF through the RS domain, and with RP9 outside the BA domain
  • direct transcriptional target of E2F1
  • interacting with KAT5 (acetylates SRSF2 on its lysine 52 residue inside the RNA recognition motif, and promotes its proteasomal degradation)
  • ZRSR2 physically interacts with U2AF2, as well as SRSF1 and SRSF2, with a distinct function from its homologue, U2AF1
  • SRSF2 is a new transcriptional target of E2F1 and both proteins cooperate to induce apoptosis in non-small cell lung carcinoma
  • SRSF2 promotes exon 11 inclusion of MST1R proto-oncogene through targeting exon 11
  • aberrant INTS3 splicing contributed to leukaemogenesis in concert with mutant IDH2 and was dependent on mutant SRSF2 binding to cis elements in INTS3 mRNA and increased DNA methylation of INTS3
  • cell & other
    activated by E2F12 (in response to DNA-damaging agents and is required for apoptosis in response to these drugs)
    repressed by PNN, that induces reduced expression of SRSF2
    Other lysine acetylation is a crucial post-translational modification regulating SRSF2 protein level and activity in response to genotoxic stress
    corresponding disease(s)
    Other morbid association(s)
    TypeGene ModificationChromosome rearrangementProtein expressionProtein Function
    constitutional     --over  
    lowering the level of secreted Abeta APP and may have a role in treating Alzheimer's disease
    tumoral germinal mutation      
    in myelodysplasia , significantly related to the shorter overall-survival in patients, which may consider as an adverse prognostic risk factor
    tumoral germinal mutation      
    in chronic myelomonocytic leukemia
    tumoral     --over  
    frequently in human hepatocellular carcinoma (HCC), where this event is associated with poor prognosis in patients
    constitutional germinal mutation      
    P95H mutation positively or negatively alters the binding affinity of SRSF2 for cognate RNA sites in target transcripts, leading to misregulation of exon inclusion
    tumoral     --low  
    decreased expression of SRSF2 in Clear cell renal cell carcinoma (ccRCC) contributes to protection of cancer cells viability
    constitutional       loss of function
    inactivation of SRSF2 in liver caused dysregulated splicing events and hepatic metabolic disorders, which trigger endoplasmic reticulum stress, oxidative stress, and finally liver failure
    constitutional     --over  
    SRSF2, as well as another tau splicing factor, TRA2B, are increased in brains of Progressive Supranuclear Palsy (PSP) patients
    Variant & Polymorphism
    Candidate gene
    Therapy target