The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

SRSF10  -  serine/arginine-rich splicing factor 10

Homo sapiens

Synonyms: 40 kDa SR-repressor protein, FUS-interacting serine-arginine-rich protein 1, FUSIP1, FUSIP2, NSSR, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of FUSIP1

  • In vivo splicing assays indicated that SC35 and TASR influence splice site selection of adenovirus E1A pre-mRNA [1].
  • Our recent studies suggest that disruption of TASR-mediated pre-mRNA splicing is involved in the pathogenesis of human leukemia and sarcomas [2].
  • Characterization and expression of the human gene encoding two translocation liposarcoma protein-associated serine-arginine (TASR) proteins [2].

High impact information on FUSIP1

  • To investigate the cellular function of SRp38, we examined its possible role in cell cycle control [3].
  • The SR protein SRp38 represses splicing in M phase cells [3].
  • Using chimeric SRp38/SC35 proteins, we show that SC35-RBD/SRp38-RS can function as a general splicing activator and that the dephosphorylated version can act as a strong splicing repressor [4].
  • The SR protein SRp38 is a general splicing repressor that is activated by dephosphorylation during mitosis and in response to heat shock [4].
  • In transient-transfection assays, the TLS-ERG fusion protein inhibits E1A pre-mRNA splicing mediated by these TLS-associated SR proteins (TASR), and stable expression of the TLS-ERG fusion protein in K562 cells alters the splicing profile of CD44 mRNA [5].

Biological context of FUSIP1

  • The mRNA transcripts for TASR-1 and -2 share an identical sequence at the 5' untranslated region (5' UTR) and in part of the coding region; however the other regions of the transcripts diverge from each other and it was not clear whether the differences resulted from alternative splicing or transcription from two distinct genes [2].
  • Here we describe the assignment of both TASR cDNAs to the same 16 kb DNA segment located on chromosome 1 [2].
  • When cloned into a luciferase reporter and transfected into human cells, the TASR promoter construct generated luciferase activity that was at least 2000 fold greater than the promoterless plasmid [2].
  • In addition, multiple polyadenylation sites and a rare U12-type intron were found within the TASR gene [2].
  • Transcription initiation site of the TASR gene was determined by primer extension; analysis of the TASR promoter revealed that it lacks the TATA box but contains a GC-rich sequence [2].

Anatomical context of FUSIP1

  • Of special interest is the finding that TASR-1 could down-regulate expression of type X collagen, a hallmark of hypertrophic chondrocytes [6].

Associations of FUSIP1 with chemical compounds

  • The phosphatase inhibitor calyculin A prevented dephosphorylation of SRp38 during a heat shock and caused complete rephosphorylation of SRp38 after a heat shock, indicating that cells recovering from a heat shock are not deficient in kinase activity [7].

Physical interactions of FUSIP1

  • We further show that dephosphorylated SRp38 interacts with a U1 small nuclear ribonucleoprotein particle (snRNP) protein, and that this interaction interferes with 5'-splice-site recognition by the U1 snRNP [8].

Regulatory relationships of FUSIP1

  • Hsp27 enhances recovery of splicing as well as rephosphorylation of SRp38 after heat shock [7].

Other interactions of FUSIP1

  • Because of the similarity to SR proteins we have named these proteins SRrp40 and SRrp35, respectively, for SR-repressor proteins of approximately 40 and approximately 35 kDa [9].
  • The effect of Hsp27 on rephosphorylation of SRp38 required phosphorylatable Hsp27 [7].
  • Raising the Hsp70 level by either a pre-heat shock or by exogenous expression had no effect on either dephosphorylation of SRp38 during heat shock or rephosphorylation after heat shock [7].
  • A Hsp90 client protein was required for the effect of Hsp27 on recovery of spicing and on rephosphorylation of SRp38 [7].

Analytical, diagnostic and therapeutic context of FUSIP1

  • Northern blot analysis showed that at least five different TASR-1 and -2 transcripts are expressed in a broad range of human tissues [2].
  • RT-PCR analysis revealed that TASR-1, but not TASR-2, influenced alternative splicing of type II and type XI collagens in ATDC5 cells [6].
  • Results from our microarray analysis of ATDC5 cells showed that TASR-1 and TASR-2 differentially affect genes involved in the differentiation of chondrocytes [6].


  1. Oncoprotein TLS interacts with serine-arginine proteins involved in RNA splicing. Yang, L., Embree, L.J., Tsai, S., Hickstein, D.D. J. Biol. Chem. (1998) [Pubmed]
  2. Characterization and expression of the human gene encoding two translocation liposarcoma protein-associated serine-arginine (TASR) proteins. Clinton, J.M., Chansky, H.A., Odell, D.D., Zielinska-Kwiatkowska, A., Hickstein, D.D., Yang, L. Gene (2002) [Pubmed]
  3. The SR protein SRp38 represses splicing in M phase cells. Shin, C., Manley, J.L. Cell (2002) [Pubmed]
  4. Multiple properties of the splicing repressor SRp38 distinguish it from typical SR proteins. Shin, C., Kleiman, F.E., Manley, J.L. Mol. Cell. Biol. (2005) [Pubmed]
  5. TLS-ERG leukemia fusion protein inhibits RNA splicing mediated by serine-arginine proteins. Yang, L., Embree, L.J., Hickstein, D.D. Mol. Cell. Biol. (2000) [Pubmed]
  6. TASR-1 regulates alternative splicing of collagen genes in chondrogenic cells. Matsushita, H., Blackburn, M.L., Klineberg, E., Zielinska-Kwiatkowska, A., Bolander, M.E., Sarkar, G., Suva, L.J., Chansky, H.A., Yang, L. Biochem. Biophys. Res. Commun. (2007) [Pubmed]
  7. Hsp27 enhances recovery of splicing as well as rephosphorylation of SRp38 after heat shock. Marin-Vinader, L., Shin, C., Onnekink, C., Manley, J.L., Lubsen, N.H. Mol. Biol. Cell (2006) [Pubmed]
  8. Dephosphorylated SRp38 acts as a splicing repressor in response to heat shock. Shin, C., Feng, Y., Manley, J.L. Nature (2004) [Pubmed]
  9. Serine-arginine (SR) protein-like factors that antagonize authentic SR proteins and regulate alternative splicing. Cowper, A.E., Cáceres, J.F., Mayeda, A., Screaton, G.R. J. Biol. Chem. (2001) [Pubmed]
WikiGenes - Universities