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Serine/arginine-rich splicing factor 2

SC35, splicing factor SC35
The protein encoded by this gene is a member of the serine/arginine (SR)-rich family of pre-mRNA splicing factors, which constitute part of the spliceosome. Each of these factors contains an RNA recognition motif (RRM) for binding RNA and an RS domain for binding other proteins. The RS domain is rich in serine and arginine residues and facilitates interaction between different SR splicing factors. In addition to being critical for mRNA splicing, the SR proteins have also been shown to be involved in mRNA export from the nucleus and in translation. Two transcript variants encoding the same protein and one non-coding transcript variant have been found for this gene. In addition, a pseudogene of this gene has been found on chromosome 11. [provided by RefSeq, Sep 2010] (from NCBI)
Top mentioned proteins: CAN, POLYMERASE, ACID, HAD, 9G8
Papers using SC35 antibodies
The 4q subtelomere harboring the FSHD locus is specifically anchored with peripheral heterochromatin unlike most human telomeres
Lawrence Jeanne B. et al., In The Journal of Cell Biology, 2003
... Pollard, Scripps Research Institute, La Jolla, CA), mouse anti-SC35 (Sigma-Aldrich), rabbit anti-lamin (Cell Signaling), and mouse anti-nucleopore (Affinity ...
Nuclear localization of EGF receptor and its potential new role as a transcription factor
Gottardi Cara, In PLoS ONE, 2000
... Monoclonal antibody against sc35 (556363) was obtained from BD Biosciences (San Jose CA) ...
Hypophosphorylated SR splicing factors transiently localize around active nucleolar organizing regions in telophase daughter nuclei
Spector David L. et al., In The Journal of Cell Biology, 1987
... PCR was used to generate a restriction site at the stop codon of human SC35 cDNA for convenient subcloning into pEYFP-N1 (CLONTECH Laboratories, Inc.) or a vector ...
Papers on SC35
HIV-1-Tat Protein Inhibits SC35-mediated Tau Exon 10 Inclusion through Up-regulation of DYRK1A Kinase.
Peruzzi et al., Richmond, United States. In J Biol Chem, Jan 2016
The splicing factor SC35/SRSF2 binds to nuclear RNA and facilitates the incorporation of exon 10 in the TAU molecule.
HIV-1 splicing is controlled by local RNA structure and binding of splicing regulatory proteins at the major 5' splice site.
Das et al., Amsterdam, Netherlands. In J Gen Virol, Jul 2015
In addition, splicing may be modulated by binding of splicing regulatory (SR) proteins, in particular SF2/ASF (SRSF1), SC35 (SRSF2), SRp40 (SRSF5) and SRp55 (SRSF6), to sequence elements in the SD region.
Molecular Characterization of UKp83/68, a Widespread Nuclear Proteins that Bind Poly(A) and Colocalize with a Nuclear Speckle's Component.
Hara et al., Tokyo, Japan. In J Med Dent Sci, 2014
The UKp83/68 protein localized within the nucleus with a fibrous or punctate structure that reflected the distribution of SC35, a known marker of nuclear speckles which are nuclear domains enriched in pre-mRNA splicing factors and located in the interchromatin regions of the nucleoplasm of mammalian cells.
PKC-Theta is a Novel SC35 Splicing Factor Regulator in Response to T Cell Activation.
Rao et al., Canberra, Australia. In Front Immunol, 2014
Collectively, our findings suggest that nuclear PKC-θ is a novel regulator of the key splicing factor SC35 in T cells.
Interplay between the alpharetroviral Gag protein and SR proteins SF2 and SC35 in the nucleus.
Parent et al., State College, United States. In Front Microbiol, 2014
In this report, we observed that RSV Gag.L219A foci appeared to be tethered in the nucleus, partially co-localizing with the splicing speckle components SC35 and SF2.
Splicing factor mutations and cancer.
Ogawa et al., Kyoto, Japan. In Wiley Interdiscip Rev Rna, 2014
These mutations were heterozygous and mainly affected U2AF1 (U2AF35), SRSF2 (SC35), SF3B1 (SF3B155 or SAP155), and ZRSR2 (URP), which are engaged in the initial steps of RNA splicing, including 3' splice-site recognition, and occur in a large mutually exclusive pattern, suggesting a common impact of these mutations on RNA splicing.
SR proteins collaborate with 7SK and promoter-associated nascent RNA to release paused polymerase.
Fu et al., Wuhan, China. In Cell, 2013
We report that SRSF2 (also known as SC35, an SR-splicing factor) is part of the 7SK complex assembled at gene promoters and plays a direct role in transcription pause release.
Serine-arginine protein kinases: new players in neurodegenerative diseases?
Ye et al., In Rev Neurosci, 2012
They are mainly involved in regulating pre-mRNA splicing via phosphorylating splicing factors, such as ASF/SF2 and SC35.
Mutation screening of IRF6 among families with non-syndromic oral clefts and identification of two novel variants: review of the literature.
Zilfalil et al., Malaysia. In Eur J Med Genet, 2012
In silico analysis revealed that both c.1380G>; T and c.-75-23G>; C variants may disrupts a putative exonic splicing enhancer and intronic splicing binding site for SC35, respectively.
Genetic analysis of patients with leukemic transformation of myeloproliferative neoplasms shows recurrent SRSF2 mutations that are associated with adverse outcome.
Verstovsek et al., New York City, United States. In Blood, 2012
SRSF2 mutations contribute to the pathogenesis of LT (leukemic transformation) and may guide novel therapeutic approaches for myeloproliferative neoplasms patients who undergo LT.
Frequency and prognostic impact of mutations in SRSF2, U2AF1, and ZRSR2 in patients with myelodysplastic syndromes.
Heuser et al., Hannover, Germany. In Blood, 2012
A negative prognostic impact of SRSF2 mutations in myelodysplastic syndromes. SRSF2 mutations may become useful for clinical risk stratification and treatment decisions in the future.
Mutations in the spliceosome machinery, a novel and ubiquitous pathway in leukemogenesis.
Maciejewski et al., Cleveland, United States. In Blood, 2012
U2AF1 and SRSF2 mutations are frequent in chronic myelomonocytic leukemia and advanced forms of MDS. U2AF1 and SRSF2 mutations are predictive for shorter survival.
The structure and selectivity of the SR protein SRSF2 RRM domain with RNA.
Lian et al., Liverpool, United Kingdom. In Nucleic Acids Res, 2012
The interactions involving the L3 loop, N- and C-termini of the RNA recognition motifs domain of SRSF2 are collectively important for determining selectivity between SRSF2 and RNA.
Spliceosomal gene aberrations are rare, coexist with oncogenic mutations, and are unlikely to exert a driver effect in childhood MDS and JMML.
European Working Group of MDS in Childhood et al., Freiburg, Germany. In Blood, 2012
SF3B1, U2AF35, SRSF2 and NRAS mutation are unlikely to operate as driver mutations in patients with myelodysplastic syndrome or juvenile myelomonocytic leukemia.
Human papillomavirus regulation of SR proteins.
Graham et al., Glasgow, United Kingdom. In Biochem Soc Trans, 2010
The HPV transcription/replication factor E2 (early 2) specifically up-regulates expression of the SR proteins SF2/ASF (splicing factor 2/alternative splicing factor), SRp20 and SC35 in infected epithelial cells.
Changing nuclear landscape and unique PML structures during early epigenetic transitions of human embryonic stem cells.
Lawrence et al., Worcester, United States. In J Cell Biochem, 2009
Observations of centromeres, telomeres, SC35 speckles, Cajal Bodies, lamin A/C and emerin, nuclear shape and size demonstrate a very different "nuclear landscape" in hESC.
Specific phosphorylation of SR proteins by mammalian DNA topoisomerase I.
Tazi et al., Montpellier, France. In Nature, 1996
These include members of the SR-protein family (SC35, SF2/ASF), the U1 small nuclear (sn) RNP protein (U1-70K) and the U2 snRNP auxiliary factor (U2AF).
Specific interactions between proteins implicated in splice site selection and regulated alternative splicing.
Maniatis et al., Cambridge, United States. In Cell, 1994
We report that the splicing factors SC35 and SF2/ASF specifically interact with both the integral U1 small nuclear ribonucleoprotein (snRNP U1-70K) and with the 35 kd subunit of the splicing factor U2AF (U2AF35).
Specific commitment of different pre-mRNAs to splicing by single SR proteins.
Fu, San Diego, United States. In Nature, 1993
These SR proteins, which include SC35 and SF2/ASF, are conserved from Drosophila to man, are required for early steps of spliceosome assembly and can influence splice-site selections.
A three-dimensional view of precursor messenger RNA metabolism within the mammalian nucleus.
Lawrence et al., Worcester, United States. In Science, 1993
Spliceosome assembly factor SC-35 localized within the center of individual domains.
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