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Gene Review

SNRPC  -  small nuclear ribonucleoprotein polypeptide C

Homo sapiens

Synonyms: U1 small nuclear ribonucleoprotein C, U1 snRNP C, U1-C, U1C, Yhc1
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Disease relevance of SNRPC

  • After cloning and expression of a full length complementary DNA (cDNA) encoding the U1-C protein, several truncated mutants of the cDNA were constructed and expressed in E. coli [1].
  • Both standard and SPOTscan methods were evaluated with antibodies raised in rabbits against synthetic peptides of U1C and sera from patients with autoimmune diseases [2].

High impact information on SNRPC

  • The results argue that binding of TIA-1 in the vicinity of a 5' ss helps to stabilize U1 snRNP recruitment, at least in part, via a direct interaction with U1-C, thus providing one molecular mechanism for the function of this splicing regulator [3].
  • We identified a hypothetical open reading frame in Saccharomyces cerevisiae as the yeast homolog of the human U1C protein [4].
  • Individual crosslinks between the U1-70K and the common D2 or B'/B protein, as well as between U1-C and B'/B, were detected [5].
  • Importantly, co-expression of U1C represses EWS/FLI-mediated transactivation, demonstrating that this interaction can have functional ramifications [6].
  • Our findings demonstrate that U1C, a well characterized splicing protein, can also function in transcriptional regulation [6].

Biological context of SNRPC

  • In this study, a putative member of SNRPC was identified from Carassius auratus gibelio oocyte cDNA library [7].
  • Using a zinc affinity labeling method, we further showed that the N-terminal U1C peptide containing a zinc-finger motif (peptide 5-34) effectively binds65Zn2+ [8].
  • Analyses of mutant U1C proteins in an in vitro dimerization assay and the yeast two hybrid system revealed that amino acids within the CH motif, i.e. between positions 22 and 30, are required for homodimerization [9].

Anatomical context of SNRPC


Physical interactions of SNRPC

  • No structural information on U1C protein either in its free state or bound to the spliceosomal U1 small nuclear ribonucleoprotein (snRNP) particle is currently available [8].

Other interactions of SNRPC

  • At least three linear regions but not the zinc-finger domain of U1C protein are exposed at the surface of the protein in solution and on the human spliceosomal U1 snRNP particle [8].
  • A consequence of this organization is that the U1-C protein makes direct contacts with the site, as it becomes cross-linked to the RNA oligo upon exposition of the reactions to shortwave UV light [11].

Analytical, diagnostic and therapeutic context of SNRPC

  • Here we show by microinjection of Xenopus laevis oocytes that the third U1 snRNP-specific protein, U1C, passively enters the nucleus [12].
  • OBJECTIVE: Autoantibodies to U1-C have been considered a minor component of anti-snRNP (nRNP, Sm) response based on Western blotting [13].
  • Human monoclonal autoantibody fragments from combinatorial antibody libraries directed to the U1snRNP associated U1C protein; epitope mapping, immunolocalization and V-gene usage [10].
  • Antibodies against recombinant U1-nRNP proteins (U1-A-, U1-C- and 70K-protein) were determined by ELISA [14].


  1. B cell epitope on the U1 snRNP-C autoantigen contains a sequence similar to that of the herpes simplex virus protein. Misaki, Y., Yamamoto, K., Yanagi, K., Miura, H., Ichijo, H., Kato, T., Mato, T., Welling-Wester, S., Nishioka, K., Ito, K. Eur. J. Immunol. (1993) [Pubmed]
  2. Comparison of two different methods using overlapping synthetic peptides for localizing linear B cell epitopes in the U1 snRNP-C autoantigen. Halimi, H., Dumortier, H., Briand, J.P., Muller, S. J. Immunol. Methods (1996) [Pubmed]
  3. The splicing regulator TIA-1 interacts with U1-C to promote U1 snRNP recruitment to 5' splice sites. Förch, P., Puig, O., Martínez, C., Séraphin, B., Valcárcel, J. EMBO J. (2002) [Pubmed]
  4. Identification and characterization of a yeast homolog of U1 snRNP-specific protein C. Tang, J., Abovich, N., Fleming, M.L., Seraphin, B., Rosbash, M. EMBO J. (1997) [Pubmed]
  5. The association of the U1-specific 70K and C proteins with U1 snRNPs is mediated in part by common U snRNP proteins. Nelissen, R.L., Will, C.L., van Venrooij, W.J., Lührmann, R. EMBO J. (1994) [Pubmed]
  6. The splicing factor U1C represses EWS/FLI-mediated transactivation. Knoop, L.L., Baker, S.J. J. Biol. Chem. (2000) [Pubmed]
  7. Identification of a putative oocyte-specific small nuclear ribonucleoprotein polypeptide C in gibel carp. Wang, H.Y., Zhou, L., Gui, J.F. Comp. Biochem. Physiol. B, Biochem. Mol. Biol. (2007) [Pubmed]
  8. At least three linear regions but not the zinc-finger domain of U1C protein are exposed at the surface of the protein in solution and on the human spliceosomal U1 snRNP particle. Dumortier, H., Klein Gunnewiek, J., Roussel, J.P., van Aarssen, Y., Briand, J.P., van Venrooij, W.J., Muller, S. Nucleic Acids Res. (1998) [Pubmed]
  9. Homodimerization of the human U1 snRNP-specific protein C. Gunnewiek, J.M., van Aarssen, Y., Wassenaar, R., Legrain, P., van Venrooij, W.J., Nelissen, R.L. Nucleic Acids Res. (1995) [Pubmed]
  10. Human monoclonal autoantibody fragments from combinatorial antibody libraries directed to the U1snRNP associated U1C protein; epitope mapping, immunolocalization and V-gene usage. Hoet, R.M., Raats, J.M., de Wildt, R., Dumortier, H., Muller, S., van den Hoogen, F., van Venrooij, W.J. Mol. Immunol. (1998) [Pubmed]
  11. Involvement of U1 small nuclear ribonucleoproteins (snRNP) in 5' splice site-U1 snRNP interaction. Rossi, F., Forné, T., Antoine, E., Tazi, J., Brunel, C., Cathala, G. J. Biol. Chem. (1996) [Pubmed]
  12. Nuclear accumulation of the U1 snRNP-specific protein C is due to diffusion and retention in the nucleus. Klein Gunnewiek, J.M., van Aarssen, Y., van der Kemp, A., Nelissen, R., Pruijn, G.J., van Venrooij, W.J. Exp. Cell Res. (1997) [Pubmed]
  13. Autoantibodies that stabilize U1snRNP are a significant component of human autoantibodies to snRNP and delay proteolysis of sm antigens in vitro. Satoh, M., Akaogi, J., Kuroda, Y., Nacionales, D.C., Yoshida, H., Yamasaki, Y., Reeves, W.H. J. Rheumatol. (2004) [Pubmed]
  14. HLA class II genes and antibodies against recombinant U1-nRNP proteins in patients with systemic lupus erythematosus. SLE Study Group. Yao, Z., Seelig, H.P., Ehrfeld, H., Renz, M., Hartung, K., Deicher, H., Keller, E., Nevinny-Stickel, C., Albert, E.D. Rheumatol. Int. (1994) [Pubmed]
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