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Gene Review

SNRNP27  -  small nuclear ribonucleoprotein 27kDa...

Homo sapiens

Synonyms: 27K, Nucleic acid-binding protein RY-1, RY1, U4/U6.U5 small nuclear ribonucleoprotein 27 kDa protein, U4/U6.U5 snRNP 27 kDa protein, ...
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Disease relevance of RY1

  • All the aberrant RY-1 cDNAs derived from TL-Su cells terminated at the poly(A) site of the R region of the HTLV-1 long terminal repeat and initiated in the intron, approx. 800 bp upstream from the putative second exon [1].
  • By analysing a genomic DNA clone derived from the human T cell lymphotropic virus type 1 (HTLV-1)-infected cell line, TL-Su, we found that an integrated HTLV-1 provirus interrupted the poly(A) signal-containing exon of a novel gene, RY-1 [1].
  • In murine erythroleukemia cells three mature glycophorins (gp-2, gp-3, 34K) and four putative precursors (21K, 23K, 26K, and 27K) are expressed [2].
  • Synechococcus 6301 mutant, strain AN112, produces phycobilisomes containing two major biliproteins, phycocyanin and allophycocyanin, and two major linker polypeptides of 27 and 75 kilodaltons (27K and 75K) [3].
  • In adenovirus type 16, eight other major polypeptides are found, with apparent molecular weights of 59,000 (59K), 46K, 31K, 30K, 28K, 27K, 26K, and 19K [4].

High impact information on RY1

  • First, signal sequences, if present, are apparently not cleaved upon translocation across the endoplasmic reticulum membrane; second, the 26K and 27K putative precursors are inefficiently translocated [2].
  • A comparison of the immunologically reactive components of the highly conserved Sm and RNP autoantigens from various mammalian tissue sources suggested the complete absence of a major 26K to 27K Sm-specific polypeptide in rabbit thymus extracts prepared by conventional procedures [5].
  • The 27K protein can be phosphorylated in vitro by the snRNP-associated protein kinase and exhibits several isoelectric variants upon 2D gel electrophoresis [6].
  • Thus, the tri-snRNP-specific 27K protein could potentially be involved in SR protein-mediated protein/protein interactions and, additionally, its phosphorylation state could modulate pre-mRNA splicing [6].
  • None of the transfected NIH 3T3 cells processed much pro-IGF-II intracellularly, as the appMr 21K, 23K, and 27K forms had terminal E domain amino acid sequences that were recognized by antibodies to the homologous rat peptide sequence Met117 to Gln156 [7].

Chemical compound and disease context of RY1

  • Biosynthesis of a novel thyroxine-binding protein (27K protein) in human hepatoma (Hep G2) cells [8].

Biological context of RY1

  • Nucleotide sequence analysis of a cDNA derived from Jurkat cells revealed that the normal RY-1 mRNA could encode a novel protein that has an unique primary structure, suggesting that a nucleic acid binding property was involved [1].
  • The kinetics of secretion of 27K protein were similar to those of albumin and faster than those of TBG, which is also in keeping with the nonglycoprotein nature of 27K protein [8].
  • The absence of carbohydrates was further supported by the observation that [3H]mannose was not covalently bound to the 27K protein when Hep G2 cells were labeled with [3H]mannose, nor was there a shift in apparent mol wt when the cells were treated with the glycosylation inhibitor tunicamycin [8].
  • The 27K ORF probably encodes the viral coat protein (CP), based on both the existence of some conserved sequences observed in many other rod-shaped or flexuous virus CPs and an overall amino acid sequence similarity to potexvirus and carlavirus CPs [9].

Anatomical context of RY1

  • The mRNA coding for this protein was characterized by immunoprecipitation of [125I]T4 bound to 27K protein secreted into the medium of oocytes injected with total Hep G2 RNA [8].

Associations of RY1 with chemical compounds

  • Purification and partial characterization of a novel thyroxine-binding protein (27K protein) from human plasma [10].
  • By contrast, when a radioiodinated derivative of the octapeptide analog octreotide ([125I-Tyr3]SMS) was used as ligand, the 27K protein was preferentially labeled, whereas the 57K and 42K bands were detected only as minor components [11].
  • On immunoblotting, only one component with an Mr of 27K was detected 2 to 24 h after infection of cells with CPV in either the presence or absence of Ara C [12].
  • Instead of the normal peptide pattern--which is comprised of three heavy chain fragments (27K, 50K, and 20K)--only two fragments (27K and 20K) appeared on the sodium dodecyl sulfate-gel electrophoregram after limited tryptic digestion of thermally treated S-1 [13].
  • The molecular weight of PrP 27-30 was reduced from 27K-30K by PNGase F digestion to 20K-22K while anhydrous hydrogen fluoride or trifluoromethanesulfonic acid treatment reduced the molecular weight to 19K-21K and 20K-22K, respectively [14].

Other interactions of RY1

  • The [U4/U6.U5] tri-snRNP-specific 27K protein is a novel SR protein that can be phosphorylated by the snRNP-associated protein kinase [6].

Analytical, diagnostic and therapeutic context of RY1

  • In the current study, growth hormone (GH) variants were measured by Western blotting techniques, which resulted in the quantitation of 4 GH size variants: 27K (27,000 Daltons), 22K, 20K, and 17K [15].
  • In immunoelectrophoresis in agar at pH 8.6, 27K protein moves slightly faster than TBG [10].
  • Four major structural polypeptides of MrS 60K, 52K, 33K and 27K were detected by SDS-PAGE [16].
  • However, direct homogenization of liver tissue in gel electrophoresis sample buffer, followed by PAGE and immunoblotting resulted in identification of HDV-associated proteins of 27K and 29K, indicating that HDV proteins in liver tissue are the same size as those in serum, but that they degrade rapidly [17].


  1. Altered expression of a novel cellular gene as a consequence of integration of human T cell lymphotropic virus type 1. Nakamura, Y., Moriuchi, R., Nakayama, D., Yamashita, I., Higashiyama, Y., Yamamoto, T., Kusano, Y., Hino, S., Miyamoto, T., Katamine, S. J. Gen. Virol. (1994) [Pubmed]
  2. Anomalies in the translocation and processing of glycophorin precursors in murine erythroleukemia cells. Ulmer, J.B., Palade, G.E. J. Biol. Chem. (1989) [Pubmed]
  3. Molecular architecture of a light-harvesting antenna. Isolation and characterization of phycobilisome subassembly particles. Yamanaka, G., Lundell, D.J., Glazer, A.N. J. Biol. Chem. (1982) [Pubmed]
  4. Structural polypeptides of adenovirus type 16 incomplete particles. Winberg, G., Wadell, G. J. Virol. (1977) [Pubmed]
  5. Isolation of intact Sm/RNP antigens from rabbit thymus. Billings, P.B., Hoch, S.O. J. Immunol. (1983) [Pubmed]
  6. The [U4/U6.U5] tri-snRNP-specific 27K protein is a novel SR protein that can be phosphorylated by the snRNP-associated protein kinase. Fetzer, S., Lauber, J., Will, C.L., Lührmann, R. RNA (1997) [Pubmed]
  7. The expression and characterization of human recombinant proinsulin-like growth factor II and a mutant that is defective in the O-glycosylation of its E domain. Yang, C.Q., Zhan, X., Hu, X., Kondepudi, A., Perdue, J.F. Endocrinology (1996) [Pubmed]
  8. Biosynthesis of a novel thyroxine-binding protein (27K protein) in human hepatoma (Hep G2) cells. Bartalena, L., Grimaldi, S., Fleischmann, K., Robbins, J. Endocrinology (1986) [Pubmed]
  9. Novel rod-shaped viruses isolated from garlic, Allium sativum, possessing a unique genome organization. Sumi, S., Tsuneyoshi, T., Furutani, H. J. Gen. Virol. (1993) [Pubmed]
  10. Purification and partial characterization of a novel thyroxine-binding protein (27K protein) from human plasma. Grimaldi, S., Bartalena, L., Carlini, F., Robbins, J. Endocrinology (1986) [Pubmed]
  11. Evidence for multiple protein constituents of the somatostatin receptor in pituitary tumor cells: affinity cross-linking and molecular characterization. Murthy, K.K., Srikant, C.B., Patel, Y.C. Endocrinology (1989) [Pubmed]
  12. Virus-specific early antigen expressed in the nucleus of cowpox virus-infected cells. Kitamoto, N., Hiroi, K., Miyamoto, K., Tanaka, T., Miyamoto, H. J. Gen. Virol. (1990) [Pubmed]
  13. Effect of mild heat treatment on the ATPase activity and proteolytic sensitivity of myosin subfragment-1. Setton, A., Muhlrad, A. Arch. Biochem. Biophys. (1984) [Pubmed]
  14. Asparagine-linked glycosylation of the scrapie and cellular prion proteins. Haraguchi, T., Fisher, S., Olofsson, S., Endo, T., Groth, D., Tarentino, A., Borchelt, D.R., Teplow, D., Hood, L., Burlingame, A. Arch. Biochem. Biophys. (1989) [Pubmed]
  15. Potential abnormalities in molecular forms of growth hormone in schizophrenia: a pilot study. Warner, M.D., Sinha, Y.N., Peabody, C.A. Biol. Psychiatry (1993) [Pubmed]
  16. Biophysical and biochemical properties of an unusual birnavirus pathogenic for rotifers. Comps, M., Mari, J., Poisson, F., Bonami, J.R. J. Gen. Virol. (1991) [Pubmed]
  17. Characterization of proteins associated with hepatitis delta virus. Roggendorf, M., Pahlke, C., Böhm, B., Rasshofer, R. J. Gen. Virol. (1987) [Pubmed]
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