Gene Symbol: SRP14
Description: signal recognition particle 14
Alias: ALURBP, signal recognition particle 14 kDa protein, 18 kDa Alu RNA-binding protein, homologous Alu RNA binding protein
Species: human
Products:     SRP14

Top Publications

  1. Chang D, Nelson B, Bilyeu T, Hsu K, Darlington G, Maraia R. A human Alu RNA-binding protein whose expression is associated with accumulation of small cytoplasmic Alu RNA. Mol Cell Biol. 1994;14:3949-59 pubmed
    ..The possibility that the primate-specific structure of this protein may have contributed to Alu evolution is considered. ..
  2. Bovia F, Wolff N, Ryser S, Strub K. The SRP9/14 subunit of the human signal recognition particle binds to a variety of Alu-like RNAs and with higher affinity than its mouse homolog. Nucleic Acids Res. 1997;25:318-26 pubmed
    ..RNAs analyzed and this difference is not explained by the additional C-terminal domain present in the anthropoid SRP14. The conservation of high affinity interactions between SRP9/14 and Alu-like RNAs strongly indicates that these ..
  3. Mary C, Scherrer A, Huck L, Lakkaraju A, Thomas Y, Johnson A, et al. Residues in SRP9/14 essential for elongation arrest activity of the signal recognition particle define a positively charged functional domain on one side of the protein. RNA. 2010;16:969-79 pubmed publisher
    ..identified two patches of basic amino acid residues that are essential for activity, whereas the internal loop of SRP14 was found to be dispensable...
  4. Bovia F, Fornallaz M, Leffers H, Strub K. The SRP9/14 subunit of the signal recognition particle (SRP) is present in more than 20-fold excess over SRP in primate cells and exists primarily free but also in complex with small cytoplasmic Alu RNAs. Mol Biol Cell. 1995;6:471-84 pubmed
    ..The Alu RNAs of primate cells are believed to be derived from SRP RNA and have been shown to bind to an SRP14-related protein in vitro...
  5. Weichenrieder O, Wild K, Strub K, Cusack S. Structure and assembly of the Alu domain of the mammalian signal recognition particle. Nature. 2000;408:167-73 pubmed
    The Alu domain of the mammalian signal recognition particle (SRP) comprises the heterodimer of proteins SRP9 and SRP14 bound to the 5' and 3' terminal sequences of SRP RNA...
  6. Lakkaraju A, Mary C, Scherrer A, Johnson A, Strub K. SRP keeps polypeptides translocation-competent by slowing translation to match limiting ER-targeting sites. Cell. 2008;133:440-51 pubmed publisher
    ..We complemented mammalian cells depleted of SRP14 by expressing mutant versions of the protein lacking the elongation arrest function...
  7. Zhao G, Hou J, Xu G, Xiang A, Kang Y, Yan Y, et al. Cellular microRNA miR-10a-5p inhibits replication of porcine reproductive and respiratory syndrome virus by targeting the host factor signal recognition particle 14. J Gen Virol. 2017;98:624-632 pubmed publisher
    ..A direct interaction between miR-10a-5p and signal recognition particle 14 (SRP14) was confirmed using bioinformatic prediction and experimental verification...
  8. Strub K, Walter P. Assembly of the Alu domain of the signal recognition particle (SRP): dimerization of the two protein components is required for efficient binding to SRP RNA. Mol Cell Biol. 1990;10:777-84 pubmed
    ..This function is carried out by the Alu domain, which consists of two proteins, SRP9 and SRP14, and the portion of SRP (7SL) RNA which is homologous to the Alu family of repetitive sequences...
  9. Strub K, Walter P. Isolation of a cDNA clone of the 14-kDa subunit of the signal recognition particle by cross-hybridization of differently primed polymerase chain reactions. Proc Natl Acad Sci U S A. 1989;86:9747-51 pubmed
    ..Using an enhancement of the polymerase chain reaction (PCR) technique, we have isolated a complementary DNA encoding SRP14 (14-kDa subunit), one of six proteins contained in the signal recognition particle (SRP)...

More Information


  1. Yoshida M, Kabe Y, Wada T, Asai A, Handa H. A new mechanism of 6-((2-(dimethylamino)ethyl)amino)-3-hydroxy-7H-indeno(2,1-c)quinolin-7-one dihydrochloride (TAS-103) action discovered by target screening with drug-immobilized affinity beads. Mol Pharmacol. 2008;73:987-94 pubmed
    ..The results revealed that TAS-103 disrupts SRP complex formation and reduces the amount of SRP14 and SRP19...
  2. Postel Vinay S, Veron A, Tirode F, Pierron G, Reynaud S, Kovar H, et al. Common variants near TARDBP and EGR2 are associated with susceptibility to Ewing sarcoma. Nat Genet. 2012;44:323-7 pubmed publisher
    ..Variants at these loci were associated with expression levels of TARDBP, ADO (encoding cysteamine dioxygenase) and EGR2. ..
  3. Piazzon N, Schlotter F, Lefebvre S, Dodré M, Mereau A, Soret J, et al. Implication of the SMN complex in the biogenesis and steady state level of the signal recognition particle. Nucleic Acids Res. 2013;41:1255-72 pubmed publisher
    ..Our data show that reduced levels of the SMN protein lead to defect in SRP steady-state level and describe the SMN complex as the first identified cellular factor required for SRP biogenesis. ..
  4. Ivanova E, Berger A, Scherrer A, Alkalaeva E, Strub K. Alu RNA regulates the cellular pool of active ribosomes by targeted delivery of SRP9/14 to 40S subunits. Nucleic Acids Res. 2015;43:2874-87 pubmed publisher
    ..Alu RNPs also inhibit the translation of cellular mRNAs resuming translation after stress and of viral mRNAs suggesting a role of Alu RNPs in adapting the translational output in response to stress and viral infection. ..