RecName: Full=Signal recognition particle subunit SRP14; AltName: Full - Protein

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A truncation in the 14 kDa protein of the signal recognition particle leads to tertiary structure changes in the RNA and abolishes the elongation arrest activity of the particle. [Nucleic Acids Res. 1997]
A truncation in the 14 kDa protein of the signal recognition particle leads to tertiary structure changes in the RNA and abolishes the elongation arrest activity of the particle.
Thomas Y, Bui N, Strub K. Nucleic Acids Res. 1997 May 15; 25(10):1920-9.
The Alu domain homolog of the yeast signal recognition particle consists of an Srp14p homodimer and a yeast-specific RNA structure. [RNA. 1999]
The Alu domain homolog of the yeast signal recognition particle consists of an Srp14p homodimer and a yeast-specific RNA structure.
Strub K, Fornallaz M, Bui N. RNA. 1999 Oct; 5(10):1333-47.
The sequence of a 16,691 bp segment of Saccharomyces cerevisiae chromosome IV identifies the DUN1, PMT1, PMT5, SRP14 and DPR1 genes, and five new open reading frames. [Yeast. 1996]
The sequence of a 16,691 bp segment of Saccharomyces cerevisiae chromosome IV identifies the DUN1, PMT1, PMT5, SRP14 and DPR1 genes, and five new open reading frames.
Boskovic J, Soler-Mira A, García-Cantalejo JM, Ballesta JP, Jiménez A, Remacha M. Yeast. 1996 Oct; 12(13):1377-84.

RefSeq protein
See the reference protein sequence for RNA-binding signal recognition particle subunit SRP14 (NP_010191.1).

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MODBASE, Database of Comparative Protein Structure Models (Sali Lab/UCSF) [MODBASE, Database of Comparat...]
MODBASE, Database of Comparative Protein Structure Models (Sali Lab/UCSF)
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Protein