60S ribosomal protein L14

Ribosomal protein L14
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols RPL14 ; CAG-ISL-7; CTG-B33; L14; RL14; hRL14
External IDs MGI: 1914365 HomoloGene: 68375 GeneCards: RPL14 Gene
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez 9045 67115
Ensembl ENSG00000188846 ENSMUSG00000025794
UniProt P50914 Q9CR57
RefSeq (mRNA) NM_001034996 NM_025974
RefSeq (protein) NP_001030168 NP_080250
Location (UCSC) Chr 3:
40.46 – 40.47 Mb
Chr 9:
120.57 – 120.57 Mb
PubMed search

60S ribosomal protein L14' is a protein that in humans is encoded by the RPL14 gene.[1][2]

Function

Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a ribosomal protein that is a component of the 60S subunit. The protein belongs to the L14E family of ribosomal proteins. It contains a basic region-leucine zipper (bZIP)-like domain. The protein is located in the cytoplasm. This gene contains a trinucleotide (GCT) repeat tract whose length is highly polymorphic; these triplet repeats result in a stretch of alanine residues in the encoded protein. Transcript variants utilizing alternative polyA signals and alternative 5'-terminal exons exist but all encode the same protein. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.[2]

Interactions

RPL14 has been shown to interact with PHLDA1.[3]

References

  1. Tanaka M, Tanaka T, Harata M, Suzuki T, Mitsui Y (March 1998). "Triplet repeat-containing ribosomal protein L14 gene in immortalized human endothelial cell line (t-HUE4)". Biochem Biophys Res Commun 243 (2): 531–7. doi:10.1006/bbrc.1998.8125. PMID 9480843.
  2. 1 2 "Entrez Gene: RPL14 ribosomal protein L14".
  3. Hinz T, Flindt S, Marx A, Janssen O, Kabelitz D (May 2001). "Inhibition of protein synthesis by the T cell receptor-inducible human TDAG51 gene product". Cell. Signal. 13 (5): 345–52. doi:10.1016/S0898-6568(01)00141-3. PMID 11369516.

Further reading

  • Wool IG, Chan YL, Glück A (1996). "Structure and evolution of mammalian ribosomal proteins.". Biochem. Cell Biol. 73 (11-12): 933–47. doi:10.1139/o95-101. PMID 8722009. 
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298. 
  • Dave VP, Larché M, Rencher SD, Koop BF, Hurwitz JL (1994). "Restricted usage of T-cell receptor V alpha sequence and variable-joining pairs after normal T-cell development and bone marrow transplantation.". Hum. Immunol. 37 (3): 178–84. doi:10.1016/0198-8859(93)90183-2. PMID 8244780. 
  • Li SH, McInnis MG, Margolis RL, Antonarakis SE, Ross CA (1993). "Novel triplet repeat containing genes in human brain: cloning, expression, and length polymorphisms.". Genomics 16 (3): 572–9. doi:10.1006/geno.1993.1232. PMID 8325628. 
  • Aoki M, Koranyi L, Riggs AC, Wasson J, Chiu KC, Vaxillaire M, Froguel P, Gough S, Liu L, Donis-Keller H (1996). "Identification of trinucleotide repeat-containing genes in human pancreatic islets.". Diabetes 45 (2): 157–64. doi:10.2337/diabetes.45.2.157. PMID 8549859. 
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149. 
  • Reddy PH, Stockburger E, Gillevet P, Tagle DA (1998). "Mapping and characterization of novel (CAG)n repeat cDNAs from adult human brain derived by the oligo capture method.". Genomics 46 (2): 174–82. doi:10.1006/geno.1997.5044. PMID 9417904. 
  • Hinz T, Flindt S, Marx A, Janssen O, Kabelitz D (2001). "Inhibition of protein synthesis by the T cell receptor-inducible human TDAG51 gene product.". Cell. Signal. 13 (5): 345–52. doi:10.1016/S0898-6568(01)00141-3. PMID 11369516. 
  • Uechi T, Tanaka T, Kenmochi N (2001). "A complete map of the human ribosomal protein genes: assignment of 80 genes to the cytogenetic map and implications for human disorders.". Genomics 72 (3): 223–30. doi:10.1006/geno.2000.6470. PMID 11401437. 
  • Andersen JS, Lyon CE, Fox AH, Leung AK, Lam YW, Steen H, Mann M, Lamond AI (2002). "Directed proteomic analysis of the human nucleolus.". Curr. Biol. 12 (1): 1–11. doi:10.1016/S0960-9822(01)00650-9. PMID 11790298. 
  • Yoshihama M, Uechi T, Asakawa S, Kawasaki K, Kato S, Higa S, Maeda N, Minoshima S, Tanaka T, Shimizu N, Kenmochi N (2002). "The human ribosomal protein genes: sequencing and comparative analysis of 73 genes.". Genome Res. 12 (3): 379–90. doi:10.1101/gr.214202. PMC 155282. PMID 11875025. 
  • Odintsova TI, Müller EC, Ivanov AV, Egorov TA, Bienert R, Vladimirov SN, Kostka S, Otto A, Wittmann-Liebold B, Karpova GG (2004). "Characterization and analysis of posttranslational modifications of the human large cytoplasmic ribosomal subunit proteins by mass spectrometry and Edman sequencing.". J. Protein Chem. 22 (3): 249–58. doi:10.1023/A:1025068419698. PMID 12962325. 
  • Andersen JS, Lam YW, Leung AK, Ong SE, Lyon CE, Lamond AI, Mann M (2005). "Nucleolar proteome dynamics.". Nature 433 (7021): 77–83. doi:10.1038/nature03207. PMID 15635413. 
  • Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.". Cell 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983. 
This article is issued from Wikipedia - version of the Saturday, July 25, 2015. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.