60S ribosomal protein L14

60S ribosomal protein L14 is a protein that in humans is encoded by the RPL14 gene.[5][6]

RPL14
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 5AJ0, 4UG0, 4V6X
Identifiers
Aliases	RPL14, CAG-ISL-7, CTG-B33, L14, RL14, hRL14, ribosomal protein L14
External IDs	OMIM: 617414 MGI: 1914365 HomoloGene: 68375 GeneCards: RPL14
Gene location (Human) Chr. Chromosome 3 (human)[1] Band 3p22.1 Start 40,457,292 bp[1] End 40,468,587 bp[1]
Gene location (Mouse) Chr. Chromosome 9 (mouse)[2] Band 9|9 F4 Start 120,571,444 bp[2] End 120,574,654 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • GO:0001948 protein binding • cadherin binding • RNA binding • structural constituent of ribosome Cellular component • cytosol • ribosome • membrane • intracellular • cytosolic large ribosomal subunit • extracellular exosome • GO:0097483, GO:0097481 postsynaptic density Biological process • viral transcription • SRP-dependent cotranslational protein targeting to membrane • ribosomal large subunit biogenesis • translational initiation • nuclear-transcribed mRNA catabolic process, nonsense-mediated decay • rRNA processing • protein biosynthesis Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	9045	67115
Ensembl	ENSG00000188846	ENSMUSG00000025794
UniProt	P50914	Q9CR57
RefSeq (mRNA)	NM_003973 NM_001034996	NM_025974
RefSeq (protein)	NP_001030168 NP_003964	NP_080250
Location (UCSC)	Chr 3: 40.46 – 40.47 Mb	Chr 9: 120.57 – 120.57 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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.[6]

Interactions

RPL14 has been shown to interact with PHLDA1.[7]

References

1. GRCh38: Ensembl release 89: ENSG00000188846 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000025794 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. "Entrez Gene: RPL14 ribosomal protein L14".
7. 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.

External links

• Human RPL14 genome location and RPL14 gene details page in the UCSC Genome Browser.

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.