60S ribosomal protein L14

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 120,400,510 bp [2] End 120,403,720 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in body of pancreas ganglionic eminence skin of abdomen canal of the cervix gastric mucosa body of stomach right uterine tube right lung right lobe of thyroid gland left lobe of thyroid gland Top expressed in morula lip yolk sac superior frontal gyrus neural tube primitive streak condyle fossa otic placode lens More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding cadherin binding RNA binding structural constituent of ribosome Cellular component cytosol ribosome membrane intracellular anatomical structure cytosolic large ribosomal subunit extracellular exosome 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: 120.4 – 120.4 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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

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. Bibcode:2002CBio...12....1A. doi: 10.1016/S0960-9822(01)00650-9 . PMID   11790298. S2CID   14132033.
• 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. S2CID   10710245.
• Andersen JS, Lam YW, Leung AK, Ong SE, Lyon CE, Lamond AI, Mann M (2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. Bibcode:2005Natur.433...77A. doi:10.1038/nature03207. PMID   15635413. S2CID   4344740.
• 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. S2CID   7827573.