60S ribosomal protein L12

RPL12
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4V6X, 5AJ0, 3J92, 4V5Z, 5A8L
Identifiers
Aliases	RPL12, L12, ribosomal protein L12
External IDs	MGI: 98002 HomoloGene: 128047 GeneCards: RPL12
Gene ontology Molecular function • protein binding • poly(A) RNA binding • RNA binding • structural constituent of ribosome • rRNA binding Cellular component • nucleus • nucleolus • intracellular ribonucleoprotein complex • cytosol • extracellular exosome • membrane • cytosolic large ribosomal subunit • cytoplasm • focal adhesion • ribosome • extracellular matrix Biological process • translational initiation • SRP-dependent cotranslational protein targeting to membrane • nuclear-transcribed mRNA catabolic process, nonsense-mediated decay • ribosomal large subunit assembly • viral transcription • translation • rRNA processing Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	6136	269261
Ensembl	ENSG00000197958	ENSMUSG00000038900
UniProt	P30050	P35979
RefSeq (mRNA)	NM_000976	NM_009076
RefSeq (protein)	NP_000967.1	NP_033102.2
Location (UCSC)	Chr 9: 127.45 – 127.45 Mb	Chr 2: 32.96 – 32.97 Mb
PubMed search	[1]	[2]
Wikidata

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60S ribosomal protein L12' is a protein that in humans is encoded by the RPL12 gene.^[3][4]

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 L11P family of ribosomal proteins. It is located in the cytoplasm. The protein binds directly to the 26S rRNA. This gene is co-transcribed with the U65 snoRNA, which is located in its fourth intron. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.^[4]

Interactions

RPL12 has been shown to interact with CDC5L.^[5]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. Chu W, Presky DH, Swerlick RA, Burns DK (March 1993). "The primary structure of human ribosomal protein L12". Nucleic Acids Res. 21 (3): 749. doi:10.1093/nar/21.3.749. PMC 309184. PMID 8441690.
4. "Entrez Gene: RPL12 ribosomal protein L12".
5. Ajuh P, Kuster B, Panov K, Zomerdijk JC, Mann M, Lamond AI (December 2000). "Functional analysis of the human CDC5L complex and identification of its components by mass spectrometry". EMBO J. 19 (23): 6569–81. doi:10.1093/emboj/19.23.6569. PMC 305846. PMID 11101529.

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.
• Kato S, Sekine S, Oh SW, Kim NS, Umezawa Y, Abe N, Yokoyama-Kobayashi M, Aoki T (1995). "Construction of a human full-length cDNA bank". Gene. 150 (2): 243–50. doi:10.1016/0378-1119(94)90433-2. PMID 7821789.
• Uchiumi T, Kominami R (1997). "Binding of mammalian ribosomal protein complex P0.P1.P2 and protein L12 to the GTPase-associated domain of 28 S ribosomal RNA and effect on the accessibility to anti-28 S RNA autoantibody". J. Biol. Chem. 272 (6): 3302–8. doi:10.1074/jbc.272.6.3302. PMID 9013569.
• Kenmochi N, Kawaguchi T, Rozen S, Davis E, Goodman N, Hudson TJ, Tanaka T, Page DC (1998). "A map of 75 human ribosomal protein genes". Genome Res. 8 (5): 509–23. doi:10.1101/gr.8.5.509. PMID 9582194.
• Ajuh P, Kuster B, Panov K, Zomerdijk JC, Mann M, Lamond AI (2001). "Functional analysis of the human CDC5L complex and identification of its components by mass spectrometry". EMBO J. 19 (23): 6569–81. doi:10.1093/emboj/19.23.6569. PMC 305846. PMID 11101529.
• 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.
• Plafker SM, Macara IG (2002). "Ribosomal Protein L12 Uses a Distinct Nuclear Import Pathway Mediated by Importin 11". Mol. Cell. Biol. 22 (4): 1266–75. doi:10.1128/MCB.22.4.1266-1275.2002. PMC 134630. PMID 11809816.
• Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nat. Biotechnol. 23 (1): 94–101. doi:10.1038/nbt1046. PMID 15592455.
• 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.
• Beausoleil SA, Villén J, Gerber SA, Rush J, Gygi SP (2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nat. Biotechnol. 24 (10): 1285–92. doi:10.1038/nbt1240. PMID 16964243.
• 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.