60S ribosomal protein L11

For the programming language RPL-11, see Filetab.

60S ribosomal protein L11 is a protein that in humans is encoded by the RPL11 gene.

RPL11
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4UG0, 4V6X, 4XXB, 5AJ0, 4V5Z, 4UJD, 4D67, 4D5Y, 4UJE, 4UJC,%%s4UJE, 4XXB, 4UJD, 4D67, 4V5Z, 4V6X, 5AJ0, 4UJC, 4D5Y, 4UG0
Identifiers
Aliases	RPL11, DBA7, GIG34, L11, ribosomal protein L11, uL5
External IDs	OMIM: 604175; MGI: 1914275; HomoloGene: 37376; GeneCards: RPL11; OMA:RPL11 - orthologs
Gene location (Human) Chr. Chromosome 1 (human) Band 1p36.11 Start 23,691,742 bp End 23,696,835 bp
Gene location (Mouse) Chr. Chromosome 4 (mouse) Band 4|4 D3 Start 135,755,576 bp End 135,780,739 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in ganglionic eminence monocyte ventricular zone granulocyte left ovary skin of hip right ovary right lung body of stomach lymph node Top expressed in yolk sac embryo embryo lip tail of embryo genital tubercle ventricular zone dentate gyrus of hippocampal formation granule cell morula blastocyst More reference expression data BioGPS More reference expression data
Gene ontology Molecular function rRNA binding protein binding RNA binding structural constituent of ribosome 5S rRNA binding ubiquitin protein ligase binding ubiquitin ligase inhibitor activity Cellular component cytosol ribosome membrane intracellular anatomical structure nucleolus cytosolic large ribosomal subunit extracellular exosome nucleus extracellular matrix nucleoplasm cytoplasm protein-containing complex polysomal ribosome Biological process protein targeting 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 ribosomal large subunit assembly positive regulation of gene expression positive regulation of protein binding protein stabilization negative regulation of ubiquitin protein ligase activity negative regulation of ubiquitin-dependent protein catabolic process negative regulation of protein neddylation regulation of signal transduction by p53 class mediator negative regulation of proteasomal ubiquitin-dependent protein catabolic process protein localization to nucleus positive regulation of signal transduction by p53 class mediator positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator cytoplasmic translation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 6135 67025 Ensembl ENSG00000142676 ENSMUSG00000059291 UniProt P62913 Q5VVD0 Q9CXW4 RefSeq (mRNA) NM_001199802 NM_000975 NM_025919 RefSeq (protein) NP_000966 NP_001186731 NP_000966.2 NP_080195 Location (UCSC) Chr 1: 23.69 – 23.7 Mb Chr 4: 135.76 – 135.78 Mb PubMed search
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 L5P family of ribosomal proteins. It is located in the cytoplasm. The protein probably associates with the 5S rRNA. Alternative splice variants encoding different isoforms may exist, but they have not been fully characterized. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.

Interactions

RPL11 has been shown to interact with:

• BLMH,
• Mdm2,
• NOP53,
• P16,
• P53, and
• Promyelocytic leukemia protein

Further reading

• Wool IG, Chan YL, Glück A (1996). "Structure and evolution of mammalian ribosomal proteins". Biochem. Cell Biol. 73 (11–12): 933–947. doi:10.1139/o95-101. PMID 8722009.
• Mishin VP, Filipenko ML, Muravlev AI, Karpova GG, Mertvetsov NP (1995). "[Cloning and determination of the primary structure of DNA complementary to the mRNA of human ribosomal protein L11]". Bioorg. Khim. 21 (2): 158–60. PMID 7748210.
• 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): 243–250. doi:10.1016/0378-1119(94)90433-2. PMID 7821789.
• Koldamova RP, Lefterov IM, DiSabella MT, Almonte C, Watkins SC, Lazo JS (1999). "Human bleomycin hydrolase binds ribosomal proteins". Biochemistry. 38 (22): 7111–7117. doi:10.1021/bi990135l. PMID 10353821.
• 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.
• Voronina EN, Kolokol'tsova TD, Nechaeva EA, Filipenko ML (2003). "[Structural and functional analysis of the human ribosomal protein L11 gene]". Mol. Biol. (Mosk.). 37 (3): 425–35. PMID 12815950.
• Lohrum MA, Ludwig RL, Kubbutat MH, Hanlon M, Vousden KH (2004). "Regulation of HDM2 activity by the ribosomal protein L11". Cancer Cell. 3 (6): 577–587. doi:10.1016/S1535-6108(03)00134-X. PMID 12842086.
• 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): 249–258. doi:10.1023/A:1025068419698. PMID 12962325. S2CID 10710245.
• Zhang Y, Wolf GW, Bhat K, Jin A, Allio T, Burkhart WA, Xiong Y (2003). "Ribosomal protein L11 negatively regulates oncoprotein MDM2 and mediates a p53-dependent ribosomal-stress checkpoint pathway". Mol. Cell. Biol. 23 (23): 8902–8912. doi:10.1128/MCB.23.23.8902-8912.2003. PMC 262682. PMID 14612427.
• Bhat KP, Itahana K, Jin A, Zhang Y (2004). "Essential role of ribosomal protein L11 in mediating growth inhibition-induced p53 activation". EMBO J. 23 (12): 2402–2412. doi:10.1038/sj.emboj.7600247. PMC 423289. PMID 15152193.
• Bernardi R, Scaglioni PP, Bergmann S, Horn HF, Vousden KH, Pandolfi PP (2004). "PML regulates p53 stability by sequestering Mdm2 to the nucleolus". Nat. Cell Biol. 6 (7): 665–672. doi:10.1038/ncb1147. PMID 15195100. S2CID 26281860.
• Dai MS, Lu H (2004). "Inhibition of MDM2-mediated p53 ubiquitination and degradation by ribosomal protein L5". J. Biol. Chem. 279 (43): 44475–44482. doi:10.1074/jbc.M403722200. PMID 15308643.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–1178. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
• Dai MS, Shi D, Jin Y, Sun XX, Zhang Y, Grossman SR, Lu H (2006). "Regulation of the MDM2-p53 pathway by ribosomal protein L11 involves a post-ubiquitination mechanism". J. Biol. Chem. 281 (34): 24304–24313. doi:10.1074/jbc.M602596200. PMC 1783840. PMID 16803902.
• Lindström MS, Jin A, Deisenroth C, White Wolf G, Zhang Y (2007). "Cancer-associated mutations in the MDM2 zinc finger domain disrupt ribosomal protein interaction and attenuate MDM2-induced p53 degradation". Mol. Cell. Biol. 27 (3): 1056–1068. doi:10.1128/MCB.01307-06. PMC 1800693. PMID 17116689.

External links

• GeneReviews/NCBI/NIH/UW entry on Diamond-Blackfan Anemia