60S ribosomal protein L11
60S ribosomal protein L11 is a protein that in humans is encoded by the RPL11 gene.[5][6]
Function
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.[citation needed
]
Interactions
RPL11 has been shown to
interact
with:
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000142676 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000059291 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- PMID 9582194.
- S2CID 26672114.
- PMID 10353821.
- ^ PMID 14612427.
- PMID 18426907.
- PMID 24045667.
- S2CID 26281860.
Further reading
- Wool IG, Chan YL, Glück A (1996). "Structure and evolution of mammalian ribosomal proteins". Biochem. Cell Biol. 73 (11–12): 933–947. 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. 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. 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. 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. 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. 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. 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. 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. 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. 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, 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. 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. PMID 17116689.
External links
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