Ubiquitin A-52 residue ribosomal protein fusion product 1

Ubiquitin A-52 residue ribosomal protein fusion product 1
PDB rendering based on 1aar.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 2LJ5​, 2MBH​, 2MJB​, 2MUR​, 2RSU​, 4HJK​, 4JIO​, 4P4H​, 4PIG​, 4PIH​, 4PIJ​, 4RF0​, 4RF1​, 4S1Z​, 4V6X​, 5AJ0​
Identifiers
Symbols	UBA52 ; CEP52; HUBCEP52; L40; RPL40
External IDs	OMIM: 191321 HomoloGene: 68307 GeneCards: UBA52 Gene
Gene ontology Molecular function • structural constituent of ribosome • protein binding Cellular component • extracellular space • nucleus • nucleoplasm • lysosomal membrane • cytosol • ribosome • plasma membrane • endosome membrane • cytosolic large ribosomal subunit • endocytic vesicle membrane • extracellular exosome Biological process • G1/S transition of mitotic cell cycle • G2/M transition of mitotic cell cycle • negative regulation of transcription from RNA polymerase II promoter • nuclear-transcribed mRNA catabolic process, nonsense-mediated decay • activation of MAPK activity • protein polyubiquitination • mitotic cell cycle • stimulatory C-type lectin receptor signaling pathway • toll-like receptor signaling pathway • positive regulation of defense response to virus by host • antigen processing and presentation of peptide antigen via MHC class I • antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent • MyD88-dependent toll-like receptor signaling pathway • MyD88-independent toll-like receptor signaling pathway • carbohydrate metabolic process • glycogen biosynthetic process • glucose metabolic process • DNA repair • transcription, DNA-templated • transcription initiation from RNA polymerase II promoter • translation • translational initiation • translational elongation • translational termination • cellular protein modification process • SRP-dependent cotranslational protein targeting to membrane • apoptotic process • DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest • epidermal growth factor receptor signaling pathway • transforming growth factor beta receptor signaling pathway • Notch signaling pathway • Notch receptor processing • I-kappaB kinase/NF-kappaB signaling • JNK cascade • circadian rhythm • fibroblast growth factor receptor signaling pathway • gene expression • regulation of necrotic cell death • programmed cell death • viral process • endosomal transport • viral life cycle • virion assembly • viral protein processing • viral transcription • cytokine-mediated signaling pathway • translesion synthesis • negative regulation of transforming growth factor beta receptor signaling pathway • anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process • regulation of type I interferon production • negative regulation of type I interferon production • positive regulation of type I interferon production • toll-like receptor 2 signaling pathway • toll-like receptor 3 signaling pathway • toll-like receptor 4 signaling pathway • toll-like receptor 5 signaling pathway • toll-like receptor 9 signaling pathway • toll-like receptor 10 signaling pathway • ion transmembrane transport • TRIF-dependent toll-like receptor signaling pathway • nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway • Fc-epsilon receptor signaling pathway • toll-like receptor TLR1:TLR2 signaling pathway • toll-like receptor TLR6:TLR2 signaling pathway • negative regulation of epidermal growth factor receptor signaling pathway • error-prone translesion synthesis • antigen processing and presentation of exogenous peptide antigen via MHC class I • DNA damage response, detection of DNA damage • regulation of apoptotic process • positive regulation of apoptotic process • negative regulation of apoptotic process • positive regulation of I-kappaB kinase/NF-kappaB signaling • cellular protein metabolic process • small molecule metabolic process • innate immune response • positive regulation of transcription from RNA polymerase II promoter • neurotrophin TRK receptor signaling pathway • T cell receptor signaling pathway • positive regulation of NF-kappaB transcription factor activity • stress-activated MAPK cascade • negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle • positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition • regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle • transmembrane transport • membrane organization • regulation of transcription from RNA polymerase II promoter in response to hypoxia • necroptotic process • nucleotide-binding oligomerization domain containing signaling pathway • error-free translesion synthesis • cellular response to hypoxia • intracellular transport of virus • negative regulation of canonical Wnt signaling pathway • positive regulation of canonical Wnt signaling pathway • apoptotic signaling pathway • programmed necrotic cell death Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	7311	22186
Ensembl	ENSG00000221983	ENSMUSG00000055553
UniProt	P62987	P62984
RefSeq (mRNA)	NM_001033930	NM_019883
RefSeq (protein)	NP_001029102	NP_063936
Location (UCSC)	Chr 19: 18.57 – 18.58 Mb	Chr 4: 3.97 – 3.97 Mb
PubMed search

60S ribosomal protein L40 (RPL40) is a protein that in humans is encoded by the UBA52 gene.^[1][2]

Function

Ubiquitin is a highly conserved nuclear and cytoplasmic protein that has a major role in targeting cellular proteins for degradation by the 26S proteosome. It is also involved in the maintenance of chromatin structure, the regulation of gene expression, and the stress response. Ubiquitin is synthesized as a precursor protein consisting of either polyubiquitin chains or a single ubiquitin moiety fused to an unrelated protein. This gene encodes a fusion protein consisting of ubiquitin at the N-terminus and ribosomal protein L40 at the C-terminus, a C-terminal extension protein (CEP). Multiple processed pseudogenes derived from this gene are present in the genome.^[2]

Clinical significance

The cell's ribosomal protein L40 (rpL40), a part of the large 60S subunit. rpL40 is used by certain RNA viruses to translate messenger RNAs (mRNAs) into proteins while few host mRNAs require rpL40. Hence targeting this protein may provide a means to combat viral infections with minimum side effects to the host.^[3]

References

1. Webb GC, Baker RT, Coggan M, Board PG (Jun 1994). "Localization of the human UBA52 ubiquitin fusion gene to chromosome band 19p13.1-p12". Genomics 19 (3): 567–9. doi:10.1006/geno.1994.1108. PMID 8188300.
2. "Entrez Gene: UBA52 ubiquitin A-52 residue ribosomal protein fusion product 1".
3. Lee AS, Burdeinick-Kerr R, Whelan SP (November 2012). "A ribosome-specialized translation initiation pathway is required for cap-dependent translation of vesicular stomatitis virus mRNAs". Proc. Natl. Acad. Sci. U.S.A. 110 (1): 324–9. doi:10.1073/pnas.1216454109. PMID 23169626. Lay summary – Harvard Medical School.

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.
• Murphey RK, Godenschwege TA (2002). "New roles for ubiquitin in the assembly and function of neuronal circuits.". Neuron 36 (1): 5–8. doi:10.1016/S0896-6273(02)00943-1. PMID 12367500.
• Baker RT, Board PG (1992). "The human ubiquitin/52-residue ribosomal protein fusion gene subfamily (UbA52) is composed primarily of processed pseudogenes.". Genomics 14 (2): 520–2. doi:10.1016/S0888-7543(05)80258-7. PMID 1330885.
• Baker RT, Board PG (1991). "The human ubiquitin-52 amino acid fusion protein gene shares several structural features with mammalian ribosomal protein genes.". Nucleic Acids Res. 19 (5): 1035–40. doi:10.1093/nar/19.5.1035. PMC 333777. PMID 1850507.
• Monia BP, Ecker DJ, Jonnalagadda S, et al. (1989). "Gene synthesis, expression, and processing of human ubiquitin carboxyl extension proteins.". J. Biol. Chem. 264 (7): 4093–103. PMID 2537304.
• Lund PK, Moats-Staats BM, Simmons JG, et al. (1985). "Nucleotide sequence analysis of a cDNA encoding human ubiquitin reveals that ubiquitin is synthesized as a precursor.". J. Biol. Chem. 260 (12): 7609–13. PMID 2581967.
• Salvesen G, Lloyd C, Farley D (1987). "cDNA encoding a human homolog of yeast ubiquitin 1.". Nucleic Acids Res. 15 (13): 5485. doi:10.1093/nar/15.13.5485. PMC 305980. PMID 3037496.
• Cross SH, Charlton JA, Nan X, Bird AP (1994). "Purification of CpG islands using a methylated DNA binding column.". Nat. Genet. 6 (3): 236–44. doi:10.1038/ng0394-236. PMID 8012384.
• Cook WJ, Jeffrey LC, Kasperek E, Pickart CM (1994). "Structure of tetraubiquitin shows how multiubiquitin chains can be formed.". J. Mol. Biol. 236 (2): 601–9. doi:10.1006/jmbi.1994.1169. PMID 8107144.
• Vadlamudi RK, Joung I, Strominger JL, Shin J (1996). "p62, a phosphotyrosine-independent ligand of the SH2 domain of p56lck, belongs to a new class of ubiquitin-binding proteins.". J. Biol. Chem. 271 (34): 20235–7. doi:10.1074/jbc.271.34.20235. PMID 8702753.
• Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
• Kenmochi N, Kawaguchi T, Rozen S, et al. (1998). "A map of 75 human ribosomal protein genes.". Genome Res. 8 (5): 509–23. doi:10.1101/gr.8.5.509. PMID 9582194.
• Cruz C, Ventura F, Bartrons R, Rosa JL (2001). "HERC3 binding to and regulation by ubiquitin.". FEBS Lett. 488 (1-2): 74–80. doi:10.1016/S0014-5793(00)02371-1. PMID 11163799.
• Lee TA, Tyers M (2002). "Ubiquitin junction, what's your function?". Genome Biol. 2 (10): REPORTS4025. doi:10.1186/gb-2001-2-10-reports4025. PMC 138970. PMID 11597332.
• Yoshihama M, Uechi T, Asakawa S, et al. (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.
• Bishop N, Horman A, Woodman P (2002). "Mammalian class E vps proteins recognize ubiquitin and act in the removal of endosomal protein-ubiquitin conjugates.". J. Cell Biol. 157 (1): 91–101. doi:10.1083/jcb.200112080. PMC 2173266. PMID 11916981.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.