Ubiquitin A-52 residue ribosomal protein fusion product 1

UBA52
Available structures
PDB	Human UniProt search: PDBe RCSB
List of PDB id codes
	2LJ5, 2MBH, 2MJB, 2MUR, 2RSU, 4HJK, 4JIO, 4P4H, 4PIG, 4PIH, 4PIJ, 4RF0, 4RF1, 4S1Z, 4UG0, 4V6X, 5AJ0, 4UJD, 4D67, 4UJC, 3J7P, 3J7Q, 4XKL, 3J92, 4D5Y, 3J7O, 3J7R, 3PHD, 2KOX, 4UJE, 5A5B, 2N3V, 2N3U, 2N3W, 2NBD, 2NBE, 3VDZ, 5HPS, 3I3T, 5HPT, 5JBV, 5HPL, 5HPK, 5J8P
Identifiers
Aliases	UBA52, CEP52, HUBCEP52, L40, RPL40, Ubiquitin A-52 residue ribosomal protein fusion product 1
External IDs	OMIM: 191321 MGI: 3644625 HomoloGene: 68307 GeneCards: UBA52
Gene location (Human)
Chr.	Chromosome 19 (human)[1]
End	18,577,550 bp[1]
RNA expression pattern
	More reference expression data
Gene ontology
Molecular function	• structural constituent of ribosome; • GO:0001948 protein binding; • protein tag; • ubiquitin protein ligase binding;
Cellular component	• cytoplasm; • endocytic vesicle membrane; • cell nucleus; • ribosome; • extracellular exosome; • endosome membrane; • intracellular ribonucleoprotein complex; • lysosomal membrane; • extracellular; • nucleoplasm; • mitochondrial outer membrane; • endoplasmic reticulum; • cytosol; • cell membrane; • endoplasmic reticulum quality control compartment; • vesicle; • endoplasmic reticulum membrane; • host cell; • cytosolic large ribosomal subunit; • cytosolic small ribosomal subunit; • synapse;
Biological process	• DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; • negative regulation of epidermal growth factor receptor signaling pathway; • interstrand cross-link repair; • nucleotide-excision repair, DNA damage recognition; • positive regulation of canonical Wnt signaling pathway; • tumor necrosis factor-mediated signaling pathway; • regulation of type I interferon production; • TRIF-dependent toll-like receptor signaling pathway; • Fc-epsilon receptor signaling pathway; • endosomal transport; • global genome nucleotide-excision repair; • cellular protein modification process; • NIK/NF-kappaB signaling; • G2/M transition of mitotic cell cycle; • stress-activated MAPK cascade; • negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; • transforming growth factor beta receptor signaling pathway; • macroautophagy; • negative regulation of canonical Wnt signaling pathway; • DNA damage response, detection of DNA damage; • nucleotide-excision repair, DNA gap filling; • viral transcription; • error-free translesion synthesis; • regulation of tumor necrosis factor-mediated signaling pathway; • stimulatory C-type lectin receptor signaling pathway; • negative regulation of transforming growth factor beta receptor signaling pathway; • SRP-dependent cotranslational protein targeting to membrane; • JNK cascade; • regulation of transcription from RNA polymerase II promoter in response to hypoxia; • nucleotide-excision repair, DNA incision; • I-kappaB kinase/NF-kappaB signaling; • innate immune system; • positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition; • Notch signaling pathway; • regulation of mRNA stability; • protein polyubiquitination; • negative regulation of apoptotic process; • negative regulation of transcription from RNA polymerase II promoter; • virion assembly; • activation of MAPK activity; • positive regulation of NF-kappaB transcription factor activity; • anaphase-promoting complex-dependent catabolic process; • negative regulation of type I interferon production; • nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; • nucleotide-binding oligomerization domain containing signaling pathway; • cellular protein metabolic process; • intracellular transport of virus; • viral life cycle; • MyD88-dependent toll-like receptor signaling pathway; • error-prone translesion synthesis; • MAPK cascade; • fibroblast growth factor receptor signaling pathway; • ion transmembrane transport; • glycogen biosynthetic process; • positive regulation of apoptotic process; • translational initiation; • positive regulation of I-kappaB kinase/NF-kappaB signaling; • translesion synthesis; • transcription-coupled nucleotide-excision repair; • T cell receptor signaling pathway; • MyD88-independent toll-like receptor signaling pathway; • positive regulation of transcription from RNA polymerase II promoter; • positive regulation of epidermal growth factor receptor signaling pathway; • protein ubiquitination involved in ubiquitin-dependent protein catabolic process; • proteasome-mediated ubiquitin-dependent protein catabolic process; • regulation of signal transduction by p53 class mediator; • Wnt signaling pathway, planar cell polarity pathway; • nucleotide-excision repair, DNA incision, 5'-to lesion; • protein biosynthesis; • nucleotide-excision repair, preincision complex assembly; • rRNA processing; • Wnt signaling pathway; • ERBB2 signaling pathway; • nucleotide-excision repair, DNA duplex unwinding; • protein folding; • negative regulation of G2/M transition of mitotic cell cycle; • protein ubiquitination; • protein deubiquitination; • SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; • entry of bacterium into host cell; • transmembrane transport; • regulation of necroptotic process; • membrane organization; • endoplasmic reticulum mannose trimming; • cellular iron ion homeostasis; • regulation of hematopoietic stem cell differentiation; • protein targeting to peroxisome; • cytokine-mediated signaling pathway; • modification-dependent protein catabolic process; • interleukin-1-mediated signaling pathway; • response to insecticide;
	Sources:Amigo / QuickGO
Orthologs
	7311
	665964
	ENSG00000221983
	n/a
	P62987
	n/a
NM_001033930; NM_003333; NM_001321017; NM_001321018; NM_001321019;
	NM_001321020; NM_001321021; NM_001321022
	n/a
NP_001029102; NP_001307946; NP_001307947; NP_001307948; NP_001307949;
	NP_001307950; NP_001307951; NP_003324
	n/a
	Wikidata
View/Edit Human	View/Edit Mouse

60S ribosomal protein L40 (RPL40) is a protein that in humans is encoded by the UBA52 gene.[4][5]

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.[5]

Clinical significance

The cell's ribosomal protein eL40 (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.[6]

References

GRCh38: Ensembl release 89: ENSG00000221983 - 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.
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.
"Entrez Gene: UBA52 ubiquitin A-52 residue ribosomal protein fusion product 1".
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. PMC 3538191. PMID 23169626. Lay summary – Harvard Medical School.

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.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000221983 - Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[3] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid8188300-4] 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.

[entrez-5] "Entrez Gene: UBA52 ubiquitin A-52 residue ribosomal protein fusion product 1".

[pmid23169626-6] 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. PMC 3538191. PMID 23169626. Lay summary – Harvard Medical School.

Ubiquitin A-52 residue ribosomal protein fusion product 1

Function

Clinical significance

References

Further reading