Ubiquitin A-52 residue ribosomal protein fusion product 1

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

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; OMA:UBA52 - orthologs
Gene location (Human) Chr. Chromosome 19 (human)[1] Band 19p13.11 Start 18,571,730 bp[1] End 18,577,550 bp[1]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in blood right testis left testis granulocyte sperm stromal cell of endometrium lymph node left ovary mononuclear cell monocyte n/a More reference expression data BioGPS More reference expression data
Gene ontology Molecular function structural constituent of ribosome protein binding protein tag ubiquitin protein ligase binding Cellular component cytoplasm endocytic vesicle membrane nucleus ribosome extracellular exosome endosome membrane lysosomal membrane extracellular space nucleoplasm mitochondrial outer membrane endoplasmic reticulum cytosol plasma 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 NIK/NF-kappaB signaling G2/M transition of mitotic cell cycle stress-activated MAPK cascade transforming growth factor beta receptor signaling pathway macroautophagy negative regulation of canonical Wnt signaling pathway 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 response Notch signaling pathway regulation of mRNA stability protein polyubiquitination negative regulation of apoptotic process negative regulation of transcription by RNA polymerase II virion assembly 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 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 by RNA polymerase II positive regulation of epidermal growth factor receptor signaling pathway 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 Species Human Mouse Entrez 7311 665964 Ensembl ENSG00000221983 n/a UniProt P62987 n/a RefSeq (mRNA) NM_001033930 NM_003333 NM_001321017 NM_001321018 NM_001321019 NM_001321020 NM_001321021 NM_001321022 n/a RefSeq (protein) NP_001029102 NP_001307946 NP_001307947 NP_001307948 NP_001307949 NP_001307950 NP_001307951 NP_003324 n/a Location (UCSC) Chr 19: 18.57 – 18.58 Mb n/a PubMed search [2] [3]
Wikidata
View/Edit Human View/Edit Mouse

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]

References

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

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. S2CID 15764136.
• 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. doi:10.1016/S0021-9258(19)84967-0. 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. doi:10.1016/S0021-9258(17)39652-7. 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. S2CID 12847618.
• 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. S2CID 20091003.
• 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.