UBA52

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Ubiquitin A-52 residue ribosomal protein fusion product 1
File:PBB Protein UBA52 image.jpg
PDB rendering based on 1aar.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols UBA52 ; CEP52; HUBCEP52; MGC126879; MGC126881; MGC57125; RPL40
External IDs Template:OMIM5 HomoloGene: 68307
RNA expression pattern
File:PBB GE UBA52 221700 s at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Ubiquitin A-52 residue ribosomal protein fusion product 1, also known as UBA52, is a human gene.[1]

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.[1]

References

  1. ↑ 1.0 1.1 "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. PMID 8722009.
  • Murphey RK, Godenschwege TA (2002). "New roles for ubiquitin in the assembly and function of neuronal circuits". Neuron. 36 (1): 5–8. 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. 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. 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. 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.
  • Webb GC, Baker RT, Coggan M, Board PG (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.
  • 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. PMID 8702753.
  • Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. 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. 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. PMID 11163799.
  • Lee TA, Tyers M (2002). "Ubiquitin junction, what's your function?". Genome Biol. 2 (10): REPORTS4025. 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. 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. 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. PMID 12477932.

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