UBA52

UBA52

Ubiquitin A-52 residue ribosomal protein fusion product 1, also known as UBA52, is a human gene.cite web | title = Entrez Gene: UBA52 ubiquitin A-52 residue ribosomal protein fusion product 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7311| accessdate = ]

PBB_Summary
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summary_text = 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.cite web | title = Entrez Gene: UBA52 ubiquitin A-52 residue ribosomal protein fusion product 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7311| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Wool IG, Chan YL, Glück A |title=Structure and evolution of mammalian ribosomal proteins. |journal=Biochem. Cell Biol. |volume=73 |issue= 11-12 |pages= 933–47 |year= 1996 |pmid= 8722009 |doi=
*cite journal | author=Murphey RK, Godenschwege TA |title=New roles for ubiquitin in the assembly and function of neuronal circuits. |journal=Neuron |volume=36 |issue= 1 |pages= 5–8 |year= 2002 |pmid= 12367500 |doi=
*cite journal | author=Baker RT, Board PG |title=The human ubiquitin/52-residue ribosomal protein fusion gene subfamily (UbA52) is composed primarily of processed pseudogenes. |journal=Genomics |volume=14 |issue= 2 |pages= 520–2 |year= 1992 |pmid= 1330885 |doi=
*cite journal | author=Baker RT, Board PG |title=The human ubiquitin-52 amino acid fusion protein gene shares several structural features with mammalian ribosomal protein genes. |journal=Nucleic Acids Res. |volume=19 |issue= 5 |pages= 1035–40 |year= 1991 |pmid= 1850507 |doi=
*cite journal | author=Monia BP, Ecker DJ, Jonnalagadda S, "et al." |title=Gene synthesis, expression, and processing of human ubiquitin carboxyl extension proteins. |journal=J. Biol. Chem. |volume=264 |issue= 7 |pages= 4093–103 |year= 1989 |pmid= 2537304 |doi=
*cite journal | author=Lund PK, Moats-Staats BM, Simmons JG, "et al." |title=Nucleotide sequence analysis of a cDNA encoding human ubiquitin reveals that ubiquitin is synthesized as a precursor. |journal=J. Biol. Chem. |volume=260 |issue= 12 |pages= 7609–13 |year= 1985 |pmid= 2581967 |doi=
*cite journal | author=Salvesen G, Lloyd C, Farley D |title=cDNA encoding a human homolog of yeast ubiquitin 1. |journal=Nucleic Acids Res. |volume=15 |issue= 13 |pages= 5485 |year= 1987 |pmid= 3037496 |doi=
*cite journal | author=Cross SH, Charlton JA, Nan X, Bird AP |title=Purification of CpG islands using a methylated DNA binding column. |journal=Nat. Genet. |volume=6 |issue= 3 |pages= 236–44 |year= 1994 |pmid= 8012384 |doi= 10.1038/ng0394-236
*cite journal | author=Cook WJ, Jeffrey LC, Kasperek E, Pickart CM |title=Structure of tetraubiquitin shows how multiubiquitin chains can be formed. |journal=J. Mol. Biol. |volume=236 |issue= 2 |pages= 601–9 |year= 1994 |pmid= 8107144 |doi= 10.1006/jmbi.1994.1169
*cite journal | author=Webb GC, Baker RT, Coggan M, Board PG |title=Localization of the human UBA52 ubiquitin fusion gene to chromosome band 19p13.1-p12. |journal=Genomics |volume=19 |issue= 3 |pages= 567–9 |year= 1994 |pmid= 8188300 |doi= 10.1006/geno.1994.1108
*cite journal | author=Vadlamudi RK, Joung I, Strominger JL, Shin J |title=p62, a phosphotyrosine-independent ligand of the SH2 domain of p56lck, belongs to a new class of ubiquitin-binding proteins. |journal=J. Biol. Chem. |volume=271 |issue= 34 |pages= 20235–7 |year= 1996 |pmid= 8702753 |doi=
*cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791–806 |year= 1997 |pmid= 8889548 |doi=
*cite journal | author=Kenmochi N, Kawaguchi T, Rozen S, "et al." |title=A map of 75 human ribosomal protein genes. |journal=Genome Res. |volume=8 |issue= 5 |pages= 509–23 |year= 1998 |pmid= 9582194 |doi=
*cite journal | author=Cruz C, Ventura F, Bartrons R, Rosa JL |title=HERC3 binding to and regulation by ubiquitin. |journal=FEBS Lett. |volume=488 |issue= 1-2 |pages= 74–80 |year= 2001 |pmid= 11163799 |doi=
*cite journal | author=Lee TA, Tyers M |title=Ubiquitin junction, what's your function? |journal=Genome Biol. |volume=2 |issue= 10 |pages= REPORTS4025 |year= 2002 |pmid= 11597332 |doi=
*cite journal | author=Yoshihama M, Uechi T, Asakawa S, "et al." |title=The human ribosomal protein genes: sequencing and comparative analysis of 73 genes. |journal=Genome Res. |volume=12 |issue= 3 |pages= 379–90 |year= 2002 |pmid= 11875025 |doi= 10.1101/gr.214202
*cite journal | author=Bishop N, Horman A, Woodman P |title=Mammalian class E vps proteins recognize ubiquitin and act in the removal of endosomal protein-ubiquitin conjugates. |journal=J. Cell Biol. |volume=157 |issue= 1 |pages= 91–101 |year= 2002 |pmid= 11916981 |doi= 10.1083/jcb.200112080
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899

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