USP16

USP16

Ubiquitin specific peptidase 16, also known as USP16, is a human gene.cite web | title = Entrez Gene: USP16 ubiquitin specific peptidase 16| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10600| accessdate = ]

PBB_Summary
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summary_text = This gene encodes a deubiquitinating enzyme that is phosphorylated at the onset of mitosis and then dephosphorylated at the metaphase/anaphase transition. It can deubiquitinate H2A, one of two major ubiquitinated proteins of chromatin, in vitro and a mutant form of the protein was shown to block cell division. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.cite web | title = Entrez Gene: USP16 ubiquitin specific peptidase 16| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10600| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=D'Andrea A, Pellman D |title=Deubiquitinating enzymes: a new class of biological regulators. |journal=Crit. Rev. Biochem. Mol. Biol. |volume=33 |issue= 5 |pages= 337–52 |year= 1999 |pmid= 9827704 |doi=
*cite journal | author=Puente XS, Sánchez LM, Overall CM, López-Otín C |title=Human and mouse proteases: a comparative genomic approach. |journal=Nat. Rev. Genet. |volume=4 |issue= 7 |pages= 544–58 |year= 2003 |pmid= 12838346 |doi= 10.1038/nrg1111
*cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=
*cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, "et al." |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=
*cite journal | author=Cai SY, Babbitt RW, Marchesi VT |title=A mutant deubiquitinating enzyme (Ubp-M) associates with mitotic chromosomes and blocks cell division. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 6 |pages= 2828–33 |year= 1999 |pmid= 10077596 |doi=
*cite journal | author=Hattori M, Fujiyama A, Taylor TD, "et al." |title=The DNA sequence of human chromosome 21. |journal=Nature |volume=405 |issue= 6784 |pages= 311–9 |year= 2000 |pmid= 10830953 |doi= 10.1038/35012518
*cite journal | author=Wistow G, Bernstein SL, Wyatt MK, "et al." |title=Expressed sequence tag analysis of human retina for the NEIBank Project: retbindin, an abundant, novel retinal cDNA and alternative splicing of other retina-preferred gene transcripts. |journal=Mol. Vis. |volume=8 |issue= |pages= 196–204 |year= 2002 |pmid= 12107411 |doi=
*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
*cite journal | author=Ota T, Suzuki Y, Nishikawa T, "et al." |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285
*cite journal | author=Lehner B, Sanderson CM |title=A protein interaction framework for human mRNA degradation. |journal=Genome Res. |volume=14 |issue= 7 |pages= 1315–23 |year= 2004 |pmid= 15231747 |doi= 10.1101/gr.2122004
*cite journal | author=Beausoleil SA, Jedrychowski M, Schwartz D, "et al." |title=Large-scale characterization of HeLa cell nuclear phosphoproteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 33 |pages= 12130–5 |year= 2004 |pmid= 15302935 |doi= 10.1073/pnas.0404720101
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Rual JF, Venkatesan K, Hao T, "et al." |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209
*cite journal | author=Pai MT, Tzeng SR, Kovacs JJ, "et al." |title=Solution structure of the Ubp-M BUZ domain, a highly specific protein module that recognizes the C-terminal tail of free ubiquitin. |journal=J. Mol. Biol. |volume=370 |issue= 2 |pages= 290–302 |year= 2007 |pmid= 17512543 |doi= 10.1016/j.jmb.2007.04.015
*cite journal | author=Joo HY, Zhai L, Yang C, "et al." |title=Regulation of cell cycle progression and gene expression by H2A deubiquitination. |journal=Nature |volume=449 |issue= 7165 |pages= 1068–72 |year= 2007 |pmid= 17914355 |doi= 10.1038/nature06256

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  • Deubiquitinating enzyme — Deubiquitinating enzymes (DUBs) are a large group of proteases[1] (more than 60 known) that regulate ubiquitin dependent metabolic pathways by cleaving ubiquitin protein bonds. DUBs are also commonly referred to as deubiquitinating peptidases,… …   Wikipedia

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