USP16

USP16
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2I50
Identifiers
Aliases	USP16, UBP-M, UBPM, ubiquitin specific peptidase 16
External IDs	MGI: 1921362 HomoloGene: 38183 GeneCards: USP16
Gene ontology Molecular function • cysteine-type peptidase activity • thiol-dependent ubiquitinyl hydrolase activity • transcription coactivator activity • histone binding • zinc ion binding • metal ion binding • peptidase activity • ubiquitin binding • thiol-dependent ubiquitin-specific protease activity • cysteine-type endopeptidase activity • hydrolase activity Cellular component • cytoplasm • nucleus Biological process • mitotic nuclear division • regulation of transcription, DNA-templated • ubiquitin-dependent protein catabolic process • positive regulation of translational elongation • regulation of transcription from RNA polymerase II promoter • monoubiquitinated histone H2A deubiquitination • transcription, DNA-templated • proteolysis • regulation of cell cycle • cellular response to DNA damage stimulus • cell division • positive regulation of transcription, DNA-templated • protein deubiquitination • histone deubiquitination • regulation of gene expression • cell cycle • histone H2A K63-linked deubiquitination • protein homotetramerization • positive regulation of transcription from RNA polymerase II promoter • covalent chromatin modification Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	10600	74112
Ensembl	ENSG00000156256	ENSMUSG00000025616
UniProt	Q9Y5T5	Q99LG0
RefSeq (mRNA)	NM_006447 NM_001001992 NM_001032410	NM_024258
RefSeq (protein)	NP_001001992.1 NP_001027582.1 NP_006438.1	NP_077220.2
Location (UCSC)	Chr 21: 29.02 – 29.05 Mb	Chr 16: 87.45 – 87.48 Mb
PubMed search	[1]	[2]
Wikidata

View/Edit Human

View/Edit Mouse

Ubiquitin carboxyl-terminal hydrolase 16 is an enzyme that in humans is encoded by the USP16 gene.^[3][4]

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.^[4]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. Puente XS, Sanchez LM, Overall CM, Lopez-Otin C (Jul 2003). "Human and mouse proteases: a comparative genomic approach". Nat Rev Genet. 4 (7): 544–58. doi:10.1038/nrg1111. PMID 12838346.
4. "Entrez Gene: USP16 ubiquitin specific peptidase 16".

Further reading

• D'Andrea A, Pellman D (1999). "Deubiquitinating enzymes: a new class of biological regulators". Crit. Rev. Biochem. Mol. Biol. 33 (5): 337–52. doi:10.1080/10409239891204251. PMID 9827704.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Cai SY, Babbitt RW, Marchesi VT (1999). "A mutant deubiquitinating enzyme (Ubp-M) associates with mitotic chromosomes and blocks cell division". Proc. Natl. Acad. Sci. U.S.A. 96 (6): 2828–33. doi:10.1073/pnas.96.6.2828. PMC 15854. PMID 10077596.
• Hattori M, Fujiyama A, Taylor TD, et al. (2000). "The DNA sequence of human chromosome 21". Nature. 405 (6784): 311–9. doi:10.1038/35012518. PMID 10830953.
• Wistow G, Bernstein SL, Wyatt MK, et al. (2002). "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". Mol. Vis. 8: 196–204. PMID 12107411.
• 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.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Lehner B, Sanderson CM (2004). "A protein interaction framework for human mRNA degradation". Genome Res. 14 (7): 1315–23. doi:10.1101/gr.2122004. PMC 442147. PMID 15231747.
• Beausoleil SA, Jedrychowski M, Schwartz D, et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
• Pai MT, Tzeng SR, Kovacs JJ, et al. (2007). "Solution structure of the Ubp-M BUZ domain, a highly specific protein module that recognizes the C-terminal tail of free ubiquitin". J. Mol. Biol. 370 (2): 290–302. doi:10.1016/j.jmb.2007.04.015. PMC 2870993. PMID 17512543.
• Joo HY, Zhai L, Yang C, et al. (2007). "Regulation of cell cycle progression and gene expression by H2A deubiquitination". Nature. 449 (7165): 1068–72. doi:10.1038/nature06256. PMID 17914355.