USP16

Ubiquitin carboxyl-terminal hydrolase 16 is an enzyme that in humans is encoded by the USP16 gene.

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	OMIM: 604735; MGI: 1921362; HomoloGene: 38183; GeneCards: USP16; OMA:USP16 - orthologs
Gene location (Human) Chr. Chromosome 21 (human) Band 21q21.3 Start 29,024,629 bp End 29,054,488 bp
Gene location (Mouse) Chr. Chromosome 16 (mouse) Band 16|16 C3.3 Start 87,454,703 bp End 87,483,517 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in oocyte sperm epithelium of nasopharynx Achilles tendon pylorus secondary oocyte epithelium of colon tendon of biceps brachii parietal pleura cardia Top expressed in zygote morula tail of embryo genital tubercle spermatid muscle of thigh seminiferous tubule parotid gland soleus muscle seminal vesicula More reference expression data BioGPS More reference expression data
Gene ontology Molecular function cysteine-type peptidase activity zinc ion binding metal ion binding peptidase activity hydrolase activity transcription coactivator activity cysteine-type endopeptidase activity histone binding ubiquitin binding thiol-dependent deubiquitinase Cellular component cytoplasm nucleus nucleoplasm Biological process regulation of transcription, DNA-templated ubiquitin-dependent protein catabolic process positive regulation of translational elongation regulation of transcription by RNA polymerase II monoubiquitinated histone H2A deubiquitination transcription, DNA-templated proteolysis cellular response to DNA damage stimulus cell division histone H2A K63-linked deubiquitination positive regulation of transcription by RNA polymerase II protein deubiquitination positive regulation of transcription, DNA-templated protein homotetramerization regulation of gene expression histone deubiquitination regulation of cell cycle mitotic cell cycle chromatin organization cell cycle mitotic nuclear division Sources:Amigo / QuickGO
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 NP_001027582 NP_006438 NP_077220 Location (UCSC) Chr 21: 29.02 – 29.05 Mb Chr 16: 87.45 – 87.48 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

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.

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. Bibcode:1999PNAS...96.2828C. 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. Bibcode:2000Natur.405..311H. 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. Bibcode:2002PNAS...9916899M. 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. Bibcode:2004PNAS..10112130B. 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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
• 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. Bibcode:2007Natur.449.1068J. doi:10.1038/nature06256. PMID 17914355. S2CID 4417239.