USP16

Protein-coding gene in the species Homo sapiens
USP16
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2I50

Identifiers
AliasesUSP16, UBP-M, UBPM, ubiquitin specific peptidase 16
External IDsOMIM: 604735; MGI: 1921362; HomoloGene: 38183; GeneCards: USP16; OMA:USP16 - orthologs
Gene location (Human)
Chromosome 21 (human)
Chr.Chromosome 21 (human)[1]
Chromosome 21 (human)
Genomic location for USP16
Genomic location for USP16
Band21q21.3Start29,024,629 bp[1]
End29,054,488 bp[1]
Gene location (Mouse)
Chromosome 16 (mouse)
Chr.Chromosome 16 (mouse)[2]
Chromosome 16 (mouse)
Genomic location for USP16
Genomic location for USP16
Band16|16 C3.3Start87,454,703 bp[2]
End87,483,517 bp[2]
RNA expression pattern
Bgee
HumanMouse (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
SpeciesHumanMouse
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 MbChr 16: 87.45 – 87.48 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Ubiquitin carboxyl-terminal hydrolase 16 is an enzyme that in humans is encoded by the USP16 gene.[5][6]

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.[6]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000156256 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000025616 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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. S2CID 2856065.
  6. ^ a b "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. 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.


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