Ubiquitin-specific protease 14 is an
enzyme that in humans is encoded by the USP14gene.[5][6]
This gene encodes a member of the ubiquitin-specific processing (UBP) family of proteases that is a
deubiquitinating enzyme (DUB) with His and Cys domains. This protein is located in the
cytoplasm and cleaves the
ubiquitinmoiety from ubiquitin-fused precursors and ubiquitinylated proteins. Mice with a mutation that results in reduced expression of the ortholog of this protein are retarded for growth, develop severe tremors by 2 to 3 weeks of age followed by hindlimb paralysis and death by 6 to 10 weeks of age. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.[6]
Wilson SM, Bhattacharyya B, Rachel RA, Coppola V, Tessarollo L, Householder DB, Fletcher CF, Miller RJ, Copeland NG, Jenkins NA (2002). "Synaptic defects in ataxia mice result from a mutation in Usp14, encoding a ubiquitin-specific protease". Nature Genetics. 32 (3): 420–425.
doi:
10.1038/ng1006.
PMID12368914.
S2CID23542012.
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.
PMID9827704.
Deshpande KL, Seubert PH, Tillman DM, Farkas WR, Katze JR (1996). "Cloning and characterization of cDNA encoding the rabbit tRNA-guanine transglycosylase 60-kilodalton subunit". Arch. Biochem. Biophys. 326 (1): 1–7.
doi:
10.1006/abbi.1996.0039.
PMID8579355.
Reuter TY, Medhurst AL, Waisfisz Q, Zhi Y, Herterich S, Hoehn H, Gross HJ, Joenje H, Hoatlin ME, Mathew CG, Huber PA (2003). "Yeast two-hybrid screens imply involvement of Fanconi anemia proteins in transcription regulation, cell signaling, oxidative metabolism, and cellular transport". Exp. Cell Res. 289 (2): 211–21.
doi:
10.1016/S0014-4827(03)00261-1.
PMID14499622.
Dennehey BK, Gutches DG, McConkey EH, Krauter KS (2004). "Inversion, duplication, and changes in gene context are associated with human chromosome 18 evolution". Genomics. 83 (3): 493–501.
doi:
10.1016/j.ygeno.2003.08.017.
PMID14962675.
Ubiquitin-specific protease 14 is an
enzyme that in humans is encoded by the USP14gene.[5][6]
This gene encodes a member of the ubiquitin-specific processing (UBP) family of proteases that is a
deubiquitinating enzyme (DUB) with His and Cys domains. This protein is located in the
cytoplasm and cleaves the
ubiquitinmoiety from ubiquitin-fused precursors and ubiquitinylated proteins. Mice with a mutation that results in reduced expression of the ortholog of this protein are retarded for growth, develop severe tremors by 2 to 3 weeks of age followed by hindlimb paralysis and death by 6 to 10 weeks of age. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.[6]
Wilson SM, Bhattacharyya B, Rachel RA, Coppola V, Tessarollo L, Householder DB, Fletcher CF, Miller RJ, Copeland NG, Jenkins NA (2002). "Synaptic defects in ataxia mice result from a mutation in Usp14, encoding a ubiquitin-specific protease". Nature Genetics. 32 (3): 420–425.
doi:
10.1038/ng1006.
PMID12368914.
S2CID23542012.
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.
PMID9827704.
Deshpande KL, Seubert PH, Tillman DM, Farkas WR, Katze JR (1996). "Cloning and characterization of cDNA encoding the rabbit tRNA-guanine transglycosylase 60-kilodalton subunit". Arch. Biochem. Biophys. 326 (1): 1–7.
doi:
10.1006/abbi.1996.0039.
PMID8579355.
Reuter TY, Medhurst AL, Waisfisz Q, Zhi Y, Herterich S, Hoehn H, Gross HJ, Joenje H, Hoatlin ME, Mathew CG, Huber PA (2003). "Yeast two-hybrid screens imply involvement of Fanconi anemia proteins in transcription regulation, cell signaling, oxidative metabolism, and cellular transport". Exp. Cell Res. 289 (2): 211–21.
doi:
10.1016/S0014-4827(03)00261-1.
PMID14499622.
Dennehey BK, Gutches DG, McConkey EH, Krauter KS (2004). "Inversion, duplication, and changes in gene context are associated with human chromosome 18 evolution". Genomics. 83 (3): 493–501.
doi:
10.1016/j.ygeno.2003.08.017.
PMID14962675.