Ubiquitin specific peptidase 10, also known as USP10, is an
enzyme which in humans is encoded by the USP10gene.[5]
Function
Ubiquitin is a highly conserved protein that is covalently linked to other proteins to regulate their function and degradation. This gene encodes a member of the ubiquitin-specific protease family of
cysteine proteases. The enzyme specifically cleaves ubiquitin from ubiquitin-conjugated protein substrates. The protein is found in the nucleus and cytoplasm. It functions as a co-factor of the DNA-bound
androgen receptor complex, and is inhibited by a protein in the
Ras-
GTPase pathway. The human genome contains several
pseudogenes similar to this gene.[5]
Interactions
USP10 has been shown to
interact with
G3BP1.[6]
In the endothelium, USP10 regulates Notch signaling by slowing down the degradation of the intracellular domain of
NOTCH1. [7]
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.
Puente XS, Sánchez LM, Overall CM, López-Otín C (2003). "Human and mouse proteases: a comparative genomic approach". Nat. Rev. Genet. 4 (7): 544–58.
doi:
10.1038/nrg1111.
PMID12838346.
S2CID2856065.
Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (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.
PMID16189514.
S2CID4427026.
Faus H, Meyer HA, Huber M, Bahr I, Haendler B (2006). "The ubiquitin-specific protease USP10 modulates androgen receptor function". Mol. Cell. Endocrinol. 245 (1–2): 138–46.
doi:
10.1016/j.mce.2005.11.011.
PMID16368182.
S2CID24365493.
Grunda JM, Nabors LB, Palmer CA, Chhieng DC, Steg A,
Mikkelsen T, Diasio RB, Zhang K, Allison D, Grizzle WE, Wang W, Gillespie GY, Johnson MR (2007). "Increased expression of thymidylate synthetase (TS), ubiquitin specific protease 10 (USP10) and survivin is associated with poor survival in glioblastoma multiforme (GBM)". J. Neurooncol. 80 (3): 261–74.
doi:
10.1007/s11060-006-9191-4.
PMID16773218.
S2CID42007677.
Beausoleil SA, Villén J, Gerber SA, Rush J, Gygi SP (2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nat. Biotechnol. 24 (10): 1285–92.
doi:
10.1038/nbt1240.
PMID16964243.
S2CID14294292.
Deng S, Zhou H, Xiong R, Lu Y, Yan D, Xing T, Dong L, Tang E, Yang H (2007). "Over-expression of genes and proteins of ubiquitin specific peptidases (USPs) and proteasome subunits (PSs) in breast cancer tissue observed by the methods of RFDD-PCR and proteomics". Breast Cancer Res. Treat. 104 (1): 21–30.
doi:
10.1007/s10549-006-9393-7.
PMID17004105.
S2CID29643544.
Ubiquitin specific peptidase 10, also known as USP10, is an
enzyme which in humans is encoded by the USP10gene.[5]
Function
Ubiquitin is a highly conserved protein that is covalently linked to other proteins to regulate their function and degradation. This gene encodes a member of the ubiquitin-specific protease family of
cysteine proteases. The enzyme specifically cleaves ubiquitin from ubiquitin-conjugated protein substrates. The protein is found in the nucleus and cytoplasm. It functions as a co-factor of the DNA-bound
androgen receptor complex, and is inhibited by a protein in the
Ras-
GTPase pathway. The human genome contains several
pseudogenes similar to this gene.[5]
Interactions
USP10 has been shown to
interact with
G3BP1.[6]
In the endothelium, USP10 regulates Notch signaling by slowing down the degradation of the intracellular domain of
NOTCH1. [7]
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.
Puente XS, Sánchez LM, Overall CM, López-Otín C (2003). "Human and mouse proteases: a comparative genomic approach". Nat. Rev. Genet. 4 (7): 544–58.
doi:
10.1038/nrg1111.
PMID12838346.
S2CID2856065.
Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (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.
PMID16189514.
S2CID4427026.
Faus H, Meyer HA, Huber M, Bahr I, Haendler B (2006). "The ubiquitin-specific protease USP10 modulates androgen receptor function". Mol. Cell. Endocrinol. 245 (1–2): 138–46.
doi:
10.1016/j.mce.2005.11.011.
PMID16368182.
S2CID24365493.
Grunda JM, Nabors LB, Palmer CA, Chhieng DC, Steg A,
Mikkelsen T, Diasio RB, Zhang K, Allison D, Grizzle WE, Wang W, Gillespie GY, Johnson MR (2007). "Increased expression of thymidylate synthetase (TS), ubiquitin specific protease 10 (USP10) and survivin is associated with poor survival in glioblastoma multiforme (GBM)". J. Neurooncol. 80 (3): 261–74.
doi:
10.1007/s11060-006-9191-4.
PMID16773218.
S2CID42007677.
Beausoleil SA, Villén J, Gerber SA, Rush J, Gygi SP (2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nat. Biotechnol. 24 (10): 1285–92.
doi:
10.1038/nbt1240.
PMID16964243.
S2CID14294292.
Deng S, Zhou H, Xiong R, Lu Y, Yan D, Xing T, Dong L, Tang E, Yang H (2007). "Over-expression of genes and proteins of ubiquitin specific peptidases (USPs) and proteasome subunits (PSs) in breast cancer tissue observed by the methods of RFDD-PCR and proteomics". Breast Cancer Res. Treat. 104 (1): 21–30.
doi:
10.1007/s10549-006-9393-7.
PMID17004105.
S2CID29643544.