ubiquitin specific protease 3 fragment

ApexBio

Short Summary : Deubiquitinates uH2A/uH2B

Category : Cancer Biology|Cancer Biology Peptides

Purity : 0.9699

CAS Number :

Formula : C38H68N10O15S

Molecular Weight : 937.07

SMILE : NC(CO)C(NC(C(O)C)C(NC(C(C)O)C(NC(C)C(NC(C(C)CC)C(NC(CS)C(NC(C)C(NC(C(O)C)C(NCC(NC(CC(C)C)C(O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O

Solubility : >93.7mg/mL in DMSO

Storage : Store at -20°C

Description : The ubiquitin speci c protease 3 USP3 is a deubiquitinating enzyme for uH2A and uH2B. USP3 dynamically associates with chromatin and deubiquitinates H2A/H2B in vivo. The ZnF-UBP domain of USP3 mediates uH2AUSP3 interaction. Functional ablation of USP3 by RNAi leads to delay of S phase progression and to accumulation of DNA breaks, with ensuing activation of DNA damage checkpoint pathways. In response to ionizing radiation, (1) uH2A redistributes and colocalizes in g-H2AX DNA repair foci and (2) USP3 is required for full deubiquitination of ubiquitin-conjugates/uH2A and g-H2AX dephosphorylation. USP3 is a novel regulator of H2A and H2B ubiquitination, highlight its role in preventing replication stress, and suggest its involvement in the response to DNA double-strand breaks1.
USP3 has been characterized as a functional DUB in vitro, and it is the human DUB most homologous to S. cerevisiae Ubp8, which regulates H2B deubiquitination2-4.
Figure1. Formula of Ubiquitin specific protease 3 fragment
Ref:
1.F. Nicassio, N. Corrado et al. Human USP3 Is a Chromatin Modi er Required for S Phase Progression and Genome Stability. Current Biology 17, 1972–1977.
2.Sloper-Mould, K.E., Eyre, H.J., Wang, X.W., Sutherland, G.R., and Baker, R.T. (1999). Characterization and chromosomal localization of USP3, a novel human ubiquitin-speci c protease. J. Biol. Chem. 274, 26878–26884.
3.Henry, K.W., Wyce, A., Lo, W.S., Duggan, L.J., Emre, N.C., Kao, C.F., Pillus, L., Shilatifard, A., Osley, M.A., and Berger, S.L. (2003). Transcriptional activation via sequential histone H2B ubiquitylation and deubiquitylation, mediated by SAGA-associated Ubp8. Genes Dev. 17, 2648–2663.
4.Zhang, Y. (2003). Transcriptional regulation by histone ubiquitination and deubiquitination. Genes Dev. 17, 2733–2740.

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