人 USP20 抗体对
01AB02703
Ubiquitin specific peptidase 20 (USP20) is a cysteine protease deubiquitinating enzyme encoded by the USP20 gene located on chromosome 9q34.11. It is a 914-amino acid protein containing conserved cysteine and histidine residues at its catalytic site and has four domains: an N-terminal zinc finger ubiquitin-binding domain, a catalytic domain, and two C-terminal DUSP domains. USP20 functions by cleaving ubiquitin molecules from substrate proteins, thereby regulating protein stability and recycling. It is known to deubiquitinate proteins such as thyronine deiodinase type 2, hypoxia-inducible factor 1α, and β2-adrenergic receptor, impacting various cellular processes including proliferation and migration. Dysregulation of USP20 is implicated in diseases such as cancer, particularly in tumorigenesis where it stabilizes tumorigenic or antitumor proteins, as well as in inflammation-related conditions like atherosclerosis and cancer through modulation of NF-κB signaling. Its alteration has been linked to colorectal cancer metastasis, antiviral immunity, metabolic disorders, and neurological diseases, highlighting USP20's potential as a therapeutic target.
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技术参数
- 靶点基因名
- USP20
- 基因别名
- KIAA1003; LSFR3A; VDU2
- 蛋白别名
- ubiquitin specific peptidase 20; USP20
- UniProt
- Q9Y2K6
- 物种
- Human
产品详情
- 靶点名称
- USP20
- 蛋白名称
- ubiquitin specific peptidase 20
- 蛋白别名
- Ubiquitin carboxyl-terminal hydrolase 20; Deubiquitinating enzyme 20; Ubiquitin thioesterase 20; Ubiquitin-specific-processing protease 20; VHL-interacting deubiquitinating enzyme 2; hVDU2
- 靶点基因名
- USP20
- 基因别名
- KIAA1003; LSFR3A; VDU2
- UniProt
- Q9Y2K6
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Ubiquitin specific peptidase 20 (USP20) is a cysteine protease deubiquitinating enzyme encoded by the USP20 gene located on chromosome 9q34.11. It is a 914-amino acid protein containing conserved cysteine and histidine residues at its catalytic site and has four domains: an N-terminal zinc finger ubiquitin-binding domain, a catalytic domain, and two C-terminal DUSP domains. USP20 functions by cleaving ubiquitin molecules from substrate proteins, thereby regulating protein stability and recycling. It is known to deubiquitinate proteins such as thyronine deiodinase type 2, hypoxia-inducible factor 1α, and β2-adrenergic receptor, impacting various cellular processes including proliferation and migration. Dysregulation of USP20 is implicated in diseases such as cancer, particularly in tumorigenesis where it stabilizes tumorigenic or antitumor proteins, as well as in inflammation-related conditions like atherosclerosis and cancer through modulation of NF-κB signaling. Its alteration has been linked to colorectal cancer metastasis, antiviral immunity, metabolic disorders, and neurological diseases, highlighting USP20's potential as a therapeutic target.