Iterative Crystallography Service：Ubiquitin Carboxyl-terminal Hydrolase 7
产品名称： Iterative Crystallography Service：Ubiquitin Carboxyl-terminal Hydrolase 7
英文名称： Iterative Crystallography Service：Ubiquitin Carboxyl-terminal Hydrolase 7
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http://www.creative-biostructure.com/Iterative-crystallography/Iterative-crystallography-CBCRY35.htm
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Cat. No. |
CBCRY35 |
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Background |
Herpesvirus-associated ubiquitin-specific protease (HAUSP, also known as USP7), a deubiquitylating enzyme of the ubiquitin-specific processing protease family, specifically deubiquitylates both p53 and MDM2, hence playing an important yet enigmatic role in the p53-MDM2 pathway. |
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Molecular description |
Protein Classification |
Hydrolase |
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Structure Weight |
121067.00 Da |
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Polymer |
1 |
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Molecule |
Ubiquitin carboxyl-terminal hydrolase 7 |
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Chain Length |
522 amino acids |
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Crystal Description |
PDB ID |
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MMDB ID |
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Source |
E.coli |
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Method |
X-Ray Diffraction |
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Resolution |
3.2Å |
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Gene information |
Gene Name |
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Synonyms |
HAUSP; TEF1; EC 3.1.2.15; Herpes virus-associated ubiquitin-specific protease; ubiquitin specific peptidase 7; ubiquitin specific protease 7 (herpes virus-associated); deubiquitinating enzyme 7; Ubiquitin thioesterase 7 |
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UniProt ID |
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GeneID |
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Chromosome Location |
16p13.3 |
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Function |
cysteine-type endopeptidase activity; ubiquitin thiolesterase activity; protein binding; protein C-terminus binding; peptidase activity; cysteine-type peptidase activity; hydrolase activity |
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Reference |
Hu, M., Gu, L., Li, M., Jeffrey, P.D., Gu, W., Shi, Y. (2006) Structural Basis of Competitive Recognition of p53 and MDM2 by HAUSP/USP7: Implications for the Regulation of the p53-MDM2 Pathway. Plos Biol. 4: e27-e27 |
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