3ihp
Covalent Ubiquitin-Usp5 ComplexCovalent Ubiquitin-Usp5 Complex
Structural highlights
Function[UBP5_HUMAN] Cleaves linear and branched multiubiquitin polymers with a marked preference for branched polymers. Involved in unanchored 'Lys-48'-linked polyubiquitin disassembly. Binds linear and 'Lys-63'-linked polyubiquitin with a lower affinity. Knock-down of USP5 causes the accumulation of p53/TP53 and an increase in p53/TP53 transcriptional activity because the unanchored polyubiquitin that accumulates is able to compete with ubiquitinated p53/TP53 but not with MDM2 for proteasomal recognition.[1] Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See AlsoReferences
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OCACategories:
- Human
- Large Structures
- Ubiquitin thiolesterase
- Arrowsmith, C H
- Avvakumov, G V
- Bochkarev, A
- Bountra, C
- Butler-Cole, C
- Dhe-Paganon, S
- Edwards, A M
- Structural genomic
- Walker, J R
- Weigelt, J
- Xue, S
- Acetylation
- Alternative splicing
- Cytoplasm
- Hydrolase
- Isopeptide bond
- Metal-binding
- Nucleus
- Phosphoprotein
- Protease
- Sgc
- Thiol protease
- Ubl conjugation
- Ubl conjugation pathway
- Zinc
- Zinc-finger