USP5

USP5 cleaves linear and branched multiubiquitin polymers with a marked preference for branched polymers. USP5 is involved in unanchored 'Lys-48'-linked polyubiquitin disassembly. USP5 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.

USP5 Alternative Names

USP5, ISOT [Homo sapiens]

Usp5, AA407472, ISOT, ISOT-1, Ucht [Mus musculus]

Summaries for USP5

Entrez Gene summary for USP5:

Ubiquitin (see MIM 191339)-dependent proteolysis is a complex pathway of protein metabolism implicated in such diverse cellular functions as maintenance of chromatin structure, receptor function, and degradation of abnormal proteins. A late step of the process involves disassembly of the polyubiquitin chains on degraded proteins into ubiquitin monomers. USP5 disassembles branched polyubiquitin chains by a sequential exo mechanism, starting at the proximal end of the chain (Wilkinson et al., 1995 ).[supplied by OMIM, Mar 2010]

OMIM - description for USP5:

Ubiquitin (see 191339)-dependent proteolysis is a complex pathway of protein metabolism implicated in such diverse cellular functions as maintenance of chromatin structure, receptor function, and degradation of abnormal proteins. A late step of the process involves disassembly of the polyubiquitin chains on degraded proteins into ubiquitin monomers. USP5 disassembles branched polyubiquitin chains by a sequential exo mechanism, starting at the proximal end of the chain (Wilkinson et al., 1995).

Wikipedia summary for USP5:

Ubiquitin carboxyl-terminal hydrolase 5 is an enzyme that in humans is encoded by the USP5 gene.

Human USP5 Protein General Information

 

• Protein names: Ubiquitin-specific-processing protease 5
  Short name=USP5
• Sequence length: 858 AA.
• Domain: The UBP-type zinc finger domain interacts selectively with an unmodified C-terminus of the proximal ubiquitin. Both UBA domains are involved in polyubiquitin recognition.
• Sequence similarities: Belongs to the peptidase C19 family.
  Contains 2 UBA domains.
  Contains 1 UBP-type zinc finger.
• Catalytic activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
• Subunit structure: Interacts with TRIML1
• Cofactor: Binds 1 zinc ion.
• Miscellaneous: The UBP-type zinc finger domain crystallizes as a dimer linked by a disulfide bond between the Cys-195 residues of both molecules, but there is no evidence that the full-length USP5 exists as a dimer.

General information above from UniProt

Function for USP5 Protein

UniProtKB:

USP5 cleaves linear and branched multiubiquitin polymers with a marked preference for branched polymers. USP5 is involved in unanchored 'Lys-48'-linked polyubiquitin disassembly. USP5 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.

Genatlas:

• USP5 is zinc-binding deubiquitinating enzyme, clearing bonds between UB and unfolded polypeptide or UB and small substituents, also disassembling branched polyubiquitin chains

Homology for human USP5

• paralog to ubiquitin C terminal hydrolases ucl+