Target Name: USP13
NCBI ID: G8975
Other Name(s): Ubiquitin specific peptidase 13 | ubiquitin-specific-processing protease 13 | ISOT3 | Ubiquitin carboxyl-terminal hydrolase 13 | ubiquitin thiolesterase 13 | ubiquitin thioesterase 13 | ubiquitin specific peptidase 13 | OTTHUMP00000212449 | Ubiquitin thiolesterase 13 | ubiquitin specific protease 13 (isopeptidase T-3) | Ubiquitin specific protease 13 (isopeptidase T-3) | deubiquitinating enzyme 13 | ubiquitin specific peptidase 13 (isopeptidase T-3) | IsoT-3 | ISOT-3 | Ubiquitin-specific-processing protease 13 | UBP13_HUMAN | Deubiquitinating enzyme 13 | Isopeptidase T-3 | Ubiquitin thioesterase 13 | OTTHUMP00000212450

USP13: A Protein Involved in Ubiquitination and Protein-protein Interactions

USP13 (Ubiquitin Specific Peptidase 13) is a protein that is expressed in a wide range of tissues throughout the body, including the liver, pancreas, and muscle. It is a 21-kDa protein that is characterized by its ability to catalyze the hydrolysis of a specific ubiquitin epitope, which is a covalent modification that is attached to proteins. This modification is known as ubiquitination, and it is a critical process that helps to regulate protein-protein interactions and intracellular signaling pathways.

USP13 is a key enzyme in the ubiquitin system, and it is involved in the turnover of ubiquitin proteins. It is a highly conserved protein that has been identified in a variety of organisms, including bacteria, yeast, and eukaryotes. USP13 is often used as a biomarker to study protein-protein interactions and to identify potential drug targets.

One of the unique features of USP13 is its specificity for the ubiquitin epitope that it recognizes. This epitope is a covalent modification that is attached to the protein alpha-2 (HN) domain, and it is located at the N-terminus of the protein. The specificity of USP13 for this epitope allows it to be a useful tool for the study of protein-protein interactions and ubiquitination.

In addition to its role in ubiquitination, USP13 is also involved in the regulation of protein-protein interactions. It is a key enzyme in the ubiquitin-protein interaction, and it is involved in the formation of protein-protein bonds. This interaction between proteins is critical for a variety of cellular processes, including cell signaling, DNA replication, and protein folding.

USP13 is also involved in the regulation of protein stability. It is a key enzyme in the ubiquitin degradation pathway, and it is involved in the removal of damaged or unnecessary ubiquitin proteins. This helps to maintain the levels of stable proteins in the cell and ensures that they are not harmful to the cell.

As a drug target, USP13 is an attractive target for researchers because of its unique structure and its involvement in a variety of cellular processes. Its specificity for the ubiquitin epitope makes it a promising target for small molecules and other therapeutic agents that can modulate its activity. Additionally, its role in the ubiquitin system makes it an attractive target for drugs that are aimed at modulating protein-protein interactions or at regulating protein stability.

In conclusion, USP13 is a protein that is characterized by its ability to catalyze the hydrolysis of a specific ubiquitin epitope. It is a key enzyme in the ubiquitin system and is involved in a variety of cellular processes. As a drug target, it is an attractive target for small molecules and other therapeutic agents that can modulate its activity. Further research is needed to fully understand its role in the ubiquitin system and to develop effective drugs that can target it.

Protein Name: Ubiquitin Specific Peptidase 13

Functions: Deubiquitinase that mediates deubiquitination of target proteins such as BECN1, MITF, SKP2 and USP10 and is involved in various processes such as autophagy and endoplasmic reticulum-associated degradation (ERAD). Component of a regulatory loop that controls autophagy and p53/TP53 levels: mediates deubiquitination of BECN1, a key regulator of autophagy, leading to stabilize the PIK3C3/VPS34-containing complexes. Also deubiquitinates USP10, an essential regulator of p53/TP53 stability. In turn, PIK3C3/VPS34-containing complexes regulate USP13 stability, suggesting the existence of a regulatory system by which PIK3C3/VPS34-containing complexes regulate p53/TP53 protein levels via USP10 and USP13. Recruited by nuclear UFD1 and mediates deubiquitination of SKP2, thereby regulating endoplasmic reticulum-associated degradation (ERAD). Also regulates ERAD through the deubiquitination of UBL4A a component of the BAG6/BAT3 complex. Mediates stabilization of SIAH2 independently of deubiquitinase activity: binds ubiquitinated SIAH2 and acts by impairing SIAH2 autoubiquitination. Has a weak deubiquitinase activity in vitro and preferentially cleaves 'Lys-63'-linked polyubiquitin chains. In contrast to USP5, it is not able to mediate unanchored polyubiquitin disassembly. Able to cleave ISG15 in vitro; however, additional experiments are required to confirm such data

More Common Targets

USP14 | USP15 | USP16 | USP17L1 | USP17L10 | USP17L11 | USP17L12 | USP17L13 | USP17L14P | USP17L15 | USP17L17 | USP17L18 | USP17L2 | USP17L20 | USP17L21 | USP17L24 | USP17L25 | USP17L26 | USP17L27 | USP17L29 | USP17L3 | USP17L5 | USP17L6P | USP17L7 | USP17L8 | USP17L9P | USP18 | USP19 | USP2 | USP2-AS1 | USP20 | USP21 | USP22 | USP24 | USP25 | USP26 | USP27X | USP27X-DT | USP28 | USP29 | USP3 | USP3-AS1 | USP30 | USP30-AS1 | USP31 | USP32 | USP32P1 | USP32P2 | USP32P3 | USP33 | USP34 | USP35 | USP36 | USP37 | USP38 | USP39 | USP4 | USP40 | USP41 | USP42 | USP43 | USP44 | USP45 | USP46 | USP46-DT | USP47 | USP48 | USP49 | USP5 | USP50 | USP51 | USP53 | USP54 | USP6 | USP6NL | USP6NL intronic transcript 1 (non-protein coding), transcript variant 1 | USP7 | USP8 | USP8P1 | USP9X | USP9Y | USPL1 | UST | UTF1 | UTP11 | UTP14A | UTP14C | UTP15 | UTP18 | UTP20 | UTP23 | UTP25 | UTP3 | UTP4 | UTP6 | UTRN | UTS2 | UTS2B | UTS2R | UTY