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Related Concept Videos

The Proteasome01:13

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin...
The Proteasome02:18

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
Regulated Protein Degradation02:58

Regulated Protein Degradation

It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
The Proteasome Structure01:17

The Proteasome Structure

The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
The proteasome is an...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...

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Related Experiment Video

Updated: Jul 14, 2026

In Vitro Analysis of E3 Ubiquitin Ligase Function
06:06

In Vitro Analysis of E3 Ubiquitin Ligase Function

Published on: May 14, 2021

UBE1L2, a novel E1 enzyme specific for ubiquitin.

Christiane Pelzer1, Ingrid Kassner, Konstantin Matentzoglu

  • 1Division of Immunology, Department of Biology, University of Constance, 78457 Konstanz, Germany.

The Journal of Biological Chemistry
|June 21, 2007
PubMed
Summary

Researchers discovered UBE1L2, a novel human ubiquitin-activating enzyme (E1) crucial for protein ubiquitylation. This enzyme, highly expressed in testes, plays a role in essential cellular processes like p53 modification.

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Measuring Enzymatic Activity of Neurodevelopmental Disorder-Associated Deubiquitylating Enzymes via an In Vitro Ubiquitin Chain Cleavage Assay
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Measuring Enzymatic Activity of Neurodevelopmental Disorder-Associated Deubiquitylating Enzymes via an In Vitro Ubiquitin Chain Cleavage Assay

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Functional Characterization of RING-Type E3 Ubiquitin Ligases In Vitro and In Planta
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Functional Characterization of RING-Type E3 Ubiquitin Ligases In Vitro and In Planta

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Last Updated: Jul 14, 2026

In Vitro Analysis of E3 Ubiquitin Ligase Function
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Measuring Enzymatic Activity of Neurodevelopmental Disorder-Associated Deubiquitylating Enzymes via an In Vitro Ubiquitin Chain Cleavage Assay
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Measuring Enzymatic Activity of Neurodevelopmental Disorder-Associated Deubiquitylating Enzymes via an In Vitro Ubiquitin Chain Cleavage Assay

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Functional Characterization of RING-Type E3 Ubiquitin Ligases In Vitro and In Planta
10:27

Functional Characterization of RING-Type E3 Ubiquitin Ligases In Vitro and In Planta

Published on: December 5, 2019

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Biology

Background:

  • The human ubiquitin-activating enzyme (UBE1) is essential for ubiquitin activation, a critical step in protein degradation and signaling.
  • Understanding the ubiquitin-activating enzyme family is key to deciphering cellular regulation.

Purpose of the Study:

  • To identify and characterize novel human ubiquitin-activating enzymes.
  • To investigate the enzymatic activity and biological relevance of the newly identified UBE1L2.

Main Methods:

  • Sequence homology analysis to identify UBE1L2.
  • In vitro enzymatic assays to assess ubiquitin activation and transfer.
  • In vivo studies to confirm covalent linkage and ubiquitylation.
  • mRNA expression analysis to determine tissue specificity.

Main Results:

  • A novel human ubiquitin-activating enzyme, UBE1L2, was identified with significant homology to UBE1.
  • UBE1L2 demonstrated ATP-dependent activation and covalent linking of ubiquitin in vitro and in vivo.
  • Activated ubiquitin by UBE1L2 facilitated ubiquitylation of p53 by MDM2 and supported autoubiquitylation of E3 ligases.
  • UBE1L2 mRNA expression was highest in the testis, indicating potential organ-specific function.

Conclusions:

  • UBE1L2 is a functional human ubiquitin-activating enzyme with conserved E1 family characteristics.
  • UBE1L2 participates in the ubiquitylation cascade, impacting key proteins like p53 and E3 ligases.
  • The testis-specific expression of UBE1L2 suggests a specialized role in reproductive tissues.