Ubiquitin-conjugating enzyme E2E1 (UBE2E1) is a member of the ubiquitin-donjugating enzyme family. UBE2E1 is a protein localized to the nucleus. The modification of proteins with ubiquitin is an importantly step for targeting abnormal or short-lived proteins for degeneration. It has been demonstrated to be released to Sjogrens's syndrome and systemic lupus Erythematosus. Patients with the systemic autoimmune diseases Sjogrens's syndrome and systemic lupus erythematosus often have autoantibodies against the intracellular protein Ro52 that is an E3 ligase dependent on the ubiquitin conjugation enzymes UBE2E1. Ro52 mediates ubiquitination through UBE2D1 in the cytoplasm and through UBE2E1 in the nucleus.
UBE2E1 (UbcH6) Proteins
UBE2E1 (UbcH6) Antibodies
UBE2E1 (UbcH6) ELISA Pair sets
UBE2E1 (UbcH6) cDNA Clones
UbcM3, Ubce5, ubcM2[Mus musculus]
Entrez Gene summary for UBE2E1 (UbcH6):
The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. UBE2E1 gene encodes a member of the E2 ubiquitin-conjugating enzyme family. Three alternatively spliced transcript variants encoding distinct isoforms have been found for UBE2E1 gene. [provided by RefSeq, Jan 2011]
OMIM - description for UBE2E1 (UbcH6):
The ubiquitin system plays a major role in selective protein degradation. This pathway first requires the covalent attachment of ubiquitin, a highly conserved 76-amino acid protein, to defined lysine residues of substrate proteins. Ubiquitin-protein conjugates are then recognized and degraded by a specific protease complex, the 26 S proteasome. Protein ubiquitination involves 3 classes of enzymes: the ubiquitin-activating enzymes E1 (e.g., UBE1 ), the ubiquitin-conjugating enzymes E2, and the ubiquitin-protein ligases E3 (e.g., UBE3A ). One evolutionarily conserved subfamily of E2s includes human UBCH5A (UBE2D1 ), S. cerevisiae UBC4 and UBC5, and Arabidopsis thaliana UBC8.
Wikipedia summary for UBE2E1 (UbcH6):
Ubiquitin-conjugating enzyme E2 E1 is a protein that in humans is encoded by the UBE2E1 gene.
The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.
Ubiquitin-conjugating enzyme E2 E1
Protein modification; protein ubiquitination.
Belongs to the ubiquitin-conjugating enzyme family.
ISGylation suppresses ubiquitin E2 enzyme activity.
Interacts with RNF14.
ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.
General information above from UniProt
UBE2E1 accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. UBE2E1 catalyzes the covalent attachment of ISG15 to other proteins. UBE2E1 mediates the selective degradation of short-lived and abnormal proteins. In vitro, UBE2E1 also catalyzes 'Lys-48'-linked polyubiquitination.
- UBE2E1 is E2 enzymes for ubiquitin conjugation, that may be involved in the ubiquitination of various proteins
- UBE2E1 modulates the transcriptional repression activity of ATXN1 by modulating the degradation of ATXN1