Other Proteins

UBE2F or ubiquitin-conjugating enzyme E2F is part of the ubiquitin network for protein degradation and is involved in protein neddylation. UBE2F has been shown to function as a NEDD8-conjugating enzyme in vitro and in vivo (1). Covalent attachment of the ubiquitin-like protein NEDD8 to a conserved C-terminal domain (ctd) lysine stimulates Cullin Ring ligase (CRL) ubiquitination activity and prevents binding of the inhibitor CAND1 (2). UBE2F Protein is ideal for investigators involved in Signaling Proteins, Ubiquitin Proteins, Cancer, Cell Cycle, and Neurobiology research.

UBE2H or ubiquitin-conjugating enzyme E2H is a member of the E2 ubiquitin-conjugating enzyme family which is located on chromosome 7 (1). UBE2H is known to act on histones and cytoskeletal proteins, both involved in the degenerative pathway of the motor neuron. UBE2H expression is increased during erythroid differentiation of hCD34 (+) cells. Tal1 transcription factor, which is essential for the development of the hematopoietic system and plays a role during definitive erythropoiesis in the adult, activates UBE2H expression, whereas Tal1 knock-down reduced UBE2H expression and ubiquitin transfer activity (2). UBE2H Protein is ideal for investigators involved in Signaling Proteins, Ubiquitin Proteins, Cancer, Cell Cycle, and Neurobiology research.

UBE2J1 is a member of the E2 ubiquitin-conjugating enzyme family which is located in the membrane of the endoplasmic reticulum (ER) and may contribute to quality control ER-associated degradation by the ubiquitin-proteasome system. UBE2J1 play an important role in the homeostatic regulation of MHC class I assembly and expression (1). HRD1 and UBE2J1 associate in a complex together with non-β2m bound MHC class I heavy chains, Derlin 1, and p97 and discriminate misfolded MHC class I from conformational MHC I-β2m-peptide heterotrimers. UBE2J1 Protein is ideal for investigators involved in Signaling Proteins, Ubiquitin Proteins, Cancer, Cell Cycle, and Neurobiology research.

UBE2R1 is a member of the ubiquitin-conjugating enzyme family which catalyzes the covalent attachment of ubiquitin to other proteins. UBE2R1 is a part of the large multiprotein complex which is required for ubiquitin-mediated degradation of cell cycle G1 regulators and for the initiation of DNA replication (1). CK2 can phosphorylate CDC34 and UBC3B at corresponding serine residue in the C terminus of each protein. Phosphorylated UBC3B and CDC34 binds specifically to the F-box protein beta-TRCP which results in enhanced degradation of beta-catenin, a substrate of BTRC. CK2-dependent phosphorylation of CDC34 and UBC3B functions by regulating BTRC substrate recognition (2). UBE2R1 Protein is ideal for investigators involved in Signaling Proteins, Ubiquitin Proteins, Cancer, Cell Cycle, and Neurobiology research.

UBE2R2 (UBC3B) or ubiquitin-conjugating enzyme E2R 2 encodes a protein similar to the E2 ubiquitin conjugating enzyme UBC3/CDC34. CK2-dependent phosphorylation of this ubiquitin-conjugating enzyme functions by regulating beta-TrCP substrate recognition and induces its interaction with beta-TrCP thereby enhancing beta-catenin degradation. CK2-dependent phosphorylation of CDC34 and UBC3B functions by regulating BTRC substrate recognition (1). UBE2R2 complements a yeast cdc34 temperature-sensitive mutant. Deletion and site-directed mutagenesis demonstrated that CK2 phosphorylated UBE2R2 in the C-terminal domain at serine-233; mutagenesis of the corresponding serine residue at position 231 of human CDC34/UBC3 showed that this was the major CK2-phosphorylation site in this protein. UBE2R2 Protein is ideal for investigators involved in Signaling Proteins, Ubiquitin Proteins, Cancer, Cell Cycle, and Neurobiology research.

UBE2U, or Ubiquitin-conjugating enzyme E2 U, belongs to the ubiquitin-conjugating enzyme family. In the global yeast two-hybrid (Y2H) screens to study the specificity of interactions between catalytic domains of the human E2s with RING-type E3s, the analysis showed the UBE2U had a high-quality and physical interactions with a few E3 ligases (1) and (2). UBE2U Protein is ideal for investigators involved in Signaling Proteins, Ubiquitin Proteins, Cancer, Cell Cycle, and Neurobiology research.

UBE2V2 or ubiquitin-conjugating enzyme E2 variant 2 constitutes a distinct subfamily within the E2 protein family which is critical for the catalytic activity of E2s and also shares homology with ubiquitin-conjugating enzyme E2 variant 1 and yeast MMS2 gene product. UBE2V2 may be involved in the differentiation of monocytes and enterocytes (1). UBE2V2 functions in assembly of novel polyubiquitin chains for DNA repair (2). UBE2V2 Protein is ideal for investigators involved in Signaling Proteins, Ubiquitin Proteins, Cancer, Cell Cycle, and Neurobiology research.

UBE2W or ubiquitin-conjugating enzyme E2W (putative) encodes a nuclear-localized ubiquitin-conjugating enzyme (E2) (1). Ubiquitin-conjugating enzyme (E2) along with ubiquitin-activating (E1) and ligating (E3) enzymes coordinates the addition of an ubiquitin moiety to existing proteins. UBE2W interacts with FANCL and regulates the monoubiquitination of Fanconi anemia protein FANCD2 and may be important in the repair of DNA damage (2). UBE2W is highly expressed in heart, brain, liver, and pancreas. UBE2W Protein is ideal for investigators involved in Signaling Proteins, Ubiquitin Proteins, Cancer, Cell Cycle, and Neurobiology research.

UBE2W or ubiquitin-conjugating enzyme E2W (putative) encodes a nuclear-localized ubiquitin-conjugating enzyme (E2) (1). Ubiquitin-conjugating enzyme (E2) along with ubiquitin-activating (E1) and ligating (E3) enzymes coordinates the addition of an ubiquitin moiety to existing proteins. UBE2W interacts with FANCL and regulates the monoubiquitination of Fanconi anemia protein FANCD2 and may be important in the repair of DNA damage (2). UBE2W is highly expressed in heart, brain, liver, and pancreas. UBE2W Protein is ideal for investigators involved in Signaling Proteins, Ubiquitin Proteins, Cancer, Cell Cycle, and Neurobiology research.