CDC34
CDC34 (cell division cycle 34, ubiquitin conjugating enzyme), also known as UBE2R1, UBC3 and E2-CDC34, is an E2 enzyme that accepts ubiquitin from an E1 enzyme and helps attach it to substrates via E3 ligase complexes. It contributes to cell cycle control and protein degradation. Browse Assay Genie's current range of CDC34 research reagents below, or read on for the biology behind the target.
CDC34 is an E2 ubiquitin-conjugating enzyme. It accepts ubiquitin from an E1 ubiquitin-activating protein and catalyses its covalent attachment to other proteins, working together with an E3 ubiquitin-protein ligase complex. In vitro, it catalyses Lys-48-linked polyubiquitination. In several pathways it acts as a chain-elongating E2: with the SCF(FBXW11) E3 complex it cooperates with UBCH5C (UBE2D3), which primes phosphorylated NFKBIA at Lys-21 and/or Lys-22 with a monoubiquitin, and CDC34 then extends the chain, leading to proteasomal degradation of NFKBIA.
With the SCF(SKP2) E3 complex, CDC34 regulates cell proliferation through ubiquitination and degradation of MYBL2 and KIP1. It is also involved in the ubiquitin-dependent degradation of CREM isoform ICERIIgamma and ATF15, which relieves ICERIIgamma- and ATF5-mediated repression of cAMP-induced transcription in meiotic and mitotic cell cycles. It targets the WEE1 kinase for degradation, thereby regulating the G2/M phase of the cell cycle, and is also involved in beta-catenin degradation. The herpes virus 1 protein ICP0 targets CDC34, leading to an ICP0-dependent dynamic interaction with proteasomes.
The CDC34 gene encodes a member of the ubiquitin-conjugating enzyme family, assigned by HGNC to the ubiquitin conjugating enzymes E2 group. The protein is part of a large multiprotein complex required for ubiquitin-mediated degradation of cell cycle G1 regulators and for the initiation of DNA replication. UniProt reports it in the cytoplasm and nucleus. The gene was formerly named cell division cycle 34, and the mouse ortholog is Cdc34.
CDC34 drives degradation of G1 regulators and WEE1, making it a key enzyme for studying G1/S progression, G2/M control and DNA replication initiation.
As an E2 that elongates Lys-48-linked chains with SCF E3 ligases, CDC34 is used to study ubiquitin transfer and proteasomal targeting.
CDC34 extends ubiquitin chains on phosphorylated NFKBIA primed by UBE2D3, linking E2 cooperation to NF-κB pathway regulation.
Through SCF(SKP2)-dependent degradation of MYBL2 and KIP1, and degradation of beta-catenin, CDC34 connects ubiquitination to proliferation control.
CDC34 is an E2 ubiquitin-conjugating enzyme. It accepts ubiquitin from an E1 enzyme and, with E3 ligase complexes such as SCF(SKP2) and SCF(FBXW11), builds Lys-48-linked chains on substrates including NFKBIA, MYBL2, KIP1, WEE1 and beta-catenin, marking them for proteasomal degradation.
CDC34 is also called UBE2R1, UBC3 and E2-CDC34. UniProt lists the protein as ubiquitin-conjugating enzyme E2 R1, and the gene was previously named cell division cycle 34. Its enzymatic activity is classed under EC 2.3.2.23, the E2 ubiquitin-conjugating enzyme activity.
A mouse ortholog, Cdc34, is recognised, and the protein belongs to the broadly conserved ubiquitin-conjugating enzyme family. Researchers working in other species should check the datasheet of any product for its validated reactivity.
Other cell division cycle proteins, anaphase-promoting complex subunits and DNA replication regulators with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P49427; product specifications from Assay Genie datasheets.