CDC34

CDC34 (Cell Division Cycle 34) is a Protein Coding gene. Among its related pathways are Metabolism of proteins and CLEC7A (Dectin-1) signaling. Gene Ontology (GO) annotations related to this gene include ligase activity and ubiquitin protein ligase binding. An important paralog of this gene is UBE2R2.

Cell Division Cycle 34

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination (PubMed:22496338).
Cooperates with the E2 UBCH5C and the SCF(FBXW11) E3 ligase complex for the polyubiquitination of NFKBIA leading to its subsequent proteasomal degradation. Performs ubiquitin chain elongation building ubiquitin chains from the UBE2D3-primed NFKBIA-linked ubiquitin. UBE2D3 acts as an initiator E2, priming the phosphorylated NFKBIA target at positions 'Lys-21' and/or 'Lys-22' with a monoubiquitin. Cooperates with the SCF(SKP2) E3 ligase complex to regulate cell proliferation through ubiquitination and degradation of MYBL2 and KIP1. Involved in ubiquitin conjugation and degradation of CREM isoform ICERIIgamma and ATF15 resulting in abrogation of ICERIIgamma- and ATF5-mediated repression of cAMP-induced transcription during both meiotic and mitotic cell cycles. Involved in the regulation of the cell cycle G2/M phase through its targeting of the WEE1 kinase for ubiquitination and degradation. Also involved in the degradation of beta-catenin. Is target of human herpes virus 1 protein ICP0, leading to ICP0-dependent dynamic interaction with proteasomes (PubMed:10329681, PubMed:10373550, PubMed:10871850, PubMed:11675391, PubMed:12037680, PubMed:15652359, PubMed:17461777, PubMed:17698585, PubMed:19112177, PubMed:19126550, PubMed:19945379, PubMed:20061386, PubMed:20347421).

Cellular protein modification process Source: UniProtKB
Cellular response to interferon-beta Source: UniProtKB
DNA replication initiation Source: UniProtKB
G1/S transition of mitotic cell cycle Source: UniProtKB
Negative regulation of cAMP-mediated signaling Source: UniProtKB
Positive regulation of inclusion body assembly Source: Ensembl
Positive regulation of neuron apoptotic process Source: Ensembl
Proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
Protein K48-linked ubiquitination Source: UniProtKB
Protein polyubiquitination Source: UniProtKB
Protein ubiquitination Source: UniProtKB
Response to growth factor Source: Ensembl
Ubiquitin-dependent protein catabolic process Source: GO_Central

Nucleus; Cytoplasm. The phosphorylation of the C-terminal tail plays an important role in mediating nuclear localization. Colocalizes with beta-tubulin on mitotic spindles in anaphase.

Autoubiquitinated (PubMed:22496338, PubMed:11805320, PubMed:12060736). Autoubiquitination is promoted by the human herpes virus 1 protein ICP0 and leads to degradation by the Ubiquitin-proteasomal pathway (PubMed:11805320, PubMed:12060736).
Phosphorylated by CK2. Phosphorylation of the C-terminal tail by CK2 controles the nuclear localization.