CDC7 siRNA – Cell Division Cycle 7-Related Protein Kinase Isoform 1 (Mouse)

CDC7: an evolutionarily conserved serine/threonine protein kinase of the CDC7 family. Predominantly localized in the nucleus, it plays a pivotal role in linking cell cycle regulation to genome duplication, being essential for the firing of DNA replication origins. Plays an essential role in initiating DNA replication at replication origins by phosphorylating the MCM2 and MCM4 subunits of the MCM2-7 helicase complex. The human protein requires phosphorylation by CDK1 at T376 and binding to activator of S-phase kinase (ASK)/DBF4B to be fully activated. The interaction between Cdc7 and DBFK subunits facilitates ATP binding and substrate recognition by the Cdc7 kinase. Although CDC7 expression levels appear to be constant throughout the cell cycle, the expression levels of DBF4B is cell cycle-regulated. Thus, the CDC7 activity is activated during S phase in eukaryotes. The Cdc7/ DBF4B complex regulates initiation of DNA replication by phosphorylating chromatin-bound mini-chromosome maintenance protein 2 (MCM2). Impaired Cdc7 kinase activity leads to S-phase arrest. Plays a role in the TGF-beta regulation of smooth muscle cell (SMC) differentiation. Interacts with Smad3 to facilitate Smad3 binding to SMC marker promoter, leading to the activation of SMC marker gene transcription.

Protein type: Kinase, protein; Protein kinase, Other; Protein kinase, Ser/Thr (non-receptor); EC 2.7.11.1; Other group; CDC7 family

Cellular Component: microtubule cytoskeleton; nucleoplasm; intercellular bridge; cytoplasm; nucleus

Molecular Function: transferase activity; protein serine/threonine kinase activity; metal ion binding; transferase activity, transferring phosphorus-containing groups; nucleotide binding; kinase activity; ATP binding; protein kinase activity

Biological Process: regulation of cell shape; peptidyl-serine phosphorylation; DNA replication initiation; cell division; positive regulation of cell proliferation; cell cycle; phosphorylation; protein amino acid phosphorylation; phagocytosis; double-strand break repair via break-induced replication