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27401 Ensembl ENSG00000145604 ENSMUSG00000054115 UniProt Q13309 Q9Z0Z3 RefSeq (mRNA) NM_001243120 NM_005983 NM_032637 NM_001285980 NM_013787 NM_145468 RefSeq (protein) NP_001230049 NP_005974 NP_116026 NP_001272909 NP_038815 Location (UCSC) Chr 5: 36.15 – 36.2 Mb Chr 15: 9.11 – 9.16 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse S-phase kinase-associated protein 2 is an enzyme ...
Skp, Cullin, F-box containing complex (or SCF complex) is a multi-protein E3 ubiquitin ligase complex that catalyzes the ubiquitination of proteins destined for 26S proteasomal degradation. [1] Along with the anaphase-promoting complex, [2] SCF has important roles in the ubiquitination of proteins involved in the cell cycle. The SCF complex ...
The kinesin-13 family, unlike other kinesins, has an internally positioned motor domain. They were initially named KIF-M because of the unique location of their catalytic core in the middle of the polypeptide between the N-terminal globular domain and the C-terminal stalk but they are truly special due to their versatile nature.
During S phase, Cdc6 and Cdt1 are degraded or inactivated to block additional pre-RC formation, and bidirectional DNA replication ensues. When the replication fork encounters lesions in the DNA, the S-phase checkpoint response slows or stops fork progression and stabilizes the association of MCM2-7 with the replication fork during DNA repair.
DNA ligase 1 also DNA ligase I, is an enzyme that in humans is encoded by the LIG1 gene. DNA ligase 1 is the only known eukaryotic DNA ligase involved in both DNA replication and repair, making it the most studied of the ligases.
In biochemistry, a ligase is an enzyme that can catalyze the joining of two molecules by forming a new chemical bond. This is typically via hydrolysis of a small pendant chemical group on one of the molecules, typically resulting in the formation of new C-O, C-S, or C-N bonds.
DNA ligase is an enzyme that joins together ends of DNA molecules. Although commonly represented as joining two pairs of ends at once, as in the ligation of restriction enzyme fragments, ligase can also join the ends on only one of the two strands (for example, when the other strand is already continuous or lacks a terminal phosphate necessary for ligation).
The RING protein appears to function as a docking site for ubiquitin-conjugating enzymes (E2s). Other proteins contain a cullin-homology domain, such as CUL9 , also known as p53 cytoplasmic anchor PARC , and the ANAPC2 subunit of the anaphase-promoting complex/cyclosome; both CUL9 and ANAPC2 have ubiquitin ligase activity.