{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["25(21)"],"submitter":["Hara T"],"pubmed_abstract":["KPC2 (Kip1 ubiquitylation-promoting complex 2) together with KPC1 forms the ubiquitin ligase KPC, which regulates degradation of the cyclin-dependent kinase inhibitor p27 at the G(1) phase of the cell cycle. KPC2 contains a ubiquitin-like (UBL) domain, two ubiquitin-associated (UBA) domains, and a heat shock chaperonin-binding (STI1) domain. We now show that KPC2 interacts with KPC1 through its UBL domain, with the 26S proteasome through its UBL and NH(2)-terminal UBA domains, and with polyubiquitylated proteins through its UBA domains. The association of KPC2 with KPC1 was found to stabilize KPC1 in a manner dependent on the STI1 domain of KPC2. KPC2 mutants that lacked either the NH(2)-terminal or the COOH-terminal UBA domain supported the polyubiquitylation of p27 in vitro, whereas a KP"],"journal":["Molecular and cellular biology"],"pagination":["9292-303"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC1265808"],"repository":["biostudies-literature"],"pubmed_title":["Role of the UBL-UBA protein KPC2 in degradation of p27 at G1 phase of the cell cycle."],"pmcid":["PMC1265808"],"pubmed_authors":["Kotoshiba S","Fujiwara K","Mizushima N","Onoyama I","Shirakawa M","Hara T","Nakayama KI","Kamura T","Takahashi H"],"additional_accession":[]},"is_claimable":false,"name":"Role of the UBL-UBA protein KPC2 in degradation of p27 at G1 phase of the cell cycle.","description":"KPC2 (Kip1 ubiquitylation-promoting complex 2) together with KPC1 forms the ubiquitin ligase KPC, which regulates degradation of the cyclin-dependent kinase inhibitor p27 at the G(1) phase of the cell cycle. KPC2 contains a ubiquitin-like (UBL) domain, two ubiquitin-associated (UBA) domains, and a heat shock chaperonin-binding (STI1) domain. We now show that KPC2 interacts with KPC1 through its UBL domain, with the 26S proteasome through its UBL and NH(2)-terminal UBA domains, and with polyubiquitylated proteins through its UBA domains. The association of KPC2 with KPC1 was found to stabilize KPC1 in a manner dependent on the STI1 domain of KPC2. KPC2 mutants that lacked either the NH(2)-terminal or the COOH-terminal UBA domain supported the polyubiquitylation of p27 in vitro, whereas a KP","dates":{"release":"2005-01-01T00:00:00Z","publication":"2005 Nov","modification":"2025-04-25T21:21:16.964Z","creation":"2019-03-27T01:25:21Z"},"accession":"S-EPMC1265808","cross_references":{"pubmed":["16227581"],"doi":["10.1128/mcb.25.21.9292-9303.2005","10.1128/MCB.25.21.9292-9303.2005"]}}