{"metadata":{"accession":"PF12014","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":null,"hierarchy":null,"name":{"name":"Cyclin D1 binding domain","short":"Cyclin_D1_bind"},"description":[{"text":"<p>Ubiquitin-dependent proteolysis of cyclin D1 is associated with normal and tumour cell proliferation and survival. The best characterised member of this family is the SCF FBXO31 (Skp1-Cul1-Rbx1-FBXO31) ubiquitin ligase complex mediates genotoxic stress-induced cyclin D1 degradation [[cite:PUB00098610]]. FBXO31 possesses a unique substrate-binding beta barrel domain, whereas cyclin D1 binds to FBXO31 by tucking its free C-terminal carboxylate tail into an open cavity of the C-terminal FBXO31 beta-barrel. Biophysical and functional studies demonstrated that SCFFBXO31 is capable of recruiting and ubiquitinating cyclin D1 in a phosphorylation-independent manner.</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00098610":{"PMID":29279382,"ISBN":null,"volume":"115","issue":"2","year":2018,"title":"Structural basis of the phosphorylation-independent recognition of cyclin D1 by the SCF<sup>FBXO31</sup> ubiquitin ligase.","URL":null,"raw_pages":"319-324","medline_journal":"Proc Natl Acad Sci U S A","ISO_journal":"Proc Natl Acad Sci U S A","authors":["Li Y","Jin K","Bunker E","Zhang X","Luo X","Liu X","Hao B."],"DOI_URL":null}},"set_info":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":87,"interactions":0,"matches":5032,"pathways":0,"proteins":5016,"proteomes":2194,"sets":0,"structural_models":{"alphafold":4473,"bfvd":0},"structures":2,"taxa":6206},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":91,"alignment:full":3341},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}