"accession"	"counters"	"cross_references"	"description"	"entry_id"	"go_terms"	"hierarchy"	"integrated"	"is_llm"	"is_reviewed_llm"	"is_updated_llm"	"literature"	"member_databases"	"name"	"overlaps_with"	"representative_structure"	"set_info"	"source_database"	"type"	"wikipedia"
"PF12014"	"{'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}"	"{}"	"[{'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}]"	""	""	""	""	False	False	False	"{'PUB00098610': {'PMID': 29279382, 'ISBN': None, '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': None, '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': None}}"	""	"{'name': 'Cyclin D1 binding domain', 'short': 'Cyclin_D1_bind'}"	""	""	""	"pfam"	"domain"	""