"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"
"PS51376"	"{'subfamilies': 0, 'domain_architectures': 0, 'interactions': 0, 'matches': 2599, 'pathways': 0, 'proteins': 2598, 'proteomes': 1011, 'sets': 0, 'structural_models': {'alphafold': 2230, 'bfvd': 0}, 'structures': 1, 'taxa': 3548}"	"{}"	"[{'text': '<p>The following proteins share a number of distinct parts, namely, ankyrin\nrepeats, a coiled coil, and a stretch of approximately 140\namino acid residues upstream of the ankyrin repeats, which has been called the\nDof/BCAP/BANK (DBB) domain [[cite:PUB00043704]][[cite:PUB00043705]]:\n\n - Drosophila  Downstream-of-EGF  receptor  (Dof), a protein essential for the\n   morphogenesis of  both  the mesoderm and the tracheae. It has been proposed\n   to mediate the transmission of a signal from an activated receptor to other\n   components of the cell, including the MAP kinase cascade.\n - Vertebrate BANK and BCAP proteins that function in B-cell signaling.\n\nThese proteins are involved in signaling; however, unlike Dof, BANK and BCAP\nare not implicated in FGF signaling but appear to have undergone rapid change\nduring the course of evolution to acquire a novel function with the\ndevelopment of the immune system in higher vertebrates.\n\nThe DBB domain in both Dof and BCAP is required to mediate self-association in\nyeast cells, indicating that this domain may have a more general role in\nmediating protein-protein interactions [[cite:PUB00043704]].\n\nThe profile we developed covers the entire DBB domain.</p>', 'llm': False, 'checked': False, 'updated': False}]"	""	""	""	"IPR017893"	False	False	False	"{'PUB00043704': {'PMID': 12767830, 'ISBN': None, 'volume': '329', 'issue': '3', 'year': 2003, 'title': 'Isolation of proteins that interact with the signal transduction molecule Dof and identification of a functional domain conserved between Dof and vertebrate BCAP.', 'URL': None, 'raw_pages': '479-93', 'medline_journal': 'J Mol Biol', 'ISO_journal': 'J. Mol. Biol.', 'authors': ['Battersby A', 'Csiszar A', 'Leptin M', 'Wilson R.'], 'DOI_URL': 'http://dx.doi.org/10.1016/S0022-2836(03)00489-3'}, 'PUB00043705': {'PMID': 14993266, 'ISBN': None, 'volume': '24', 'issue': '6', 'year': 2004, 'title': 'A functional domain of Dof that is required for fibroblast growth factor signaling.', 'URL': None, 'raw_pages': '2263-76', 'medline_journal': 'Mol Cell Biol', 'ISO_journal': 'Mol. Cell. Biol.', 'authors': ['Wilson R', 'Battersby A', 'Csiszar A', 'Vogelsang E', 'Leptin M.'], 'DOI_URL': 'http://dx.doi.org/10.1128/MCB.24.6.2263-2276.2004'}}"	""	"{'name': 'DBB domain profile', 'short': 'DBB'}"	""	""	""	"profile"	"domain"	""