"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"
"SM01299"	"{'subfamilies': 0, 'domain_architectures': 0, 'interactions': 0, 'matches': 3308, 'pathways': 0, 'proteins': 3308, 'proteomes': 922, 'sets': 0, 'structural_models': {'alphafold': 3033, 'bfvd': 0}, 'structures': 0, 'taxa': 3040}"	"{}"	"[{'text': '<p>The FAM69 family of cysteine-rich type II transmembrane proteins localise to the endoplasmic reticulum (ER) in cultured cells, probably via N-terminal di-arginine motifs. These proteins carry at least 14 luminal cysteines which are conserved in all FAM69s. There are currently few indications of the involvement of FAM69 members in human diseases [cite:PUB00066680]. It would appear that FAM69 proteins are predicted to be have a protein kinase structure and function. Analysis of three-dimensional structure models and conservation of the classic catalytic motifs of protein kinases in four of human FAM69 proteins suggests they might have retained catalytic phosphotransferase activity. An EF-hand Ca2+-binding domain, inserted within the structure of the kinase domain, suggests they function as Ca2+-dependent kinases (unpublished).</p>', 'llm': False, 'checked': False, 'updated': False}]"	""	""	""	"IPR029244"	False	False	False	"{'PUB00066680': {'PMID': 21334309, 'ISBN': None, 'volume': '406', 'issue': '3', 'year': 2011, 'title': 'Characterisation of the FAM69 family of cysteine-rich endoplasmic reticulum proteins.', 'URL': None, 'raw_pages': '471-7', 'medline_journal': 'Biochem Biophys Res Commun', 'ISO_journal': 'Biochem. Biophys. Res. Commun.', 'authors': ['Tennant-Eyles AJ', 'Moffitt H', 'Whitehouse CA', 'Roberts RG.'], 'DOI_URL': 'http://dx.doi.org/10.1016/j.bbrc.2011.02.076'}}"	""	"{'name': 'N-term cysteine-rich ER, FAM69', 'short': 'PIP49_N'}"	""	""	""	"smart"	"domain"	""