{
    "uniprot_canonical_ac": "A2AMT1-1", 
    "publication_count": 9, 
    "reported_interactions": 0, 
    "record_type": "protein", 
    "predicted_glycosites": 0, 
    "protein_names_refseq": "beaded filament structural protein in lens-CP94; filensin; lens fiber cell beaded-filament structural protein CP 95; filensin isoform a", 
    "refseq_ac": "NP_001277990.1", 
    "reported_n_glycosites": 0, 
    "refseq_name": "filensin isoform a", 
    "record_id": "A2AMT1-1", 
    "protein_names_uniprotkb": "Filensin C-terminal fragment; Filensin N-terminal fragment; Filensin; Beaded filament structural protein 1; CP95; Lens fiber cell beaded-filament structural protein CP 95", 
    "pathway": " (mmu:12075)", 
    "function": "AQP0 modulates GJs in the presence of BF proteins to maintain lens transparency and homeostasis., [RefSeq]; CP49 and filensin have been considered robust markers for mouse lens fiber cell differentiation. The data reported here, however, document both proteins in the mouse lens epithelium, but only after 5 weeks of age, when lens epithelial growth and mitotic activity have slowed. Publication Status: Online-Only, [RefSeq]; Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (PubMed:27559293). Involved in altering the calcium regulation of MIP water permeability (By similarity)., [UniProtKB]", 
    "protein_name": "Filensin C-terminal fragment; Filensin N-terminal fragment; Filensin", 
    "reported_mutagensis": 0, 
    "reported_phosphosites": 4, 
    "reported_o_glycosites_with_glycan": 0, 
    "tax_id": 10090, 
    "organism": "Mus musculus", 
    "disease": "cataract 33 (Disease Ontology:DOID:0110264)", 
    "reported_glycation": 0, 
    "reported_snv": 0, 
    "mass": 73669.0, 
    "gene_names_uniprotkb": "Bfsp1", 
    "reported_n_glycosites_with_glycan": 0, 
    "reported_o_glycosites": 0, 
    "gene_names_refseq": "Bfsp1; CP95; fi", 
    "gene_name": "Bfsp1"
}