ID:FYCO1_HUMAN DESCRIPTION: RecName: Full=FYVE and coiled-coil domain-containing protein 1; AltName: Full=Zinc finger FYVE domain-containing protein 7; FUNCTION: May mediate microtubule plus end-directed vesicle transport. SUBUNIT: Can form homodimers. Interacts (via C-terminus) with MAP1LC3B. Interacts with RAB7A; the interaction with RAB7A induces FYCO1 recruitment to late endosomal/lysosomal compartments. INTERACTION: O95166:GABARAP; NbExp=2; IntAct=EBI-2869338, EBI-712001; Q9H0R8:GABARAPL1; NbExp=2; IntAct=EBI-2869338, EBI-746969; P60520:GABARAPL2; NbExp=2; IntAct=EBI-2869338, EBI-720116; Q9GZQ8:MAP1LC3B; NbExp=7; IntAct=EBI-2869338, EBI-373144; Q9BXW4:MAP1LC3C; NbExp=2; IntAct=EBI-2869338, EBI-2603996; SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome. Endosome. Lysosome. Note=Localizes to the external but not to the internal membrane of autophagosomes, and upon autophagosome/late endosome/lysosome fusion, it stays on the external surface of autolysosomes. TISSUE SPECIFICITY: Expressed in heart and skeletal muscle. PTM: Phosphorylated upon DNA damage, probably by ATM or ATR. DISEASE: Defects in FYCO1 are the cause of cataract congenital autosomal recessive type 2 (CATC2) [MIM:610019]. An opacification of the crystalline lens of the eye becoming evident at birth or in infancy. It frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function. Note=Pathogenic mutations in FYCO1 can affect intracellular transport of autophagocytic vesicles from the perinuclear area to the periphery, leading to an accumulation of large numbers of vesicles and hence loss of lens transparency (PubMed:21636066). SIMILARITY: Contains 1 FYVE-type zinc finger. SIMILARITY: Contains 1 GOLD domain. SIMILARITY: Contains 1 RUN domain. SEQUENCE CAUTION: Sequence=AAH07218.1; Type=Erroneous initiation; Note=Translation N-terminally extended; Sequence=BAB14559.1; Type=Erroneous initiation; Note=Translation N-terminally extended; Sequence=BAB84991.1; Type=Frameshift; Positions=1402;
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q9BQS8
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
Gene Ontology (GO) Annotations with Structured Vocabulary
Molecular Function: GO:0005515 protein binding GO:0044183 protein binding involved in protein folding GO:0046872 metal ion binding GO:0051082 unfolded protein binding
Biological Process: GO:0006458 'de novo' protein folding GO:0061077 chaperone-mediated protein folding GO:0072383 plus-end-directed vesicle transport along microtubule GO:1901098 positive regulation of autophagosome maturation
US Server
Sequence and Links to Tools and Databases 
Common Gene Haplotype Alleles 
