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IID01011
 UniprotQ9BQS8
ProteinFYVE and coiled-coil domain-containing protein 1
GeneFYCO1
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
 Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
1478
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 1-178 Monomer :
 Evidence X-RAY 7bqi A Reference
       Region 7bqi A 1-4 disorder
       Region 7bqi A 5-178 order
Seq 1273-1298 Hetero tetramer : IID01019Complex
 Evidence X-RAY 5cx3 E Reference
       Region 5cx3 E 1273-1292 order
       Region 5cx3 E 1293-1298 disorder
 Evidence X-RAY 5cx3 G Reference
       Region 5cx3 G 1273-1275 disorder
       Region 5cx3 G 1276-1294 order
       Region 5cx3 G 1295-1298 disorder
 Evidence X-RAY 5cx3 F Reference
       Region 5cx3 F 1273-1275 disorder
       Region 5cx3 F 1276-1298 order
 Evidence X-RAY 5cx3 H Reference
       Region 5cx3 H 1273-1276 disorder
       Region 5cx3 H 1277-1292 order
       Region 5cx3 H 1293-1298 disorder
Seq 1276-1288 Hetero dimer : IID00346Complex
 Evidence X-RAY 5d94 B Reference
       Region 5d94 B 1276-1276 disorder
       Region 5d94 B 1277-1288 order
SeqProS predicted 1273-1298 This region is predicted to be disordered by NeProc and AlphaFold (pLDDT < 68.5). Hetero tetramer : IID01019Complex
       Region 5cx3 E 1273-1292 order
       Region 5cx3 F 1276-1298 order
       Region 5cx3 G 1276-1294 order
       Region 5cx3 H 1277-1292 order
SeqProS predicted 1277-1288 This region is predicted to be disordered by NeProc and AlphaFold (pLDDT < 68.5). Hetero dimer : IID00346Complex
       Region 5d94 B 1277-1288 order
Seqphosphorylation
    342-342 Phosphoserine
    196-196 Phosphoserine
    381-381 Phosphothreonine
    878-878 Phosphoserine
Seqacetylation
    2-2 N-acetylalanine
 
Prediction
NeProc
Disorder 1-7,182-224,281-336,365-392,557-592,667-680,751-763,912-918,1060-1066,1113-1119,1155-1170,1230-1351
Order 8-181,225-280,337-364,393-556,593-666,681-750,764-911,919-1059,1067-1112,1120-1154,1171-1213,1219-1229,1352-1478
ProS 204-222,281-336,365-392,557-592,667-680,751-756,762-763,912-918,1060-1066,1113-1119,1155-1170,1230-1233,1274-1293,1321-1324,1332-1341,1348-1351
AlphaFold
Disorder 1-7,63-64,82-84,180-236,239-239,277-277,280-280,282-282,284-284,326-327,330-330,333-333,351-401,403-403,452-452,553-613,748-763,967-1014,1159-1176,1213-1218,1231-1334,1470-1478
Order 8-62,65-81,85-179,237-238,240-276,278-279,281-281,283-283,285-325,328-329,331-332,334-350,402-402,404-451,453-552,614-747,764-966,1015-1158,1177-1212,1219-1230,1335-1469
SEG 196-207 ,427-439 ,484-507 ,639-651 ,686-700 ,763-779 ,854-877 ,885-899 ,953-996 ,1231-1247 ,1249-1262
Function
Function in SwissProt
May mediate microtubule plus end-directed vesicle transport.
Biological Process
Diagram with PDB data
FYCO1/MAP1LC3BCrystal structure of LC3-LIR peptide complex