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IID50419
 UniprotO88339
ProteinEpsin-1
GeneEpn1
OrganismRattus norvegicus
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
 xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
575
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 1-160 Monomer :
 Evidence X-RAY 1edu A Reference
       Region 1edu A 12-160 order
 Evidence X-RAY 1eyh A Reference
       Region 1eyh A 15-158 order
 Evidence X-RAY 1h0a A Reference
       Region 1h0a A 1-158 order
Seqdisorder 229-407
 Evidence CD Reference
       Region 229-407 disorder
Seq 375-381 Hetero dimer : P17427
 Evidence X-RAY 1ky6 P Reference
       Region 1ky6 P 375-381 order
SeqProS verified 375-381 Hetero dimer : P17427
       Region 1ky6 P 375-381 order
       Region 229-407 disorder
Seqphosphorylation
    459-459 Phosphothreonine
    493-493 Phosphothreonine
    472-472 Phosphoserine
    469-469 Phosphothreonine
    463-463 Phosphothreonine
    453-453 Phosphoserine
    446-446 Phosphoserine
    434-434 Phosphoserine
    420-420 Phosphothreonine
    419-419 Phosphoserine
    418-418 Phosphoserine
    382-382 Phosphoserine
 
Prediction
NeProc
Disorder 1-2,158-575
Order 3-157
ProS 178-200,208-236,257-265,273-280,292-297,305-309,319-322,332-336,349-352,437-443,468-485,499-503,527-532,569-575
AlphaFold
Disorder 1-1,160-180,201-206,249-565,567-575
Order 2-159,181-200,207-248,566-566
Pfam Hmmer
182->199 17-140 207->224
SEG 133-144 ,157-174 ,183-193 ,279-316 ,333-346 ,363-379 ,454-466 ,536-545 ,550-566
Function
Function in SwissProt
Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) (PubMed:11161217). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations (PubMed:9723620, PubMed:12353027). Regulates receptor-mediated endocytosis (By similarity).