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IID00748
 UniprotO00499
ProteinMyc box-dependent-interacting protein 1
GeneBIN1
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
593
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 1-33 Monomer :
 Evidence NMR 2rnd A Reference
       Region 2rnd A 1-33 order
       Region 2rnd A 1-7 high_rmsd
 Evidence NMR 2rmy A Reference
       Region 2rmy A 1-33 order
       Region 2rmy A 1-5 high_rmsd
Seq 1-173,205-272 Homo dimer :
 Evidence X-RAY 2fic B Reference
       Region 2fic B 1-39 disorder
       Region 2fic B 40-173 order
       Region 2fic B 205-271 order
       Region 2fic B 272-272 disorder
 Evidence X-RAY 2fic A Reference
       Region 2fic A 1-41 disorder
       Region 2fic A 42-162 order
       Region 2fic A 163-169 disorder
       Region 2fic A 170-173 order
       Region 2fic A 205-270 order
       Region 2fic A 271-272 disorder
Seq 301-376,457-593 Monomer :
 Evidence NMR 1mv3 A Reference
       Region 1mv3 A 301-376 order
       Region 1mv3 A 457-593 order
Seqdisorder 458-512
 Evidence NMR Reference
       Region 458-512 disorder
Seq 513-593 Hetero dimer : Q8JUX6
 Evidence NMR 5i22 A Reference
       Region 5i22 A 513-593 order
Seq 513-593 Hetero dimer : IID00012Complex
 Evidence NMR 1mv0 B Reference
       Region 1mv0 B 513-593 order
Seq 513-593 Monomer :
 Evidence NMR 1muz A Reference
       Region 1muz A 513-593 order
SeqProS verified 8-33 Residues 8-34 in SDS micelles (2rmy) and 10-34 in DPC micelles (2rnd) are well-ordered (PMID: 18658220). :
       Region 2rmy A 1-33 order
       Region 2rnd A 1-33 order
       Region 2fic B 1-39 disorder
Seqphosphorylation
    296-296 Phosphoserine
    298-298 Phosphoserine
    303-303 Phosphoserine
    307-307 Phosphothreonine
    323-323 Phosphothreonine
    331-331 Phosphoserine
Seqacetylation
    2-2 N-acetylalanine
 
Prediction
NeProc
Disorder 1-14,164-182,282-549
Order 15-163,183-281,550-593
ProS 11-14,164-178,282-286,384-397,405-420,442-453,480-528,538-549
AlphaFold
Disorder 1-14,36-36,164-176,275-515
Order 15-35,37-163,177-274,516-593
Pfam Hmmer
PF03114 18-269 6.5e-66
PF00018 523-592 3.4e-07
SEG 339-345 ,390-400 ,481-489
Function
Function in SwissProt
Is a key player in the control of plasma membrane curvature, membrane shaping and membrane remodeling. Required in muscle cells for the formation of T-tubules, tubular invaginations of the plasma membrane that function in depolarization-contraction coupling (PubMed:24755653). Is a negative regulator of endocytosis (By similarity). Is also involved in the regulation of intracellular vesicles sorting, modulation of BACE1 trafficking and the control of amyloid-beta production (PubMed:27179792). In neuronal circuits, endocytosis regulation may influence the internalization of PHF-tau aggregates (By similarity). May be involved in the regulation of MYC activity and the control cell proliferation (PubMed:8782822). Has actin bundling activity and stabilizes actin filaments against depolymerization in vitro (PubMed:28893863).
Biological Process
See also
Diagram with PDB data
MYC/BIN1NMR STRUCTURE OF THE TUMOR SUPPRESSOR BIN1: ALTERNATIVE SPLICING IN MELANOMA AND INTERACTION WITH C-MYC