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IID00959
 UniprotP78314
ProteinSH3 domain-binding protein 2
GeneSH3BP2
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
 xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
561
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 410-425 Hetero octamer : Q9H2K2
 Evidence X-RAY 3twr E Reference
       Region 3twr E 410-412 disorder
       Region 3twr E 413-425 order
 Evidence X-RAY 3twr F Reference
       Region 3twr F 410-412 disorder
       Region 3twr F 413-425 order
 Evidence X-RAY 3twr G Reference
       Region 3twr G 410-414 disorder
       Region 3twr G 415-425 order
 Evidence X-RAY 3twr H Reference
       Region 3twr H 410-413 disorder
       Region 3twr H 414-425 order
Seq 446-558 Monomer :
 Evidence NMR 2cr4 A Reference
       Region 2cr4 A 446-558 order
SeqProS possible 413-425 The conformation of the 3BP2 peptide in the complex is similar to that of the Arpin peptide in complex with the ARD (PDB: 4Z68); Tankyrases recruit specific motifs; This region is predicted to be disordered by AlphaFold (pLDDT <68.5) and NeProc. Hetero octamer : Q9H2K2
       Region 3twr E 413-425 order
       Region 3twr F 413-425 order
       Region 3twr G 415-425 order
       Region 3twr H 414-425 order
Seqphosphorylation
    174-174 Phosphotyrosine; by SYK
    183-183 Phosphotyrosine; by SYK
    278-278 Phosphoserine
    416-416 Phosphoserine
    427-427 Phosphoserine
    448-448 Phosphotyrosine; by SYK
 
Prediction
NeProc
Disorder 1-5,138-449
Order 6-137,450-561
ProS 138-195,243-249,286-299,306-311,329-339,374-379,413-429,438-449
AlphaFold
Disorder 1-6,38-44,131-147,163-204,207-207,210-235,237-451,524-524,558-561
Order 7-37,45-130,148-162,205-206,208-209,236-236,452-523,525-557
SEG 141-151 ,170-181 ,201-215 ,229-245 ,316-328 ,341-353
Function
Function in SwissProt
Binds differentially to the SH3 domains of certain proteins of signal transduction pathways. Binds to phosphatidylinositols; linking the hemopoietic tyrosine kinase fes to the cytoplasmic membrane in a phosphorylation dependent mechanism.