BAIT

SHANK1

SPANK-1, SSTRIP, synamon
SH3 and multiple ankyrin repeat domains 1
Homo sapiens
PREY

SHANK1

SPANK-1, SSTRIP, synamon
SH3 and multiple ankyrin repeat domains 1
Homo sapiens

Two-hybrid

Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.

Publication

SHANK3 gene mutations associated with autism facilitate ligand binding to the Shank3 ankyrin repeat region.

Mameza MG, Dvoretskova E, Bamann M, Hoenck HH, Gueler T, Boeckers TM, Schoen M, Verpelli C, Sala C, Barsukov I, Dityatev A, Kreienkamp HJ

Shank/ProSAP proteins are major scaffold proteins of the postsynaptic density; mutations in the human SHANK3 gene are associated with intellectual disability or autism spectrum disorders. We have analyzed the functional relevance of several SHANK3 missense mutations affecting the N-terminal portion of the protein by expression of wild-type and mutant Shank3 in cultured neurons and by binding assays in heterologous cells. ... [more]

J. Biol. Chem. Sep. 13, 2013; 288(37);26697-708 [Pubmed: 23897824]

Throughput

  • Low Throughput

Additional Notes

  • Shank1 SPN domain found to interact with Shank1 ARR domain

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
SHANK1 SHANK1
Affinity Capture-Western
Affinity Capture-Western

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.

Low-BioGRID
-
SHANK1 SHANK1
Co-crystal Structure
Co-crystal Structure

Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Low-BioGRID
-

Curated By

  • BioGRID