PREY

CAPNS1

CALPAIN4, CANP, CANPS, CAPN4, CDPS, CSS1
calpain, small subunit 1
Homo sapiens

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.

Publication

Structural basis for possible calcium-induced activation mechanisms of calpains.

Reverter D, Strobl S, Fernandez-Catalan C, Sorimachi H, Suzuki K, Bode W

The calpains form a growing family of structurally related intracellular multidomainal cysteine proteinases, which exhibit a catalytic domain distantly related to papain. In contrast to papain, however, their activity in most cases depends on calcium. The calpains are believed to play important roles in cytoskeletal remodeling processes, cell differentiation, apoptosis and signal transduction, but have also been implicated in muscular ... [more]

Biol. Chem. May. 01, 2001; 382(5);753-66 [Pubmed: 11517928]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
CAPN2 CAPNS1
Affinity Capture-MS
Affinity Capture-MS

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 is identified by mass spectrometric methods.

High0.9928BioGRID
3108185
CAPNS1 CAPN2
Co-fractionation
Co-fractionation

Interaction inferred from the presence of two or more protein subunits in a partially purified protein preparation. If co-fractionation is demonstrated between 3 or more proteins, then add them as a complex.

High-BioGRID
3434890

Curated By

  • BioGRID