pdi-1 : pdi-2

"C. elegans PDI/beta polypeptide forms an active prolyl 4-hydroxylase alpha2-beta2 tetramer with the human alpha subunit and an alpha-beta dimer with the C. elegans alpha subunit, whereas the C.elegans PDI isoform formed no prolyl 4-hydroxylase with either alpha subunit. Removal of the 32-residue C-terminal extension from the C. elegans alpha subunit totally eliminated alpha-beta dimer formation."

pdi-1 : pdi-2

"C. elegans PDI/beta polypeptide forms an active prolyl 4-hydroxylase alpha2-beta2 tetramer with the human alpha subunit and an alpha-beta dimer with the C. elegans alpha subunit, whereas the C.elegans PDI isoform formed no prolyl 4-hydroxylase with either alpha subunit. Removal of the 32-residue C-terminal extension from the C. elegans alpha subunit totally eliminated alpha-beta dimer formation."

rod-1 : spdl-1

The C-terminal domain of Spindly (SPDL-1) binds to the ROD-1 beta-propeller.

egl-10 : gpb-2

"The N-terminal fragment complexes with the C-terminal fragment and its associated G beta subunit, GPB-2."

hmp-2 : hmr-1

"HMP-2 is the only beta-catenin homologue that interacts with the single cadherin of C. elegans, HMR-1."

hmp-2 : hmr-1

"HMP-2 is the only beta-catenin homologue that interacts with the single cadherin of C. elegans, HMR-1."

Interaction involving zyg-1

"CPB of C. elegans ZYG-1, which forms a Z-shaped dimer containing an intermolecular beta-sheet with an extended basic surface patch."

pop-1 : sys-1

The C terminus of POP-1 is essential for LIT-1 mediated phosphorylation and is specifically bound by the diverged beta-catenin WRM-1.

lit-1 : pop-1

The C terminus of POP-1 is essential for LIT-1 mediated phosphorylation and is specifically bound by the diverged beta-catenin WRM-1.

pop-1 : wrm-1

The C terminus of POP-1 is essential for LIT-1 mediated phosphorylation and is specifically bound by the diverged beta-catenin WRM-1.