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.

Publication

A novel type of co-chaperone mediates transmembrane recruitment of DnaK-like chaperones to ribosomes.

Dudek J, Volkmer J, Bies C, Guth S, Mueller A, Lerner M, Feick P, Schaefer KH, Morgenstern E, Hennessy F, Blatch GL, Janoscheck K, Heim N, Scholtes P, Frien M, Nastainczyk W, Zimmermann R

Recently, the homolog of yeast protein Sec63p was identified in dog pancreas microsomes. This pancreatic DnaJ-like protein was shown to be an abundant protein, interacting with both the Sec61p complex and lumenal DnaK-like proteins, such as BiP. The pancreatic endoplasmic reticulum contains a second DnaJ-like membrane protein, which had been termed Mtj1p in mouse. Mtj1p is present in pancreatic microsomes ... [more]

EMBO J. Jun. 17, 2002; 21(12);2958-67 [Pubmed: 12065409]

Throughput

Low Throughput

Curated By

BioGRID

Interaction Summary

DNAJC1

Gene Ontology Biological Process

Gene Ontology Molecular Function

chaperone binding [IDA]protein binding [IPI]ribosome binding [TAS]

Gene Ontology Cellular Component

SEC61A1