BAIT

HSPA5

AL022860, AU019543, Bip, D2Wsu141e, D2Wsu17e, Grp78, Hsce70, SEZ-7, Sez7, baffled, mBiP, RP23-446N16.1
heat shock protein 5
GO Process (15)
GO Function (8)
GO Component (17)
Mus musculus
PREY

HSPA5

AL022860, AU019543, Bip, D2Wsu141e, D2Wsu17e, Grp78, Hsce70, SEZ-7, Sez7, baffled, mBiP, RP23-446N16.1
heat shock protein 5
GO Process (15)
GO Function (8)
GO Component (17)
Mus musculus

Co-purification

An interaction is inferred from the identification of two or more protein subunits in a purified protein complex, as obtained by classical biochemical fractionation or affinity purification and one or more additional fractionation steps.

Publication

A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins.

Meunier L, Usherwood YK, Chung KT, Hendershot LM

We demonstrate the existence of a large endoplasmic reticulum (ER)-localized multiprotein complex that is comprised of the molecular chaperones BiP; GRP94; CaBP1; protein disulfide isomerase (PDI); ERdj3, a recently identified ER Hsp40 cochaperone; cyclophilin B; ERp72; GRP170; UDP-glucosyltransferase; and SDF2-L1. This complex is associated with unassembled, incompletely folded immunoglobulin heavy chains. Except for ERdj3, and to a lesser extent PDI, ... [more]

Mol. Biol. Cell Dec. 01, 2002; 13(12);4456-69 [Pubmed: 12475965]

Throughput

  • Low Throughput

Curated By

  • BioGRID