BAIT

HSPA4

APG-2, HEL-S-5a, HS24/P52, HSPH2, RY, hsp70, hsp70RY
heat shock 70kDa protein 4
GO Process (3)
GO Function (1)
GO Component (3)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Homo sapiens
PREY

HOPX

CAMEO, HOD, HOP, LAGY, NECC1, OB1, SMAP31, TOTO
HOP homeobox
GO Process (2)
GO Function (0)
GO Component (1)

Gene Ontology Biological Process

Gene Ontology Cellular Component

Homo sapiens

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.

Publication

C-terminal phosphorylation of Hsp70 and Hsp90 regulates alternate binding to co-chaperones CHIP and HOP to determine cellular protein folding/degradation balances.

Muller P, Ruckova E, Halada P, Coates PJ, Hrstka R, Lane DP, Vojtesek B

Heat shock proteins Hsp90 and Hsp70 facilitate protein folding but can also direct proteins for ubiquitin-mediated degradation. The mechanisms regulating these opposite activities involve Hsp binding to co-chaperones including CHIP and HOP at their C-termini. We demonstrated that the extreme C-termini of Hsp70 and Hsp90 contain phosphorylation sites targeted by kinases including CK1, CK2 and GSK3-β in vitro. The phosphorylation ... [more]

Unknown Jul. 23, 2012; 0(0); [Pubmed: 22824801]

Throughput

  • Low Throughput

Curated By

  • BioGRID