BAIT

STIP1

HEL-S-94n, HOP, IEF-SSP-3521, P60, STI1, STI1L

stress-induced phosphoprotein 1

GO Process (1)

GO Function (2)

GO Component (2)

Gene Ontology Biological Process

response to stress [TAS]

Gene Ontology Molecular Function

poly(A) RNA binding [IDA]
protein binding [IPI]

Gene Ontology Cellular Component

Golgi apparatus [TAS]

CRISPR Database HGNC Alliance of Genome Resources VEGA OMIM Entrez Gene RefSeq UniprotKB Ensembl HPRD

Homo sapiens

PREY

DNAJC10

ERdj5, JPDI, MTHr, PDIA19, UNQ495/PRO1012

DnaJ (Hsp40) homolog, subfamily C, member 10

GO Process (6)

GO Function (9)

GO Component (4)

Gene Ontology Biological Process

ER-associated ubiquitin-dependent protein catabolic process [IMP]

intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [IDA]

negative regulation of protein phosphorylation [IDA]

positive regulation of ATPase activity [ISS]

protein folding in endoplasmic reticulum [IDA]

response to endoplasmic reticulum stress [IDA]

Gene Ontology Molecular Function

ATPase activator activity [ISS]
ATPase binding [IPI]
Hsp70 protein binding [IPI]
chaperone binding [IDA]
disulfide oxidoreductase activity [ISS]
misfolded protein binding [IDA]
oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor [ISS]
protein binding [IPI]
protein disulfide oxidoreductase activity [IDA, ISS]

Gene Ontology Cellular Component

endoplasmic reticulum [IDA]

endoplasmic reticulum chaperone complex [IDA]

endoplasmic reticulum lumen [IDA]

CRISPR Database HGNC Alliance of Genome Resources OMIM Entrez Gene RefSeq UniprotKB Ensembl HPRD

Homo sapiens

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.

Publication

The Hsp70-Hsp90 co-chaperone Hop/Stip1 shifts the proteostatic balance from folding towards degradation.

Bhattacharya K, Weidenauer L, Luengo TM, Pieters EC, Echeverria PC, Bernasconi L, Wider D, Sadian Y, Koopman MB, Villemin M, Bauer C, Ruediger SGD, Quadroni M, Picard D

Hop/Stip1/Sti1 is thought to be essential as a co-chaperone to facilitate substrate transfer between the Hsp70 and Hsp90 molecular chaperones. Despite this proposed key function for protein folding and maturation, it is not essential in a number of eukaryotes and bacteria lack an ortholog. We set out to identify and to characterize its eukaryote-specific function. Human cell lines and the ... [more]

Nat Commun Nov. 25, 2020; 11(1);5975 [Pubmed: 33239621]

Throughput

High Throughput

Curated By

BioGRID