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p(HGNC:STIP1)

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Entity

Name
STIP1
Namespace
hgnc
Namespace Version
20180906
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/b46b65c3da259b6e86026514dfececab7c22a11b/external/hgnc-names.belns

Appears in Networks 5

A chaperome subnetwork safeguards proteostasis in aging and neurodegenerative disease. v1.0.0

A Quantitative Chaperone Interaction Network Reveals the Architecture of Cellular Protein Homeostasis Pathways v1.0.0

Molecular chaperones and regulation of tau quality control: strategies for drug discovery in tauopathies v1.0.0

Imbalances in the Hsp90 Chaperone Machinery: Implications for Tauopathies v1.0.0

Molecular Chaperone Functions in Protein Folding and Proteostasis v1.0.0

In-Edges 6

complex(p(HGNC:CDC37L1), p(HGNC:STIP1)) hasComponent p(HGNC:STIP1) View Subject | View Object

Appears in Networks:

complex(p(HGNC:STIP1), p(INTERPRO:"Heat shock protein 70 family"), p(INTERPRO:"Heat shock protein Hsp90 family")) hasComponent p(HGNC:STIP1) View Subject | View Object

Appears in Networks:

complex(p(HGNC:STIP1), p(HGNC:VHL)) hasComponent p(HGNC:STIP1) View Subject | View Object

Appears in Networks:

bp(GO:"chaperone-mediated autophagy") association p(HGNC:STIP1) View Subject | View Object

Hsp90 and Hop are both involved in the CMA system; PubMed:29311797

Appears in Networks:

bp(MESH:Aging) decreases p(HGNC:STIP1) View Subject | View Object

For instance, CyP40, FKBP52, PP5, Hop, p23, and Aha1 are all repressed in the aged brain. PubMed:29311797

Appears in Networks:
Annotations
MeSH
Brain

complex(p(FPLX:HSP90), p(HGNC:FKBP4), p(HGNC:PTGES3), p(HGNC:STIP1)) hasComponent p(HGNC:STIP1) View Subject | View Object

Appears in Networks:

Out-Edges 5

p(HGNC:STIP1) association bp(GO:"chaperone-mediated autophagy") View Subject | View Object

Hsp90 and Hop are both involved in the CMA system; PubMed:29311797

Appears in Networks:

p(HGNC:STIP1) decreases a(CHEBI:"amyloid-beta polypeptide 42") View Subject | View Object

This functional screen identified 18 genes (Figure 3D), corresponding to ten ATP-dependent chaperones, HSC70 (hsp-1), HSP90 (daf-21), and eight subunits of the CCT/TRiC chaperonin complex; the co-chaperones, HSP40 (dnj-12) and CDC37 (cdc-37); and the TPR-domain pro- tein STI1 that upon knockdown significantly enhanced A b 42 pro- teotoxicity (Figure 3D). PubMed:25437566

Appears in Networks:
Annotations
MeSH
Brain
MeSH
Alzheimer Disease
MeSH
Huntington Disease
MeSH
Parkinson Disease

p(HGNC:STIP1) increases complex(p(HGNC:STIP1), p(INTERPRO:"Heat shock protein 70 family"), p(INTERPRO:"Heat shock protein Hsp90 family")) View Subject | View Object

Two subnetworks emerged within this central network, corresponding to known Hsp90 and Hsp70 chaperone complexes (Figure 2, blue and orange squares, respectively). These two subnetworks were bridged by a unique set of cochaperones (Figure 2, tan squares). Among these were the wellknown bridging factors HOP/STIP1, TPR2/DNAJC7, and CHIP/ STUB1, validating our approach (Brychzy et al., 2003; Schmid et al., 2012; Xu et al., 2002). Other bridging factors in this first tier of organization included members of the Hsp40 chaperone family (DNAJB1 and DNAJB6), HSP70-binding protein 1 (HSPBP1), the TPR domain protein EDRF1, and the E3 ligase NRDP1/RNF41 PubMed:25036637

Appears in Networks:

p(HGNC:STIP1) decreases p(HGNC:MAPT) View Subject | View Object

A previous study found that when Hop was depleted using siRNA, there was an accumulation of tau (Jinwal et al., 2013). PubMed:29311797

Appears in Networks:
Annotations
MeSH
Cerebral Cortex

p(HGNC:STIP1) decreases act(p(FPLX:HSP90), ma(GO:"ATPase activity")) View Subject | View Object

Cochaperones HOP (Sti1) and Cdc37 (p50) stabilize the open conformation of the Hsp90 dimer (81, 174, 175, 188), inhibit ATP hydrolysis, and facilitate substrate protein binding. PubMed:23746257

Appears in Networks:

About

BEL Commons is developed and maintained in an academic capacity by Charles Tapley Hoyt and Daniel Domingo-Fernández at the Fraunhofer SCAI Department of Bioinformatics with support from the IMI project, AETIONOMY. It is built on top of PyBEL, an open source project. Please feel free to contact us here to give us feedback or report any issues. Also, see our Publishing Notes and Data Protection information.

If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.