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hsp90aa1.2 hsp90aa1.2 hsp90ab1 hsp90ab1 hsp90b1 hsp90b1 trap1 trap1 hsp90aa1.1 hsp90aa1.1
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
hsp90aa1.2Heat shock protein 90, alpha (cytosolic), class A member 1, tandem duplicate 2. (734 aa)
hsp90ab1Heat shock protein HSP 90-beta; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co- chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a range of client protein classes via its interact [...] (725 aa)
hsp90b1Heat shock protein 90, beta (Grp94), member 1. (793 aa)
trap1TNF receptor-associated protein 1. (719 aa)
hsp90aa1.1Heat shock protein HSP 90-alpha 1; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a [...] (725 aa)
Your Current Organism:
Danio rerio
NCBI taxonomy Id: 7955
Other names: Brachydanio rerio, Brachydanio rerio frankei, Cyprinus rerio, D. rerio, Danio frankei, Danio rerio frankei, leopard danio, zebra danio, zebra fish, zebrafish
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