STRINGSTRING
Hsph1 Hsph1 Dnajb9 Dnajb9 Hspa2 Hspa2 Dnaja1 Dnaja1 Bag1 Bag1 Bag5l1 Bag5l1 Hspa4l Hspa4l Bag2 Bag2 Dnaja4 Dnaja4 Hspa14 Hspa14 Dnaja2 Dnaja2 Hspa4 Hspa4 Hspbp1 Hspbp1 Hspa12a Hspa12a St13 St13 Stub1 Stub1 Bag3 Bag3 Hspa12b Hspa12b Dnajb1 Dnajb1 Hspb8 Hspb8 Dnajb6 Dnajb6 Hspa8 Hspa8 LOC680121 LOC680121 Hspa1l Hspa1l Hspa1a Hspa1a Hspa13 Hspa13 Dnajb2 Dnajb2
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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
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Hsph1Heat shock protein 105 kDa; Acts as a nucleotide-exchange factor (NEF) for chaperone proteins HSPA1A and HSPA1B, promoting the release of ADP from HSPA1A/B thereby triggering substrate release. Prevents the aggregation of denatured proteins in cells under severe stress, on which the ATP levels decrease markedly. Inhibits HSPA8/HSC70 ATPase and chaperone activities. (858 aa)
Dnajb9DnaJ homolog subfamily B member 9; Co-chaperone for Hsp70 protein HSPA5/BiP that acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR) (By similarity). J domain-containing co-chaperones stimulate the ATPase activity of Hsp70 proteins and are required for efficient substrate recognition by Hsp70 proteins (By similarity). In the unstressed endoplasmic reticulum, interacts with the luminal region of ERN1/IRE1 and selectively recruits HSPA5/BiP: HSPA5/BiP disrupts the dimerization of the active ERN1/IRE1 luminal region, thereby inactivating ERN1/IRE1 (By similar [...] (222 aa)
Hspa2Heat shock-related 70 kDa protein 2; Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis [...] (633 aa)
Dnaja1DnaJ homolog subfamily A member 1; Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (By similarity). Co- chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. (397 aa)
Bag1BAG family molecular chaperone regulator 1; Co-chaperone for HSP70 and HSC70 chaperone proteins. Acts as a nucleotide-exchange factor (NEF) promoting the release of ADP from the HSP70 and HSC70 proteins thereby triggering client/substrate protein release. Nucleotide release is mediated via its binding to the nucleotide-binding domain (NBD) of HSPA8/HSC70 where as the substrate release is mediated via its binding to the substrate-binding domain (SBD) of HSPA8/HSC70. Inhibits the pro-apoptotic function of PPP1R15A, and has anti-apoptotic activity. Markedly increases the anti-cell death f [...] (358 aa)
Bag5l1BAG family molecular chaperone regulator 5; May function as a nucleotide exchange factor for HSP/HSP70, promoting ADP release, and activating Hsp70-mediated refolding. Inhibits both auto-ubiquitination of PRKN and ubiquitination of target proteins by PRKN. (447 aa)
Hspa4lHeat shock 70 kDa protein 4L. (1017 aa)
Bag2BAG cochaperone 2. (212 aa)
Dnaja4DnaJ heat shock protein family (Hsp40) member A4. (555 aa)
Hspa14Heat shock 70 kDa protein 14; Component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding- competent state. In the RAC complex, binds to the nascent polypeptide chain, while DNAJC2 stimulates its ATPase activity (By similarity). (509 aa)
Dnaja2DnaJ homolog subfamily A member 2; Co-chaperone of Hsc70. Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro). (412 aa)
Hspa4Heat shock 70 kDa protein 4; Belongs to the heat shock protein 70 family. (840 aa)
Hspbp1Hsp70-binding protein 1; Inhibits HSPA1A chaperone activity by changing the conformation of the ATP-binding domain of HSPA1A and interfering with ATP binding. Interferes with ubiquitination mediated by STUB1 and inhibits chaperone-assisted degradation of target proteins (By similarity). (357 aa)
Hspa12aHeat shock 70kDa protein 12A (Predicted), isoform CRA_a. (675 aa)
St13Hsc70-interacting protein; One HIP oligomer binds the ATPase domains of at least two HSC70 molecules dependent on activation of the HSC70 ATPase by HSP40. Stabilizes the ADP state of HSC70 that has a high affinity for substrate protein. Through its own chaperone activity, it may contribute to the interaction of HSC70 with various target proteins. Belongs to the FAM10 family. (368 aa)
Stub1STIP1 homology and U-Box containing protein 1, isoform CRA_b. (304 aa)
Bag3Bcl2-associated athanogene 3. (574 aa)
Hspa12bHeat shock protein family A (Hsp70) member 12B. (685 aa)
Dnajb1DnaJ (Hsp40) homolog, subfamily B, member 1 (Predicted), isoform CRA_a. (371 aa)
Hspb8Heat shock protein beta-8; Displays temperature-dependent chaperone activity. (196 aa)
Dnajb6DnaJ homolog subfamily B member 6; Plays an indispensable role in the organization of KRT8/KRT18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Suppresses aggregation and toxicity of polyglutamine-containing, aggregation-prone proteins (By similarity). Has a stimulatory effect on the ATPase activity of HSP70 in a dose- dependent and time-dependent manner and hence acts as a co-chaperone of HSP70. Also reduces cellular toxicity and caspase-3 activity (By similarity). (357 aa)
Hspa8Heat shock cognate 71 kDa protein; Belongs to the heat shock protein 70 family. (645 aa)
LOC680121Heat shock cognate 71 kDa protein; Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis a [...] (646 aa)
Hspa1lHeat shock 70 kDa protein 1-like; Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis an [...] (641 aa)
Hspa1aHeat shock 70 kDa protein 1A; Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and AD [...] (641 aa)
Hspa13Heat shock 70 kDa protein 13; Has peptide-independent ATPase activity. (471 aa)
Dnajb2DnaJ heat shock protein family (Hsp40) member B2. (277 aa)
Your Current Organism:
Rattus norvegicus
NCBI taxonomy Id: 10116
Other names: Buffalo rat, Norway rat, R. norvegicus, Rattus PC12 clone IS, Rattus sp. strain Wistar, Sprague-Dawley rat, Wistar rats, brown rat, laboratory rat, rat, rats, zitter rats
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