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Hsph1 Hsph1 Ankrd45 Ankrd45 Dnajb9 Dnajb9 Hspa2 Hspa2 Dnajc10 Dnajc10 Dnaja1 Dnaja1 Bag1 Bag1 Bag5l1 Bag5l1 Hspa4l Hspa4l Bag2 Bag2 Dnaja4 Dnaja4 Hspa14 Hspa14 Dnaja2 Dnaja2 Yme1l1 Yme1l1 Hspa4 Hspa4 Hspbp1 Hspbp1 Dnajb13 Dnajb13 Hspa12a Hspa12a St13 St13 Hspa9 Hspa9 Sil1 Sil1 Stub1 Stub1 Bag3 Bag3 Hspa12b Hspa12b Dnajb1 Dnajb1 Hspb8 Hspb8 Dnajb6 Dnajb6 Hspa8 Hspa8 Dnajb8 Dnajb8 Dnajb12 Dnajb12 Clpx Clpx LOC680121 LOC680121 Grpel2 Grpel2 Hspd1 Hspd1 Hspa1l Hspa1l M0R8M9_RAT M0R8M9_RAT Clpp Clpp Lonp1 Lonp1 M0RCB1_RAT M0RCB1_RAT Hspa1a Hspa1a Hspe1 Hspe1 Dnajb14 Dnajb14 A0A0G2JVI0_RAT A0A0G2JVI0_RAT A0A0G2JVI3_RAT A0A0G2JVI3_RAT Hspa13 Hspa13 Grpel1 Grpel1 Clpb Clpb Dnaja3 Dnaja3 Dnajb2 Dnajb2 Dnajb5 Dnajb5 A0A0G2K9V8_RAT A0A0G2K9V8_RAT Dnajb4 Dnajb4 Tmem59l Tmem59l
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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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query proteins and first shell of interactors
white nodes:
second shell of interactors
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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
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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)
Ankrd45ANK_REP_REGION domain-containing protein. (163 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)
Dnajc10DnaJ homolog subfamily C member 10; Endoplasmic reticulum disulfide reductase involved both in the correct folding of proteins and degradation of misfolded proteins. Required for efficient folding of proteins in the endoplasmic reticulum by catalyzing the removal of non-native disulfide bonds formed during the folding of proteins, such as LDLR. Also involved in endoplasmic reticulum-associated degradation (ERAD) by reducing incorrect disulfide bonds in misfolded glycoproteins recognized by EDEM1. Interaction with HSPA5 is required its activity, not for the disulfide reductase activity, [...] (793 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)
Yme1l1ATP-dependent zinc metalloprotease YME1L1; ATP-dependent metalloprotease that catalyzes the degradation of folded and unfolded proteins with a suitable degron sequence in the mitochondrial intermembrane region (By similarity). Plays an important role in regulating mitochondrial morphology and function by cleaving OPA1 at position S2, giving rise to a form of OPA1 that promotes maintenance of normal mitochondrial structure (By similarity). Ensures cell proliferation, maintains normal cristae morphology and complex I respiration activity, promotes antiapoptotic activity and protects mito [...] (715 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)
Dnajb13DnaJ (Hsp40) related, subfamily B, member 13, isoform CRA_a. (316 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)
Hspa9Stress-70 protein, mitochondrial; Chaperone protein which plays an important role in mitochondrial iron-sulfur cluster (ISC) biogenesis. Interacts with and stabilizes ISC cluster assembly proteins FXN, NFU1, NFS1 and ISCU. Regulates erythropoiesis via stabilization of ISC assembly. May play a role in the control of cell proliferation and cellular aging. (679 aa)
Sil1Nucleotide exchange factor SIL1; Required for protein translocation and folding in the endoplasmic reticulum (ER). Functions as a nucleotide exchange factor for the ER lumenal chaperone HSPA5 (By similarity); Belongs to the SIL1 family. (465 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)
Dnajb8DnaJ heat shock protein family (Hsp40) member B8. (235 aa)
Dnajb12DnaJ heat shock protein family (Hsp40) member B12. (378 aa)
ClpxATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial; ATP-dependent specificity component of the Clp protease complex. Hydrolyzes ATP. Targets specific substrates for degradation by the Clp complex. Can perform chaperone functions in the absence of CLPP. Enhances the DNA-binding activity of TFAM and is required for maintaining a normal mitochondrial nucleoid structure. ATP-dependent unfoldase that stimulates the incorporation of the pyridoxal phosphate cofactor into 5-aminolevulinate synthase, thereby activating 5- aminolevulinate (ALA) synthesis, the first step in h [...] (633 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)
Grpel2GrpE protein homolog; Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner; Belongs to the GrpE family. (224 aa)
Hspd160 kDa heat shock protein, mitochondrial; Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per rin [...] (573 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)
M0R8M9_RATUncharacterized protein; Belongs to the heat shock protein 70 family. (661 aa)
ClppATP-dependent Clp protease proteolytic subunit. (272 aa)
Lonp1Lon protease homolog, mitochondrial; ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial promoters and RNA in a single-stranded, site-specific, and strand- specific manner. May regulate mi [...] (950 aa)
M0RCB1_RATUncharacterized protein; Belongs to the heat shock protein 70 family. (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)
Hspe110 kDa heat shock protein, mitochondrial; Co-chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp60, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per [...] (89 aa)
Dnajb14Similar to DnaJ (Hsp40) homolog, subfamily B, member 14 isoform 1, isoform CRA_b. (377 aa)
A0A0G2JVI0_RATUncharacterized protein; Belongs to the GroES chaperonin family. (102 aa)
A0A0G2JVI3_RATUncharacterized protein; Belongs to the heat shock protein 70 family. (566 aa)
Hspa13Heat shock 70 kDa protein 13; Has peptide-independent ATPase activity. (471 aa)
Grpel1GrpE protein homolog 1, mitochondrial; Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. Seems to control the nucleotide-dependent binding of mitochondrial HSP70 to substrate proteins; Belongs to the GrpE family. (230 aa)
ClpbCaseinolytic peptidase B protein homolog; May function as a regulatory ATPase and be related to secretion/protein trafficking process. (707 aa)
Dnaja3DnaJ heat shock protein family (Hsp40) member A3. (480 aa)
Dnajb2DnaJ heat shock protein family (Hsp40) member B2. (277 aa)
Dnajb5DnaJ heat shock protein family (Hsp40) member B5. (420 aa)
A0A0G2K9V8_RATUncharacterized protein. (81 aa)
Dnajb4DnaJ (Hsp40) homolog, subfamily B, member 4, isoform CRA_a. (337 aa)
Tmem59lTransmembrane protein 59-like; Modulates the O-glycosylation and complex N-glycosylation steps occurring during the Golgi maturation of APP. Inhibits APP transport to the cell surface and further shedding (By similarity). Belongs to the TMEM59 family. (354 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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