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DNAJC7 DNAJC7 ATF6 ATF6 HSP90B1 HSP90B1 ERN1 ERN1 HSPA5 HSPA5 DNAJB6 DNAJB6 DNAJC10 DNAJC10 PDIA3 PDIA3 CANX CANX DNAJB1 DNAJB1 DNAJB11 DNAJB11
"HSPA5" - Heat shock 70kDa protein 5 (glucose-regulated protein, 78kDa) in Homo sapiens
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HSPA5Heat shock 70kDa protein 5 (glucose-regulated protein, 78kDa); Probably plays a role in facilitating the assembly of multimeric protein complexes inside the endoplasmic reticulum. Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10, probably to facilitate the release of DNAJC10 from its substrate (654 aa)    
Predicted Functional Partners:
HSP90B1
Heat shock protein 90kDa beta (Grp94), member 1; Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity). Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity (803 aa)
      score_image score_image score_image score_image   0.999
CANX
Calnexin; Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins. Associated with partial T-cell antigen receptor complexes that escape the ER of immature thymocytes, it may function as a signaling complex regulating thymocyte maturation. Additionally it may play a role in receptor- mediated endocytosis at [...] (592 aa)
      score_image score_image score_image score_image   0.996
DNAJC10
DnaJ (Hsp40) 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 [...] (793 aa)
score_image     score_image score_image score_image score_image   0.996
ERN1
Endoplasmic reticulum to nucleus signaling 1; Senses unfolded proteins in the lumen of the endoplasmic reticulum via its N-terminal domain which leads to enzyme auto- activation. The active endoribonuclease domain splices XBP1 mRNA to generate a new C-terminus, converting it into a potent unfolded-protein response transcriptional activator and triggering growth arrest and apoptosis (977 aa)
      score_image score_image score_image score_image   0.996
DNAJB1
DnaJ (Hsp40) homolog, subfamily B, member 1; Interacts with HSP70 and can stimulate its ATPase activity. Stimulates the association between HSC70 and HIP (340 aa)
score_image   score_image score_image score_image score_image score_image   0.996
ATF6
Activating transcription factor 6; Transmembrane glycoprotein of the endoplasmic reticulum that functions as a transcription activator and initiates the unfolded protein response (UPR) during endoplasmic reticulum stress. Cleaved upon ER stress, the N-terminal processed cyclic AMP-dependent transcription factor ATF-6 alpha translocates to the nucleus where it activates transcription of genes involved in the UPR. Binds DNA on the 5’-CCAC[GA]-3’half of the ER stress response element (ERSE) (5’-CCAAT-N(9)-CCAC[GA]-3’) and of ERSE II (5’- ATTGG-N-CCACG-3’). Binding to ERSE requires binding [...] (670 aa)
      score_image score_image score_image score_image   0.995
PDIA3
Protein disulfide isomerase family A, member 3 (505 aa)
score_image     score_image score_image score_image score_image   0.993
DNAJB11
DnaJ (Hsp40) homolog, subfamily B, member 11; Serves as a co-chaperone for HSPA5. Binds directly to both unfolded proteins that are substrates for ERAD and nascent unfolded peptide chains, but dissociates from the HSPA5-unfolded protein complex before folding is completed. May help recruiting HSPA5 and other chaperones to the substrate. Stimulates HSPA5 ATPase activity (358 aa)
score_image   score_image score_image score_image score_image score_image   0.990
DNAJB6
DnaJ (Hsp40) 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. Isoform B but not isoform A inhibits huntingtin aggregation. 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 (326 aa)
score_image   score_image score_image score_image score_image score_image   0.990
DNAJC7
DnaJ (Hsp40) homolog, subfamily C, member 7; Acts as co-chaperone regulating the molecular chaperones HSP70 and HSP90 in folding of steroid receptors, such as the glucocorticoid receptor and the progesterone receptor. Proposed to act as a recycling chaperone by facilitating the return of chaperone substrates to early stages of chaperoning if further folding is required. In vitro, induces ATP-independent dissociation of HSP90 but not of HSP70 from the chaperone- substrate complexes. Recruits NR1I3 to the cytoplasm (By similarity) (494 aa)
score_image     score_image score_image score_image score_image   0.988
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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