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HSPA5 HSPA5 HSPA1L HSPA1L DNAJA3 DNAJA3 HSPA2 HSPA2 HSPA1A HSPA1A HSPA8 HSPA8 HSPA1B HSPA1B STIP1 STIP1 DNAJB13 DNAJB13 CLPB CLPB PPME1 PPME1
"DNAJB13" - DnaJ homolog subfamily B member 13 in Homo sapiens
Nodes:
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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
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
some 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 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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[Homology]
Score
DNAJB13DnaJ homolog subfamily B member 13; May play a role in the formation of the central complex of ciliary and flagellar axonemes; DNAJ heat shock proteins (316 aa)    
Predicted Functional Partners:
STIP1
Stress-induced-phosphoprotein 1; Acts as a co-chaperone for HSP90AA1. Mediates the association of the molecular chaperones HSPA8/HSC70 and HSP90 (By similarity); Tetratricopeptide repeat domain containing (590 aa)
     
 
  0.804
PPME1
Protein phosphatase methylesterase 1; Demethylates proteins that have been reversibly carboxymethylated. Demethylates PPP2CB (in vitro) and PPP2CA. Binding to PPP2CA displaces the manganese ion and inactivates the enzyme; Protein phosphatase 2 modulatory subunits (400 aa)
       
 
  0.778
HSPA2
Heat 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 [...] (639 aa)
 
 
  0.775
CLPB
Caseinolytic peptidase B protein homolog; May function as a regulatory ATPase and be related to secretion/protein trafficking process; AAA ATPases (707 aa)
   
 
  0.770
DNAJA3
DnaJ homolog subfamily A member 3, mitochondrial; Modulates apoptotic signal transduction or effector structures within the mitochondrial matrix. Affect cytochrome C release from the mitochondria and caspase 3 activation, but not caspase 8 activation. Isoform 1 increases apoptosis triggered by both TNF and the DNA-damaging agent mytomycin C; in sharp contrast, isoform 2 suppresses apoptosis. Can modulate IFN-gamma- mediated transcriptional activity. Isoform 2 may play a role in neuromuscular junction development as an effector of the MUSK signaling pathway; DNAJ heat shock proteins (480 aa)
   
   
0.727
HSPA5
78 kDa glucose-regulated protein; 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 (By similarity); Belongs to the heat shock protein 70 family (654 aa)
 
 
  0.726
HSPA1L
Heat 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)
 
 
  0.717
HSPA1A
Heat 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)
 
 
  0.716
HSPA1B
Heat shock protein family A member 1B (641 aa)
 
 
  0.714
HSPA8
Heat 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)
 
 
  0.712
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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