Full Link:
  • Version:
  • 10.0 (archived version)
STRINGSTRING
HSPA14 HSPA14 HSPA13 HSPA13 HSPA6 HSPA6 HSPA2 HSPA2 HSPA8 HSPA8 C19orf70 C19orf70 HSPA5 HSPA5 DNAJC11 DNAJC11 GRPEL1 GRPEL1 CHCHD3 CHCHD3 HSPH1 HSPH1 ANKRD45 ANKRD45 APOOL APOOL GRPEL2 GRPEL2 HYOU1 HYOU1 IMMT IMMT CLPB CLPB HSPA4 HSPA4 HSPA4L HSPA4L HSPA1A HSPA1A PITPNB PITPNB HSPA9 HSPA9 HSPA1L HSPA1L HSPA12A HSPA12A HSPA12B HSPA12B HSPA1B HSPA1B
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 Size
small protein node
small nodes:
protein of unknown 3D structure
large protein node
large nodes:
some 3D structure is known or predicted
Node Color
colored protein node
colored nodes:
query proteins and first shell of interactors
non-colored protein node
white nodes:
second shell of interactors
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 each other.
Known Interactions
database edge
from curated databases
experiment edge
experimentally determined
Predicted Interactions
neighborhood edge
gene neighborhood
fusion edge
gene fusions
cooccurrence edge
gene co-occurrence
Others
textmining edge
textmining
coexpression edge
co-expression
homology edge
protein homology
Your Input:
HSPA8heat shock 70kDa protein 8; Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Chaperone. Component of the PRP19- CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex (646 aa)
HSPA2heat shock 70kDa protein 2; In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage (639 aa)
HSPA12Bheat shock 70kD protein 12B (686 aa)
CHCHD3coiled-coil-helix-coiled-coil-helix domain containing 3; Required for maintenance of mitochondrial crista integrity and mitochondrial function. May act as a scaffolding protein that stabilizes protein complexes involved in crista architecture and protein import. Has also been shown to function as a transcription factor which binds to the BAG1 promoter and represses BAG1 transcription (227 aa)
GRPEL1GrpE-like 1, mitochondrial (E. coli); 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 (217 aa)
HSPA13heat shock protein 70kDa family, member 13; Has peptide-independent ATPase activity (471 aa)
CLPBClpB caseinolytic peptidase B homolog (E. coli); May function as a regulatory ATPase and be related to secretion/protein trafficking process (707 aa)
HSPA4Lheat shock 70kDa protein 4-like; Possesses chaperone activity in vitro where it inhibits aggregation of citrate synthase (By similarity) (839 aa)
HSPA9heat shock 70kDa protein 9 (mortalin) (679 aa)
HSPA4heat shock 70kDa protein 4 (840 aa)
C19orf70chromosome 19 open reading frame 70 (118 aa)
HSPA6heat shock 70kDa protein 6 (HSP70B’); In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage (By similarity) (643 aa)
HSPH1heat shock 105kDa/110kDa protein 1; 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 (By similarity) (858 aa)
HSPA5heat shock 70kDa protein 5 (glucose-regulated protein, 78kDa); Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER (654 aa)
GRPEL2GrpE-like 2, mitochondrial (E. coli); 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. Stimulates ATPase activity of mt-HSP70. May also serve to modulate the interconversion of oligomeric (inactive) and monomeric (active) forms of mt-HSP70 (By similarity) (225 aa)
ANKRD45ankyrin repeat domain 45 (266 aa)
PITPNBphosphatidylinositol transfer protein, beta; Catalyzes the transfer of PtdIns and phosphatidylcholine between membranes (271 aa)
HSPA12Aheat shock 70kDa protein 12A (675 aa)
APOOLapolipoprotein O-like (268 aa)
HSPA1Bheat shock 70kDa protein 1B (641 aa)
HSPA1Aheat shock 70kDa protein 1A (641 aa)
HSPA1Lheat shock 70kDa protein 1-like (641 aa)
DNAJC11DnaJ (Hsp40) homolog, subfamily C, member 11 (559 aa)
HSPA14heat shock 70kDa 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 (509 aa)
HYOU1hypoxia up-regulated 1; Has a pivotal role in cytoprotective cellular mechanisms triggered by oxygen deprivation. May play a role as a molecular chaperone and participate in protein folding (999 aa)
IMMTinner membrane protein, mitochondrial (758 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
Server load: low (37%)