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HSPA12B HSPA12B HSPA9 HSPA9 HSPA1B HSPA1B HSPA6 HSPA6 RAD9A RAD9A HUS1 HUS1 HSPA4L HSPA4L HSPH1 HSPH1 ANKRD45 ANKRD45 GRPEL1 GRPEL1 RAD1 RAD1 HSP90AA1 HSP90AA1 GRPEL2 GRPEL2 CLPB CLPB DNAJC7 DNAJC7 DNAJC10 DNAJC10 CAD CAD HSPA4 HSPA4 HSPA8 HSPA8 HYOU1 HYOU1 HSPA12A HSPA12A UBE4B UBE4B HSPA5 HSPA5 HSPA1L HSPA1L HSPA14 HSPA14 NF1 NF1
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
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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
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gene neighborhood
fusion edge
gene fusions
cooccurrence edge
gene co-occurrence
Others
textmining edge
textmining
coexpression edge
co-expression
homology edge
protein homology
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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)
HSPA12Bheat shock 70kD protein 12B (686 aa)
HUS1HUS1 checkpoint homolog (S. pombe); Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3’-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavag [...] (280 aa)
DNAJC10DnaJ (Hsp40) homolog, subfamily C, member 10 (793 aa)
CADcarbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase; This protein is a "fusion" protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase) (2225 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)
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)
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)
RAD9ARAD9 homolog A (S. pombe); Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3’-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activit [...] (391 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)
HSP90AA1heat shock protein 90kDa alpha (cytosolic), class A member 1; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (854 aa)
RAD1RAD1 homolog (S. pombe); Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3’-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity [...] (282 aa)
UBE4Bubiquitination factor E4B; Binds to the ubiquitin moieties of preformed conjugates and catalyzes ubiquitin chain assembly in conjunction with E1, E2, and E3 (By similarity) (1302 aa)
NF1neurofibromin 1; Stimulates the GTPase activity of Ras. NF1 shows greater affinity for Ras GAP, but lower specific activity. May be a regulator of Ras activity (2839 aa)
HSPA12Aheat shock 70kDa protein 12A (675 aa)
HSPA1Bheat shock 70kDa protein 1B (641 aa)
HSPA1Lheat shock 70kDa protein 1-like (641 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)
DNAJC7DnaJ (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)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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