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KIAA0664 KIAA0664 GRPEL2 GRPEL2 GRPEL1 GRPEL1 STIP1 STIP1 ISCU ISCU SUGT1 SUGT1 CLPB CLPB DNAJB13 DNAJB13 DNAJA4 DNAJA4 TRAP1 TRAP1 DNAJA1 DNAJA1 HSP90B1 HSP90B1 HSP90AB1 HSP90AB1 HSCB HSCB HSPA1L HSPA1L HYOU1 HYOU1 DNAJA2 DNAJA2 HSP90AA1 HSP90AA1 DNAJB4 DNAJB4 DNAJB1 DNAJB1 DNAJC10 DNAJC10 GAK GAK BAG3 BAG3 CANX CANX STUB1 STUB1 CLGN CLGN
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:
HSCBHscB iron-sulfur cluster co-chaperone homolog (E. coli); Acts as a co-chaperone in iron-sulfur cluster assembly in mitochondria (235 aa)
STUB1STIP1 homology and U-box containing protein 1, E3 ubiquitin protein ligase; E3 ubiquitin-protein ligase which targets misfolded chaperone substrates towards proteasomal degradation. Collaborates with ATXN3 in the degradation of misfolded chaperone substrates- ATXN3 restricting the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension. Ubiquitinates NOS1 in concert with Hsp70 and Hsp40. Modulates the activity of several chaperone complexes, including Hsp70, Hsc70 and Hsp90. Mediates transfer of non-canonical short ubiquitin chains to HSPA8 th [...] (303 aa)
TRAP1TNF receptor-associated protein 1; Chaperone that expresses an ATPase activity (704 aa)
CANXcalnexin; 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)
DNAJB1DnaJ (Hsp40) homolog, subfamily B, member 1; Interacts with HSP70 and can stimulate its ATPase activity. Stimulates the association between HSC70 and HIP (340 aa)
DNAJC10DnaJ (Hsp40) homolog, subfamily C, member 10 (793 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)
HSP90B1heat 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)
STIP1stress-induced-phosphoprotein 1; Mediates the association of the molecular chaperones HSC70 and HSP90 (HSPCA and HSPCB) (543 aa)
ISCUiron-sulfur cluster scaffold homolog (E. coli); Involved in the assembly or repair of the [Fe-S] clusters present in iron-sulfur proteins. Binds iron (167 aa)
DNAJA2DnaJ (Hsp40) homolog, subfamily A, member 2; Co-chaperone of Hsc70 (412 aa)
GAKcyclin G associated kinase; Associates with cyclin G and CDK5. Seems to act as an auxilin homolog that is involved in the uncoating of clathrin- coated vesicles by Hsc70 in non-neuronal cells. Expression oscillates slightly during the cell cycle, peaking at G1 (1311 aa)
HSP90AB1heat shock protein 90kDa alpha (cytosolic), class B 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 (724 aa)
CLGNcalmegin; Probably plays an important role in spermatogenesis. Binds calcium ions (610 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)
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)
DNAJB13DnaJ (Hsp40) homolog, subfamily B, member 13; May be involved in inhibiting testis spermatogenesis apoptosis (316 aa)
BAG3BCL2-associated athanogene 3; Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. Has anti-apoptotic activity (575 aa)
DNAJB4DnaJ (Hsp40) homolog, subfamily B, member 4; Probable chaperone (337 aa)
HSPA1Lheat shock 70kDa protein 1-like (641 aa)
SUGT1SGT1, suppressor of G2 allele of SKP1 (S. cerevisiae); May play a role in ubiquitination and subsequent proteasomal degradation of target proteins (365 aa)
DNAJA1DnaJ (Hsp40) homolog, subfamily A, member 1; Co-chaperone of Hsc70. Seems to play a role in protein import into mitochondria (397 aa)
DNAJA4DnaJ (Hsp40) homolog, subfamily A, member 4 (426 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)
KIAA0664KIAA0664; Involved in proper cytoplasmic distribution of mitochondria (By similarity) (1309 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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