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 nodes:
protein of unknown 3D structure
protein of unknown 3D structure
large nodes:
some 3D structure is known or predicted
some 3D structure is known or predicted
Node Color
colored nodes:
query proteins and first shell of interactors
query proteins and first shell of interactors
white nodes:
second shell of interactors
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
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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Your Input:
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 | HSCB | HscB iron-sulfur cluster co-chaperone homolog (E. coli); Acts as a co-chaperone in iron-sulfur cluster assembly in mitochondria (235 aa) | ||
 | STUB1 | STIP1 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) | ||
 | DNAJC17 | DnaJ (Hsp40) homolog, subfamily C, member 17 (304 aa) | ||
 | DNAJC12 | DnaJ (Hsp40) homolog, subfamily C, member 12 (198 aa) | ||
 | TTC31 | tetratricopeptide repeat domain 31 (519 aa) | ||
 | TRAP1 | TNF receptor-associated protein 1; Chaperone that expresses an ATPase activity (704 aa) | ||
 | 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) | ||
 | HACE1 | HECT domain and ankyrin repeat containing E3 ubiquitin protein ligase 1 (909 aa) | ||
 | DNAJC10 | DnaJ (Hsp40) homolog, subfamily C, member 10 (793 aa) | ||
 | PIKFYVE | phosphoinositide kinase, FYVE finger containing; The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Catalyzes the phosphorylation of phosphatidylinositol 3-phosphate on the fifth hydroxyl of the myo- inositol ring, to form phosphatidylinositol 3,5-bisphosphate. Required for endocytic-vacuolar pathway and nuclear migration. Plays a role in the biogenesis of endosome carrier vesicles (ECV)/ multivesicular bodies (MVB) transport intermediates from early endosomes (2098 aa) | ||
 | GRPEL1 | GrpE-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) | ||
 | CLPB | ClpB caseinolytic peptidase B homolog (E. coli); May function as a regulatory ATPase and be related to secretion/protein trafficking process (707 aa) | ||
 | 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) | ||
 | STIP1 | stress-induced-phosphoprotein 1; Mediates the association of the molecular chaperones HSC70 and HSP90 (HSPCA and HSPCB) (543 aa) | ||
 | ISCU | iron-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) | ||
 | HSP90AB1 | heat 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) | ||
 | CLGN | calmegin; Probably plays an important role in spermatogenesis. Binds calcium ions (610 aa) | ||
 | GRPEL2 | GrpE-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) | ||
 | ANKRD45 | ankyrin repeat domain 45 (266 aa) | ||
 | MAGEA2B | melanoma antigen family A, 2B (314 aa) | ||
 | HSP90AA1 | heat 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) | ||
 | DNLZ | DNL-type zinc finger; May function as a co-chaperone towards HSPA9/mortalin which, by itself, is prone to self-aggregation (178 aa) | ||
 | DNAJC9 | DnaJ (Hsp40) homolog, subfamily C, member 9 (260 aa) | ||
 | MS4A13 | membrane-spanning 4-domains, subfamily A, member 13; May be involved in signal transduction as a component of a multimeric receptor complex (By similarity) (152 aa) | ||
 | TTC12 | tetratricopeptide repeat domain 12 (705 aa) | ||
 | SUGT1P3 | suppressor of G2 allele of SKP1 (S. cerevisiae) pseudogene 3 (91 aa) | ||
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
Other names: H. sapiens, Homo, Homo sapiens, human, man
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