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) | ||
 | SGTA | small glutamine-rich tetratricopeptide repeat (TPR)-containing, alpha; Co-chaperone that binds directly to HSC70 and HSP70 and regulates their ATPase activity (313 aa) | ||
 | TTC31 | tetratricopeptide repeat domain 31 (519 aa) | ||
 | NFYB | nuclear transcription factor Y, beta; Stimulates the transcription of various genes by recognizing and binding to a CCAAT motif in promoters, for example in type 1 collagen, albumin and beta-actin genes (207 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) | ||
 | DNAJC10 | DnaJ (Hsp40) homolog, subfamily C, member 10 (793 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) | ||
 | HSPA13 | heat shock protein 70kDa family, member 13; Has peptide-independent ATPase activity (471 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) | ||
 | GAK | cyclin 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) | ||
 | 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) | ||
 | 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) | ||
 | UBC | ubiquitin C (685 aa) | ||
 | UBQLN2 | ubiquilin 2; Increases the half-life of proteins destined to be degraded by the proteasome; may modulate proteasome-mediated protein degradation (624 aa) | ||
 | BAG3 | BCL2-associated athanogene 3; Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. Has anti-apoptotic activity (575 aa) | ||
 | UBQLN1 | ubiquilin 1; Links CD47 to the cytoskeleton. Promotes the surface expression of GABA-A receptors (By similarity). Promotes the accumulation of uncleaved PSEN1 and PSEN2 by stimulating their biosynthesis. Has no effect on PSEN1 and PSEN2 degradation (589 aa) | ||
 | SUGT1 | SGT1, suppressor of G2 allele of SKP1 (S. cerevisiae); May play a role in ubiquitination and subsequent proteasomal degradation of target proteins (365 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) | ||
 | TTC28 | tetratricopeptide repeat domain 28 (2481 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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