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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 | HSCB | HscB iron-sulfur cluster co-chaperone homolog (E. coli); Acts as a co-chaperone in iron-sulfur cluster assembly in mitochondria (235 aa) | ||
 | HSPA8 | heat 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) | ||
 | BBS2 | Bardet-Biedl syndrome 2; The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and promotes docking and fusion of carrier vesicles to the base of [...] (721 aa) | ||
 | HSPA2 | heat 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) | ||
 | HSPA12B | heat shock 70kD protein 12B (686 aa) | ||
 | BBS4 | Bardet-Biedl syndrome 4; May be required for the dynein-mediated transport of pericentriolar proteins to the centrosome. Required for microtubule anchoring at the centrosome but not for microtubule nucleation. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane [...] (519 aa) | ||
 | SOD1 | superoxide dismutase 1, soluble; Destroys radicals which are normally produced within the cells and which are toxic to biological systems (By similarity) (154 aa) | ||
 | HSPA13 | heat shock protein 70kDa family, member 13; Has peptide-independent ATPase activity (471 aa) | ||
 | HSPA4L | heat shock 70kDa protein 4-like; Possesses chaperone activity in vitro where it inhibits aggregation of citrate synthase (By similarity) (839 aa) | ||
 | HSPA9 | heat shock 70kDa protein 9 (mortalin) (679 aa) | ||
 | CLPX | ClpX caseinolytic peptidase X homolog (E. coli); ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of clpP (By similarity) (633 aa) | ||
 | HSPA4 | heat shock 70kDa protein 4 (840 aa) | ||
 | HSPA6 | heat 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) | ||
 | 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) | ||
 | BBS1 | Bardet-Biedl syndrome 1; The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and promotes docking and fusion of carrier vesicles to the base of [...] (593 aa) | ||
 | TIMM50 | translocase of inner mitochondrial membrane 50 homolog (S. cerevisiae); Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane. Has some phosphatase activity in vitro; however such activity may not be relevant in vivo. Isoform 2 may participate in the release of snRNPs and SMN from the Cajal body (456 aa) | ||
 | HSPH1 | heat 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) | ||
 | HSPA5 | heat 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) | ||
 | ANKRD45 | ankyrin repeat domain 45 (266 aa) | ||
 | NFS1 | NFS1 nitrogen fixation 1 homolog (S. cerevisiae); Catalyzes the removal of elemental sulfur from cysteine to produce alanine. It supplies the inorganic sulfur for iron- sulfur (Fe-S) clusters. May be involved in the biosynthesis of molybdenum cofactor (457 aa) | ||
 | HSPA1B | heat shock 70kDa protein 1B (641 aa) | ||
 | HSPA1A | heat shock 70kDa protein 1A (641 aa) | ||
 | HSPA1L | heat shock 70kDa protein 1-like (641 aa) | ||
 | HSPA14 | heat 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) | ||
 | SOD3 | superoxide dismutase 3, extracellular; Protect the extracellular space from toxic effect of reactive oxygen intermediates by converting superoxide radicals into hydrogen peroxide and oxygen (240 aa) | ||
 | CCS | copper chaperone for superoxide dismutase; Destroys radicals which are normally produced within the cells and which are toxic to biological systems (By similarity) (274 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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