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STRINGSTRING
HSPA9 HSPA9 POM121 POM121 HSPA12B HSPA12B HSPA12A HSPA12A HSPA2 HSPA2 HSPA4 HSPA4 NUP88 NUP88 NUP35 NUP35 HSPH1 HSPH1 NUP210 NUP210 HSPA4L HSPA4L GAK GAK NUPL2 NUPL2 HSPA5 HSPA5 NUP188 NUP188 DNAJC6 DNAJC6 NUP214 NUP214 NUP43 NUP43 AAAS AAAS HSPA8 HSPA8 HSPA6 HSPA6 NUP37 NUP37 NUP160 NUP160 ST13 ST13 HSPA13 HSPA13 HSPA14 HSPA14
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:
AAASachalasia, adrenocortical insufficiency, alacrimia; Plays a role in the normal development of the peripheral and central nervous system (546 aa)
ST13suppression of tumorigenicity 13 (colon carcinoma) (Hsp70 interacting protein); One HIP oligomer binds the ATPase domains of at least two HSC70 molecules dependent on activation of the HSC70 ATPase by HSP40. Stabilizes the ADP state of HSC70 that has a high affinity for substrate protein. Through its own chaperone activity, it may contribute to the interaction of HSC70 with various target proteins (By similarity) (369 aa)
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)
HSPA2heat 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)
NUP37nucleoporin 37kDa; Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment, mitotic progression and chromosome segregation (326 aa)
NUP210nucleoporin 210kDa; Nucleoporin essential for nuclear pore assembly and fusion, nuclear pore spacing, as well as structural integrity (1887 aa)
HSPA12Bheat shock 70kD protein 12B (686 aa)
POM121POM121 transmembrane nucleoporin (984 aa)
NUPL2nucleoporin like 2; Required for the export of mRNAs containing poly(A) tails from the nucleus into the cytoplasm. In case of infection by HIV-1, it may participate in the docking of viral Vpr at the nuclear envelope (423 aa)
HSPA13heat shock protein 70kDa family, member 13; Has peptide-independent ATPase activity (471 aa)
NUP35nucleoporin 35kDa; Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs). Can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. May play a role in the association of MAD1 with the NPC (326 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)
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)
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)
NUP43nucleoporin 43kDa; Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment, mitotic progression and chromosome segregation (380 aa)
NUP214nucleoporin 214kDa; May serve as a docking site in the receptor-mediated import of substrates across the nuclear pore complex (2090 aa)
HSPA12Aheat shock 70kDa protein 12A (675 aa)
NUP188nucleoporin 188kDa; May function as a component of the nuclear pore complex (NPC) (1749 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)
NUP160nucleoporin 160kDa; Involved in poly(A)+ RNA transport (1436 aa)
DNAJC6DnaJ (Hsp40) homolog, subfamily C, member 6; Recruits HSPA8/HSC70 to clathrin-coated vesicles and promotes uncoating of clathrin-coated vesicles (By similarity) (913 aa)
NUP88nucleoporin 88kDa; Essential component of nuclear pore complex (741 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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