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ANKRD45 ANKRD45 HSPA13 HSPA13 GRPEL2 GRPEL2 SPATA13 SPATA13 HSPA12B HSPA12B DNAJC10 DNAJC10 GRPEL1 GRPEL1 HSPA12A HSPA12A HSPA9 HSPA9 CAD CAD DNAJC22 DNAJC22 HSPA1B HSPA1B HSPA2 HSPA2 HSPA4L HSPA4L HSPA4 HSPA4 HSPA8 HSPA8 HSPH1 HSPH1 DNAJA1 DNAJA1 DNAJA4 DNAJA4 CLPB CLPB HSPA5 HSPA5 DNAJA2 DNAJA2 HSPA6 HSPA6 UBC UBC GSPT2 GSPT2 GSPT1 GSPT1
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:
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)
HSPA12Bheat shock 70kD protein 12B (686 aa)
DNAJC10DnaJ (Hsp40) homolog, subfamily C, member 10 (793 aa)
CADcarbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase; This protein is a "fusion" protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase) (2225 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)
HSPA13heat shock protein 70kDa family, member 13; Has peptide-independent ATPase activity (471 aa)
CLPBClpB caseinolytic peptidase B homolog (E. coli); May function as a regulatory ATPase and be related to secretion/protein trafficking process (707 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)
DNAJA2DnaJ (Hsp40) homolog, subfamily A, member 2; Co-chaperone of Hsc70 (412 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)
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)
ANKRD45ankyrin repeat domain 45 (266 aa)
GSPT2G1 to S phase transition 2; Involved in translation termination in response to the termination codons UAA, UAG and UGA. May play a role as a potent stimulator of the release factor activity of ETF1. Exhibits GTPase activity, which is ribosome- and ETF1-dependent. May play a role in cell cycle progression. Component of the transient SURF complex which recruits UPF1 to stalled ribosomes in the context of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons (628 aa)
UBCubiquitin C (685 aa)
HSPA12Aheat shock 70kDa protein 12A (675 aa)
HSPA1Bheat shock 70kDa protein 1B (641 aa)
DNAJA1DnaJ (Hsp40) homolog, subfamily A, member 1; Co-chaperone of Hsc70. Seems to play a role in protein import into mitochondria (397 aa)
SPATA13spermatogenesis associated 13 (1277 aa)
DNAJA4DnaJ (Hsp40) homolog, subfamily A, member 4 (426 aa)
DNAJC22DnaJ (Hsp40) homolog, subfamily C, member 22; May function as a co-chaperone (341 aa)
GSPT1G1 to S phase transition 1; Involved in translation termination in response to the termination codons UAA, UAG and UGA. Stimulates the activity of ERF1. Involved in regulation of mammalian cell growth. Component of the transient SURF complex which recruits UPF1 to stalled ribosomes in the context of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons (637 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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