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STRINGSTRING
HSPA2 HSPA2 HSPA1B HSPA1B HSPA1L HSPA1L SGTA SGTA HSPA4 HSPA4 DNAJC5 DNAJC5 HSPA1A HSPA1A HSPA5 HSPA5 HSPA8 HSPA8 HSPA6 HSPA6 SYT1 SYT1
"DNAJC5" - DnaJ in Homo sapiens
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:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
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Textmining
[Homology]
Score
DNAJC5DnaJ (Hsp40) homolog, subfamily C, member 5; May have an important role in presynaptic function. May be involved in calcium-dependent neurotransmitter release at nerve endings (By similarity) (198 aa)    
Predicted Functional Partners:
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)
score_image   score_image score_image score_image score_image score_image   0.995
SYT1
synaptotagmin I; May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2 (422 aa)
          score_image score_image   0.950
HSPA1A
heat shock 70kDa protein 1A (641 aa)
score_image   score_image score_image score_image   score_image   0.942
HSPA4
heat shock 70kDa protein 4 (840 aa)
score_image   score_image score_image score_image   score_image   0.935
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)
score_image   score_image score_image score_image   score_image   0.934
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)
score_image   score_image score_image score_image   score_image   0.934
HSPA1B
heat shock 70kDa protein 1B (641 aa)
score_image   score_image score_image score_image   score_image   0.933
HSPA1L
heat shock 70kDa protein 1-like (641 aa)
score_image   score_image score_image score_image   score_image   0.933
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)
score_image   score_image score_image score_image   score_image   0.933
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)
        score_image   score_image   0.932
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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