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STRINGSTRING
DMWD DMWD SDF2 SDF2 DNAJB11 DNAJB11 DNAJC3 DNAJC3 HSPA5 HSPA5 DNAJB5 DNAJB5 HNRNPD HNRNPD DNAJB1 DNAJB1 DNAJB4 DNAJB4 DNAJA2 DNAJA2
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:
SDF2stromal cell-derived factor 2 (211 aa)
DNAJB1DnaJ (Hsp40) homolog, subfamily B, member 1; Interacts with HSP70 and can stimulate its ATPase activity. Stimulates the association between HSC70 and HIP (340 aa)
DNAJB11DnaJ (Hsp40) homolog, subfamily B, member 11; Serves as a co-chaperone for HSPA5. Binds directly to both unfolded proteins that are substrates for ERAD and nascent unfolded peptide chains, but dissociates from the HSPA5-unfolded protein complex before folding is completed. May help recruiting HSPA5 and other chaperones to the substrate. Stimulates HSPA5 ATPase activity (358 aa)
DMWDdystrophia myotonica, WD repeat containing; Could have a regulatory function in meiosis (674 aa)
HNRNPDheterogeneous nuclear ribonucleoprotein D (AU-rich element RNA binding protein 1, 37kDa) (355 aa)
DNAJA2DnaJ (Hsp40) homolog, subfamily A, member 2; Co-chaperone of Hsc70 (412 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)
DNAJB4DnaJ (Hsp40) homolog, subfamily B, member 4; Probable chaperone (337 aa)
DNAJC3DnaJ (Hsp40) homolog, subfamily C, member 3; Involved in the unfolded protein response (UPR) during ER stress. Co-chaperone of HSPA8/HSC70, it stimulates its ATPase activity. May inhibit both the autophosphorylation of EIF2AK2/PKR and the ability of EIF2AK2 to catalyze phosphorylation of the EIF2A. May inhibit EIF2AK3/PERK activity (504 aa)
DNAJB5DnaJ (Hsp40) homolog, subfamily B, member 5 (462 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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