STRINGSTRING
DNAJC5B DNAJC5B CDK5R2 CDK5R2 HSPA13 HSPA13 PRPF19 PRPF19 CDC5L CDC5L CRNKL1 CRNKL1 BUD31 BUD31 TFIP11 TFIP11 HSPA5 HSPA5 CETN3 CETN3 HSPA6 HSPA6
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.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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 to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
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Textmining
[Homology]
Score
DNAJC5BDnaJ homolog subfamily C member 5B. (199 aa)    
Predicted Functional Partners:
CDK5R2
Cyclin-dependent kinase 5 activator.
      
 0.879
HSPA13
Heat shock protein family A (Hsp70) member 13.
  
 0.862
PRPF19
Pre-mRNA-processing factor 19.
    
 
 0.839
CDC5L
Cell division cycle 5-like protein.
   
 
 0.835
CRNKL1
Crooked neck pre-mRNA splicing factor 1.
   
 
 0.809
BUD31
Protein BUD31 homolog isoform X2.
    
   0.798
TFIP11
Tuftelin-interacting protein 11; Involved in pre-mRNA splicing, specifically in spliceosome disassembly during late-stage splicing events. Intron turnover seems to proceed through reactions in two lariat-intron associated complexes termed Intron Large (IL) and Intron Small (IS). In cooperation with DHX15 seems to mediate the transition of the U2, U5 and U6 snRNP- containing IL complex to the snRNP-free IS complex leading to efficient debranching and turnover of excised introns. May play a role in the differentiation of ameloblasts and odontoblasts or in the forming of the enamel extrac [...]
    
 
 0.793
HSPA5
Endoplasmic reticulum chaperone BiP; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to dis [...]
  
 0.743
CETN3
Centrin 3.
    
 
 0.738
HSPA6
Heat shock 70 kDa protein 6; Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP [...]
  
 0.725
Your Current Organism:
Sus scrofa
NCBI taxonomy Id: 9823
Other names: S. scrofa, pig, pigs, swine, wild boar
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