STRINGSTRING
STRING protein interaction network
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 Color
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
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 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
Databases
Textmining
[Homology]
Score
marc-4RING-CH-type domain-containing protein. (317 aa)    
Predicted Functional Partners:
C27A7.6
Uncharacterized protein.
      
 0.971
erd-2
ER lumen protein-retaining receptor erd-2.1; Required for the retention of luminal endoplasmic reticulum proteins. Determines the specificity of the luminal ER protein retention system. Also required for normal vesicular traffic through the Golgi (By similarity); Belongs to the ERD2 family.
      
 0.910
ntl-2
NOT2_3_5 domain-containing protein.
    
 
 0.456
tag-153
NOT2_3_5 domain-containing protein.
    
 
 0.456
ubc-14
UBIQUITIN_CONJUGAT_2 domain-containing protein; Belongs to the ubiquitin-conjugating enzyme family.
    
 
 0.425
ubr-1
E3 ubiquitin-protein ligase ubr-1; E3 ubiquitin-protein ligase which is a component of the N-end rule pathway (By similarity). Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N- end rule, leading to their ubiquitination and subsequent degradation (By similarity). In complex with ced-3, required for the ced-3-mediated cleavage and subsequent degradation of the heterochronic protein lin-28 to regulate seam cell fate patterning during larval development. Negatively regulates glutamate metabolism through the aspartate aminotrans [...]
   
 
 0.403
cdc-48.1
Transitional endoplasmic reticulum ATPase homolog 1; ATP-dependent chaperone which probably uses the energy provided by ATP hydrolysis to generate mechanical force to unfold substrate proteins, disassemble protein complexes, and disaggregate protein aggregates. Can also prevent aggregation of unfolded proteins also in an ATP- independent manner. Targets polyubiquitinated proteins for proteasomal degradation by binding to 'Lys-48'-linked polyubiquitin chains. Involved in the cytoplasmic elimination of misfolded proteins exported from the ER. This pathway, known as ERAD, prevents the act [...]
    
 
 0.400
cdc-48.2
Transitional endoplasmic reticulum ATPase homolog 2; ATP-dependent chaperone which probably uses the energy provided by ATP hydrolysis to generate mechanical force to unfold substrate proteins, disassemble protein complexes, and disaggregate protein aggregates. However, able to prevent aggregation of unfolded proteins also in an ATP-independent manner. Targets polyubiquitinated proteins for proteasomal degradation by binding to 'Lys-48'-linked polyubiquitin chains. Involved in the cytoplasmic elimination of misfolded proteins exported from the ER. This pathway, known as ERAD, prevents [...]
    
 
 0.400
cdc-48.3
ATPase family protein 2 homolog; ATP-dependent chaperone which uses the energy provided by ATP hydrolysis to generate mechanical force to disassemble protein complexes (By similarity). Required for various steps of embryonic mitosis including centrosome duplication, spindle assembly, ER dynamics and cell cycle progression. Regulates the stability and activity of kinase air-2, a component of the chromosomal passenger complex (CPC). Inhibits air-2 kinase activity from metaphase to late telophase and negatively regulates air-2 stability during mitotic exit. Controls ER transition into she [...]
    
 
 0.400
Your Current Organism:
Caenorhabditis elegans
NCBI taxonomy Id: 6239
Other names: C. elegans, Rhabditis elegans, roundworm
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