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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
ERP6Protein ERP6; Member of the p24 family involved in ER to Golgi transport; similar to Emp24p and Erv25p; the authentic, non-tagged protein is detected in highly purified mitochondria in high-throughput studies; ERP6 has a paralog, ERP1, that arose from the whole genome duplication; Belongs to the EMP24/GP25L family. (216 aa)    
Predicted Functional Partners:
ERP1
Protein ERP1; Member of the p24 family involved in ER to Golgi transport; role in misfolded protein quality control; forms heterotrimeric complex with Erp2p, Emp24p, and Erv25p; localized to COPII-coated vesicles; ERP1 has a paralog, ERP6, that arose from the whole genome duplication.
  
0.999
ERV25
Endoplasmic reticulum vesicle protein 25; Member of the p24 family involved in ER to Golgi transport; role in misfolded protein quality control; forms a heterotrimeric complex with Erp1, Erp2p, and Emp24.
   
 0.999
ERP4
Protein ERP4; Member of the p24 family involved in ER to Golgi transport; similar to Emp24p and Erv25p; ERP4 has a paralog, ERP2, that arose from the whole genome duplication; Belongs to the EMP24/GP25L family.
  
 0.999
ERP2
Protein ERP2; Member of the p24 family involved in ER to Golgi transport; similar to Emp24p and Erv25p; role in misfolded protein quality control; forms a heterotrimeric complex with Erp1p, Emp24p, and Erv25p; localized to COPII-coated vesicles; ERP2 has a paralog, ERP4, that arose from the whole genome duplication.
   
 0.993
ERP3
Protein with similarity to Emp24p and Erv25p; member of the p24 family involved in ER to Golgi transport.
   
 0.988
EMP24
Endosomal protein P24B; Component of the p24 complex; role in misfolded protein quality control; binds to GPI anchor proteins and mediates their efficient transport from the ER to the Golgi; integral membrane protein that associates with endoplasmic reticulum-derived COPII-coated vesicles.
  
0.972
RRT6
Regulator of rDNA transcription protein 6; Putative protein of unknown function; non-essential gene identified in a screen for mutants with increased levels of rDNA transcription; contains two putative transmembrane spans, but no significant homology to other known proteins.
   
  
 0.835
ERP5
Protein with similarity to Emp24p and Erv25p; member of the p24 family involved in ER to Golgi transport.
  
 
0.713
SEC28
Epsilon-COP subunit of the coatomer; regulates retrograde Golgi-to-ER protein traffic; stabilizes Cop1p, the alpha-COP and the coatomer complex; non-essential for cell growth; protein abundance increases in response to DNA replication stress.
   
 
  0.642
SEC26
Coatomer subunit beta; Essential beta-coat protein of the COPI coatomer; involved in ER-to-Golgi protein trafficking and maintenance of normal ER morphology; shares 43% sequence identity with mammalian beta-coat protein (beta-COP).
   
  0.639
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: ATCC 18824, Candida robusta, Mycoderma cerevisiae, NRRL Y-12632, S. cerevisiae, Saccharomyces capensis, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, yeast
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