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
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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
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[Homology]
Score
RER1Protein involved in retention of membrane proteins; including Sec12p, in the ER; localized to Golgi; functions as a retrieval receptor in returning membrane proteins to the ER. (188 aa)    
Predicted Functional Partners:
ERD2
ER lumen protein-retaining receptor; HDEL receptor; an integral membrane protein that binds to the HDEL motif in proteins destined for retention in the endoplasmic reticulum; has a role in maintenance of normal levels of ER-resident proteins; Belongs to the ERD2 family.
   
 
 0.982
CNE1
Calnexin; integral membrane ER chaperone involved in folding and quality control of glycoproteins; chaperone activity is inhibited by Mpd1p, with which Cne1p interacts; 24% identical to mammalian calnexin; Ca+ binding not yet shown in yeast.
    
 
 0.981
SEC27
Coatomer subunit beta; Essential beta'-coat protein of the COPI coatomer; involved in ER-to-Golgi and Golgi-to-ER transport; contains WD40 domains that mediate cargo selective interactions; 45% sequence identity to mammalian beta'-COP.
   
 
 0.972
ERV29
Protein localized to COPII-coated vesicles; involved in vesicle formation and incorporation of specific secretory cargo; protein abundance increases in response to DNA replication stress; Belongs to the SURF4 family.
   
 
 0.960
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.
   
 
 0.957
ERV46
Protein localized to COPII-coated vesicles; forms a complex with Erv41p; involved in the membrane fusion stage of transport; Belongs to the ERGIC family.
   
 
 0.938
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.
   
 
 0.926
SEC12
Guanine nucleotide exchange factor (GEF); activates Sar1p by catalyzing the exchange of GDP for GTP; required for the initiation of COPII vesicle formation in ER to Golgi transport; glycosylated integral membrane protein of the ER; SEC12 has a paralog, SED4, that arose from the whole genome duplication; Belongs to the WD repeat SEC12 family.
    
 
 0.925
WBP1
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit WBP1; Beta subunit of the oligosaccharyl transferase glycoprotein complex; required for N-linked glycosylation of proteins in the endoplasmic reticulum; human homolog DDOST can complement yeast growth defect during down-regulation of yeast gene.
   
 
 0.923
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.
   
 
 0.911
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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