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
SED4Putative guanine nucleotide-exchange factor SED4; Putative guanine nucleotide-exchange factor (GEF) involved in the formation or budding of transport vesicles from the ER. Positive regulator of SAR1 probably through inhibition of the GTPase activation by SEC23 (By similarity); Belongs to the WD repeat SEC12 family. (1029 aa)    
Predicted Functional Partners:
SAR1
Small COPII coat GTPase SAR1; Small GTPase component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. SAR1 controls the coat assembly in a stepwise manner. Activated SAR1-GTP binds to membranes first and recruits the SEC23/24 complex. These SEC23/24-SAR1 prebudding intermediates are then collected by the SEC13/31 complex as subunits polymerize to form coated trans [...]
   
 0.990
SEC12
Guanine nucleotide-exchange factor SEC12; Guanine nucleotide-exchange factor (GEF) required for the formation or budding of transport vesicles from the ER. This function involves the cytoplasmic domain of the protein, which is thought to interact with the small GTP-binding protein SAR1. Required for autophagy (By similarity); Belongs to the WD repeat SEC12 family.
   
 
0.909
SEC16
COPII coat assembly protein SEC16; Involved in the initiation of assembly of the COPII coat required for the formation of transport vesicles from the endoplasmic reticulum (ER) and the selection of cargo molecules. Also involved in autophagy (By similarity); Belongs to the SEC16 family.
   
 
 0.864
SEC31
Protein transport protein SEC31; Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules (By similarity).
   
  
 0.851
SEY1
Protein SEY1; Cooperates with the reticulon proteins and tubule-shaping DP1 family proteins to generate and maintain the structure of the tubular endoplasmic reticulum network. Has GTPase activity, which is required for its function in ER organization; Belongs to the TRAFAC class dynamin-like GTPase superfamily. GB1/RHD3-type GTPase family. RHD3 subfamily.
   
   0.677
Q6FY14_CANGA
Uncharacterized protein.
   
 0.677
BOS1
Protein transport protein BOS1; SNARE required for protein transport between the ER and the Golgi complex; Belongs to the BOS1 family.
   
 
 0.623
Q6FW97_CANGA
t-SNARE coiled-coil homology domain-containing protein; Belongs to the syntaxin family.
   
 
 0.604
DSS4
Uncharacterized protein.
      
 0.528
Q6FR72_CANGA
Uncharacterized protein.
   
 
 0.518
Your Current Organism:
Candida glabrata
NCBI taxonomy Id: 284593
Other names: Candida glabrata ATCC 2001, Candida glabrata ATCC2001, Candida glabrata CBS 138, Candida glabrata CBS138, [. glabrata CBS 138, [Candida] glabrata CBS 138
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.