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
BN2166_0013540BY PROTMAP: gi|342321418|gb|EGU13352.1| Pyruvate carboxylase [Rhodotorula glutinis ATCC 204091]. (310 aa)    
Predicted Functional Partners:
BN2166_0058500
annotation not available
    
 0.584
BN2166_0024420
FGENESH: predicted gene_4.218 protein.
   
 
 0.553
BN2166_0052610
annotation not available
    
 
 0.546
BN2166_0020380
annotation not available
    
 
 0.500
BN2166_0048090
Mitochondrial distribution and morphology protein 10; Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. MDM10 is involved in the late assembly steps of the general translocase of the mitochondrial outer membrane (TOM complex). Functions in the TOM40-specific route of the assembly of outer membrane beta-barrel proteins, including the association of TOM40 with the recepto [...]
      
 0.453
MDM34
Mitochondrial distribution and morphology protein 34; Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. MDM34 is required for the interaction of the ER-resident membrane protein MMM1 and the outer mitochondrial membrane-resident beta-barrel protein MDM10.
    
 
 0.441
BN2166_0016000
Mitochondrial distribution and morphology protein 12; Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. MDM12 is required for the interaction of the ER-resident membrane protein MMM1 and the outer mitochondrial membrane-resident beta-barrel protein MDM10. The MDM12-MMM1 subcomplex functions in the major beta-barrel assembly pat [...]
      
 0.440
BN2166_0031420
DNA_MISMATCH_REPAIR_2 domain-containing protein.
    
 
 0.434
BN2166_0030050
Pterin-binding domain-containing protein.
      
 0.433
MMM1
Maintenance of mitochondrial morphology protein 1; Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. The MDM12-MMM1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all outer membrane beta- barrel proteins, and acts in a late step after the SAM complex. The MDM10-MDM12-MMM1 su [...]
    
 
 0.425
Your Current Organism:
Rhodotorula toruloides
NCBI taxonomy Id: 5286
Other names: CBS 6016, IFO 8766, IGC 5615, MUCL 28631, NRRL Y-6987, R. toruloides, Rhodosporidium toruloides, Rhodotorula gracilis, Rhodotorula rubescens, Rhodotorula toruloides (I. Banno) Q.M. Wang, F.Y. Bai, M. Groenew. & Boekhout, 2015
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