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
LIP2Lipoyl ligase; involved in the modification of mitochondrial enzymes by the attachment of lipoic acid groups; Belongs to the LipB family. (328 aa)    
Predicted Functional Partners:
LIP5
Lipoyl synthase, mitochondrial; Protein involved in biosynthesis of the coenzyme lipoic acid; has similarity to E. coli lipoic acid synthase; Belongs to the radical SAM superfamily. Lipoyl synthase family.
 
 
 0.994
GCV3
H subunit of the mitochondrial glycine decarboxylase complex; glycine decarboxylase is required for the catabolism of glycine to 5,10-methylene-THF; also required for all protein lipoylation; expression is regulated by levels of 5,10-methylene-THF; Belongs to the GcvH family.
   
 0.983
AIM22
Putative lipoate-protein ligase; required along with Lip2 and Lip5 for lipoylation of Lat1p and Kgd2p; similar to E. coli LplA; null mutant displays reduced frequency of mitochondrial genome loss; Belongs to the LplA family.
  
 0.960
ETR1
Enoyl-[acyl-carrier-protein] reductase, mitochondrial; 2-enoyl thioester reductase; member of the medium chain dehydrogenase/reductase family; localized to mitochondria, where it has a probable role in fatty acid synthesis; human MECR functionally complements the respiratory growth defect of the null mutant.
   
 
 0.899
CEM1
3-oxoacyl-[acyl-carrier-protein] synthase homolog; Mitochondrial beta-keto-acyl synthase; possible role in fatty acid synthesis; required for mitochondrial respiration; human homolog OXSM can complement yeast cem1 null mutant; Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family.
   
 0.891
ACP1
Mitochondrial matrix acyl carrier protein; involved in biosynthesis of octanoate, which is a precursor to lipoic acid; activated by phosphopantetheinylation catalyzed by Ppt2p.
  
 0.880
FAS2
3-oxoacyl-[acyl-carrier-protein] reductase; Alpha subunit of fatty acid synthetase; complex catalyzes the synthesis of long-chain saturated fatty acids; contains the acyl-carrier protein domain and beta-ketoacyl reductase, beta-ketoacyl synthase and self-pantetheinylation activities.
   
 0.810
FAS1
3-hydroxyacyl-[acyl-carrier-protein] dehydratase; Beta subunit of fatty acid synthetase; complex catalyzes the synthesis of long-chain saturated fatty acids; contains acetyltransacylase, dehydratase, enoyl reductase, malonyl transacylase, and palmitoyl transacylase activities.
    
 0.803
MEC3
DNA damage and meiotic pachytene checkpoint protein; subunit of a heterotrimeric complex (Rad17p-Mec3p-Ddc1p) that forms a sliding clamp, loaded onto partial duplex DNA by a clamp loader complex; homolog of human and S. pombe Hus1.
   
   0.704
HTD2
Mitochondrial 3-hydroxyacyl-thioester dehydratase; involved in fatty acid biosynthesis, required for respiratory growth and for normal mitochondrial morphology.
   
  
 0.674
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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