STRINGSTRING
LEM3 protein (Saccharomyces cerevisiae) - STRING interaction network
"LEM3" - Membrane protein of the plasma membrane and ER, interacts specifically in vivo with the phospholipid translocase in Saccharomyces cerevisiae
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:
some 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 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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
LEM3Membrane protein of the plasma membrane and ER, interacts specifically in vivo with the phospholipid translocase (flippase) Dnf1p; involved in translocation of phospholipids and alkylphosphocholine drugs across the plasma membrane; Involved in the asymmetrical organization of phosphatidylethanolamine in the plasma membrane (414 aa)    
Predicted Functional Partners:
DNF1
Aminophospholipid translocase (flippase) that localizes primarily to the plasma membrane; contributes to endocytosis, protein transport and cell polarity; type 4 P-type ATPase; This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of phospholipids (1571 aa)
     
  0.995
DNF2
Aminophospholipid translocase (flippase) that localizes primarily to the plasma membrane; contributes to endocytosis, protein transport and cell polarity; type 4 P-type ATPase; This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of phospholipids. Required for protein transport from Golgi to vacuoles (1612 aa)
     
 
  0.991
DNF3
Aminophospholipid translocase (flippase) that maintains membrane lipid asymmetry in post-Golgi secretory vesicles; localizes to the trans-Golgi network; likely involved in protein transport; type 4 P-type ATPase; This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of phospholipids (1656 aa)
     
 
  0.936
DRS2
Aminophospholipid translocase (flippase) that maintains membrane lipid asymmetry in post-Golgi secretory vesicles; contributes to clathrin-coated vesicle formation and endocytosis; mutations in human homolog ATP8B1 result in liver disease; This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of phospholipids (Potential). Seems to be involved in ribosome assembly (1355 aa)
     
 
  0.923
NEO1
Putative aminophospholipid translocase (flippase) involved in endocytosis and vacuolar biogenesis; localizes to endosomes and the Golgi aparatus; This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of phospholipids (Potential). Leads to neomycin-resistance when overexpressed. Required for traffic between late Golgi and early endosomes (1151 aa)
     
 
  0.869
NBP35
Essential cytoplasmic iron-sulfur cluster binding protein; forms a complex with Cfd1p that is involved in iron-sulfur protein assembly in the cytosol; similar to P-loop NTPases; Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The NBP35-CFD1 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins. Required for biogenesis and export of both ribosomal subunits, which may reflect a role in assembly of the Fe/S clusters i [...] (328 aa)
         
  0.729
CFD1
Highly conserved iron-sulfur cluster binding protein; localized in the cytoplasm; forms a complex with Nbp35p that is involved in iron-sulfur protein assembly in the cytosol; Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The NBP35-CFD1 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins. Nucleotide binding/hydrolysis seems to be critcal for loading of Fe-S clusters onto CFD1 and NBP35. Required for biogenesis a [...] (293 aa)
         
    0.720
PMT1
Protein O-mannosyltransferase, transfers mannose from dolichyl phosphate-D-mannose to protein Ser/Thr residues; 1 of 7 related proteins involved in O-glycosylation which is essential for cell wall rigidity; involved in ER quality control; Protein O-mannosyltransferase involved in O- glycosylation which is essential for cell wall rigidity. Forms a heterodimeric complex with PMT2 and more rarely with PMT3 to transfer mannose from Dol-P-mannose to Ser or Thr residues on proteins. The PMT1-PMT2 complex participates to oxidative protein folding, ER-associated protein degradation (ERAD), as [...] (817 aa)
       
      0.683
CDC50
Endosomal protein that interacts with phospholipid flippase Drs2p; interaction with Cdc50p is essential for Drs2p catalytic activity; mutations affect cell polarity and polarized growth; similar to Ynr048wp and Lem3p; Required for polarized cell growth (391 aa)
       
 
0.679
UBC7
Ubiquitin conjugating enzyme, involved in the ER-associated protein degradation pathway; requires Cue1p for recruitment to the ER membrane; proposed to be involved in chromatin assembly; Catalyzes the covalent attachment of ubiquitin to other proteins. Functions in degradation of misfolded or regulated proteins localized in the endoplasmic reticulum (ER) lumen or membrane via the ubiquitin-proteasome system. Cognate E2 conjugating enzyme for the DOA10 ubiquitin ligase complex, which is part of the ERAD-C pathway responsible for the rapid degradation of membrane proteins with misfolded [...] (165 aa)
       
 
  0.676
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: Candida robusta, Pachytichospora, S. cerevisiae, Saccharomyces, Saccharomyces capensis, Saccharomyces cerevisiae, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, lager beer yeast, yeast
Server load: low (7%) [HD]