STRINGSTRING
LCB1 protein (Saccharomyces cerevisiae) - STRING interaction network
"LCB1" - Component of serine palmitoyltransferase, responsible along with Lcb2p for the first committed step in sphingolipid synthesis, which is the condensation of serine with palmitoyl-CoA to form 3-ketosphinganine 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
LCB1Component of serine palmitoyltransferase, responsible along with Lcb2p for the first committed step in sphingolipid synthesis, which is the condensation of serine with palmitoyl-CoA to form 3-ketosphinganine; Component of serine palmitoyltransferase (SPT), which catalyzes the committed step in the synthesis of sphingolipids, the condensation of serine with palmitoyl CoA to form the long chain base 3-ketosphinganine (558 aa)    
Predicted Functional Partners:
LCB2
Component of serine palmitoyltransferase, responsible along with Lcb1p for the first committed step in sphingolipid synthesis, which is the condensation of serine with palmitoyl-CoA to form 3-ketosphinganine; Catalytic subunit of serine palmitoyltransferase (SPT), which catalyzes the committed step in the synthesis of sphingolipids, the condensation of serine with palmitoyl CoA to form the long chain base 3-ketosphinganine (561 aa)
   
0.999
TSC3
Protein that stimulates the activity of serine palmitoyltransferase (Lcb1p, Lcb2p) several-fold; involved in sphingolipid biosynthesis; Stimulates the activity of serine palmitoyltransferase (SPT) (80 aa)
       
  0.992
TSC10
3-ketosphinganine reductase, catalyzes the second step in phytosphingosine synthesis, essential for growth in the absence of exogenous dihydrosphingosine or phytosphingosine, member of short chain dehydrogenase/reductase protein family; Catalyzes the reduction of 3-ketodihydrosphingosine (KDS) to dihydrosphingosine (DHS) (320 aa)
   
  0.985
ORM1
Evolutionarily conserved protein, similar to Orm2p, required for resistance to agents that induce unfolded protein response; Orm1p and Orm2p together control membrane biogenesis by coordinating lipid homeostasis with protein quality control; Component of the SPOTS complex that acts as a negative regulator of sphingolipid synthesis. Acts by inhibiting serine palmitoyltransferases (LCB1 and LCB2) activity (222 aa)
     
  0.980
ORM2
Evolutionarily conserved protein, similar to Orm1p, required for resistance to agents that induce unfolded protein response; Orm1p and Orm2p together control membrane biogenesis by coordinating lipid homeostasis with protein quality control; Component of the SPOTS complex that acts as a negative regulator of sphingolipid synthesis. Acts by inhibiting serine palmitoyltransferases (LCB1 and LCB2) activity (216 aa)
     
  0.977
SAC1
Phosphatidylinositol phosphate (PtdInsP) phosphatase involved in hydrolysis of PtdIns[4]P; transmembrane protein localizes to ER and Golgi; involved in protein trafficking and processing, secretion, and cell wall maintenance; Phosphoinositide phosphatase that hydrolyzes PtdIns(3)P and PtdIns(4)P. Has low activity towards PtdIns(3,5)P2. May be involved in the coordination of the activities of the secretory pathway and the actin cytoskeleton (623 aa)
     
  0.955
SCS7
Sphingolipid alpha-hydroxylase, functions in the alpha-hydroxylation of sphingolipid-associated very long chain fatty acids, has both cytochrome b5-like and hydroxylase/desaturase domains, not essential for growth; Ceramide hydroxylase involved in the alpha-hydroxylation of sphingolipid-associated very long chain fatty acids. Hydroxylates the very long chain fatty acid of ceramides at C2 and C3 (384 aa)
       
 
  0.908
SUR2
Sphinganine C4-hydroxylase, catalyses the conversion of sphinganine to phytosphingosine in sphingolipid biosyntheis; Required for hydroxylation of C-4 in the sphingoid moiety of ceramide. Involved in the response to syringomycin (349 aa)
       
 
  0.906
TRP5
Tryptophan synthase, catalyzes the last step of tryptophan biosynthesis; regulated by the general control system of amino acid biosynthesis (707 aa)
   
 
  0.898
ELO3
Elongase, involved in fatty acid and sphingolipid biosynthesis; synthesizes very long chain 20-26-carbon fatty acids from C18-CoA primers; involved in regulation of sphingolipid biosynthesis; Component of a microsomal membrane bound long-chain fatty acid elongation system, which produces the 20-26-carbon very long-chain fatty acids (VLCFA) from long-chain fatty acid precursors and is involved ceramide and inositol sphingolipid biosynthesis. Component of elongase III, which synthesizes 20-26- carbon fatty acids from 18-carbon-fatty acyl-CoA primers such as stearoyl-CoA by incorporation [...] (345 aa)
       
 
  0.881
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 (8%) [HD]