• Version:
  • 11.0 [archived version]
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OSGEP OSGEP STAT6 STAT6 MAT2B MAT2B TSTA3 TSTA3 SLC35C1 SLC35C1 GALE GALE FUK FUK GMDS GMDS GMPPB GMPPB FPGT FPGT MPI MPI
"TSTA3" - GDP-L-fucose synthase in Homo sapiens
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query proteins and first shell of interactors
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second shell of interactors
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filled nodes:
some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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TSTA3GDP-L-fucose synthase; Catalyzes the two-step NADP-dependent conversion of GDP- 4-dehydro-6-deoxy-D-mannose to GDP-fucose, involving an epimerase and a reductase reaction; Short chain dehydrogenase/reductase superfamily (321 aa)    
Predicted Functional Partners:
GMDS
GDP-mannose 4,6 dehydratase; Catalyzes the conversion of GDP-D-mannose to GDP-4- dehydro-6-deoxy-D-mannose; Belongs to the NAD(P)-dependent epimerase/dehydratase family. GDP-mannose 4,6-dehydratase subfamily (372 aa)
  0.999
FPGT
Fucose-1-phosphate guanylyltransferase; Catalyzes the formation of GDP-L-fucose from GTP and L- fucose-1-phosphate. Functions as a salvage pathway to reutilize L- fucose arising from the turnover of glycoproteins and glycolipids (607 aa)
         
  0.979
FUK
L-fucose kinase; Takes part in the salvage pathway for reutilization of fucose from the degradation of oligosaccharides (1084 aa)
   
   
  0.874
MAT2B
Methionine adenosyltransferase 2 subunit beta; Regulatory subunit of S-adenosylmethionine synthetase 2, an enzyme that catalyzes the formation of S-adenosylmethionine from methionine and ATP. Regulates MAT2A catalytic activity by changing its kinetic properties, increasing its affinity for L- methionine. Can bind NADP (in vitro); Short chain dehydrogenase/reductase superfamily (334 aa)
     
 
  0.869
STAT6
Signal transducer and activator of transcription 6; Carries out a dual function- signal transduction and activation of transcription. Involved in IL4/interleukin-4- and IL3/interleukin-3-mediated signaling; SH2 domain containing (847 aa)
       
      0.850
GALE
UDP-glucose 4-epimerase; Catalyzes two distinct but analogous reactions- the reversible epimerization of UDP-glucose to UDP-galactose and the reversible epimerization of UDP-N-acetylglucosamine to UDP-N- acetylgalactosamine. The reaction with UDP-Gal plays a critical role in the Leloir pathway of galactose catabolism in which galactose is converted to the glycolytic intermediate glucose 6- phosphate. It contributes to the catabolism of dietary galactose and enables the endogenous biosynthesis of both UDP-Gal and UDP- GalNAc when exogenous sources are limited. Both UDP-sugar interconver [...] (348 aa)
   
 
  0.794
GMPPB
Mannose-1-phosphate guanyltransferase beta; Catalyzes the formation of GDP-mannose, an essential precursor of glycan moieties of glycoproteins and glycolipids; Belongs to the transferase hexapeptide repeat family (387 aa)
   
   
  0.720
SLC35C1
GDP-fucose transporter 1; Involved in GDP-fucose import from the cytoplasm into the Golgi lumen; Belongs to the TPT transporter family. SLC35C subfamily (364 aa)
     
   
  0.700
MPI
Mannose-6-phosphate isomerase; Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions; Belongs to the mannose-6-phosphate isomerase type 1 family (423 aa)
   
   
  0.696
OSGEP
Probable tRNA N6-adenosine threonylcarbamoyltransferase; Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. OSGEP likely plays a direct catalytic role in this reaction, but requires other protein(s) of the complex to fulfill this activity; Belongs to the KAE1 / TsaD family (335 aa)
   
   
  0.633
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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