STRINGSTRING
USP USP PPA5 PPA5 PPA3 PPA3 PPA2 PPA2 PPA1 PPA1 GLCAK1 GLCAK1 GLYK GLYK PPA4 PPA4 PPA6 PPA6 GLCAK2 GLCAK2 GAL1 GAL1
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:
USPUDP-sugar pyrophosphorylase; Required for the synthesis of the intine, the pectocellulosic inner wall of developing pollen. May function as the terminal enzyme of the myo-inositol oxidation (MIO) pathway. May also play a role in the salvage pathway for synthesis of nucleotide sugars. Can use a wide range of substrates including glucose-1-phosphate, galactose-1-phosphate, xylose-1- phosphate, arabinose-1-phosphate and glucuronate-1-phosphate. (614 aa)
PPA5Soluble inorganic pyrophosphatase 5. (216 aa)
PPA3Soluble inorganic pyrophosphatase 3; Belongs to the PPase family. (216 aa)
PPA2Soluble inorganic pyrophosphatase 2. (218 aa)
PPA1Soluble inorganic pyrophosphatase 1; Catalyzes the irreversible hydrolysis of pyrophosphate (PPi) to phosphate. The MgPPi(2-) complex binds to the enzyme only after a free Mg(2+) ion has bound. No activity with glycerol-3- phosphate, glucose-6-phosphate, p-nitrophenylphosphate, ADP, NADP(+), NAD(+),NADH, NADPH or phosphoribosyl pyrophosphate as substrates. Controls the equilibrium of gluconeogenic reactions in the heterotrophic growth phase of early seedling establishment. Determinates the rate of cytosolic glycolysis, providing carbon for seed storage lipid accumulation. (212 aa)
GLCAK1Glucuronokinase 1; Sugar-1-kinase with a strict substrate specificity for D- glucuronic acid and ATP. Involved in the biosynthesis of UDP-glucuronic acid (UDP-GlcA), providing nucleotide sugars for cell-wall polymers. May be also involved in a salvage pathway for glucuronic acid. (362 aa)
GLYKD-glycerate 3-kinase, chloroplastic; Catalyzes the concluding reaction of the photorespiratory C2 cycle, an indispensable ancillary metabolic pathway to the photosynthetic C3 cycle that enables land plants to grow in an oxygen- containing atmosphere; Belongs to the GLYK kinase family. (456 aa)
PPA4Soluble inorganic pyrophosphatase 4; Catalyzes the irreversible hydrolysis of pyrophosphate (PPi) to phosphate. The MgPPi(2-) complex binds to the enzyme only after a free Mg(2+) ion has bound. No activity with glycerol-3-phosphate, glucose-6-phosphate, p-nitrophenylphosphate, ADP, NADP(+), NAD(+),NADH, NADPH or phosphoribosyl pyrophosphate as substrates. (216 aa)
PPA6Soluble inorganic pyrophosphatase 6, chloroplastic; Belongs to the PPase family. (300 aa)
GLCAK2Probable glucuronokinase 2; Sugar-1-kinase with a strict substrate specificity for D- glucuronic acid and ATP. Involved in the biosynthesis of UDP-glucuronic acid (UDP-GlcA), providing nucleotide sugars for cell-wall polymers. May be also involved in a salvage pathway for glucuronic acid (By similarity). (366 aa)
GAL1Galactokinase; Sugar-1-kinase with a very high substrate specificity for the alpha-anomeric configuration of D-galacose (D-Gal). Converts also efficiently 2-deoxy-D-Gal to 2-deoxy-D-al-1-phosphate. Belongs to the GHMP kinase family. GalK subfamily. (496 aa)
Your Current Organism:
Arabidopsis thaliana
NCBI taxonomy Id: 3702
Other names: A. thaliana, Arabidopsis thaliana (L.) Heynh., mouse-ear cress, thale cress, thale-cress
Server load: low (18%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.