STRINGSTRING
A0A0E0MZ49 A0A0E0MZ49 atpH atpH A0A0E0RG28 A0A0E0RG28 A0A0E0REB6 A0A0E0REB6 A0A0E0R4Q6 A0A0E0R4Q6 A0A0E0PGF5 A0A0E0PGF5 A0A0E0P6A1 A0A0E0P6A1 A0A0E0NG88 A0A0E0NG88 A0A0E0N7Y1 A0A0E0N7Y1
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:
A0A0E0MZ49Uncharacterized protein; Belongs to the V-ATPase proteolipid subunit family. (176 aa)
atpHATP synthase subunit c, chloroplastic; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. (81 aa)
A0A0E0RG28ATP-synt_C domain-containing protein; Belongs to the ATPase C chain family. (74 aa)
A0A0E0REB6V-type proton ATPase proteolipid subunit; Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. (165 aa)
A0A0E0R4Q6V-type proton ATPase proteolipid subunit; Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. (165 aa)
A0A0E0PGF5V-type proton ATPase proteolipid subunit; Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. (166 aa)
A0A0E0P6A1Uncharacterized protein. (359 aa)
A0A0E0NG88V-type proton ATPase proteolipid subunit; Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. (167 aa)
A0A0E0N7Y1V-type proton ATPase proteolipid subunit; Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. (165 aa)
Your Current Organism:
Oryza rufipogon
NCBI taxonomy Id: 4529
Other names: O. rufipogon, Oryza rufipogon Griff., common wild rice, red rice
Server load: low (24%) [HD]