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.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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.
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experimentally determined
co-expression
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gene neighborhood
gene co-occurrence
gene fusions
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VOA1ER protein that functions in assembly of the V0 sector of V-ATPase; functions with other assembly factors; null mutation enhances the vacuolar ATPase (V-ATPase) deficiency of a vma21 mutant impaired in endoplasmic reticulum (ER) retrieval; Belongs to the VOA1 family. (265 aa)    
Predicted Functional Partners:
VPH1
Subunit a of vacuolar-ATPase V0 domain; one of two isoforms (Vph1p and Stv1p); Vph1p is located in V-ATPase complexes of the vacuole while Stv1p is located in V-ATPase complexes of the Golgi and endosomes; relative distribution to the vacuolar membrane decreases upon DNA replication stress; human homolog ATP6V0A4 implicated in renal tubular acidosis, can complement yeast null mutant.
   
 0.999
VMA13
Subunit H of the V1 peripheral membrane domain of V-ATPase; part of the electrogenic proton pump found throughout the endomembrane system; serves as an activator or a structural stabilizer of the V-ATPase; the V1 peripheral membrane domain of the vacuolar H+-ATPase (V-ATPase) has eight subunits.
   
 0.998
VMA6
Subunit d of the V0 integral membrane domain of V-ATPase; part of the electrogenic proton pump found in the endomembrane system; required for V1 domain assembly on the vacuolar membrane; the V0 integral membrane domain of vacuolar H+-ATPase (V-ATPase) has five subunits.
   
 0.995
VMA16
Subunit c'' of the vacuolar ATPase; v-ATPase functions in acidification of the vacuole; one of three proteolipid subunits of the V0 domain.
   
 0.994
VMA9
Vacuolar H+ ATPase subunit e of the V-ATPase V0 subcomplex; essential for vacuolar acidification; interacts with the V-ATPase assembly factor Vma21p in the ER; involved in V0 biogenesis.
    
 0.990
VMA11
Vacuolar ATPase V0 domain subunit c'; involved in proton transport activity; hydrophobic integral membrane protein (proteolipid) containing four transmembrane segments; N and C termini are in the vacuolar lumen.
   
 0.990
YPR170W-B
Uncharacterized protein YPR170W-B; Putative protein of unknown function; conserved in fungi; SWAT-GFP fusion protein localizes to the vacuole membrane; partially overlaps the dubious genes YPR169W-A, YPR170W-A and YRP170C.
   
 0.990
VMA21
Integral membrane protein required for V-ATPase function; not an actual component of the vacuolar H+-ATPase (V-ATPase) complex; diverged ortholog of human XMEA (X-linked Myopathy with Excessive Autophagy); functions in the assembly of the V-ATPase; localized to the yeast endoplasmic reticulum (ER).
   
   0.989
VMA5
Subunit C of the V1 peripheral membrane domain of V-ATPase; part of the electrogenic proton pump found throughout the endomembrane system; required for the V1 domain to assemble onto the vacuolar membrane; the V1 peripheral membrane domain of vacuolar H+-ATPase (V-ATPase) has eight subunits.
   
 0.989
STV1
V-type proton ATPase subunit a, Golgi isoform; Subunit a of the vacuolar-ATPase V0 domain; one of two isoforms (Stv1p and Vph1p); Stv1p is located in V-ATPase complexes of the Golgi and endosomes while Vph1p is located in V-ATPase complexes of the vacuole; Belongs to the V-ATPase 116 kDa subunit family.
   
 0.987
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: ATCC 18824, Candida robusta, Mycoderma cerevisiae, NRRL Y-12632, S. cerevisiae, Saccharomyces capensis, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, yeast
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