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VMA2 VMA2 CRD1 CRD1 VMA1 VMA1 VMA3 VMA3 VMA5 VMA5 VPH2 VPH2 VMA6 VMA6 VMA11 VMA11 VMA13 VMA13
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second shell of interactors
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VMA2V-type proton ATPase subunit B; Subunit B of V1 peripheral membrane domain of vacuolar H+-ATPase; electrogenic proton pump found throughout the endomembrane system; contains nucleotide binding sites; also detected in the cytoplasm; protein abundance increases in response to DNA replication stress; human homolog ATP6V1B1, implicated in autosomal-recessive distal renal tubular acidosis (RTA) with sensorineural deafness, complements yeast null mutant; Belongs to the ATPase alpha/beta chains family. (517 aa)
CRD1Cardiolipin synthase; produces cardiolipin, which is a phospholipid of the mitochondrial inner membrane that is required for normal mitochondrial membrane potential and function and for correct integration of membrane-multispanning proteins into the mitochondrial outer membrane; required to maintain tubular mitochondrial morphology and functions in mitochondrial fusion; also required for normal vacuolar ion homeostasis; Belongs to the CDP-alcohol phosphatidyltransferase class-I family. (283 aa)
VMA1Subunit A of the V1 peripheral membrane domain of V-ATPase; protein precursor undergoes self-catalyzed splicing to yield the extein Tfp1p and the intein Vde (PI-SceI), which is a site-specific endonuclease; the V1 peripheral membrane domain of the vacuolar H+-ATPase (V-ATPase) has eight subunits; involved in methionine restriction extension of chronological lifespan in an autophagy-dependent manner; Belongs to the ATPase alpha/beta chains family. (1071 aa)
VMA3V-type proton ATPase subunit c; Proteolipid subunit c of the V0 domain of vacuolar H(+)-ATPase; dicyclohexylcarbodiimide binding subunit; required for vacuolar acidification and important for copper and iron metal ion homeostasis; Belongs to the V-ATPase proteolipid subunit family. (160 aa)
VMA5Subunit 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. (392 aa)
VPH2Integral membrane protein required for V-ATPase function; not an actual component of the vacuolar H+-ATPase (V-ATPase) complex; functions in the assembly of the V-ATPase; localized to the endoplasmic reticulum (ER); involved in methionine restriction extension of chronological lifespan in an autophagy-dependent manner. (215 aa)
VMA6Subunit 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. (345 aa)
VMA11Vacuolar 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. (164 aa)
VMA13Subunit 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. (478 aa)
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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