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CUP1-1 CUP1-1 SEC17 SEC17 IPP1 IPP1 SEC18 SEC18 PHO8 PHO8 VMA3 VMA3 VMA16 VMA16 CUP1-2 CUP1-2 NYV1 NYV1 VMA6 VMA6 YPT7 YPT7 PPA2 PPA2 VAM3 VAM3 VPH1 VPH1 VMA11 VMA11
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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.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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CUP1-1Metallothionein; binds copper and mediates resistance to high concentrations of copper and cadmium; locus is variably amplified in different strains, with two copies, CUP1-1 and CUP1-2, in the genomic sequence reference strain S288C; CUP1-1 has a paralog, CUP1-2, that arose from a segmental duplication. (61 aa)
SEC17Alpha-soluble NSF attachment protein; Alpha-SNAP cochaperone; SNARE-complex adaptor for Sec18 (NSF) during the disassembly of postfusion cis-SNARE complexes; stimulates the ATPase activity of Sec18p; peripheral membrane protein required for vesicular transport between ER and Golgi, the 'priming' step in homotypic vacuole fusion, and autophagy; similar to mammalian alpha-SNAP. (292 aa)
IPP1Cytoplasmic inorganic pyrophosphatase (PPase); homodimer that catalyzes the rapid exchange of oxygens from Pi with water, highly expressed and essential for viability, active-site residues show identity to those from E. coli PPase. (287 aa)
SEC18Vesicular-fusion protein SEC18; AAA ATPase and SNARE disassembly chaperone; required for vesicular transport between ER and Golgi, the 'priming' step in homotypic vacuole fusion, autophagy, and protein secretion; releases Sec17p from SNAP complexes; has similarity to mammalian N-ethylmaleimide-sensitive factor (NSF). (758 aa)
PHO8Repressible vacuolar alkaline phosphatase; regulated by levels of Pi and by Pho4p, Pho9p, Pho80p, Pho81p and Pho85p; dephosphorylates phosphotyrosyl peptides; contributes to NAD+ metabolism by producing nicotinamide riboside from NMN. (566 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)
VMA16Subunit c'' of the vacuolar ATPase; v-ATPase functions in acidification of the vacuole; one of three proteolipid subunits of the V0 domain. (213 aa)
CUP1-2Metallothionein; binds copper and mediates resistance to high concentrations of copper and cadmium; locus is variably amplified in different strains, with two copies, CUP1-1 and CUP1-2, in the genomic sequence reference strain S288C; CUP1-2 has a paralog, CUP1-1, that arose from a segmental duplication. (61 aa)
NYV1v-SNARE component of the vacuolar SNARE complex; involved in vesicle fusion; inhibits ATP-dependent Ca(2+) transport activity of Pmc1p in the vacuolar membrane. (253 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)
YPT7Rab family GTPase; GTP-binding protein of the rab family; required for homotypic fusion event in vacuole inheritance, for endosome-endosome fusion; localizes to sites of contact between the vacuole and mitochondria (vCLAMPs); interacts with the cargo selection/retromer complex for retrograde sorting; similar to mammalian Rab7. (208 aa)
PPA2Mitochondrial inorganic pyrophosphatase; required for mitochondrial function and possibly involved in energy generation from inorganic pyrophosphate; human ortholog, PPA2, functionally complements the null mutant; mutations in human PPA2 cause a mitochondrial disease resulting in sudden unexpected cardiac arrest in infants; Belongs to the PPase family. (310 aa)
VAM3Syntaxin-like vacuolar t-SNARE; functions with Vam7p in vacuolar protein trafficking; mediates docking/fusion of late transport intermediates with the vacuole; has an acidic di-leucine sorting signal and C-terminal transmembrane region. (283 aa)
VPH1Subunit 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. (840 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)
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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