STRINGSTRING
SEC12 SEC12 CNE1 CNE1 SHR3 SHR3 VMA3 VMA3 ANP1 ANP1 VMA16 VMA16 VMA22 VMA22 KAR2 KAR2 VMA6 VMA6 PRC1 PRC1 VPH1 VPH1 VMA11 VMA11 VMA13 VMA13
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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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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
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SEC12Guanine nucleotide exchange factor (GEF); activates Sar1p by catalyzing the exchange of GDP for GTP; required for the initiation of COPII vesicle formation in ER to Golgi transport; glycosylated integral membrane protein of the ER; SEC12 has a paralog, SED4, that arose from the whole genome duplication; Belongs to the WD repeat SEC12 family. (471 aa)
CNE1Calnexin; integral membrane ER chaperone involved in folding and quality control of glycoproteins; chaperone activity is inhibited by Mpd1p, with which Cne1p interacts; 24% identical to mammalian calnexin; Ca+ binding not yet shown in yeast. (502 aa)
SHR3Secretory component protein SHR3; Endoplasmic reticulum packaging chaperone; required for incorporation of amino acid permeases into COPII coated vesicles for transport to the cell surface. (210 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)
ANP1Subunit of the alpha-1,6 mannosyltransferase complex; type II membrane protein; has a role in retention of glycosyltransferases in the Golgi; involved in osmotic sensitivity and resistance to aminonitrophenyl propanediol. (500 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)
VMA22Protein that is required for vacuolar H+-ATPase (V-ATPase) function; peripheral membrane protein; not an actual component of the V-ATPase complex; functions in the assembly of the V-ATPase; localized to the yeast endoplasmic reticulum (ER). (181 aa)
KAR2Endoplasmic reticulum chaperone BiP; ATPase involved in protein import into the ER; also acts as a chaperone to mediate protein folding in the ER and may play a role in ER export of soluble proteins; regulates the unfolded protein response via interaction with Ire1p. (682 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)
PRC1Vacuolar carboxypeptidase Y (proteinase C, CPY); broad-specificity C-terminal exopeptidase involved in non-specific protein degradation in the vacuole; member of the serine carboxypeptidase family. (532 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)
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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