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SIP3 SIP3 LAM6 LAM6 IRA1 IRA1 TPI1 TPI1 YSP2 YSP2 CRH1 CRH1 LAM5 LAM5 LAM4 LAM4
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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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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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SIP3Membrane-anchored lipid-binding protein SIP3; Putative sterol transfer protein; has a probable role in retrograde transport of sterols from the plasma membrane to the ER; co-localizes to puncta in the cortical ER with Ysp2p; contains GRAM, StART-like (VASt) and two PH-like domains; one of 6 StART-like domain-containing proteins in yeast that may be involved in sterol transfer between intracellular membranes; conserved across eukaryotes; previously identified as a transcription cofactor that interacts with DNA-bound Snf1p. (1229 aa)
LAM6Membrane-anchored lipid-binding protein LAM6; Sterol transporter that transfers sterols between membranes; may regulate and coordinate formation of contact sites between organelles; localizes to ER-mitochondrial contact sites in a Tom70p- and Tom71p-dependent manner; mitochondrial localization requires GRAM domain; also localizes to ER-vacuole contact sites, in a Vac8p-dependent manner; has GRAM and StART-like (VASt) domains; one of six StART-like domain-containing proteins in yeast; conserved across eukaryotes; Belongs to the YSP2 family. (693 aa)
IRA1Inhibitory regulator protein IRA1; GTPase-activating protein; negatively regulates RAS by converting it from GTP- to the GDP-bound inactive form, required for reducing cAMP levels under nutrient limiting conditions, mediates membrane association of adenylate cyclase; mutations cause catalase T deficiency, defective glycogen synthesis and defective trehalose accumulation; IRA1 has a paralog, IRA2, that arose from the whole genome duplication; defects in human homolog NF1 are associated with neurofibromatosis. (3092 aa)
TPI1Triose phosphate isomerase, abundant glycolytic enzyme; mRNA half-life is regulated by iron availability; transcription is controlled by activators Reb1p, Gcr1p, and Rap1p through binding sites in the 5' non-coding region; inhibition of Tpi1p activity by PEP (phosphoenolpyruvate) stimulates redox metabolism in respiring cells; E104D mutation in human homolog TPI1 causes a rare autosomal disease; human TPI1 can complement yeast null mutant. (248 aa)
YSP2Membrane-anchored lipid-binding protein YSP2; Sterol-binding protein; has a probable role in retrograde transport of sterols from the plasma membrane to the ER; contains two StART-like domains that bind sterols and a GRAM domain; co-localizes to puncta in the cortical ER with Sip3p; one of six StART-like domain-containing proteins in yeast that may be involved in sterol transfer between intracellular membranes; conserved across eukaryotes. (1438 aa)
CRH1Probable glycosidase CRH1; Chitin transglycosylase; functions in the transfer of chitin to beta(1-6) and beta(1-3) glucans in the cell wall; similar and functionally redundant to Utr2; localizes to sites of polarized growth; expression induced by cell wall stress. (507 aa)
LAM5Membrane-anchored lipid-binding protein LAM5; Putative sterol transfer protein; one of six StART-like domain-containing proteins in yeast that may be involved in sterol transfer between intracellular membranes; conserved across eukaryotes; has both GRAM and StART-like (VASt) domains; localizes to membrane contact sites throughout the cell, including nucleus-vacuole junctions and ER-mitochondrial contact sites. (674 aa)
LAM4Membrane-anchored lipid-binding protein LAM4; Sterol-binding protein that localizes to puncta in the cortical ER; sterol binding occurs via two StART-like domains; one of six StART-like domain-containing proteins in yeast that may be involved in intracellular sterol transfer between membranes; conserved across eukaryotes; has both GRAM and StART-like (VASt) domains; the authentic, non-tagged protein is detected in highly purified mitochondria in high-throughput studies. (1345 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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