#ID(s) interactor A	ID(s) interactor B	Alt. ID(s) interactor A	Alt. ID(s) interactor B	Alias(es) interactor A	Alias(es) interactor B	Interaction detection method(s)	Publication 1st author(s)	Publication Identifier(s)	Taxid interactor A	Taxid interactor B	Interaction type(s)	Source database(s)	Interaction identifier(s)	Confidence value(s)	Expansion method(s)	Biological role(s) interactor A	Biological role(s) interactor B	Experimental role(s) interactor A	Experimental role(s) interactor B	Type(s) interactor A	Type(s) interactor B	Xref(s) interactor A	Xref(s) interactor B	Interaction Xref(s)	Annotation(s) interactor A	Annotation(s) interactor B	Interaction annotation(s)	Host organism(s)	Interaction parameter(s)	Creation date	Update date	Checksum(s) interactor A	Checksum(s) interactor B	Interaction Checksum(s)	Negative	Feature(s) interactor A	Feature(s) interactor B	Stoichiometry(s) interactor A	Stoichiometry(s) interactor B	Identification method participant A	Identification method participant B
uniprotkb:P11413	uniprotkb:P11413	intact:EBI-4289891|uniprotkb:Q8IU88|uniprotkb:D3DWX9|uniprotkb:Q16000|uniprotkb:Q16765|uniprotkb:Q8IUA6|uniprotkb:Q8IU70|uniprotkb:Q96PQ2|ensembl:ENSP00000377192|ensembl:ENSP00000377194	intact:EBI-4289891|uniprotkb:Q8IU88|uniprotkb:D3DWX9|uniprotkb:Q16000|uniprotkb:Q16765|uniprotkb:Q8IUA6|uniprotkb:Q8IU70|uniprotkb:Q96PQ2|ensembl:ENSP00000377192|ensembl:ENSP00000377194	psi-mi:g6pd_human(display_long)|uniprotkb:G6PD(gene name)|psi-mi:G6PD(display_short)	psi-mi:g6pd_human(display_long)|uniprotkb:G6PD(gene name)|psi-mi:G6PD(display_short)	psi-mi:"MI:0007"(anti tag coimmunoprecipitation)	Wang et al. (2014)	imex:IM-23514|pubmed:24769394	taxid:9606(human)|taxid:9606(Homo sapiens)	taxid:9606(human)|taxid:9606(Homo sapiens)	psi-mi:"MI:0915"(physical association)	psi-mi:"MI:0471"(MINT)	intact:EBI-9830927|imex:IM-23514-1	-	-	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0498"(prey)	psi-mi:"MI:0496"(bait)	psi-mi:"MI:0326"(protein)	psi-mi:"MI:0326"(protein)	refseq:NP_000393.4|refseq:NP_001035810.1|ensembl:ENSG00000160211(gene)|ensembl:ENST00000393562(transcript)|ensembl:ENST00000393564(transcript)|go:"GO:0004345"(glucose-6-phosphate dehydrogenase activity)|go:"GO:0005536"(glucose binding)|go:"GO:0005634"(nucleus)|go:"GO:0005737"(cytoplasm)|go:"GO:0005829"(cytosol)|go:"GO:0006006"(glucose metabolic process)|go:"GO:0006098"(pentose-phosphate shunt)|go:"GO:0006629"(lipid metabolic process)|go:"GO:0006695"(cholesterol biosynthetic process)|go:"GO:0006739"(NADP metabolic process)|go:"GO:0006740"(NADPH regeneration)|go:"GO:0006749"(glutathione metabolic process)|go:"GO:0009051"(pentose-phosphate shunt, oxidative branch)|go:"GO:0009898"(cytoplasmic side of plasma membrane)|go:"GO:0010041"("response to iron(III) ion")|go:"GO:0010734"(negative regulation of protein glutathionylation)|go:"GO:0014070"(response to organic cyclic compound)|go:"GO:0016020"(membrane)|go:"GO:0019322"(pentose biosynthetic process)|go:"GO:0021762"(substantia nigra development)|go:"GO:0032094"(response to food)|go:"GO:0034451"(centriolar satellite)|go:"GO:0034599"(cellular response to oxidative stress)|go:"GO:0042802"(identical protein binding)|go:"GO:0042803"(protein homodimerization activity)|go:"GO:0043231"(intracellular membrane-bounded organelle)|go:"GO:0043249"(erythrocyte maturation)|go:"GO:0043523"(regulation of neuron apoptotic process)|go:"GO:0045471"(response to ethanol)|go:"GO:0046390"(ribose phosphate biosynthetic process)|go:"GO:0050661"(NADP binding)|go:"GO:0051156"(glucose 6-phosphate metabolic process)|go:"GO:0061052"(negative regulation of cell growth involved in cardiac muscle cell development)|go:"GO:0070062"(extracellular exosome)|go:"GO:1904879"(positive regulation of calcium ion transmembrane transport via high voltage-gated calcium channel)|go:"GO:2000378"(negative regulation of reactive oxygen species metabolic process)|interpro:IPR001282(Glucose-6-phosphate dehydrogenase)|interpro:IPR019796|interpro:IPR022674|interpro:IPR022675|interpro:IPR036291|rcsb pdb:1QKI|rcsb pdb:2BH9|rcsb pdb:2BHL|rcsb pdb:5UKW|rcsb pdb:6E07|rcsb pdb:6E08|rcsb pdb:6JYU|rcsb pdb:6VA0|rcsb pdb:6VA7|rcsb pdb:6VA8|rcsb pdb:6VA9|rcsb pdb:6VAQ|reactome:R-HSA-5628897|reactome:R-HSA-71336	refseq:NP_000393.4|refseq:NP_001035810.1|ensembl:ENSG00000160211(gene)|ensembl:ENST00000393562(transcript)|ensembl:ENST00000393564(transcript)|go:"GO:0004345"(glucose-6-phosphate dehydrogenase activity)|go:"GO:0005536"(glucose binding)|go:"GO:0005634"(nucleus)|go:"GO:0005737"(cytoplasm)|go:"GO:0005829"(cytosol)|go:"GO:0006006"(glucose metabolic process)|go:"GO:0006098"(pentose-phosphate shunt)|go:"GO:0006629"(lipid metabolic process)|go:"GO:0006695"(cholesterol biosynthetic process)|go:"GO:0006739"(NADP metabolic process)|go:"GO:0006740"(NADPH regeneration)|go:"GO:0006749"(glutathione metabolic process)|go:"GO:0009051"(pentose-phosphate shunt, oxidative branch)|go:"GO:0009898"(cytoplasmic side of plasma membrane)|go:"GO:0010041"("response to iron(III) ion")|go:"GO:0010734"(negative regulation of protein glutathionylation)|go:"GO:0014070"(response to organic cyclic compound)|go:"GO:0016020"(membrane)|go:"GO:0019322"(pentose biosynthetic process)|go:"GO:0021762"(substantia nigra development)|go:"GO:0032094"(response to food)|go:"GO:0034451"(centriolar satellite)|go:"GO:0034599"(cellular response to oxidative stress)|go:"GO:0042802"(identical protein binding)|go:"GO:0042803"(protein homodimerization activity)|go:"GO:0043231"(intracellular membrane-bounded organelle)|go:"GO:0043249"(erythrocyte maturation)|go:"GO:0043523"(regulation of neuron apoptotic process)|go:"GO:0045471"(response to ethanol)|go:"GO:0046390"(ribose phosphate biosynthetic process)|go:"GO:0050661"(NADP binding)|go:"GO:0051156"(glucose 6-phosphate metabolic process)|go:"GO:0061052"(negative regulation of cell growth involved in cardiac muscle cell development)|go:"GO:0070062"(extracellular exosome)|go:"GO:1904879"(positive regulation of calcium ion transmembrane transport via high voltage-gated calcium channel)|go:"GO:2000378"(negative regulation of reactive oxygen species metabolic process)|interpro:IPR001282(Glucose-6-phosphate dehydrogenase)|interpro:IPR019796|interpro:IPR022674|interpro:IPR022675|interpro:IPR036291|rcsb pdb:1QKI|rcsb pdb:2BH9|rcsb pdb:2BHL|rcsb pdb:5UKW|rcsb pdb:6E07|rcsb pdb:6E08|rcsb pdb:6JYU|rcsb pdb:6VA0|rcsb pdb:6VA7|rcsb pdb:6VA8|rcsb pdb:6VA9|rcsb pdb:6VAQ|reactome:R-HSA-5628897|reactome:R-HSA-71336	-	-	-	figure legend:F2B F2D SF5 F4E|comment:"To test this hypothesis, we determined the interaction between  two differentially tagged G6PD proteins, G6PD-Flag and GFP-G6PD,  in HEK293T cells. We found that mutation of K171 to either R  (K171R) or Q (K171Q) did not affect the interaction between G6PD  subunits (Fig 2B). In contrast, substitution of K386Q, but not  K386R, impaired the interaction between G6PD subunits (Fig 2B).  Strikingly, substitution of K403Q, but not K403R, entirely disrupted  the interaction between G6PD subunits (Fig 2B). In addition, glutaraldehyde  cross-linking assay demonstrated that the K403Q mutant  displayed impaired ability to form dimers when compared to wildtype  G6PD or the K403R mutant (Fig 2C). Moreover, NAM treatment  decreased the binding by approximately 55% between the two  differentially tagged proteins of wild-type G6PD in a dose-dependent  manner (Fig 2D and Supplementary Fig S5). NAM treatment,  however, failed to affect the interaction between Flag-tagged and  GFP-tagged K403R mutant of G6PD (Fig 2D), further suggesting that  K403 acetylation largely hinders the interaction between G6PD  subunits."|comment:"Co-expression of SIRT2, but not the catalytic inactive SIRT2H187Y  mutant, increased the interaction between two differentially tagged  G6PD, and this effect could be diminished by NAM treatment  (Fig 4E)."|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:9606(human-293t)|taxid:9606(Homo sapiens 293 cells transformed with SV40 large T antigen)	-	2014/10/07	2014/10/16	rogid:qW8uk6xBGtrxlsosIH6gEG1ZfWA9606	rogid:qW8uk6xBGtrxlsosIH6gEG1ZfWA9606	intact-crc:37035B4484ACF8C7|rigid:YTSMT3uoLW5pB/lbDTIcDhOAPfY	false	green fluorescent protein tag:?-?	flag tag:?-?|mutation disrupting interaction:403-403	-	-	psi-mi:"MI:0705"(anti tag western blot)	psi-mi:"MI:0705"(anti tag western blot)
uniprotkb:P11413	uniprotkb:Q8IXJ6	intact:EBI-4289891|uniprotkb:Q8IU88|uniprotkb:D3DWX9|uniprotkb:Q16000|uniprotkb:Q16765|uniprotkb:Q8IUA6|uniprotkb:Q8IU70|uniprotkb:Q96PQ2|ensembl:ENSP00000377192|ensembl:ENSP00000377194	intact:EBI-477232|uniprotkb:O95889|uniprotkb:Q924Y7|uniprotkb:Q9P0G8|uniprotkb:Q9UNT0|uniprotkb:Q9Y6E9|ensembl:ENSP00000249396|ensembl:ENSP00000489602|uniprotkb:A8K3V1|uniprotkb:B2RB45|uniprotkb:U5TP13	psi-mi:g6pd_human(display_long)|uniprotkb:G6PD(gene name)|psi-mi:G6PD(display_short)	psi-mi:sir2_human(display_long)|uniprotkb:SIR2-like protein 2(gene name synonym)|uniprotkb:SIRT2(gene name)|psi-mi:SIRT2(display_short)|uniprotkb:SIR2L(gene name synonym)|uniprotkb:SIR2L2(gene name synonym)|uniprotkb:Regulatory protein SIR2 homolog 2(gene name synonym)	psi-mi:"MI:0007"(anti tag coimmunoprecipitation)	Wang et al. (2014)	imex:IM-23514|pubmed:24769394	taxid:9606(human)|taxid:9606(Homo sapiens)	taxid:9606(human)|taxid:9606(Homo sapiens)	psi-mi:"MI:0915"(physical association)	psi-mi:"MI:0471"(MINT)	intact:EBI-9831107|imex:IM-23514-3	-	-	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0496"(bait)	psi-mi:"MI:0498"(prey)	psi-mi:"MI:0326"(protein)	psi-mi:"MI:0326"(protein)	refseq:NP_000393.4|refseq:NP_001035810.1|ensembl:ENSG00000160211(gene)|ensembl:ENST00000393562(transcript)|ensembl:ENST00000393564(transcript)|go:"GO:0004345"(glucose-6-phosphate dehydrogenase activity)|go:"GO:0005536"(glucose binding)|go:"GO:0005634"(nucleus)|go:"GO:0005737"(cytoplasm)|go:"GO:0005829"(cytosol)|go:"GO:0006006"(glucose metabolic process)|go:"GO:0006098"(pentose-phosphate shunt)|go:"GO:0006629"(lipid metabolic process)|go:"GO:0006695"(cholesterol biosynthetic process)|go:"GO:0006739"(NADP metabolic process)|go:"GO:0006740"(NADPH regeneration)|go:"GO:0006749"(glutathione metabolic process)|go:"GO:0009051"(pentose-phosphate shunt, oxidative branch)|go:"GO:0009898"(cytoplasmic side of plasma membrane)|go:"GO:0010041"("response to iron(III) ion")|go:"GO:0010734"(negative regulation of protein glutathionylation)|go:"GO:0014070"(response to organic cyclic compound)|go:"GO:0016020"(membrane)|go:"GO:0019322"(pentose biosynthetic process)|go:"GO:0021762"(substantia nigra development)|go:"GO:0032094"(response to food)|go:"GO:0034451"(centriolar satellite)|go:"GO:0034599"(cellular response to oxidative stress)|go:"GO:0042802"(identical protein binding)|go:"GO:0042803"(protein homodimerization activity)|go:"GO:0043231"(intracellular membrane-bounded organelle)|go:"GO:0043249"(erythrocyte maturation)|go:"GO:0043523"(regulation of neuron apoptotic process)|go:"GO:0045471"(response to ethanol)|go:"GO:0046390"(ribose phosphate biosynthetic process)|go:"GO:0050661"(NADP binding)|go:"GO:0051156"(glucose 6-phosphate metabolic process)|go:"GO:0061052"(negative regulation of cell growth involved in cardiac muscle cell development)|go:"GO:0070062"(extracellular exosome)|go:"GO:1904879"(positive regulation of calcium ion transmembrane transport via high voltage-gated calcium channel)|go:"GO:2000378"(negative regulation of reactive oxygen species metabolic process)|interpro:IPR001282(Glucose-6-phosphate dehydrogenase)|interpro:IPR019796|interpro:IPR022674|interpro:IPR022675|interpro:IPR036291|rcsb pdb:1QKI|rcsb pdb:2BH9|rcsb pdb:2BHL|rcsb pdb:5UKW|rcsb pdb:6E07|rcsb pdb:6E08|rcsb pdb:6JYU|rcsb pdb:6VA0|rcsb pdb:6VA7|rcsb pdb:6VA8|rcsb pdb:6VA9|rcsb pdb:6VAQ|reactome:R-HSA-5628897|reactome:R-HSA-71336	ensembl:ENSG00000068903(gene)|ensembl:ENSG00000283100(gene)|ensembl:ENST00000249396(transcript)|ensembl:ENST00000634533(transcript)|go:"GO:0000122"(negative regulation of transcription by RNA polymerase II)|go:"GO:0000183"(rDNA heterochromatin assembly)|go:"GO:0000781"(chromosome, telomeric region)|go:"GO:0000792"(heterochromatin)|go:"GO:0003682"(chromatin binding)|go:"GO:0003950"(NAD+ ADP-ribosyltransferase activity)|go:"GO:0004407"(histone deacetylase activity)|go:"GO:0005634"(nucleus)|go:"GO:0005677"(chromatin silencing complex)|go:"GO:0005694"(chromosome)|go:"GO:0005730"(nucleolus)|go:"GO:0005737"(cytoplasm)|go:"GO:0005813"(centrosome)|go:"GO:0005814"(centriole)|go:"GO:0005819"(spindle)|go:"GO:0005829"(cytosol)|go:"GO:0005874"(microtubule)|go:"GO:0005886"(plasma membrane)|go:"GO:0006342"|go:"GO:0006348"|go:"GO:0006471"(protein ADP-ribosylation)|go:"GO:0006476"(protein deacetylation)|go:"GO:0006914"(autophagy)|go:"GO:0007084"(mitotic nuclear membrane reassembly)|go:"GO:0007096"(regulation of exit from mitosis)|go:"GO:0008134"(transcription factor binding)|rcsb pdb:6L66|rcsb pdb:6L71|rcsb pdb:6L72|rcsb pdb:6NR0|rcsb pdb:6QCN|rcsb pdb:7BOS|rcsb pdb:7BOT|reactome:R-HSA-2995383|rcsb pdb:5D7O|rcsb pdb:5D7P|rcsb pdb:5D7Q|rcsb pdb:5DY4|rcsb pdb:5DY5|rcsb pdb:5FYQ|rcsb pdb:5G4C|rcsb pdb:5MAR|rcsb pdb:5MAT|rcsb pdb:5Y0Z|rcsb pdb:5Y5N|rcsb pdb:5YQL|rcsb pdb:5YQM|rcsb pdb:5YQN|rcsb pdb:5YQO|rcsb pdb:6L65|go:"GO:0008270"(zinc ion binding)|go:"GO:0008285"(negative regulation of cell population proliferation)|go:"GO:0010507"(negative regulation of autophagy)|go:"GO:0010801"(negative regulation of peptidyl-threonine phosphorylation)|go:"GO:0014065"(phosphatidylinositol 3-kinase signaling)|go:"GO:0016575"(histone deacetylation)|go:"GO:0017136"(NAD-dependent histone deacetylase activity)|go:"GO:0021762"(substantia nigra development)|go:"GO:0022011"(myelination in peripheral nervous system)|go:"GO:0030426"(growth cone)|go:"GO:0030496"(midbody)|go:"GO:0031641"(regulation of myelination)|go:"GO:0032436"(positive regulation of proteasomal ubiquitin-dependent protein catabolic process)|go:"GO:0033010"(paranodal junction)|go:"GO:0033270"(paranode region of axon)|go:"GO:0033558"(protein deacetylase activity)|go:"GO:0034599"(cellular response to oxidative stress)|go:"GO:0034979"(NAD-dependent protein deacetylase activity)|go:"GO:0034983"(peptidyl-lysine deacetylation)|go:"GO:0035035"(histone acetyltransferase binding)|go:"GO:0035729"(cellular response to hepatocyte growth factor stimulus)|go:"GO:0042177"(negative regulation of protein catabolic process)|go:"GO:0042325"(regulation of phosphorylation)|go:"GO:0042826"(histone deacetylase binding)|go:"GO:0042903"(tubulin deacetylase activity)|go:"GO:0043130"(ubiquitin binding)|go:"GO:0043161"(proteasome-mediated ubiquitin-dependent protein catabolic process)|go:"GO:0043204"(perikaryon)|go:"GO:0043209"(myelin sheath)|go:"GO:0043219"(lateral loop)|go:"GO:0043220"(Schmidt-Lanterman incisure)|go:"GO:0043388"(positive regulation of DNA binding)|go:"GO:0043491"(protein kinase B signaling)|go:"GO:0044224"(juxtaparanode region of axon)|go:"GO:0044242"(cellular lipid catabolic process)|go:"GO:0045087"(innate immune response)|go:"GO:0045599"(negative regulation of fat cell differentiation)|go:"GO:0045836"(positive regulation of meiotic nuclear division)|go:"GO:0045843"(negative regulation of striated muscle tissue development)|go:"GO:0045892"(negative regulation of transcription, DNA-templated)|go:"GO:0045944"(positive regulation of transcription by RNA polymerase II)|go:"GO:0046970"("NAD-dependent histone deacetylase activity (H4-K16 specific)")|go:"GO:0048012"(hepatocyte growth factor receptor signaling pathway)|go:"GO:0048471"(perinuclear region of cytoplasm)|go:"GO:0051321"(meiotic cell cycle)|go:"GO:0051726"(regulation of cell cycle)|go:"GO:0051775"(response to redox state)|go:"GO:0051781"(positive regulation of cell division)|go:"GO:0051987"(positive regulation of attachment of spindle microtubules to kinetochore)|go:"GO:0061428"(negative regulation of transcription from RNA polymerase II promoter in response to hypoxia)|go:"GO:0061433"(cellular response to caloric restriction)|go:"GO:0070403"(NAD+ binding)|go:"GO:0070446"(negative regulation of oligodendrocyte progenitor proliferation)|go:"GO:0070932"(histone H3 deacetylation)|go:"GO:0070933"(histone H4 deacetylation)|go:"GO:0071219"(cellular response to molecule of bacterial origin)|go:"GO:0071456"(cellular response to hypoxia)|go:"GO:0071872"(cellular response to epinephrine stimulus)|go:"GO:0072686"(mitotic spindle)|go:"GO:0072687"(meiotic spindle)|go:"GO:0090042"(tubulin deacetylation)|go:"GO:0097386"(glial cell projection)|go:"GO:0140297"(DNA-binding transcription factor binding)|go:"GO:1900119"(positive regulation of execution phase of apoptosis)|go:"GO:1900195"(positive regulation of oocyte maturation)|go:"GO:1900425"(negative regulation of defense response to bacterium)|go:"GO:2000378"(negative regulation of reactive oxygen species metabolic process)|go:"GO:2000777"(positive regulation of proteasomal ubiquitin-dependent protein catabolic process involved in cellular response to hypoxia)|interpro:IPR003000(NAD-dependent histone deacetylase, silent information regulator Sir2)|interpro:IPR017328(NAD-dependent deacetylase sirtuin-2, eukaryota)|interpro:IPR026590|interpro:IPR026591|interpro:IPR029035|mint:Q8IXJ6|rcsb pdb:1J8F|rcsb pdb:3ZGO|rcsb pdb:3ZGV|rcsb pdb:4L3O|rcsb pdb:4R8M|rcsb pdb:4RMG|rcsb pdb:4RMH|rcsb pdb:4RMI|rcsb pdb:4RMJ|rcsb pdb:4X3O|rcsb pdb:4X3P|rcsb pdb:4Y6L|rcsb pdb:4Y6O|go:"GO:0051301"(cell division)|rcsb pdb:4Y6Q|refseq:NP_001180215.1|refseq:NP_036369.2|refseq:NP_085096.1|refseq:XP_011524956.1|refseq:XP_011524957.1|refseq:XP_006723174.1|dip:DIP-33350N	-	-	-	figure legend:f4a|comment:"To test this hypothesis, we determined the interaction between  two differentially tagged G6PD proteins, G6PD-Flag and GFP-G6PD,  in HEK293T cells. We found that mutation of K171 to either R  (K171R) or Q (K171Q) did not affect the interaction between G6PD  subunits (Fig 2B). In contrast, substitution of K386Q, but not  K386R, impaired the interaction between G6PD subunits (Fig 2B).  Strikingly, substitution of K403Q, but not K403R, entirely disrupted  the interaction between G6PD subunits (Fig 2B). In addition, glutaraldehyde  cross-linking assay demonstrated that the K403Q mutant  displayed impaired ability to form dimers when compared to wildtype  G6PD or the K403R mutant (Fig 2C). Moreover, NAM treatment  decreased the binding by approximately 55% between the two  differentially tagged proteins of wild-type G6PD in a dose-dependent  manner (Fig 2D and Supplementary Fig S5). NAM treatment,  however, failed to affect the interaction between Flag-tagged and  GFP-tagged K403R mutant of G6PD (Fig 2D), further suggesting that  K403 acetylation largely hinders the interaction between G6PD  subunits."|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:9606(human-293t)|taxid:9606(Homo sapiens 293 cells transformed with SV40 large T antigen)	-	2014/10/07	2014/10/16	rogid:qW8uk6xBGtrxlsosIH6gEG1ZfWA9606	rogid:d4mOZOyT5RubJjE+a8wQhsWR6WI9606	intact-crc:D7C3CD8423CF2D5A|rigid:hTSrmVdyJOwDZcm6RqjgnW+pEnI	false	flag tag:?-?	ha tag:?-?	-	-	psi-mi:"MI:0705"(anti tag western blot)	psi-mi:"MI:0705"(anti tag western blot)
uniprotkb:P11413	uniprotkb:P11413	intact:EBI-4289891|uniprotkb:Q8IU88|uniprotkb:D3DWX9|uniprotkb:Q16000|uniprotkb:Q16765|uniprotkb:Q8IUA6|uniprotkb:Q8IU70|uniprotkb:Q96PQ2|ensembl:ENSP00000377192|ensembl:ENSP00000377194	intact:EBI-4289891|uniprotkb:Q8IU88|uniprotkb:D3DWX9|uniprotkb:Q16000|uniprotkb:Q16765|uniprotkb:Q8IUA6|uniprotkb:Q8IU70|uniprotkb:Q96PQ2|ensembl:ENSP00000377192|ensembl:ENSP00000377194	psi-mi:g6pd_human(display_long)|uniprotkb:G6PD(gene name)|psi-mi:G6PD(display_short)	psi-mi:g6pd_human(display_long)|uniprotkb:G6PD(gene name)|psi-mi:G6PD(display_short)	psi-mi:"MI:0007"(anti tag coimmunoprecipitation)	Wang et al. (2014)	imex:IM-23514|pubmed:24769394	taxid:9606(human)|taxid:9606(Homo sapiens)	taxid:9606(human)|taxid:9606(Homo sapiens)	psi-mi:"MI:0915"(physical association)	psi-mi:"MI:0471"(MINT)	intact:EBI-9830954|imex:IM-23514-2	-	-	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0496"(bait)	psi-mi:"MI:0498"(prey)	psi-mi:"MI:0326"(protein)	psi-mi:"MI:0326"(protein)	refseq:NP_000393.4|refseq:NP_001035810.1|ensembl:ENSG00000160211(gene)|ensembl:ENST00000393562(transcript)|ensembl:ENST00000393564(transcript)|go:"GO:0004345"(glucose-6-phosphate dehydrogenase activity)|go:"GO:0005536"(glucose binding)|go:"GO:0005634"(nucleus)|go:"GO:0005737"(cytoplasm)|go:"GO:0005829"(cytosol)|go:"GO:0006006"(glucose metabolic process)|go:"GO:0006098"(pentose-phosphate shunt)|go:"GO:0006629"(lipid metabolic process)|go:"GO:0006695"(cholesterol biosynthetic process)|go:"GO:0006739"(NADP metabolic process)|go:"GO:0006740"(NADPH regeneration)|go:"GO:0006749"(glutathione metabolic process)|go:"GO:0009051"(pentose-phosphate shunt, oxidative branch)|go:"GO:0009898"(cytoplasmic side of plasma membrane)|go:"GO:0010041"("response to iron(III) ion")|go:"GO:0010734"(negative regulation of protein glutathionylation)|go:"GO:0014070"(response to organic cyclic compound)|go:"GO:0016020"(membrane)|go:"GO:0019322"(pentose biosynthetic process)|go:"GO:0021762"(substantia nigra development)|go:"GO:0032094"(response to food)|go:"GO:0034451"(centriolar satellite)|go:"GO:0034599"(cellular response to oxidative stress)|go:"GO:0042802"(identical protein binding)|go:"GO:0042803"(protein homodimerization activity)|go:"GO:0043231"(intracellular membrane-bounded organelle)|go:"GO:0043249"(erythrocyte maturation)|go:"GO:0043523"(regulation of neuron apoptotic process)|go:"GO:0045471"(response to ethanol)|go:"GO:0046390"(ribose phosphate biosynthetic process)|go:"GO:0050661"(NADP binding)|go:"GO:0051156"(glucose 6-phosphate metabolic process)|go:"GO:0061052"(negative regulation of cell growth involved in cardiac muscle cell development)|go:"GO:0070062"(extracellular exosome)|go:"GO:1904879"(positive regulation of calcium ion transmembrane transport via high voltage-gated calcium channel)|go:"GO:2000378"(negative regulation of reactive oxygen species metabolic process)|interpro:IPR001282(Glucose-6-phosphate dehydrogenase)|interpro:IPR019796|interpro:IPR022674|interpro:IPR022675|interpro:IPR036291|rcsb pdb:1QKI|rcsb pdb:2BH9|rcsb pdb:2BHL|rcsb pdb:5UKW|rcsb pdb:6E07|rcsb pdb:6E08|rcsb pdb:6JYU|rcsb pdb:6VA0|rcsb pdb:6VA7|rcsb pdb:6VA8|rcsb pdb:6VA9|rcsb pdb:6VAQ|reactome:R-HSA-5628897|reactome:R-HSA-71336	refseq:NP_000393.4|refseq:NP_001035810.1|ensembl:ENSG00000160211(gene)|ensembl:ENST00000393562(transcript)|ensembl:ENST00000393564(transcript)|go:"GO:0004345"(glucose-6-phosphate dehydrogenase activity)|go:"GO:0005536"(glucose binding)|go:"GO:0005634"(nucleus)|go:"GO:0005737"(cytoplasm)|go:"GO:0005829"(cytosol)|go:"GO:0006006"(glucose metabolic process)|go:"GO:0006098"(pentose-phosphate shunt)|go:"GO:0006629"(lipid metabolic process)|go:"GO:0006695"(cholesterol biosynthetic process)|go:"GO:0006739"(NADP metabolic process)|go:"GO:0006740"(NADPH regeneration)|go:"GO:0006749"(glutathione metabolic process)|go:"GO:0009051"(pentose-phosphate shunt, oxidative branch)|go:"GO:0009898"(cytoplasmic side of plasma membrane)|go:"GO:0010041"("response to iron(III) ion")|go:"GO:0010734"(negative regulation of protein glutathionylation)|go:"GO:0014070"(response to organic cyclic compound)|go:"GO:0016020"(membrane)|go:"GO:0019322"(pentose biosynthetic process)|go:"GO:0021762"(substantia nigra development)|go:"GO:0032094"(response to food)|go:"GO:0034451"(centriolar satellite)|go:"GO:0034599"(cellular response to oxidative stress)|go:"GO:0042802"(identical protein binding)|go:"GO:0042803"(protein homodimerization activity)|go:"GO:0043231"(intracellular membrane-bounded organelle)|go:"GO:0043249"(erythrocyte maturation)|go:"GO:0043523"(regulation of neuron apoptotic process)|go:"GO:0045471"(response to ethanol)|go:"GO:0046390"(ribose phosphate biosynthetic process)|go:"GO:0050661"(NADP binding)|go:"GO:0051156"(glucose 6-phosphate metabolic process)|go:"GO:0061052"(negative regulation of cell growth involved in cardiac muscle cell development)|go:"GO:0070062"(extracellular exosome)|go:"GO:1904879"(positive regulation of calcium ion transmembrane transport via high voltage-gated calcium channel)|go:"GO:2000378"(negative regulation of reactive oxygen species metabolic process)|interpro:IPR001282(Glucose-6-phosphate dehydrogenase)|interpro:IPR019796|interpro:IPR022674|interpro:IPR022675|interpro:IPR036291|rcsb pdb:1QKI|rcsb pdb:2BH9|rcsb pdb:2BHL|rcsb pdb:5UKW|rcsb pdb:6E07|rcsb pdb:6E08|rcsb pdb:6JYU|rcsb pdb:6VA0|rcsb pdb:6VA7|rcsb pdb:6VA8|rcsb pdb:6VA9|rcsb pdb:6VAQ|reactome:R-HSA-5628897|reactome:R-HSA-71336	-	-	-	figure legend:F2B|comment:"To test this hypothesis, we determined the interaction between  two differentially tagged G6PD proteins, G6PD-Flag and GFP-G6PD,  in HEK293T cells. We found that mutation of K171 to either R  (K171R) or Q (K171Q) did not affect the interaction between G6PD  subunits (Fig 2B). In contrast, substitution of K386Q, but not  K386R, impaired the interaction between G6PD subunits (Fig 2B).  Strikingly, substitution of K403Q, but not K403R, entirely disrupted  the interaction between G6PD subunits (Fig 2B). In addition, glutaraldehyde  cross-linking assay demonstrated that the K403Q mutant  displayed impaired ability to form dimers when compared to wildtype  G6PD or the K403R mutant (Fig 2C). Moreover, NAM treatment  decreased the binding by approximately 55% between the two  differentially tagged proteins of wild-type G6PD in a dose-dependent  manner (Fig 2D and Supplementary Fig S5). NAM treatment,  however, failed to affect the interaction between Flag-tagged and  GFP-tagged K403R mutant of G6PD (Fig 2D), further suggesting that  K403 acetylation largely hinders the interaction between G6PD  subunits."|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:9606(human-293t)|taxid:9606(Homo sapiens 293 cells transformed with SV40 large T antigen)	-	2014/10/07	2014/10/16	rogid:qW8uk6xBGtrxlsosIH6gEG1ZfWA9606	rogid:qW8uk6xBGtrxlsosIH6gEG1ZfWA9606	intact-crc:4914A314B0C90951|rigid:YTSMT3uoLW5pB/lbDTIcDhOAPfY	false	flag tag:?-?|mutation decreasing interaction:386-386	green fluorescent protein tag:?-?	-	-	psi-mi:"MI:0705"(anti tag western blot)	psi-mi:"MI:0705"(anti tag western blot)
uniprotkb:P11413	uniprotkb:Q8IXJ6	intact:EBI-4289891|uniprotkb:Q8IU88|uniprotkb:D3DWX9|uniprotkb:Q16000|uniprotkb:Q16765|uniprotkb:Q8IUA6|uniprotkb:Q8IU70|uniprotkb:Q96PQ2|ensembl:ENSP00000377192|ensembl:ENSP00000377194	intact:EBI-477232|uniprotkb:O95889|uniprotkb:Q924Y7|uniprotkb:Q9P0G8|uniprotkb:Q9UNT0|uniprotkb:Q9Y6E9|ensembl:ENSP00000249396|ensembl:ENSP00000489602|uniprotkb:A8K3V1|uniprotkb:B2RB45|uniprotkb:U5TP13	psi-mi:g6pd_human(display_long)|uniprotkb:G6PD(gene name)|psi-mi:G6PD(display_short)	psi-mi:sir2_human(display_long)|uniprotkb:SIR2-like protein 2(gene name synonym)|uniprotkb:SIRT2(gene name)|psi-mi:SIRT2(display_short)|uniprotkb:SIR2L(gene name synonym)|uniprotkb:SIR2L2(gene name synonym)|uniprotkb:Regulatory protein SIR2 homolog 2(gene name synonym)	psi-mi:"MI:0007"(anti tag coimmunoprecipitation)	Wang et al. (2014)	imex:IM-23514|pubmed:24769394	taxid:9606(human)|taxid:9606(Homo sapiens)	taxid:9606(human)|taxid:9606(Homo sapiens)	psi-mi:"MI:0915"(physical association)	psi-mi:"MI:0471"(MINT)	intact:EBI-9831119|imex:IM-23514-4	-	-	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0498"(prey)	psi-mi:"MI:0496"(bait)	psi-mi:"MI:0326"(protein)	psi-mi:"MI:0326"(protein)	refseq:NP_000393.4|refseq:NP_001035810.1|ensembl:ENSG00000160211(gene)|ensembl:ENST00000393562(transcript)|ensembl:ENST00000393564(transcript)|go:"GO:0004345"(glucose-6-phosphate dehydrogenase activity)|go:"GO:0005536"(glucose binding)|go:"GO:0005634"(nucleus)|go:"GO:0005737"(cytoplasm)|go:"GO:0005829"(cytosol)|go:"GO:0006006"(glucose metabolic process)|go:"GO:0006098"(pentose-phosphate shunt)|go:"GO:0006629"(lipid metabolic process)|go:"GO:0006695"(cholesterol biosynthetic process)|go:"GO:0006739"(NADP metabolic process)|go:"GO:0006740"(NADPH regeneration)|go:"GO:0006749"(glutathione metabolic process)|go:"GO:0009051"(pentose-phosphate shunt, oxidative branch)|go:"GO:0009898"(cytoplasmic side of plasma membrane)|go:"GO:0010041"("response to iron(III) ion")|go:"GO:0010734"(negative regulation of protein glutathionylation)|go:"GO:0014070"(response to organic cyclic compound)|go:"GO:0016020"(membrane)|go:"GO:0019322"(pentose biosynthetic process)|go:"GO:0021762"(substantia nigra development)|go:"GO:0032094"(response to food)|go:"GO:0034451"(centriolar satellite)|go:"GO:0034599"(cellular response to oxidative stress)|go:"GO:0042802"(identical protein binding)|go:"GO:0042803"(protein homodimerization activity)|go:"GO:0043231"(intracellular membrane-bounded organelle)|go:"GO:0043249"(erythrocyte maturation)|go:"GO:0043523"(regulation of neuron apoptotic process)|go:"GO:0045471"(response to ethanol)|go:"GO:0046390"(ribose phosphate biosynthetic process)|go:"GO:0050661"(NADP binding)|go:"GO:0051156"(glucose 6-phosphate metabolic process)|go:"GO:0061052"(negative regulation of cell growth involved in cardiac muscle cell development)|go:"GO:0070062"(extracellular exosome)|go:"GO:1904879"(positive regulation of calcium ion transmembrane transport via high voltage-gated calcium channel)|go:"GO:2000378"(negative regulation of reactive oxygen species metabolic process)|interpro:IPR001282(Glucose-6-phosphate dehydrogenase)|interpro:IPR019796|interpro:IPR022674|interpro:IPR022675|interpro:IPR036291|rcsb pdb:1QKI|rcsb pdb:2BH9|rcsb pdb:2BHL|rcsb pdb:5UKW|rcsb pdb:6E07|rcsb pdb:6E08|rcsb pdb:6JYU|rcsb pdb:6VA0|rcsb pdb:6VA7|rcsb pdb:6VA8|rcsb pdb:6VA9|rcsb pdb:6VAQ|reactome:R-HSA-5628897|reactome:R-HSA-71336	ensembl:ENSG00000068903(gene)|ensembl:ENSG00000283100(gene)|ensembl:ENST00000249396(transcript)|ensembl:ENST00000634533(transcript)|go:"GO:0000122"(negative regulation of transcription by RNA polymerase II)|go:"GO:0000183"(rDNA heterochromatin assembly)|go:"GO:0000781"(chromosome, telomeric region)|go:"GO:0000792"(heterochromatin)|go:"GO:0003682"(chromatin binding)|go:"GO:0003950"(NAD+ ADP-ribosyltransferase activity)|go:"GO:0004407"(histone deacetylase activity)|go:"GO:0005634"(nucleus)|go:"GO:0005677"(chromatin silencing complex)|go:"GO:0005694"(chromosome)|go:"GO:0005730"(nucleolus)|go:"GO:0005737"(cytoplasm)|go:"GO:0005813"(centrosome)|go:"GO:0005814"(centriole)|go:"GO:0005819"(spindle)|go:"GO:0005829"(cytosol)|go:"GO:0005874"(microtubule)|go:"GO:0005886"(plasma membrane)|go:"GO:0006342"|go:"GO:0006348"|go:"GO:0006471"(protein ADP-ribosylation)|go:"GO:0006476"(protein deacetylation)|go:"GO:0006914"(autophagy)|go:"GO:0007084"(mitotic nuclear membrane reassembly)|go:"GO:0007096"(regulation of exit from mitosis)|go:"GO:0008134"(transcription factor binding)|rcsb pdb:6L66|rcsb pdb:6L71|rcsb pdb:6L72|rcsb pdb:6NR0|rcsb pdb:6QCN|rcsb pdb:7BOS|rcsb pdb:7BOT|reactome:R-HSA-2995383|rcsb pdb:5D7O|rcsb pdb:5D7P|rcsb pdb:5D7Q|rcsb pdb:5DY4|rcsb pdb:5DY5|rcsb pdb:5FYQ|rcsb pdb:5G4C|rcsb pdb:5MAR|rcsb pdb:5MAT|rcsb pdb:5Y0Z|rcsb pdb:5Y5N|rcsb pdb:5YQL|rcsb pdb:5YQM|rcsb pdb:5YQN|rcsb pdb:5YQO|rcsb pdb:6L65|go:"GO:0008270"(zinc ion binding)|go:"GO:0008285"(negative regulation of cell population proliferation)|go:"GO:0010507"(negative regulation of autophagy)|go:"GO:0010801"(negative regulation of peptidyl-threonine phosphorylation)|go:"GO:0014065"(phosphatidylinositol 3-kinase signaling)|go:"GO:0016575"(histone deacetylation)|go:"GO:0017136"(NAD-dependent histone deacetylase activity)|go:"GO:0021762"(substantia nigra development)|go:"GO:0022011"(myelination in peripheral nervous system)|go:"GO:0030426"(growth cone)|go:"GO:0030496"(midbody)|go:"GO:0031641"(regulation of myelination)|go:"GO:0032436"(positive regulation of proteasomal ubiquitin-dependent protein catabolic process)|go:"GO:0033010"(paranodal junction)|go:"GO:0033270"(paranode region of axon)|go:"GO:0033558"(protein deacetylase activity)|go:"GO:0034599"(cellular response to oxidative stress)|go:"GO:0034979"(NAD-dependent protein deacetylase activity)|go:"GO:0034983"(peptidyl-lysine deacetylation)|go:"GO:0035035"(histone acetyltransferase binding)|go:"GO:0035729"(cellular response to hepatocyte growth factor stimulus)|go:"GO:0042177"(negative regulation of protein catabolic process)|go:"GO:0042325"(regulation of phosphorylation)|go:"GO:0042826"(histone deacetylase binding)|go:"GO:0042903"(tubulin deacetylase activity)|go:"GO:0043130"(ubiquitin binding)|go:"GO:0043161"(proteasome-mediated ubiquitin-dependent protein catabolic process)|go:"GO:0043204"(perikaryon)|go:"GO:0043209"(myelin sheath)|go:"GO:0043219"(lateral loop)|go:"GO:0043220"(Schmidt-Lanterman incisure)|go:"GO:0043388"(positive regulation of DNA binding)|go:"GO:0043491"(protein kinase B signaling)|go:"GO:0044224"(juxtaparanode region of axon)|go:"GO:0044242"(cellular lipid catabolic process)|go:"GO:0045087"(innate immune response)|go:"GO:0045599"(negative regulation of fat cell differentiation)|go:"GO:0045836"(positive regulation of meiotic nuclear division)|go:"GO:0045843"(negative regulation of striated muscle tissue development)|go:"GO:0045892"(negative regulation of transcription, DNA-templated)|go:"GO:0045944"(positive regulation of transcription by RNA polymerase II)|go:"GO:0046970"("NAD-dependent histone deacetylase activity (H4-K16 specific)")|go:"GO:0048012"(hepatocyte growth factor receptor signaling pathway)|go:"GO:0048471"(perinuclear region of cytoplasm)|go:"GO:0051321"(meiotic cell cycle)|go:"GO:0051726"(regulation of cell cycle)|go:"GO:0051775"(response to redox state)|go:"GO:0051781"(positive regulation of cell division)|go:"GO:0051987"(positive regulation of attachment of spindle microtubules to kinetochore)|go:"GO:0061428"(negative regulation of transcription from RNA polymerase II promoter in response to hypoxia)|go:"GO:0061433"(cellular response to caloric restriction)|go:"GO:0070403"(NAD+ binding)|go:"GO:0070446"(negative regulation of oligodendrocyte progenitor proliferation)|go:"GO:0070932"(histone H3 deacetylation)|go:"GO:0070933"(histone H4 deacetylation)|go:"GO:0071219"(cellular response to molecule of bacterial origin)|go:"GO:0071456"(cellular response to hypoxia)|go:"GO:0071872"(cellular response to epinephrine stimulus)|go:"GO:0072686"(mitotic spindle)|go:"GO:0072687"(meiotic spindle)|go:"GO:0090042"(tubulin deacetylation)|go:"GO:0097386"(glial cell projection)|go:"GO:0140297"(DNA-binding transcription factor binding)|go:"GO:1900119"(positive regulation of execution phase of apoptosis)|go:"GO:1900195"(positive regulation of oocyte maturation)|go:"GO:1900425"(negative regulation of defense response to bacterium)|go:"GO:2000378"(negative regulation of reactive oxygen species metabolic process)|go:"GO:2000777"(positive regulation of proteasomal ubiquitin-dependent protein catabolic process involved in cellular response to hypoxia)|interpro:IPR003000(NAD-dependent histone deacetylase, silent information regulator Sir2)|interpro:IPR017328(NAD-dependent deacetylase sirtuin-2, eukaryota)|interpro:IPR026590|interpro:IPR026591|interpro:IPR029035|mint:Q8IXJ6|rcsb pdb:1J8F|rcsb pdb:3ZGO|rcsb pdb:3ZGV|rcsb pdb:4L3O|rcsb pdb:4R8M|rcsb pdb:4RMG|rcsb pdb:4RMH|rcsb pdb:4RMI|rcsb pdb:4RMJ|rcsb pdb:4X3O|rcsb pdb:4X3P|rcsb pdb:4Y6L|rcsb pdb:4Y6O|go:"GO:0051301"(cell division)|rcsb pdb:4Y6Q|refseq:NP_001180215.1|refseq:NP_036369.2|refseq:NP_085096.1|refseq:XP_011524956.1|refseq:XP_011524957.1|refseq:XP_006723174.1|dip:DIP-33350N	-	-	-	figure legend:f4b|comment:"To test this hypothesis, we determined the interaction between  two differentially tagged G6PD proteins, G6PD-Flag and GFP-G6PD,  in HEK293T cells. We found that mutation of K171 to either R  (K171R) or Q (K171Q) did not affect the interaction between G6PD  subunits (Fig 2B). In contrast, substitution of K386Q, but not  K386R, impaired the interaction between G6PD subunits (Fig 2B).  Strikingly, substitution of K403Q, but not K403R, entirely disrupted  the interaction between G6PD subunits (Fig 2B). In addition, glutaraldehyde  cross-linking assay demonstrated that the K403Q mutant  displayed impaired ability to form dimers when compared to wildtype  G6PD or the K403R mutant (Fig 2C). Moreover, NAM treatment  decreased the binding by approximately 55% between the two  differentially tagged proteins of wild-type G6PD in a dose-dependent  manner (Fig 2D and Supplementary Fig S5). NAM treatment,  however, failed to affect the interaction between Flag-tagged and  GFP-tagged K403R mutant of G6PD (Fig 2D), further suggesting that  K403 acetylation largely hinders the interaction between G6PD  subunits."|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:9606(human-293t)|taxid:9606(Homo sapiens 293 cells transformed with SV40 large T antigen)	-	2014/10/07	2014/10/16	rogid:qW8uk6xBGtrxlsosIH6gEG1ZfWA9606	rogid:d4mOZOyT5RubJjE+a8wQhsWR6WI9606	intact-crc:97F8E5900F25245C|rigid:hTSrmVdyJOwDZcm6RqjgnW+pEnI	false	flag tag:?-?	ha tag:?-?	-	-	psi-mi:"MI:0705"(anti tag western blot)	psi-mi:"MI:0705"(anti tag western blot)
uniprotkb:Q8IXJ6	uniprotkb:P11413	intact:EBI-477232|uniprotkb:O95889|uniprotkb:Q924Y7|uniprotkb:Q9P0G8|uniprotkb:Q9UNT0|uniprotkb:Q9Y6E9|ensembl:ENSP00000249396|ensembl:ENSP00000489602|uniprotkb:A8K3V1|uniprotkb:B2RB45|uniprotkb:U5TP13	intact:EBI-4289891|uniprotkb:Q8IU88|uniprotkb:D3DWX9|uniprotkb:Q16000|uniprotkb:Q16765|uniprotkb:Q8IUA6|uniprotkb:Q8IU70|uniprotkb:Q96PQ2|ensembl:ENSP00000377192|ensembl:ENSP00000377194	psi-mi:sir2_human(display_long)|uniprotkb:SIR2-like protein 2(gene name synonym)|uniprotkb:SIRT2(gene name)|psi-mi:SIRT2(display_short)|uniprotkb:SIR2L(gene name synonym)|uniprotkb:SIR2L2(gene name synonym)|uniprotkb:Regulatory protein SIR2 homolog 2(gene name synonym)	psi-mi:g6pd_human(display_long)|uniprotkb:G6PD(gene name)|psi-mi:G6PD(display_short)	psi-mi:"MI:0006"(anti bait coimmunoprecipitation)	Wang et al. (2014)	imex:IM-23514|pubmed:24769394	taxid:9606(human)|taxid:9606(Homo sapiens)	taxid:9606(human)|taxid:9606(Homo sapiens)	psi-mi:"MI:0915"(physical association)	psi-mi:"MI:0471"(MINT)	intact:EBI-9831161|imex:IM-23514-5	-	-	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0498"(prey)	psi-mi:"MI:0496"(bait)	psi-mi:"MI:0326"(protein)	psi-mi:"MI:0326"(protein)	ensembl:ENSG00000068903(gene)|ensembl:ENSG00000283100(gene)|ensembl:ENST00000249396(transcript)|ensembl:ENST00000634533(transcript)|go:"GO:0000122"(negative regulation of transcription by RNA polymerase II)|go:"GO:0000183"(rDNA heterochromatin assembly)|go:"GO:0000781"(chromosome, telomeric region)|go:"GO:0000792"(heterochromatin)|go:"GO:0003682"(chromatin binding)|go:"GO:0003950"(NAD+ ADP-ribosyltransferase activity)|go:"GO:0004407"(histone deacetylase activity)|go:"GO:0005634"(nucleus)|go:"GO:0005677"(chromatin silencing complex)|go:"GO:0005694"(chromosome)|go:"GO:0005730"(nucleolus)|go:"GO:0005737"(cytoplasm)|go:"GO:0005813"(centrosome)|go:"GO:0005814"(centriole)|go:"GO:0005819"(spindle)|go:"GO:0005829"(cytosol)|go:"GO:0005874"(microtubule)|go:"GO:0005886"(plasma membrane)|go:"GO:0006342"|go:"GO:0006348"|go:"GO:0006471"(protein ADP-ribosylation)|go:"GO:0006476"(protein deacetylation)|go:"GO:0006914"(autophagy)|go:"GO:0007084"(mitotic nuclear membrane reassembly)|go:"GO:0007096"(regulation of exit from mitosis)|go:"GO:0008134"(transcription factor binding)|rcsb pdb:6L66|rcsb pdb:6L71|rcsb pdb:6L72|rcsb pdb:6NR0|rcsb pdb:6QCN|rcsb pdb:7BOS|rcsb pdb:7BOT|reactome:R-HSA-2995383|rcsb pdb:5D7O|rcsb pdb:5D7P|rcsb pdb:5D7Q|rcsb pdb:5DY4|rcsb pdb:5DY5|rcsb pdb:5FYQ|rcsb pdb:5G4C|rcsb pdb:5MAR|rcsb pdb:5MAT|rcsb pdb:5Y0Z|rcsb pdb:5Y5N|rcsb pdb:5YQL|rcsb pdb:5YQM|rcsb pdb:5YQN|rcsb pdb:5YQO|rcsb pdb:6L65|go:"GO:0008270"(zinc ion binding)|go:"GO:0008285"(negative regulation of cell population proliferation)|go:"GO:0010507"(negative regulation of autophagy)|go:"GO:0010801"(negative regulation of peptidyl-threonine phosphorylation)|go:"GO:0014065"(phosphatidylinositol 3-kinase signaling)|go:"GO:0016575"(histone deacetylation)|go:"GO:0017136"(NAD-dependent histone deacetylase activity)|go:"GO:0021762"(substantia nigra development)|go:"GO:0022011"(myelination in peripheral nervous system)|go:"GO:0030426"(growth cone)|go:"GO:0030496"(midbody)|go:"GO:0031641"(regulation of myelination)|go:"GO:0032436"(positive regulation of proteasomal ubiquitin-dependent protein catabolic process)|go:"GO:0033010"(paranodal junction)|go:"GO:0033270"(paranode region of axon)|go:"GO:0033558"(protein deacetylase activity)|go:"GO:0034599"(cellular response to oxidative stress)|go:"GO:0034979"(NAD-dependent protein deacetylase activity)|go:"GO:0034983"(peptidyl-lysine deacetylation)|go:"GO:0035035"(histone acetyltransferase binding)|go:"GO:0035729"(cellular response to hepatocyte growth factor stimulus)|go:"GO:0042177"(negative regulation of protein catabolic process)|go:"GO:0042325"(regulation of phosphorylation)|go:"GO:0042826"(histone deacetylase binding)|go:"GO:0042903"(tubulin deacetylase activity)|go:"GO:0043130"(ubiquitin binding)|go:"GO:0043161"(proteasome-mediated ubiquitin-dependent protein catabolic process)|go:"GO:0043204"(perikaryon)|go:"GO:0043209"(myelin sheath)|go:"GO:0043219"(lateral loop)|go:"GO:0043220"(Schmidt-Lanterman incisure)|go:"GO:0043388"(positive regulation of DNA binding)|go:"GO:0043491"(protein kinase B signaling)|go:"GO:0044224"(juxtaparanode region of axon)|go:"GO:0044242"(cellular lipid catabolic process)|go:"GO:0045087"(innate immune response)|go:"GO:0045599"(negative regulation of fat cell differentiation)|go:"GO:0045836"(positive regulation of meiotic nuclear division)|go:"GO:0045843"(negative regulation of striated muscle tissue development)|go:"GO:0045892"(negative regulation of transcription, DNA-templated)|go:"GO:0045944"(positive regulation of transcription by RNA polymerase II)|go:"GO:0046970"("NAD-dependent histone deacetylase activity (H4-K16 specific)")|go:"GO:0048012"(hepatocyte growth factor receptor signaling pathway)|go:"GO:0048471"(perinuclear region of cytoplasm)|go:"GO:0051321"(meiotic cell cycle)|go:"GO:0051726"(regulation of cell cycle)|go:"GO:0051775"(response to redox state)|go:"GO:0051781"(positive regulation of cell division)|go:"GO:0051987"(positive regulation of attachment of spindle microtubules to kinetochore)|go:"GO:0061428"(negative regulation of transcription from RNA polymerase II promoter in response to hypoxia)|go:"GO:0061433"(cellular response to caloric restriction)|go:"GO:0070403"(NAD+ binding)|go:"GO:0070446"(negative regulation of oligodendrocyte progenitor proliferation)|go:"GO:0070932"(histone H3 deacetylation)|go:"GO:0070933"(histone H4 deacetylation)|go:"GO:0071219"(cellular response to molecule of bacterial origin)|go:"GO:0071456"(cellular response to hypoxia)|go:"GO:0071872"(cellular response to epinephrine stimulus)|go:"GO:0072686"(mitotic spindle)|go:"GO:0072687"(meiotic spindle)|go:"GO:0090042"(tubulin deacetylation)|go:"GO:0097386"(glial cell projection)|go:"GO:0140297"(DNA-binding transcription factor binding)|go:"GO:1900119"(positive regulation of execution phase of apoptosis)|go:"GO:1900195"(positive regulation of oocyte maturation)|go:"GO:1900425"(negative regulation of defense response to bacterium)|go:"GO:2000378"(negative regulation of reactive oxygen species metabolic process)|go:"GO:2000777"(positive regulation of proteasomal ubiquitin-dependent protein catabolic process involved in cellular response to hypoxia)|interpro:IPR003000(NAD-dependent histone deacetylase, silent information regulator Sir2)|interpro:IPR017328(NAD-dependent deacetylase sirtuin-2, eukaryota)|interpro:IPR026590|interpro:IPR026591|interpro:IPR029035|mint:Q8IXJ6|rcsb pdb:1J8F|rcsb pdb:3ZGO|rcsb pdb:3ZGV|rcsb pdb:4L3O|rcsb pdb:4R8M|rcsb pdb:4RMG|rcsb pdb:4RMH|rcsb pdb:4RMI|rcsb pdb:4RMJ|rcsb pdb:4X3O|rcsb pdb:4X3P|rcsb pdb:4Y6L|rcsb pdb:4Y6O|go:"GO:0051301"(cell division)|rcsb pdb:4Y6Q|refseq:NP_001180215.1|refseq:NP_036369.2|refseq:NP_085096.1|refseq:XP_011524956.1|refseq:XP_011524957.1|refseq:XP_006723174.1|dip:DIP-33350N	refseq:NP_000393.4|refseq:NP_001035810.1|ensembl:ENSG00000160211(gene)|ensembl:ENST00000393562(transcript)|ensembl:ENST00000393564(transcript)|go:"GO:0004345"(glucose-6-phosphate dehydrogenase activity)|go:"GO:0005536"(glucose binding)|go:"GO:0005634"(nucleus)|go:"GO:0005737"(cytoplasm)|go:"GO:0005829"(cytosol)|go:"GO:0006006"(glucose metabolic process)|go:"GO:0006098"(pentose-phosphate shunt)|go:"GO:0006629"(lipid metabolic process)|go:"GO:0006695"(cholesterol biosynthetic process)|go:"GO:0006739"(NADP metabolic process)|go:"GO:0006740"(NADPH regeneration)|go:"GO:0006749"(glutathione metabolic process)|go:"GO:0009051"(pentose-phosphate shunt, oxidative branch)|go:"GO:0009898"(cytoplasmic side of plasma membrane)|go:"GO:0010041"("response to iron(III) ion")|go:"GO:0010734"(negative regulation of protein glutathionylation)|go:"GO:0014070"(response to organic cyclic compound)|go:"GO:0016020"(membrane)|go:"GO:0019322"(pentose biosynthetic process)|go:"GO:0021762"(substantia nigra development)|go:"GO:0032094"(response to food)|go:"GO:0034451"(centriolar satellite)|go:"GO:0034599"(cellular response to oxidative stress)|go:"GO:0042802"(identical protein binding)|go:"GO:0042803"(protein homodimerization activity)|go:"GO:0043231"(intracellular membrane-bounded organelle)|go:"GO:0043249"(erythrocyte maturation)|go:"GO:0043523"(regulation of neuron apoptotic process)|go:"GO:0045471"(response to ethanol)|go:"GO:0046390"(ribose phosphate biosynthetic process)|go:"GO:0050661"(NADP binding)|go:"GO:0051156"(glucose 6-phosphate metabolic process)|go:"GO:0061052"(negative regulation of cell growth involved in cardiac muscle cell development)|go:"GO:0070062"(extracellular exosome)|go:"GO:1904879"(positive regulation of calcium ion transmembrane transport via high voltage-gated calcium channel)|go:"GO:2000378"(negative regulation of reactive oxygen species metabolic process)|interpro:IPR001282(Glucose-6-phosphate dehydrogenase)|interpro:IPR019796|interpro:IPR022674|interpro:IPR022675|interpro:IPR036291|rcsb pdb:1QKI|rcsb pdb:2BH9|rcsb pdb:2BHL|rcsb pdb:5UKW|rcsb pdb:6E07|rcsb pdb:6E08|rcsb pdb:6JYU|rcsb pdb:6VA0|rcsb pdb:6VA7|rcsb pdb:6VA8|rcsb pdb:6VA9|rcsb pdb:6VAQ|reactome:R-HSA-5628897|reactome:R-HSA-71336	-	-	-	figure legend:F6D|comment:"To test this hypothesis, we determined the interaction between  two differentially tagged G6PD proteins, G6PD-Flag and GFP-G6PD,  in HEK293T cells. We found that mutation of K171 to either R  (K171R) or Q (K171Q) did not affect the interaction between G6PD  subunits (Fig 2B). In contrast, substitution of K386Q, but not  K386R, impaired the interaction between G6PD subunits (Fig 2B).  Strikingly, substitution of K403Q, but not K403R, entirely disrupted  the interaction between G6PD subunits (Fig 2B). In addition, glutaraldehyde  cross-linking assay demonstrated that the K403Q mutant  displayed impaired ability to form dimers when compared to wildtype  G6PD or the K403R mutant (Fig 2C). Moreover, NAM treatment  decreased the binding by approximately 55% between the two  differentially tagged proteins of wild-type G6PD in a dose-dependent  manner (Fig 2D and Supplementary Fig S5). NAM treatment,  however, failed to affect the interaction between Flag-tagged and  GFP-tagged K403R mutant of G6PD (Fig 2D), further suggesting that  K403 acetylation largely hinders the interaction between G6PD  subunits."|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:9606(human-293t)|taxid:9606(Homo sapiens 293 cells transformed with SV40 large T antigen)	-	2014/10/07	2014/10/16	rogid:d4mOZOyT5RubJjE+a8wQhsWR6WI9606	rogid:qW8uk6xBGtrxlsosIH6gEG1ZfWA9606	intact-crc:64CDFB84DD6D3019|rigid:hTSrmVdyJOwDZcm6RqjgnW+pEnI	false	-	-	-	-	psi-mi:"MI:0113"(western blot)	psi-mi:"MI:0113"(western blot)