#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:P09622	uniprotkb:P09622	intact:EBI-353366|uniprotkb:Q14131|uniprotkb:Q14167|uniprotkb:Q59EV8|uniprotkb:Q8WTS4|uniprotkb:B2R5X0|ensembl:ENSP00000205402|ensembl:ENSP00000390667|uniprotkb:B4DHG0|uniprotkb:B4DT69	intact:EBI-353366|uniprotkb:Q14131|uniprotkb:Q14167|uniprotkb:Q59EV8|uniprotkb:Q8WTS4|uniprotkb:B2R5X0|ensembl:ENSP00000205402|ensembl:ENSP00000390667|uniprotkb:B4DHG0|uniprotkb:B4DT69	psi-mi:dldh_human(display_long)|uniprotkb:DLD(gene name)|psi-mi:DLD(display_short)|uniprotkb:GCSL(gene name synonym)|uniprotkb:LAD(gene name synonym)|uniprotkb:PHE3(gene name synonym)|uniprotkb:Dihydrolipoamide dehydrogenase(gene name synonym)|uniprotkb:Glycine cleavage system L protein(gene name synonym)	psi-mi:dldh_human(display_long)|uniprotkb:DLD(gene name)|psi-mi:DLD(display_short)|uniprotkb:GCSL(gene name synonym)|uniprotkb:LAD(gene name synonym)|uniprotkb:PHE3(gene name synonym)|uniprotkb:Dihydrolipoamide dehydrogenase(gene name synonym)|uniprotkb:Glycine cleavage system L protein(gene name synonym)	psi-mi:"MI:0114"(x-ray crystallography)	Ciszak et al. (2006)	imex:IM-14543|pubmed:16263718	taxid:9606(human)|taxid:9606(Homo sapiens)	taxid:9606(human)|taxid:9606(Homo sapiens)	psi-mi:"MI:0407"(direct interaction)	psi-mi:"MI:0469"(IntAct)	intact:EBI-966791|rcsb pdb:1ZY8|imex:IM-14543-1	-	psi-mi:"MI:1060"(spoke expansion)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0326"(protein)	psi-mi:"MI:0326"(protein)	refseq:NP_001276679.1|refseq:NP_000099.2|rcsb pdb:6I4Z|go:"GO:0006103"(2-oxoglutarate metabolic process)|go:"GO:0006120"(mitochondrial electron transport, NADH to ubiquinone)|go:"GO:0006508"(proteolysis)|go:"GO:0007369"(gastrulation)|go:"GO:0007568"(aging)|go:"GO:0009106"(lipoate metabolic process)|go:"GO:0031514"(motile cilium)|go:"GO:0042391"(regulation of membrane potential)|go:"GO:0043159"(acrosomal matrix)|go:"GO:0043544"(lipoamide binding)|ensembl:ENSG00000091140(gene)|ensembl:ENST00000205402(transcript)|ensembl:ENST00000417551(transcript)|go:"GO:0004148"(dihydrolipoyl dehydrogenase activity)|go:"GO:0005634"(nucleus)|go:"GO:0005739"(mitochondrion)|go:"GO:0005759"(mitochondrial matrix)|reactome:R-HSA-204174|reactome:R-HSA-389661|reactome:R-HSA-5362517|reactome:R-HSA-6783984|reactome:R-HSA-70268|reactome:R-HSA-70895|reactome:R-HSA-71064|reactome:R-HSA-71403|go:"GO:0045252"(oxoglutarate dehydrogenase complex)|go:"GO:0045254"(pyruvate dehydrogenase complex)|go:"GO:0045454"(cell redox homeostasis)|go:"GO:0048240"(sperm capacitation)|go:"GO:0050660"(flavin adenine dinucleotide binding)|go:"GO:0051068"(dihydrolipoamide metabolic process)|go:"GO:0051287"(NAD binding)|go:"GO:0061732"(mitochondrial acetyl-CoA biosynthetic process from pyruvate)|go:"GO:0106077"(histone succinylation)|interpro:IPR001100(Pyridine nucleotide-disulphide oxidoreductase, class I)|interpro:IPR004099(Pyridine nucleotide-disulphide oxidoreductase, dimerisation)|interpro:IPR006258(Dihydrolipoamide dehydrogenase)|interpro:IPR012999(Pyridine nucleotide-disulphide oxidoreductase, class I, active site)|interpro:IPR016156(FAD/NAD-linked reductase, dimerisation)|interpro:IPR023753|interpro:IPR036188|mint:P09622|rcsb pdb:1ZMC|rcsb pdb:1ZMD|rcsb pdb:1ZY8|rcsb pdb:2F5Z|rcsb pdb:3RNM|rcsb pdb:5J5Z|rcsb pdb:5NHG|rcsb pdb:6HG8|rcsb pdb:6I4P|rcsb pdb:6I4Q|rcsb pdb:6I4R|rcsb pdb:6I4S|rcsb pdb:6I4T|rcsb pdb:6I4U|refseq:NP_001276680.1|refseq:NP_001276681.1|dip:DIP-29027N	refseq:NP_001276679.1|refseq:NP_000099.2|rcsb pdb:6I4Z|go:"GO:0006103"(2-oxoglutarate metabolic process)|go:"GO:0006120"(mitochondrial electron transport, NADH to ubiquinone)|go:"GO:0006508"(proteolysis)|go:"GO:0007369"(gastrulation)|go:"GO:0007568"(aging)|go:"GO:0009106"(lipoate metabolic process)|go:"GO:0031514"(motile cilium)|go:"GO:0042391"(regulation of membrane potential)|go:"GO:0043159"(acrosomal matrix)|go:"GO:0043544"(lipoamide binding)|ensembl:ENSG00000091140(gene)|ensembl:ENST00000205402(transcript)|ensembl:ENST00000417551(transcript)|go:"GO:0004148"(dihydrolipoyl dehydrogenase activity)|go:"GO:0005634"(nucleus)|go:"GO:0005739"(mitochondrion)|go:"GO:0005759"(mitochondrial matrix)|reactome:R-HSA-204174|reactome:R-HSA-389661|reactome:R-HSA-5362517|reactome:R-HSA-6783984|reactome:R-HSA-70268|reactome:R-HSA-70895|reactome:R-HSA-71064|reactome:R-HSA-71403|go:"GO:0045252"(oxoglutarate dehydrogenase complex)|go:"GO:0045254"(pyruvate dehydrogenase complex)|go:"GO:0045454"(cell redox homeostasis)|go:"GO:0048240"(sperm capacitation)|go:"GO:0050660"(flavin adenine dinucleotide binding)|go:"GO:0051068"(dihydrolipoamide metabolic process)|go:"GO:0051287"(NAD binding)|go:"GO:0061732"(mitochondrial acetyl-CoA biosynthetic process from pyruvate)|go:"GO:0106077"(histone succinylation)|interpro:IPR001100(Pyridine nucleotide-disulphide oxidoreductase, class I)|interpro:IPR004099(Pyridine nucleotide-disulphide oxidoreductase, dimerisation)|interpro:IPR006258(Dihydrolipoamide dehydrogenase)|interpro:IPR012999(Pyridine nucleotide-disulphide oxidoreductase, class I, active site)|interpro:IPR016156(FAD/NAD-linked reductase, dimerisation)|interpro:IPR023753|interpro:IPR036188|mint:P09622|rcsb pdb:1ZMC|rcsb pdb:1ZMD|rcsb pdb:1ZY8|rcsb pdb:2F5Z|rcsb pdb:3RNM|rcsb pdb:5J5Z|rcsb pdb:5NHG|rcsb pdb:6HG8|rcsb pdb:6I4P|rcsb pdb:6I4Q|rcsb pdb:6I4R|rcsb pdb:6I4S|rcsb pdb:6I4T|rcsb pdb:6I4U|refseq:NP_001276680.1|refseq:NP_001276681.1|dip:DIP-29027N	-	caution:This sequence has been withdrawn from Uniprot.|crc64:7613492C516F3835	caution:This sequence has been withdrawn from Uniprot.|crc64:7613492C516F3835	comment:"The  crystalline subcomplex was obtained from the solution containing both  proteins at a subunit molar ratio of 2:1, thus corresponding to one E3 (DLD, UniProt accession number  P09622)  dimer/E3BPdd (PDHX, UniProt accession number O00330) molecule."|3d-r-factors:R working = 20.8% R free = 27.5%|3d-resolution:2.6 Angstroms|figure legend:Figure 3 Table 2|3d-structure:The hydrophobic residues Pro133, Pro154, and Ile157 in the E3-binding domain  of E3BP insert themselves into the surface of both E3 polypeptide  chains. Numerous ionic and hydrogen bonds between the residues  of three interacting polypeptide chains adjacent to the central  hydrophobic patch add to the stability of the subcomplex.|dataset:BioCreative - Critical Assessment of Information Extraction systems in Biology|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2006/07/10	2014/10/16	rogid:7Yf9KyBWf18686aOXVUwab65rl89606	rogid:7Yf9KyBWf18686aOXVUwab65rl89606	intact-crc:016CE5237D9DB174|rigid:iQOScbotTnb6ZVcidOQORnw8jt4	false	binding-associated region:444-444|binding-associated region:348-348|binding-associated region:447-447|binding-associated region:437-437|binding-associated region:438-438|binding-associated region:413-413|binding-associated region:443-443|binding-associated region:437-437|binding-associated region:439-439|binding-associated region:348-348|binding-associated region:444-444|binding-associated region:438-438	binding-associated region:437-437|binding-associated region:444-444|binding-associated region:447-447|binding-associated region:438-438|binding-associated region:413-413|binding-associated region:443-443|binding-associated region:438-438|binding-associated region:437-437|binding-associated region:439-439|binding-associated region:444-444|binding-associated region:444-444|binding-associated region:438-438|binding-associated region:438-438|binding-associated region:447-447	-	-	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)
uniprotkb:P09622	uniprotkb:O00330	intact:EBI-353366|uniprotkb:Q14131|uniprotkb:Q14167|uniprotkb:Q59EV8|uniprotkb:Q8WTS4|uniprotkb:B2R5X0|ensembl:ENSP00000205402|ensembl:ENSP00000390667|uniprotkb:B4DHG0|uniprotkb:B4DT69	intact:EBI-751566|uniprotkb:O60221|uniprotkb:Q96FV8|uniprotkb:Q99783|uniprotkb:D3DR11|uniprotkb:E9PB14|uniprotkb:B4DW62|uniprotkb:E9PBP7|ensembl:ENSP00000227868	psi-mi:dldh_human(display_long)|uniprotkb:DLD(gene name)|psi-mi:DLD(display_short)|uniprotkb:GCSL(gene name synonym)|uniprotkb:LAD(gene name synonym)|uniprotkb:PHE3(gene name synonym)|uniprotkb:Dihydrolipoamide dehydrogenase(gene name synonym)|uniprotkb:Glycine cleavage system L protein(gene name synonym)	psi-mi:odpx_human(display_long)|uniprotkb:Dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex(gene name synonym)|uniprotkb:Lipoyl-containing pyruvate dehydrogenase complex component X(gene name synonym)|uniprotkb:E3-binding protein(gene name synonym)|uniprotkb:proX(gene name synonym)|uniprotkb:PDHX(gene name)|psi-mi:PDHX(display_short)|uniprotkb:PDX1(gene name synonym)	psi-mi:"MI:0114"(x-ray crystallography)	Ciszak et al. (2006)	imex:IM-14543|pubmed:16263718	taxid:9606(human)|taxid:9606(Homo sapiens)	taxid:9606(human)|taxid:9606(Homo sapiens)	psi-mi:"MI:0407"(direct interaction)	psi-mi:"MI:0469"(IntAct)	intact:EBI-966791|rcsb pdb:1ZY8|imex:IM-14543-1	-	psi-mi:"MI:1060"(spoke expansion)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0326"(protein)	psi-mi:"MI:0326"(protein)	refseq:NP_001276679.1|refseq:NP_000099.2|rcsb pdb:6I4Z|go:"GO:0006103"(2-oxoglutarate metabolic process)|go:"GO:0006120"(mitochondrial electron transport, NADH to ubiquinone)|go:"GO:0006508"(proteolysis)|go:"GO:0007369"(gastrulation)|go:"GO:0007568"(aging)|go:"GO:0009106"(lipoate metabolic process)|go:"GO:0031514"(motile cilium)|go:"GO:0042391"(regulation of membrane potential)|go:"GO:0043159"(acrosomal matrix)|go:"GO:0043544"(lipoamide binding)|ensembl:ENSG00000091140(gene)|ensembl:ENST00000205402(transcript)|ensembl:ENST00000417551(transcript)|go:"GO:0004148"(dihydrolipoyl dehydrogenase activity)|go:"GO:0005634"(nucleus)|go:"GO:0005739"(mitochondrion)|go:"GO:0005759"(mitochondrial matrix)|reactome:R-HSA-204174|reactome:R-HSA-389661|reactome:R-HSA-5362517|reactome:R-HSA-6783984|reactome:R-HSA-70268|reactome:R-HSA-70895|reactome:R-HSA-71064|reactome:R-HSA-71403|go:"GO:0045252"(oxoglutarate dehydrogenase complex)|go:"GO:0045254"(pyruvate dehydrogenase complex)|go:"GO:0045454"(cell redox homeostasis)|go:"GO:0048240"(sperm capacitation)|go:"GO:0050660"(flavin adenine dinucleotide binding)|go:"GO:0051068"(dihydrolipoamide metabolic process)|go:"GO:0051287"(NAD binding)|go:"GO:0061732"(mitochondrial acetyl-CoA biosynthetic process from pyruvate)|go:"GO:0106077"(histone succinylation)|interpro:IPR001100(Pyridine nucleotide-disulphide oxidoreductase, class I)|interpro:IPR004099(Pyridine nucleotide-disulphide oxidoreductase, dimerisation)|interpro:IPR006258(Dihydrolipoamide dehydrogenase)|interpro:IPR012999(Pyridine nucleotide-disulphide oxidoreductase, class I, active site)|interpro:IPR016156(FAD/NAD-linked reductase, dimerisation)|interpro:IPR023753|interpro:IPR036188|mint:P09622|rcsb pdb:1ZMC|rcsb pdb:1ZMD|rcsb pdb:1ZY8|rcsb pdb:2F5Z|rcsb pdb:3RNM|rcsb pdb:5J5Z|rcsb pdb:5NHG|rcsb pdb:6HG8|rcsb pdb:6I4P|rcsb pdb:6I4Q|rcsb pdb:6I4R|rcsb pdb:6I4S|rcsb pdb:6I4T|rcsb pdb:6I4U|refseq:NP_001276680.1|refseq:NP_001276681.1|dip:DIP-29027N	refseq:NP_001128496.1|refseq:NP_001159630.1|refseq:NP_003468.2|dip:DIP-29026N|ensembl:ENSG00000110435(gene)|ensembl:ENST00000227868(transcript)|go:"GO:0005739"(mitochondrion)|go:"GO:0005759"(mitochondrial matrix)|go:"GO:0016746"(acyltransferase activity)|go:"GO:0045254"(pyruvate dehydrogenase complex)|go:"GO:0061732"(mitochondrial acetyl-CoA biosynthetic process from pyruvate)|interpro:IPR000089(Biotin/lipoyl attachment)|interpro:IPR001078(Catalytic domain of components of various dehydrogenase complexes)|interpro:IPR003016(2-oxo acid dehydrogenase, lipoyl-binding site)|interpro:IPR004167(E3 binding)|interpro:IPR011053(Single hybrid motif)|interpro:IPR023213|interpro:IPR036625|mint:O00330|rcsb pdb:1ZY8|rcsb pdb:2DNC|rcsb pdb:2F5Z|rcsb pdb:2F60|rcsb pdb:6H60|reactome:R-HSA-204174|reactome:R-HSA-389661|reactome:R-HSA-5362517|reactome:R-HSA-70268	-	caution:This sequence has been withdrawn from Uniprot.|crc64:7613492C516F3835	-	comment:"The  crystalline subcomplex was obtained from the solution containing both  proteins at a subunit molar ratio of 2:1, thus corresponding to one E3 (DLD, UniProt accession number  P09622)  dimer/E3BPdd (PDHX, UniProt accession number O00330) molecule."|3d-r-factors:R working = 20.8% R free = 27.5%|3d-resolution:2.6 Angstroms|figure legend:Figure 3 Table 2|3d-structure:The hydrophobic residues Pro133, Pro154, and Ile157 in the E3-binding domain  of E3BP insert themselves into the surface of both E3 polypeptide  chains. Numerous ionic and hydrogen bonds between the residues  of three interacting polypeptide chains adjacent to the central  hydrophobic patch add to the stability of the subcomplex.|dataset:BioCreative - Critical Assessment of Information Extraction systems in Biology|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2006/07/10	2014/10/16	rogid:7Yf9KyBWf18686aOXVUwab65rl89606	rogid:fcQCBKmyySLi0lr+SQKUkPy+rwE9606	intact-crc:016CE5237D9DB174|rigid:iQOScbotTnb6ZVcidOQORnw8jt4	false	binding-associated region:444-444|binding-associated region:348-348|binding-associated region:447-447|binding-associated region:437-437|binding-associated region:438-438|binding-associated region:413-413|binding-associated region:443-443|binding-associated region:437-437|binding-associated region:439-439|binding-associated region:348-348|binding-associated region:444-444|binding-associated region:438-438	binding-associated region:132-132|binding-associated region:133-133|binding-associated region:134-134|binding-associated region:137-137|binding-associated region:154-154|binding-associated region:155-155|binding-associated region:157-157|binding-associated region:160-160|binding-associated region:136-136|binding-associated region:140-140|binding-associated region:155-155|sufficient binding region:1-221|binding-associated region:154-154|binding-associated region:160-160|binding-associated region:133-133|binding-associated region:136-136|binding-associated region:140-140|binding-associated region:155-155|binding-associated region:155-155|binding-associated region:133-133	-	-	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)