#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:P61823	uniprotkb:P17967	intact:EBI-908364|uniprotkb:P00656|uniprotkb:Q9TSF2|uniprotkb:A6QPW8|ensembl:ENSBTAP00000011586	intact:EBI-13012|uniprotkb:D6VQX3|ensemblfungi:YCL043C	psi-mi:rnas1_bovin(display_long)|uniprotkb:RNASE1(gene name)|psi-mi:RNASE1(display_short)|uniprotkb:RNS1(gene name synonym)|uniprotkb:RNase 1(gene name synonym)|uniprotkb:RNase A(gene name synonym)	psi-mi:pdi_yeast(display_long)|uniprotkb:TRG1(gene name synonym)|uniprotkb:YCL313(orf name)|uniprotkb:PDI1(gene name)|psi-mi:PDI1(display_short)|uniprotkb:MFP1(gene name synonym)|uniprotkb:Thioredoxin-related glycoprotein 1(gene name synonym)|uniprotkb:YCL43C(orf name)|uniprotkb:YCL043C(locus name)	psi-mi:"MI:0415"(enzymatic study)	Kulp et al. (2006)	imex:IM-14431|pubmed:16368681	taxid:9913(bovin)|taxid:9913("Bos taurus (Bovine)")	taxid:559292(yeast)|taxid:559292(Saccharomyces cerevisiae)	psi-mi:"MI:0414"(enzymatic reaction)	psi-mi:"MI:0469"(IntAct)	intact:EBI-978513|imex:IM-14431-2	-	-	psi-mi:"MI:0579"(electron donor)	psi-mi:"MI:0580"(electron acceptor)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0326"(protein)	psi-mi:"MI:0326"(protein)	refseq:NP_001014408.2|refseq:XP_005211519.1|dip:DIP-36384N|rcsb pdb:3RID|rcsb pdb:3RN3|rcsb pdb:3RSD|rcsb pdb:3RSK|rcsb pdb:3RSP|rcsb pdb:3SRN|rcsb pdb:4AO1|rcsb pdb:4G8V|rcsb pdb:4G8Y|rcsb pdb:4G90|rcsb pdb:4J5Z|rcsb pdb:4J60|rcsb pdb:4J61|rcsb pdb:4J62|rcsb pdb:4J63|rcsb pdb:4J64|rcsb pdb:4J65|rcsb pdb:4J66|rcsb pdb:3RH1|rcsb pdb:4J67|rcsb pdb:4J68|rcsb pdb:4J6A|rcsb pdb:4K7L|rcsb pdb:4K7M|rcsb pdb:4L55|rcsb pdb:4MXF|rcsb pdb:4O36|rcsb pdb:4O37|rcsb pdb:4OKF|rcsb pdb:4OOH|rcsb pdb:4OT4|rcsb pdb:4PEQ|rcsb pdb:4POU|rcsb pdb:4QH3|rcsb pdb:4RAT|rcsb pdb:4RSD|rcsb pdb:4RSK|rcsb pdb:4RTE|rcsb pdb:4S0Q|rcsb pdb:4S18|rcsb pdb:4SRN|rcsb pdb:4WYN|rcsb pdb:4WYP|rcsb pdb:4WYZ|rcsb pdb:4YGW|rcsb pdb:4ZZ4|rcsb pdb:5D6U|rcsb pdb:5D97|rcsb pdb:5E5E|rcsb pdb:5E5F|rcsb pdb:5ET4|rcsb pdb:5JLG|rcsb pdb:5JMG|rcsb pdb:4J69|rcsb pdb:5JML|rcsb pdb:5NA9|rcsb pdb:5NJ7|rcsb pdb:5OBD|rcsb pdb:5OBE|rcsb pdb:5OGH|rcsb pdb:5OLD|rcsb pdb:5RAT|rcsb pdb:5RSA|rcsb pdb:6ETK|rcsb pdb:6ETL|rcsb pdb:6ETM|rcsb pdb:6ETN|rcsb pdb:6ETO|rcsb pdb:6ETP|rcsb pdb:6ETQ|rcsb pdb:6ETR|rcsb pdb:6F60|rcsb pdb:6GOK|rcsb pdb:6PVU|rcsb pdb:6PVV|rcsb pdb:6PVW|rcsb pdb:6PVX|rcsb pdb:6QE9|rcsb pdb:6RAT|rcsb pdb:6RSA|rcsb pdb:6XHC|rcsb pdb:6XHD|rcsb pdb:6XHE|rcsb pdb:6XHF|rcsb pdb:6XVX|rcsb pdb:6XW0|rcsb pdb:6YO1|rcsb pdb:7RAT|rcsb pdb:7RSA|rcsb pdb:8RAT|rcsb pdb:8RSA|rcsb pdb:9RAT|rcsb pdb:9RSA|rcsb pdb:5OBC|ensembl:ENSBTAG00000008793(gene)|go:"GO:0003676"(nucleic acid binding)|go:"GO:0004522"(ribonuclease A activity)|go:"GO:0004540"(ribonuclease activity)|go:"GO:0005576"(extracellular region)|go:"GO:0016829"(lyase activity)|go:"GO:0090501"(RNA phosphodiester bond hydrolysis)|interpro:IPR001427(Pancreatic ribonuclease)|interpro:IPR023411|interpro:IPR023412|interpro:IPR036816|mint:P61823|rcsb pdb:1A2W|rcsb pdb:1A5P|rcsb pdb:1A5Q|rcsb pdb:1AFK|rcsb pdb:1AFL|rcsb pdb:1AFU|rcsb pdb:1AQP|rcsb pdb:1B6V|rcsb pdb:1BEL|rcsb pdb:1BZQ|rcsb pdb:1C0B|rcsb pdb:1C0C|rcsb pdb:1C8W|rcsb pdb:1C9V|rcsb pdb:1C9X|rcsb pdb:1CJQ|rcsb pdb:1CJR|rcsb pdb:1D5D|rcsb pdb:1D5E|rcsb pdb:1D5H|rcsb pdb:1DFJ|rcsb pdb:1DY5|rcsb pdb:1EIC|rcsb pdb:1EID|rcsb pdb:1EIE|rcsb pdb:1EOS|rcsb pdb:1EOW|rcsb pdb:1F0V|rcsb pdb:1FEV|ensembl:ENSBTAT00000011586(transcript)|rcsb pdb:1FS3|rcsb pdb:1GV7|rcsb pdb:1IZP|rcsb pdb:1IZQ|rcsb pdb:1IZR|rcsb pdb:1J7Z|rcsb pdb:1J80|rcsb pdb:1J81|rcsb pdb:1J82|rcsb pdb:1JN4|rcsb pdb:1JS0|rcsb pdb:1JVT|rcsb pdb:1JVU|rcsb pdb:1JVV|rcsb pdb:1KF2|rcsb pdb:1KF3|rcsb pdb:1KF4|rcsb pdb:1KF5|rcsb pdb:1KF7|rcsb pdb:1KF8|rcsb pdb:1KH8|rcsb pdb:1LSQ|rcsb pdb:1O0F|rcsb pdb:1O0H|rcsb pdb:1O0M|rcsb pdb:1O0N|rcsb pdb:1O0O|rcsb pdb:1QHC|rcsb pdb:1RAR|rcsb pdb:1RAS|rcsb pdb:1RAT|rcsb pdb:1RBB|rcsb pdb:1RBC|rcsb pdb:1RBD|rcsb pdb:1RBE|rcsb pdb:1RBF|rcsb pdb:1RBG|rcsb pdb:1RBH|rcsb pdb:1RBI|rcsb pdb:1RBJ|rcsb pdb:1RBN|rcsb pdb:1RBW|rcsb pdb:1RBX|rcsb pdb:1RCA|rcsb pdb:1RCN|rcsb pdb:1RHA|rcsb pdb:1RHB|rcsb pdb:1RNC|rcsb pdb:1RND|rcsb pdb:1RNM|rcsb pdb:1RNN|rcsb pdb:1RNO|rcsb pdb:1RNQ|rcsb pdb:1RNU|rcsb pdb:1RNV|rcsb pdb:1RNW|rcsb pdb:1RNX|rcsb pdb:1RNY|rcsb pdb:1RNZ|rcsb pdb:1ROB|rcsb pdb:1RPF|rcsb pdb:1RPG|rcsb pdb:1RPH|rcsb pdb:1RSM|rcsb pdb:1RTA|rcsb pdb:1RTB|rcsb pdb:1RUV|rcsb pdb:1SRN|rcsb pdb:1SSA|rcsb pdb:1SSB|rcsb pdb:1SSC|rcsb pdb:1U1B|rcsb pdb:1UN5|rcsb pdb:1W4O|rcsb pdb:1W4P|rcsb pdb:1W4Q|rcsb pdb:1WBU|rcsb pdb:1XPS|rcsb pdb:1XPT|rcsb pdb:1YMN|rcsb pdb:1YMR|rcsb pdb:1YMW|rcsb pdb:1Z3L|rcsb pdb:1Z3M|rcsb pdb:1Z3P|rcsb pdb:1Z6D|rcsb pdb:1Z6S|rcsb pdb:2AAS|rcsb pdb:2APQ|rcsb pdb:2APU|rcsb pdb:2BLP|rcsb pdb:2BLZ|rcsb pdb:2E33|rcsb pdb:2E3W|rcsb pdb:2G4W|rcsb pdb:2G4X|rcsb pdb:2G8Q|rcsb pdb:2G8R|rcsb pdb:2NUI|rcsb pdb:2OP2|rcsb pdb:2OQF|rcsb pdb:2P42|rcsb pdb:2P43|rcsb pdb:2P44|rcsb pdb:2P45|rcsb pdb:2P46|rcsb pdb:2P47|rcsb pdb:2P48|rcsb pdb:2P49|rcsb pdb:2P4A|rcsb pdb:2QCA|rcsb pdb:2RAT|rcsb pdb:2RLN|rcsb pdb:2RNS|rcsb pdb:2W5G|rcsb pdb:2W5I|rcsb pdb:2W5K|rcsb pdb:2W5L|rcsb pdb:2W5M|rcsb pdb:2XOG|rcsb pdb:2XOI|rcsb pdb:3A1R|rcsb pdb:3D6O|rcsb pdb:3D6P|rcsb pdb:3D6Q|rcsb pdb:3D7B|rcsb pdb:3D8Y|rcsb pdb:3D8Z|rcsb pdb:3DH5|rcsb pdb:3DH6|rcsb pdb:3DI7|rcsb pdb:3DI8|rcsb pdb:3DI9|rcsb pdb:3DIB|rcsb pdb:3DIC|rcsb pdb:3DXG|rcsb pdb:3DXH|rcsb pdb:3EUX|rcsb pdb:3EUY|rcsb pdb:3EUZ|rcsb pdb:3EV0|rcsb pdb:3EV1|rcsb pdb:3EV2|rcsb pdb:3EV3|rcsb pdb:3EV4|rcsb pdb:3EV5|rcsb pdb:3EV6|rcsb pdb:3FKZ|rcsb pdb:3FL0|rcsb pdb:3FL1|rcsb pdb:3FL3|rcsb pdb:3I67|rcsb pdb:3I6F|rcsb pdb:3I6H|rcsb pdb:3I6J|rcsb pdb:3I7W|rcsb pdb:3I7X|rcsb pdb:3I7Y|rcsb pdb:3JW1|rcsb pdb:3LXO|rcsb pdb:3MWQ|rcsb pdb:3MWR|rcsb pdb:3MX8|rcsb pdb:3MZQ|rcsb pdb:3MZR|rcsb pdb:3OQY|rcsb pdb:3OQZ|rcsb pdb:3OR0|rcsb pdb:3QL1|rcsb pdb:3QL2|rcsb pdb:3QSK|rcsb pdb:3RAT	refseq:NP_009887.1|sgd:S000000548|mint:P17967|dip:DIP-4978N|ensemblfungi:YCL043C(gene)|ensemblfungi:YCL043C_mRNA(transcript)|go:"GO:0003756"(protein disulfide isomerase activity)|go:"GO:0005783"(endoplasmic reticulum)|go:"GO:0005788"(endoplasmic reticulum lumen)|go:"GO:0006457"(protein folding)|go:"GO:0015035"(protein-disulfide reductase activity)|go:"GO:0034976"(response to endoplasmic reticulum stress)|go:"GO:0036508"(protein alpha-1,2-demannosylation)|go:"GO:0051082"(unfolded protein binding)|go:"GO:1904382"(mannose trimming involved in glycoprotein ERAD pathway)|interpro:IPR005792(Protein disulphide isomerase)|interpro:IPR013766(Thioredoxin domain)|interpro:IPR017937|interpro:IPR036249|rcsb pdb:2B5E|rcsb pdb:3BOA|reactome:R-SCE-901042	go:"GO:0016491"(oxidoreductase activity)|go:"GO:0003756"(protein disulfide isomerase activity)	-	crc64:69CF3E05D7F74C94	figure legend:2 A and B|comment:They followed native disulfide bond formation in refolding RNase A by monitoring its activity using the artificial substrate cCMP.|comment:"PDI mutant cys61ala-cys64ala and wild-type PDI have a similar ability to catalyze RNase A oxidation (Fig. 2C). Therefore, in comparing cys61ala-cys64ala and wild-type PDI, there is discordance between their rate.  of disulfide formation and the yield of native RNase A (Fig. 2, B and C)."|comment:"The re-oxidation of reduced RNaseA(15uM) was assayed by hydrolysis of  cCMP in the presence of Ero1p (0.05uM), FAD (100uM)."|comment:"even under conditions in which the rate of disulfide formation is  matched, they found that the Cys61-Al, Cys64Ala  PDI mutant has a much lower yield of functional RNase A than wild-type PDI (Fig. 3B)."|comment:"Together, the 2 PDI mutants can match the yield of refolded RNase A by wild-type PDI (Fig. 3C)."|comment:The presence of Erop1 and FAD was required.|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)	-	2006/07/27	2014/10/16	rogid:ifHI/UwVRIuj5ksIiZPB0pUY+0E9913	rogid:tyy52cf76yr9hl+9ggGGS4zDO/A559292	intact-crc:5D9BF67D32968CD1|rigid:cSKQy96Xo5VKpXhxhjbs82qbsLU	false	-	sufficient binding region:28-522|his tag:n-n|mutation decreasing interaction:61-61,64-64|mutation decreasing interaction:406-406,409-409	-	-	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)
uniprotkb:P61823	uniprotkb:P30101	intact:EBI-908364|uniprotkb:P00656|uniprotkb:Q9TSF2|uniprotkb:A6QPW8|ensembl:ENSBTAP00000011586	intact:EBI-979862|uniprotkb:Q13453|uniprotkb:Q14255|uniprotkb:Q8IYF8|uniprotkb:Q9UMU7|ensembl:ENSP00000300289	psi-mi:rnas1_bovin(display_long)|uniprotkb:RNASE1(gene name)|psi-mi:RNASE1(display_short)|uniprotkb:RNS1(gene name synonym)|uniprotkb:RNase 1(gene name synonym)|uniprotkb:RNase A(gene name synonym)	psi-mi:pdia3_human(display_long)|uniprotkb:Disulfide isomerase ER-60(gene name synonym)|uniprotkb:Endoplasmic reticulum resident protein 60(gene name synonym)|uniprotkb:58 kDa microsomal protein(gene name synonym)|uniprotkb:Endoplasmic reticulum resident protein 57(gene name synonym)|uniprotkb:58 kDa glucose-regulated protein(gene name synonym)|uniprotkb:PDIA3(gene name)|psi-mi:PDIA3(display_short)|uniprotkb:ERP60(gene name synonym)|uniprotkb:GRP58(gene name synonym)|uniprotkb:ERP57(gene name synonym)	psi-mi:"MI:0415"(enzymatic study)	Kulp et al. (2006)	imex:IM-14431|pubmed:16368681	taxid:9913(bovin)|taxid:9913("Bos taurus (Bovine)")	taxid:9606(human)|taxid:9606(Homo sapiens)	psi-mi:"MI:0414"(enzymatic reaction)	psi-mi:"MI:0469"(IntAct)	intact:EBI-979909|imex:IM-14431-1	-	-	psi-mi:"MI:0579"(electron donor)	psi-mi:"MI:0580"(electron acceptor)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0326"(protein)	psi-mi:"MI:0326"(protein)	refseq:NP_001014408.2|refseq:XP_005211519.1|dip:DIP-36384N|rcsb pdb:3RID|rcsb pdb:3RN3|rcsb pdb:3RSD|rcsb pdb:3RSK|rcsb pdb:3RSP|rcsb pdb:3SRN|rcsb pdb:4AO1|rcsb pdb:4G8V|rcsb pdb:4G8Y|rcsb pdb:4G90|rcsb pdb:4J5Z|rcsb pdb:4J60|rcsb pdb:4J61|rcsb pdb:4J62|rcsb pdb:4J63|rcsb pdb:4J64|rcsb pdb:4J65|rcsb pdb:4J66|rcsb pdb:3RH1|rcsb pdb:4J67|rcsb pdb:4J68|rcsb pdb:4J6A|rcsb pdb:4K7L|rcsb pdb:4K7M|rcsb pdb:4L55|rcsb pdb:4MXF|rcsb pdb:4O36|rcsb pdb:4O37|rcsb pdb:4OKF|rcsb pdb:4OOH|rcsb pdb:4OT4|rcsb pdb:4PEQ|rcsb pdb:4POU|rcsb pdb:4QH3|rcsb pdb:4RAT|rcsb pdb:4RSD|rcsb pdb:4RSK|rcsb pdb:4RTE|rcsb pdb:4S0Q|rcsb pdb:4S18|rcsb pdb:4SRN|rcsb pdb:4WYN|rcsb pdb:4WYP|rcsb pdb:4WYZ|rcsb pdb:4YGW|rcsb pdb:4ZZ4|rcsb pdb:5D6U|rcsb pdb:5D97|rcsb pdb:5E5E|rcsb pdb:5E5F|rcsb pdb:5ET4|rcsb pdb:5JLG|rcsb pdb:5JMG|rcsb pdb:4J69|rcsb pdb:5JML|rcsb pdb:5NA9|rcsb pdb:5NJ7|rcsb pdb:5OBD|rcsb pdb:5OBE|rcsb pdb:5OGH|rcsb pdb:5OLD|rcsb pdb:5RAT|rcsb pdb:5RSA|rcsb pdb:6ETK|rcsb pdb:6ETL|rcsb pdb:6ETM|rcsb pdb:6ETN|rcsb pdb:6ETO|rcsb pdb:6ETP|rcsb pdb:6ETQ|rcsb pdb:6ETR|rcsb pdb:6F60|rcsb pdb:6GOK|rcsb pdb:6PVU|rcsb pdb:6PVV|rcsb pdb:6PVW|rcsb pdb:6PVX|rcsb pdb:6QE9|rcsb pdb:6RAT|rcsb pdb:6RSA|rcsb pdb:6XHC|rcsb pdb:6XHD|rcsb pdb:6XHE|rcsb pdb:6XHF|rcsb pdb:6XVX|rcsb pdb:6XW0|rcsb pdb:6YO1|rcsb pdb:7RAT|rcsb pdb:7RSA|rcsb pdb:8RAT|rcsb pdb:8RSA|rcsb pdb:9RAT|rcsb pdb:9RSA|rcsb pdb:5OBC|ensembl:ENSBTAG00000008793(gene)|go:"GO:0003676"(nucleic acid binding)|go:"GO:0004522"(ribonuclease A activity)|go:"GO:0004540"(ribonuclease activity)|go:"GO:0005576"(extracellular region)|go:"GO:0016829"(lyase activity)|go:"GO:0090501"(RNA phosphodiester bond hydrolysis)|interpro:IPR001427(Pancreatic ribonuclease)|interpro:IPR023411|interpro:IPR023412|interpro:IPR036816|mint:P61823|rcsb pdb:1A2W|rcsb pdb:1A5P|rcsb pdb:1A5Q|rcsb pdb:1AFK|rcsb pdb:1AFL|rcsb pdb:1AFU|rcsb pdb:1AQP|rcsb pdb:1B6V|rcsb pdb:1BEL|rcsb pdb:1BZQ|rcsb pdb:1C0B|rcsb pdb:1C0C|rcsb pdb:1C8W|rcsb pdb:1C9V|rcsb pdb:1C9X|rcsb pdb:1CJQ|rcsb pdb:1CJR|rcsb pdb:1D5D|rcsb pdb:1D5E|rcsb pdb:1D5H|rcsb pdb:1DFJ|rcsb pdb:1DY5|rcsb pdb:1EIC|rcsb pdb:1EID|rcsb pdb:1EIE|rcsb pdb:1EOS|rcsb pdb:1EOW|rcsb pdb:1F0V|rcsb pdb:1FEV|ensembl:ENSBTAT00000011586(transcript)|rcsb pdb:1FS3|rcsb pdb:1GV7|rcsb pdb:1IZP|rcsb pdb:1IZQ|rcsb pdb:1IZR|rcsb pdb:1J7Z|rcsb pdb:1J80|rcsb pdb:1J81|rcsb pdb:1J82|rcsb pdb:1JN4|rcsb pdb:1JS0|rcsb pdb:1JVT|rcsb pdb:1JVU|rcsb pdb:1JVV|rcsb pdb:1KF2|rcsb pdb:1KF3|rcsb pdb:1KF4|rcsb pdb:1KF5|rcsb pdb:1KF7|rcsb pdb:1KF8|rcsb pdb:1KH8|rcsb pdb:1LSQ|rcsb pdb:1O0F|rcsb pdb:1O0H|rcsb pdb:1O0M|rcsb pdb:1O0N|rcsb pdb:1O0O|rcsb pdb:1QHC|rcsb pdb:1RAR|rcsb pdb:1RAS|rcsb pdb:1RAT|rcsb pdb:1RBB|rcsb pdb:1RBC|rcsb pdb:1RBD|rcsb pdb:1RBE|rcsb pdb:1RBF|rcsb pdb:1RBG|rcsb pdb:1RBH|rcsb pdb:1RBI|rcsb pdb:1RBJ|rcsb pdb:1RBN|rcsb pdb:1RBW|rcsb pdb:1RBX|rcsb pdb:1RCA|rcsb pdb:1RCN|rcsb pdb:1RHA|rcsb pdb:1RHB|rcsb pdb:1RNC|rcsb pdb:1RND|rcsb pdb:1RNM|rcsb pdb:1RNN|rcsb pdb:1RNO|rcsb pdb:1RNQ|rcsb pdb:1RNU|rcsb pdb:1RNV|rcsb pdb:1RNW|rcsb pdb:1RNX|rcsb pdb:1RNY|rcsb pdb:1RNZ|rcsb pdb:1ROB|rcsb pdb:1RPF|rcsb pdb:1RPG|rcsb pdb:1RPH|rcsb pdb:1RSM|rcsb pdb:1RTA|rcsb pdb:1RTB|rcsb pdb:1RUV|rcsb pdb:1SRN|rcsb pdb:1SSA|rcsb pdb:1SSB|rcsb pdb:1SSC|rcsb pdb:1U1B|rcsb pdb:1UN5|rcsb pdb:1W4O|rcsb pdb:1W4P|rcsb pdb:1W4Q|rcsb pdb:1WBU|rcsb pdb:1XPS|rcsb pdb:1XPT|rcsb pdb:1YMN|rcsb pdb:1YMR|rcsb pdb:1YMW|rcsb pdb:1Z3L|rcsb pdb:1Z3M|rcsb pdb:1Z3P|rcsb pdb:1Z6D|rcsb pdb:1Z6S|rcsb pdb:2AAS|rcsb pdb:2APQ|rcsb pdb:2APU|rcsb pdb:2BLP|rcsb pdb:2BLZ|rcsb pdb:2E33|rcsb pdb:2E3W|rcsb pdb:2G4W|rcsb pdb:2G4X|rcsb pdb:2G8Q|rcsb pdb:2G8R|rcsb pdb:2NUI|rcsb pdb:2OP2|rcsb pdb:2OQF|rcsb pdb:2P42|rcsb pdb:2P43|rcsb pdb:2P44|rcsb pdb:2P45|rcsb pdb:2P46|rcsb pdb:2P47|rcsb pdb:2P48|rcsb pdb:2P49|rcsb pdb:2P4A|rcsb pdb:2QCA|rcsb pdb:2RAT|rcsb pdb:2RLN|rcsb pdb:2RNS|rcsb pdb:2W5G|rcsb pdb:2W5I|rcsb pdb:2W5K|rcsb pdb:2W5L|rcsb pdb:2W5M|rcsb pdb:2XOG|rcsb pdb:2XOI|rcsb pdb:3A1R|rcsb pdb:3D6O|rcsb pdb:3D6P|rcsb pdb:3D6Q|rcsb pdb:3D7B|rcsb pdb:3D8Y|rcsb pdb:3D8Z|rcsb pdb:3DH5|rcsb pdb:3DH6|rcsb pdb:3DI7|rcsb pdb:3DI8|rcsb pdb:3DI9|rcsb pdb:3DIB|rcsb pdb:3DIC|rcsb pdb:3DXG|rcsb pdb:3DXH|rcsb pdb:3EUX|rcsb pdb:3EUY|rcsb pdb:3EUZ|rcsb pdb:3EV0|rcsb pdb:3EV1|rcsb pdb:3EV2|rcsb pdb:3EV3|rcsb pdb:3EV4|rcsb pdb:3EV5|rcsb pdb:3EV6|rcsb pdb:3FKZ|rcsb pdb:3FL0|rcsb pdb:3FL1|rcsb pdb:3FL3|rcsb pdb:3I67|rcsb pdb:3I6F|rcsb pdb:3I6H|rcsb pdb:3I6J|rcsb pdb:3I7W|rcsb pdb:3I7X|rcsb pdb:3I7Y|rcsb pdb:3JW1|rcsb pdb:3LXO|rcsb pdb:3MWQ|rcsb pdb:3MWR|rcsb pdb:3MX8|rcsb pdb:3MZQ|rcsb pdb:3MZR|rcsb pdb:3OQY|rcsb pdb:3OQZ|rcsb pdb:3OR0|rcsb pdb:3QL1|rcsb pdb:3QL2|rcsb pdb:3QSK|rcsb pdb:3RAT	interpro:IPR036249|interpro:IPR041868|mint:P30101|rcsb pdb:2ALB|rcsb pdb:2DMM|rcsb pdb:2H8L|rcsb pdb:3F8U|rcsb pdb:6ENY|reactome:R-HSA-1236974|reactome:R-HSA-901042|reactome:R-HSA-983170|interpro:IPR017937|ensembl:ENSG00000167004(gene)|ensembl:ENST00000300289(transcript)|go:"GO:0003723"(RNA binding)|go:"GO:0003756"(protein disulfide isomerase activity)|go:"GO:0004197"(cysteine-type endopeptidase activity)|go:"GO:0004629"(phospholipase C activity)|go:"GO:0005615"(extracellular space)|go:"GO:0005634"(nucleus)|go:"GO:0005783"(endoplasmic reticulum)|go:"GO:0005788"(endoplasmic reticulum lumen)|go:"GO:0005925"(focal adhesion)|go:"GO:0006457"(protein folding)|go:"GO:0009986"(cell surface)|go:"GO:0015035"(protein-disulfide reductase activity)|go:"GO:0015036"(disulfide oxidoreductase activity)|go:"GO:0034975"(protein folding in endoplasmic reticulum)|go:"GO:0034976"(response to endoplasmic reticulum stress)|go:"GO:0042470"(melanosome)|go:"GO:0042802"(identical protein binding)|go:"GO:0042824"(MHC class I peptide loading complex)|go:"GO:0045335"(phagocytic vesicle)|go:"GO:0055038"(recycling endosome membrane)|go:"GO:0070062"(extracellular exosome)|go:"GO:0098761"(cellular response to interleukin-7)|go:"GO:2001238"(positive regulation of extrinsic apoptotic signaling pathway)|interpro:IPR005788(Disulphide isomerase)|interpro:IPR005792(Protein disulphide isomerase)|interpro:IPR013766(Thioredoxin domain)|refseq:NP_005304.3|dip:DIP-29132N	go:"GO:0016491"(oxidoreductase activity)|go:"GO:0003756"(protein disulfide isomerase activity)	-	-	figure legend:6 E|comment:"The re-oxidation of reduced RNase A (15 M) was assayed by hydrolysis of cCMP in the presence of Ero1p at the indicated concentrations, FAD."|comment:ERp57 is less effective than PDI at isomerization of incorrect disulfides.|comment:The presence of Ero1p and FAD was required.|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)	-	2006/07/27	2014/10/16	rogid:ifHI/UwVRIuj5ksIiZPB0pUY+0E9913	rogid:N/XktiLWB/cPju9nCq6yeyXnO1Q9606	intact-crc:23CDEFD77CF92F5A|rigid:O8hu+ufef6wjNJqkjc87ygJr4mY	false	-	his tag:n-n	-	-	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)
uniprotkb:P61823	uniprotkb:P17967	intact:EBI-908364|uniprotkb:P00656|uniprotkb:Q9TSF2|uniprotkb:A6QPW8|ensembl:ENSBTAP00000011586	intact:EBI-13012|uniprotkb:D6VQX3|ensemblfungi:YCL043C	psi-mi:rnas1_bovin(display_long)|uniprotkb:RNASE1(gene name)|psi-mi:RNASE1(display_short)|uniprotkb:RNS1(gene name synonym)|uniprotkb:RNase 1(gene name synonym)|uniprotkb:RNase A(gene name synonym)	psi-mi:pdi_yeast(display_long)|uniprotkb:TRG1(gene name synonym)|uniprotkb:YCL313(orf name)|uniprotkb:PDI1(gene name)|psi-mi:PDI1(display_short)|uniprotkb:MFP1(gene name synonym)|uniprotkb:Thioredoxin-related glycoprotein 1(gene name synonym)|uniprotkb:YCL43C(orf name)|uniprotkb:YCL043C(locus name)	psi-mi:"MI:0017"(classical fluorescence spectroscopy)	Kulp et al. (2006)	imex:IM-14431|pubmed:16368681	taxid:9913(bovin)|taxid:9913("Bos taurus (Bovine)")	taxid:559292(yeast)|taxid:559292(Saccharomyces cerevisiae)	psi-mi:"MI:0414"(enzymatic reaction)	psi-mi:"MI:0469"(IntAct)	intact:EBI-978566|imex:IM-14431-5	-	-	psi-mi:"MI:0579"(electron donor)	psi-mi:"MI:0580"(electron acceptor)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0326"(protein)	psi-mi:"MI:0326"(protein)	refseq:NP_001014408.2|refseq:XP_005211519.1|dip:DIP-36384N|rcsb pdb:3RID|rcsb pdb:3RN3|rcsb pdb:3RSD|rcsb pdb:3RSK|rcsb pdb:3RSP|rcsb pdb:3SRN|rcsb pdb:4AO1|rcsb pdb:4G8V|rcsb pdb:4G8Y|rcsb pdb:4G90|rcsb pdb:4J5Z|rcsb pdb:4J60|rcsb pdb:4J61|rcsb pdb:4J62|rcsb pdb:4J63|rcsb pdb:4J64|rcsb pdb:4J65|rcsb pdb:4J66|rcsb pdb:3RH1|rcsb pdb:4J67|rcsb pdb:4J68|rcsb pdb:4J6A|rcsb pdb:4K7L|rcsb pdb:4K7M|rcsb pdb:4L55|rcsb pdb:4MXF|rcsb pdb:4O36|rcsb pdb:4O37|rcsb pdb:4OKF|rcsb pdb:4OOH|rcsb pdb:4OT4|rcsb pdb:4PEQ|rcsb pdb:4POU|rcsb pdb:4QH3|rcsb pdb:4RAT|rcsb pdb:4RSD|rcsb pdb:4RSK|rcsb pdb:4RTE|rcsb pdb:4S0Q|rcsb pdb:4S18|rcsb pdb:4SRN|rcsb pdb:4WYN|rcsb pdb:4WYP|rcsb pdb:4WYZ|rcsb pdb:4YGW|rcsb pdb:4ZZ4|rcsb pdb:5D6U|rcsb pdb:5D97|rcsb pdb:5E5E|rcsb pdb:5E5F|rcsb pdb:5ET4|rcsb pdb:5JLG|rcsb pdb:5JMG|rcsb pdb:4J69|rcsb pdb:5JML|rcsb pdb:5NA9|rcsb pdb:5NJ7|rcsb pdb:5OBD|rcsb pdb:5OBE|rcsb pdb:5OGH|rcsb pdb:5OLD|rcsb pdb:5RAT|rcsb pdb:5RSA|rcsb pdb:6ETK|rcsb pdb:6ETL|rcsb pdb:6ETM|rcsb pdb:6ETN|rcsb pdb:6ETO|rcsb pdb:6ETP|rcsb pdb:6ETQ|rcsb pdb:6ETR|rcsb pdb:6F60|rcsb pdb:6GOK|rcsb pdb:6PVU|rcsb pdb:6PVV|rcsb pdb:6PVW|rcsb pdb:6PVX|rcsb pdb:6QE9|rcsb pdb:6RAT|rcsb pdb:6RSA|rcsb pdb:6XHC|rcsb pdb:6XHD|rcsb pdb:6XHE|rcsb pdb:6XHF|rcsb pdb:6XVX|rcsb pdb:6XW0|rcsb pdb:6YO1|rcsb pdb:7RAT|rcsb pdb:7RSA|rcsb pdb:8RAT|rcsb pdb:8RSA|rcsb pdb:9RAT|rcsb pdb:9RSA|rcsb pdb:5OBC|ensembl:ENSBTAG00000008793(gene)|go:"GO:0003676"(nucleic acid binding)|go:"GO:0004522"(ribonuclease A activity)|go:"GO:0004540"(ribonuclease activity)|go:"GO:0005576"(extracellular region)|go:"GO:0016829"(lyase activity)|go:"GO:0090501"(RNA phosphodiester bond hydrolysis)|interpro:IPR001427(Pancreatic ribonuclease)|interpro:IPR023411|interpro:IPR023412|interpro:IPR036816|mint:P61823|rcsb pdb:1A2W|rcsb pdb:1A5P|rcsb pdb:1A5Q|rcsb pdb:1AFK|rcsb pdb:1AFL|rcsb pdb:1AFU|rcsb pdb:1AQP|rcsb pdb:1B6V|rcsb pdb:1BEL|rcsb pdb:1BZQ|rcsb pdb:1C0B|rcsb pdb:1C0C|rcsb pdb:1C8W|rcsb pdb:1C9V|rcsb pdb:1C9X|rcsb pdb:1CJQ|rcsb pdb:1CJR|rcsb pdb:1D5D|rcsb pdb:1D5E|rcsb pdb:1D5H|rcsb pdb:1DFJ|rcsb pdb:1DY5|rcsb pdb:1EIC|rcsb pdb:1EID|rcsb pdb:1EIE|rcsb pdb:1EOS|rcsb pdb:1EOW|rcsb pdb:1F0V|rcsb pdb:1FEV|ensembl:ENSBTAT00000011586(transcript)|rcsb pdb:1FS3|rcsb pdb:1GV7|rcsb pdb:1IZP|rcsb pdb:1IZQ|rcsb pdb:1IZR|rcsb pdb:1J7Z|rcsb pdb:1J80|rcsb pdb:1J81|rcsb pdb:1J82|rcsb pdb:1JN4|rcsb pdb:1JS0|rcsb pdb:1JVT|rcsb pdb:1JVU|rcsb pdb:1JVV|rcsb pdb:1KF2|rcsb pdb:1KF3|rcsb pdb:1KF4|rcsb pdb:1KF5|rcsb pdb:1KF7|rcsb pdb:1KF8|rcsb pdb:1KH8|rcsb pdb:1LSQ|rcsb pdb:1O0F|rcsb pdb:1O0H|rcsb pdb:1O0M|rcsb pdb:1O0N|rcsb pdb:1O0O|rcsb pdb:1QHC|rcsb pdb:1RAR|rcsb pdb:1RAS|rcsb pdb:1RAT|rcsb pdb:1RBB|rcsb pdb:1RBC|rcsb pdb:1RBD|rcsb pdb:1RBE|rcsb pdb:1RBF|rcsb pdb:1RBG|rcsb pdb:1RBH|rcsb pdb:1RBI|rcsb pdb:1RBJ|rcsb pdb:1RBN|rcsb pdb:1RBW|rcsb pdb:1RBX|rcsb pdb:1RCA|rcsb pdb:1RCN|rcsb pdb:1RHA|rcsb pdb:1RHB|rcsb pdb:1RNC|rcsb pdb:1RND|rcsb pdb:1RNM|rcsb pdb:1RNN|rcsb pdb:1RNO|rcsb pdb:1RNQ|rcsb pdb:1RNU|rcsb pdb:1RNV|rcsb pdb:1RNW|rcsb pdb:1RNX|rcsb pdb:1RNY|rcsb pdb:1RNZ|rcsb pdb:1ROB|rcsb pdb:1RPF|rcsb pdb:1RPG|rcsb pdb:1RPH|rcsb pdb:1RSM|rcsb pdb:1RTA|rcsb pdb:1RTB|rcsb pdb:1RUV|rcsb pdb:1SRN|rcsb pdb:1SSA|rcsb pdb:1SSB|rcsb pdb:1SSC|rcsb pdb:1U1B|rcsb pdb:1UN5|rcsb pdb:1W4O|rcsb pdb:1W4P|rcsb pdb:1W4Q|rcsb pdb:1WBU|rcsb pdb:1XPS|rcsb pdb:1XPT|rcsb pdb:1YMN|rcsb pdb:1YMR|rcsb pdb:1YMW|rcsb pdb:1Z3L|rcsb pdb:1Z3M|rcsb pdb:1Z3P|rcsb pdb:1Z6D|rcsb pdb:1Z6S|rcsb pdb:2AAS|rcsb pdb:2APQ|rcsb pdb:2APU|rcsb pdb:2BLP|rcsb pdb:2BLZ|rcsb pdb:2E33|rcsb pdb:2E3W|rcsb pdb:2G4W|rcsb pdb:2G4X|rcsb pdb:2G8Q|rcsb pdb:2G8R|rcsb pdb:2NUI|rcsb pdb:2OP2|rcsb pdb:2OQF|rcsb pdb:2P42|rcsb pdb:2P43|rcsb pdb:2P44|rcsb pdb:2P45|rcsb pdb:2P46|rcsb pdb:2P47|rcsb pdb:2P48|rcsb pdb:2P49|rcsb pdb:2P4A|rcsb pdb:2QCA|rcsb pdb:2RAT|rcsb pdb:2RLN|rcsb pdb:2RNS|rcsb pdb:2W5G|rcsb pdb:2W5I|rcsb pdb:2W5K|rcsb pdb:2W5L|rcsb pdb:2W5M|rcsb pdb:2XOG|rcsb pdb:2XOI|rcsb pdb:3A1R|rcsb pdb:3D6O|rcsb pdb:3D6P|rcsb pdb:3D6Q|rcsb pdb:3D7B|rcsb pdb:3D8Y|rcsb pdb:3D8Z|rcsb pdb:3DH5|rcsb pdb:3DH6|rcsb pdb:3DI7|rcsb pdb:3DI8|rcsb pdb:3DI9|rcsb pdb:3DIB|rcsb pdb:3DIC|rcsb pdb:3DXG|rcsb pdb:3DXH|rcsb pdb:3EUX|rcsb pdb:3EUY|rcsb pdb:3EUZ|rcsb pdb:3EV0|rcsb pdb:3EV1|rcsb pdb:3EV2|rcsb pdb:3EV3|rcsb pdb:3EV4|rcsb pdb:3EV5|rcsb pdb:3EV6|rcsb pdb:3FKZ|rcsb pdb:3FL0|rcsb pdb:3FL1|rcsb pdb:3FL3|rcsb pdb:3I67|rcsb pdb:3I6F|rcsb pdb:3I6H|rcsb pdb:3I6J|rcsb pdb:3I7W|rcsb pdb:3I7X|rcsb pdb:3I7Y|rcsb pdb:3JW1|rcsb pdb:3LXO|rcsb pdb:3MWQ|rcsb pdb:3MWR|rcsb pdb:3MX8|rcsb pdb:3MZQ|rcsb pdb:3MZR|rcsb pdb:3OQY|rcsb pdb:3OQZ|rcsb pdb:3OR0|rcsb pdb:3QL1|rcsb pdb:3QL2|rcsb pdb:3QSK|rcsb pdb:3RAT	refseq:NP_009887.1|sgd:S000000548|mint:P17967|dip:DIP-4978N|ensemblfungi:YCL043C(gene)|ensemblfungi:YCL043C_mRNA(transcript)|go:"GO:0003756"(protein disulfide isomerase activity)|go:"GO:0005783"(endoplasmic reticulum)|go:"GO:0005788"(endoplasmic reticulum lumen)|go:"GO:0006457"(protein folding)|go:"GO:0015035"(protein-disulfide reductase activity)|go:"GO:0034976"(response to endoplasmic reticulum stress)|go:"GO:0036508"(protein alpha-1,2-demannosylation)|go:"GO:0051082"(unfolded protein binding)|go:"GO:1904382"(mannose trimming involved in glycoprotein ERAD pathway)|interpro:IPR005792(Protein disulphide isomerase)|interpro:IPR013766(Thioredoxin domain)|interpro:IPR017937|interpro:IPR036249|rcsb pdb:2B5E|rcsb pdb:3BOA|reactome:R-SCE-901042	go:"GO:0016491"(oxidoreductase activity)|go:"GO:0003756"(protein disulfide isomerase activity)	-	crc64:69CF3E05D7F74C94	figure legend:3 A|kinetics:"They found that at 3 uM, the N-terminal active site has over a 4-fold defect in the initial rate of oxidation when compared with wild-type PDI (Fig. 3A). In contrast, as seen previously  the Cys61Ala, Cys64Ala  mutant has a rate of oxidation that is close to that of wild-type PDI, and when the Ero1p concentration is increased modestly (1.3-fold), the initial rates of oxidation can be matched (Fig. 3A)."|comment:The presence of Ero1p and FAD was required.|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)	-	2006/07/27	2014/10/16	rogid:ifHI/UwVRIuj5ksIiZPB0pUY+0E9913	rogid:tyy52cf76yr9hl+9ggGGS4zDO/A559292	intact-crc:95EE30DB11A371F6|rigid:cSKQy96Xo5VKpXhxhjbs82qbsLU	false	-	sufficient binding region:28-522|his tag:n-n|mutation decreasing interaction:61-61,64-64|mutation decreasing interaction:406-406,409-409	1	1	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)
uniprotkb:P17967	uniprotkb:Q03103	intact:EBI-13012|uniprotkb:D6VQX3|ensemblfungi:YCL043C	intact:EBI-27991|uniprotkb:E9P913|uniprotkb:D6W0F5|ensemblfungi:YML130C	psi-mi:pdi_yeast(display_long)|uniprotkb:TRG1(gene name synonym)|uniprotkb:YCL313(orf name)|uniprotkb:PDI1(gene name)|psi-mi:PDI1(display_short)|uniprotkb:MFP1(gene name synonym)|uniprotkb:Thioredoxin-related glycoprotein 1(gene name synonym)|uniprotkb:YCL43C(orf name)|uniprotkb:YCL043C(locus name)	psi-mi:ero1_yeast(display_long)|uniprotkb:ERO1(gene name)|psi-mi:ERO1(display_short)|uniprotkb:Endoplasmic reticulum oxidoreductase protein 1(gene name synonym)|uniprotkb:YM4987.05C(orf name)|uniprotkb:YML130C(locus name)	psi-mi:"MI:0017"(classical fluorescence spectroscopy)	Kulp et al. (2006)	imex:IM-14431|pubmed:16368681	taxid:559292(yeast)|taxid:559292(Saccharomyces cerevisiae)	taxid:559292(yeast)|taxid:559292(Saccharomyces cerevisiae)	psi-mi:"MI:0414"(enzymatic reaction)	psi-mi:"MI:0469"(IntAct)	intact:EBI-979825|imex:IM-14431-3	-	-	psi-mi:"MI:0579"(electron donor)	psi-mi:"MI:0580"(electron acceptor)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0326"(protein)	psi-mi:"MI:0326"(protein)	refseq:NP_009887.1|sgd:S000000548|mint:P17967|dip:DIP-4978N|ensemblfungi:YCL043C(gene)|ensemblfungi:YCL043C_mRNA(transcript)|go:"GO:0003756"(protein disulfide isomerase activity)|go:"GO:0005783"(endoplasmic reticulum)|go:"GO:0005788"(endoplasmic reticulum lumen)|go:"GO:0006457"(protein folding)|go:"GO:0015035"(protein-disulfide reductase activity)|go:"GO:0034976"(response to endoplasmic reticulum stress)|go:"GO:0036508"(protein alpha-1,2-demannosylation)|go:"GO:0051082"(unfolded protein binding)|go:"GO:1904382"(mannose trimming involved in glycoprotein ERAD pathway)|interpro:IPR005792(Protein disulphide isomerase)|interpro:IPR013766(Thioredoxin domain)|interpro:IPR017937|interpro:IPR036249|rcsb pdb:2B5E|rcsb pdb:3BOA|reactome:R-SCE-901042	refseq:NP_013576.1|sgd:S000004599|dip:DIP-4515N|ensemblfungi:YML130C(gene)|ensemblfungi:YML130C_mRNA(transcript)|go:"GO:0003756"(protein disulfide isomerase activity)|go:"GO:0005783"(endoplasmic reticulum)|go:"GO:0005789"(endoplasmic reticulum membrane)|go:"GO:0015035"(protein-disulfide reductase activity)|go:"GO:0016972"(thiol oxidase activity)|go:"GO:0034975"(protein folding in endoplasmic reticulum)|go:"GO:0071949"(FAD binding)|interpro:IPR007266(Endoplasmic reticulum oxidoreductin 1)|interpro:IPR037192|rcsb pdb:1RP4|rcsb pdb:1RQ1|rcsb pdb:3M31|rcsb pdb:3NVJ	go:"GO:0016491"(oxidoreductase activity)|go:"GO:0003756"(protein disulfide isomerase activity)	crc64:69CF3E05D7F74C94	-	figure legend:4 A and C, 5 A|kinetics:"the rate of oxidation is linearly dependent on PDI concentration. The rate of oxidation of PDI at the indicated concentrations was monitored in the presence of Ero1p (0.3uM) and/or FAD (20uM)"|kinetics:"the cys406ala, cys409ala mutant appeared to be oxidized more slowly than the cys61ala, cys64ala mutant and they compared their initial rates of oxidation and found that there is a 2-fold disparity in the ability of Ero1p to oxidize the two active sites (Fig.  4C). Additionally, we found that the sum of the initial rates of oxidation of the 2 mutants is equal to the rate of oxidation of PDI  strongly suggesting that the two domains are oxidized independently  (Fig. 4C)."|comment:The presence of FAD is required.|comment:"the rate of oxidation of the A prime domain is half that of the cys61ala, cys64ala mutant indicating that the enhanced rate of oxidation of the A prime domain in the full-length protein is contingent on the presence of the A domain (Fig. 4C)."|inhibition:"RNase A protects the N-terminal active site of PDI from oxidation by Ero1p and this protection depends on the presence of the substrate binding domains (B prime A prime)(Fig. 5 A)."|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)	-	2006/07/27	2014/10/16	rogid:tyy52cf76yr9hl+9ggGGS4zDO/A559292	rogid:x+wF7CknUMJq/2RnwpkuDVnNlq0559292	intact-crc:6E96134CDB0C14E3|rigid:3MvQ0TQHCvC7o9vUwV/cUUQsBKE	false	his tag:n-n|mutation decreasing interaction:61-61,64-64|mutation decreasing interaction:406-406,409-409|sufficient binding region:28-522|sufficient binding region:471-522|sufficient binding region:174-276	tag:c-c	1	-	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)
uniprotkb:P30101	uniprotkb:Q03103	intact:EBI-979862|uniprotkb:Q13453|uniprotkb:Q14255|uniprotkb:Q8IYF8|uniprotkb:Q9UMU7|ensembl:ENSP00000300289	intact:EBI-27991|uniprotkb:E9P913|uniprotkb:D6W0F5|ensemblfungi:YML130C	psi-mi:pdia3_human(display_long)|uniprotkb:Disulfide isomerase ER-60(gene name synonym)|uniprotkb:Endoplasmic reticulum resident protein 60(gene name synonym)|uniprotkb:58 kDa microsomal protein(gene name synonym)|uniprotkb:Endoplasmic reticulum resident protein 57(gene name synonym)|uniprotkb:58 kDa glucose-regulated protein(gene name synonym)|uniprotkb:PDIA3(gene name)|psi-mi:PDIA3(display_short)|uniprotkb:ERP60(gene name synonym)|uniprotkb:GRP58(gene name synonym)|uniprotkb:ERP57(gene name synonym)	psi-mi:ero1_yeast(display_long)|uniprotkb:ERO1(gene name)|psi-mi:ERO1(display_short)|uniprotkb:Endoplasmic reticulum oxidoreductase protein 1(gene name synonym)|uniprotkb:YM4987.05C(orf name)|uniprotkb:YML130C(locus name)	psi-mi:"MI:0017"(classical fluorescence spectroscopy)	Kulp et al. (2006)	imex:IM-14431|pubmed:16368681	taxid:9606(human)|taxid:9606(Homo sapiens)	taxid:559292(yeast)|taxid:559292(Saccharomyces cerevisiae)	psi-mi:"MI:0414"(enzymatic reaction)	psi-mi:"MI:0469"(IntAct)	intact:EBI-979886|imex:IM-14431-4	-	-	psi-mi:"MI:0579"(electron donor)	psi-mi:"MI:0580"(electron acceptor)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0326"(protein)	psi-mi:"MI:0326"(protein)	interpro:IPR036249|interpro:IPR041868|mint:P30101|rcsb pdb:2ALB|rcsb pdb:2DMM|rcsb pdb:2H8L|rcsb pdb:3F8U|rcsb pdb:6ENY|reactome:R-HSA-1236974|reactome:R-HSA-901042|reactome:R-HSA-983170|interpro:IPR017937|ensembl:ENSG00000167004(gene)|ensembl:ENST00000300289(transcript)|go:"GO:0003723"(RNA binding)|go:"GO:0003756"(protein disulfide isomerase activity)|go:"GO:0004197"(cysteine-type endopeptidase activity)|go:"GO:0004629"(phospholipase C activity)|go:"GO:0005615"(extracellular space)|go:"GO:0005634"(nucleus)|go:"GO:0005783"(endoplasmic reticulum)|go:"GO:0005788"(endoplasmic reticulum lumen)|go:"GO:0005925"(focal adhesion)|go:"GO:0006457"(protein folding)|go:"GO:0009986"(cell surface)|go:"GO:0015035"(protein-disulfide reductase activity)|go:"GO:0015036"(disulfide oxidoreductase activity)|go:"GO:0034975"(protein folding in endoplasmic reticulum)|go:"GO:0034976"(response to endoplasmic reticulum stress)|go:"GO:0042470"(melanosome)|go:"GO:0042802"(identical protein binding)|go:"GO:0042824"(MHC class I peptide loading complex)|go:"GO:0045335"(phagocytic vesicle)|go:"GO:0055038"(recycling endosome membrane)|go:"GO:0070062"(extracellular exosome)|go:"GO:0098761"(cellular response to interleukin-7)|go:"GO:2001238"(positive regulation of extrinsic apoptotic signaling pathway)|interpro:IPR005788(Disulphide isomerase)|interpro:IPR005792(Protein disulphide isomerase)|interpro:IPR013766(Thioredoxin domain)|refseq:NP_005304.3|dip:DIP-29132N	refseq:NP_013576.1|sgd:S000004599|dip:DIP-4515N|ensemblfungi:YML130C(gene)|ensemblfungi:YML130C_mRNA(transcript)|go:"GO:0003756"(protein disulfide isomerase activity)|go:"GO:0005783"(endoplasmic reticulum)|go:"GO:0005789"(endoplasmic reticulum membrane)|go:"GO:0015035"(protein-disulfide reductase activity)|go:"GO:0016972"(thiol oxidase activity)|go:"GO:0034975"(protein folding in endoplasmic reticulum)|go:"GO:0071949"(FAD binding)|interpro:IPR007266(Endoplasmic reticulum oxidoreductin 1)|interpro:IPR037192|rcsb pdb:1RP4|rcsb pdb:1RQ1|rcsb pdb:3M31|rcsb pdb:3NVJ	go:"GO:0016491"(oxidoreductase activity)|go:"GO:0003756"(protein disulfide isomerase activity)	-	-	figure legend:6 A, B, C|comment:the ERp57 active sites lack intrinsic asymmetry, since the rates of oxidation of the individual thioredoxin domains together add up to the rate of oxidation of ERp57.|comment:The presence of alkylated RNAse A does not affect the rate of oxidation of ERp57 by Ero1p.|comment:The presence of FAD is required.|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)	-	2006/07/27	2014/10/16	rogid:N/XktiLWB/cPju9nCq6yeyXnO1Q9606	rogid:x+wF7CknUMJq/2RnwpkuDVnNlq0559292	intact-crc:5521D80985065B37|rigid:OPoY6FPqq5Gyw/uRv1G7nLaW8LA	false	his tag:n-n|sufficient binding region:1-112|sufficient binding region:353-473	tag:c-c	-	-	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)