#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:Q2M3L1	uniprotkb:Q2M3L1	intact:EBI-8760964	intact:EBI-8760964	psi-mi:q2m3l1_human(display_long)|uniprotkb:TRPV3(gene name)|psi-mi:TRPV3(display_short)	psi-mi:q2m3l1_human(display_long)|uniprotkb:TRPV3(gene name)|psi-mi:TRPV3(display_short)	psi-mi:"MI:0071"(molecular sieving)	Kol et al. (2013)	pubmed:24028292|imex:IM-21430	taxid:9606(human)|taxid:9606(Homo sapiens)	taxid:9606(human)|taxid:9606(Homo sapiens)	psi-mi:"MI:0407"(direct interaction)	psi-mi:"MI:0471"(MINT)	intact:EBI-8760955|imex:IM-21430-1	-	-	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)	interpro:IPR036770|interpro:IPR024862|interpro:IPR002110(Ankyrin)|interpro:IPR020683|interpro:IPR005821(Ion transport)|interpro:IPR008347(Vanilloid receptor)|interpro:IPR024866|go:"GO:0005216"(ion channel activity)|go:"GO:0009266"(response to temperature stimulus)|go:"GO:0016021"(integral component of membrane)|go:"GO:0042802"(identical protein binding)	interpro:IPR036770|interpro:IPR024862|interpro:IPR002110(Ankyrin)|interpro:IPR020683|interpro:IPR005821(Ion transport)|interpro:IPR008347(Vanilloid receptor)|interpro:IPR024866|go:"GO:0005216"(ion channel activity)|go:"GO:0009266"(response to temperature stimulus)|go:"GO:0016021"(integral component of membrane)|go:"GO:0042802"(identical protein binding)	-	-	-	figure legend:f6a|comment:"All TRP channels are thought to form tetrameric assemblies [25]. To establish whether purified TRPV3 is  correctly folded and form homo-oligomers, we decided to use native PAGE. As mentioned in the previous  section TRPV3 forms a high molecular weight shoulder when eluting from a Superdex 200 column (Fig. 6A).  We pooled and analyzed the TRPV3 shoulder and peak separately into a high (HMW) and a low (LMW)  molecular weight pool and analyzed them by native PAGE. Although dimers (denoted by an asterisk at circa  200 kDa) and tetramers (denoted by an arrow at circa 400 kDa) are detected in both pools, we found that  the HMW pool has a higher fraction of tetrameric assemblies and that the LMW pool has a higher fraction  of dimeric assemblies. No monomeric or trimeric species were detected. In addition, when the LMW pool is  collected conservatively avoiding any HMW material (Fig. 6A, shaded area), and reanalyzed by gel filtration,  the tetrameric shoulder is again observed (Fig. 6A, inset). We conclude that purified TRPV3 forms both  dimers and tetramers in solution and that these species are in equilibrium."|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2013/09/13	2014/10/16	rogid:YcUgNSSqbvmuBtg9g5CyJWACaGU9606	rogid:YcUgNSSqbvmuBtg9g5CyJWACaGU9606	intact-crc:8A9EC14D4033ECB3|rigid:JngxQPmvxvNv8pqXSrUcslU5MW4	false	-	-	4	0	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)
uniprotkb:Q2M3L1	uniprotkb:Q2M3L1	intact:EBI-8760964	intact:EBI-8760964	psi-mi:q2m3l1_human(display_long)|uniprotkb:TRPV3(gene name)|psi-mi:TRPV3(display_short)	psi-mi:q2m3l1_human(display_long)|uniprotkb:TRPV3(gene name)|psi-mi:TRPV3(display_short)	psi-mi:"MI:0071"(molecular sieving)	Kol et al. (2013)	pubmed:24028292|imex:IM-21430	taxid:9606(human)|taxid:9606(Homo sapiens)	taxid:9606(human)|taxid:9606(Homo sapiens)	psi-mi:"MI:0407"(direct interaction)	psi-mi:"MI:0471"(MINT)	intact:EBI-8761045|imex:IM-21430-2	-	-	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)	interpro:IPR036770|interpro:IPR024862|interpro:IPR002110(Ankyrin)|interpro:IPR020683|interpro:IPR005821(Ion transport)|interpro:IPR008347(Vanilloid receptor)|interpro:IPR024866|go:"GO:0005216"(ion channel activity)|go:"GO:0009266"(response to temperature stimulus)|go:"GO:0016021"(integral component of membrane)|go:"GO:0042802"(identical protein binding)	interpro:IPR036770|interpro:IPR024862|interpro:IPR002110(Ankyrin)|interpro:IPR020683|interpro:IPR005821(Ion transport)|interpro:IPR008347(Vanilloid receptor)|interpro:IPR024866|go:"GO:0005216"(ion channel activity)|go:"GO:0009266"(response to temperature stimulus)|go:"GO:0016021"(integral component of membrane)|go:"GO:0042802"(identical protein binding)	-	-	-	figure legend:f6a|comment:"All TRP channels are thought to form tetrameric assemblies [25]. To establish whether purified TRPV3 is  correctly folded and form homo-oligomers, we decided to use native PAGE. As mentioned in the previous  section TRPV3 forms a high molecular weight shoulder when eluting from a Superdex 200 column (Fig. 6A).  We pooled and analyzed the TRPV3 shoulder and peak separately into a high (HMW) and a low (LMW)  molecular weight pool and analyzed them by native PAGE. Although dimers (denoted by an asterisk at circa  200 kDa) and tetramers (denoted by an arrow at circa 400 kDa) are detected in both pools, we found that  the HMW pool has a higher fraction of tetrameric assemblies and that the LMW pool has a higher fraction  of dimeric assemblies. No monomeric or trimeric species were detected. In addition, when the LMW pool is  collected conservatively avoiding any HMW material (Fig. 6A, shaded area), and reanalyzed by gel filtration,  the tetrameric shoulder is again observed (Fig. 6A, inset). We conclude that purified TRPV3 forms both  dimers and tetramers in solution and that these species are in equilibrium."|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2013/09/13	2014/10/16	rogid:YcUgNSSqbvmuBtg9g5CyJWACaGU9606	rogid:YcUgNSSqbvmuBtg9g5CyJWACaGU9606	intact-crc:5B4816B834C6B764|rigid:XZo9ZXcw30cpcphnnL+JyiakJSg	false	-	-	1	1	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)
uniprotkb:Q2M3L1	uniprotkb:Q2M3L1	intact:EBI-8760964	intact:EBI-8760964	psi-mi:q2m3l1_human(display_long)|uniprotkb:TRPV3(gene name)|psi-mi:TRPV3(display_short)	psi-mi:q2m3l1_human(display_long)|uniprotkb:TRPV3(gene name)|psi-mi:TRPV3(display_short)	psi-mi:"MI:0276"(blue native page)	Kol et al. (2013)	pubmed:24028292|imex:IM-21430	taxid:9606(human)|taxid:9606(Homo sapiens)	taxid:9606(human)|taxid:9606(Homo sapiens)	psi-mi:"MI:0407"(direct interaction)	psi-mi:"MI:0471"(MINT)	intact:EBI-8761067|imex:IM-21430-4	-	-	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)	interpro:IPR036770|interpro:IPR024862|interpro:IPR002110(Ankyrin)|interpro:IPR020683|interpro:IPR005821(Ion transport)|interpro:IPR008347(Vanilloid receptor)|interpro:IPR024866|go:"GO:0005216"(ion channel activity)|go:"GO:0009266"(response to temperature stimulus)|go:"GO:0016021"(integral component of membrane)|go:"GO:0042802"(identical protein binding)	interpro:IPR036770|interpro:IPR024862|interpro:IPR002110(Ankyrin)|interpro:IPR020683|interpro:IPR005821(Ion transport)|interpro:IPR008347(Vanilloid receptor)|interpro:IPR024866|go:"GO:0005216"(ion channel activity)|go:"GO:0009266"(response to temperature stimulus)|go:"GO:0016021"(integral component of membrane)|go:"GO:0042802"(identical protein binding)	-	-	-	figure legend:f6b|comment:"All TRP channels are thought to form tetrameric assemblies [25]. To establish whether purified TRPV3 is  correctly folded and form homo-oligomers, we decided to use native PAGE. As mentioned in the previous  section TRPV3 forms a high molecular weight shoulder when eluting from a Superdex 200 column (Fig. 6A).  We pooled and analyzed the TRPV3 shoulder and peak separately into a high (HMW) and a low (LMW)  molecular weight pool and analyzed them by native PAGE. Although dimers (denoted by an asterisk at circa  200 kDa) and tetramers (denoted by an arrow at circa 400 kDa) are detected in both pools, we found that  the HMW pool has a higher fraction of tetrameric assemblies and that the LMW pool has a higher fraction  of dimeric assemblies. No monomeric or trimeric species were detected. In addition, when the LMW pool is  collected conservatively avoiding any HMW material (Fig. 6A, shaded area), and reanalyzed by gel filtration,  the tetrameric shoulder is again observed (Fig. 6A, inset). We conclude that purified TRPV3 forms both  dimers and tetramers in solution and that these species are in equilibrium."|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2013/09/13	2014/10/16	rogid:YcUgNSSqbvmuBtg9g5CyJWACaGU9606	rogid:YcUgNSSqbvmuBtg9g5CyJWACaGU9606	intact-crc:2C9E08D11A9A967D|rigid:XZo9ZXcw30cpcphnnL+JyiakJSg	false	-	-	1	1	psi-mi:"MI:0818"(molecular weight estimation by coomasie staining)	psi-mi:"MI:0818"(molecular weight estimation by coomasie staining)
uniprotkb:Q2M3L1	uniprotkb:Q2M3L1	intact:EBI-8760964	intact:EBI-8760964	psi-mi:q2m3l1_human(display_long)|uniprotkb:TRPV3(gene name)|psi-mi:TRPV3(display_short)	psi-mi:q2m3l1_human(display_long)|uniprotkb:TRPV3(gene name)|psi-mi:TRPV3(display_short)	psi-mi:"MI:0276"(blue native page)	Kol et al. (2013)	pubmed:24028292|imex:IM-21430	taxid:9606(human)|taxid:9606(Homo sapiens)	taxid:9606(human)|taxid:9606(Homo sapiens)	psi-mi:"MI:0407"(direct interaction)	psi-mi:"MI:0471"(MINT)	intact:EBI-8761064|imex:IM-21430-3	-	-	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)	interpro:IPR036770|interpro:IPR024862|interpro:IPR002110(Ankyrin)|interpro:IPR020683|interpro:IPR005821(Ion transport)|interpro:IPR008347(Vanilloid receptor)|interpro:IPR024866|go:"GO:0005216"(ion channel activity)|go:"GO:0009266"(response to temperature stimulus)|go:"GO:0016021"(integral component of membrane)|go:"GO:0042802"(identical protein binding)	interpro:IPR036770|interpro:IPR024862|interpro:IPR002110(Ankyrin)|interpro:IPR020683|interpro:IPR005821(Ion transport)|interpro:IPR008347(Vanilloid receptor)|interpro:IPR024866|go:"GO:0005216"(ion channel activity)|go:"GO:0009266"(response to temperature stimulus)|go:"GO:0016021"(integral component of membrane)|go:"GO:0042802"(identical protein binding)	-	-	-	figure legend:f6b|comment:"All TRP channels are thought to form tetrameric assemblies [25]. To establish whether purified TRPV3 is  correctly folded and form homo-oligomers, we decided to use native PAGE. As mentioned in the previous  section TRPV3 forms a high molecular weight shoulder when eluting from a Superdex 200 column (Fig. 6A).  We pooled and analyzed the TRPV3 shoulder and peak separately into a high (HMW) and a low (LMW)  molecular weight pool and analyzed them by native PAGE. Although dimers (denoted by an asterisk at circa  200 kDa) and tetramers (denoted by an arrow at circa 400 kDa) are detected in both pools, we found that  the HMW pool has a higher fraction of tetrameric assemblies and that the LMW pool has a higher fraction  of dimeric assemblies. No monomeric or trimeric species were detected. In addition, when the LMW pool is  collected conservatively avoiding any HMW material (Fig. 6A, shaded area), and reanalyzed by gel filtration,  the tetrameric shoulder is again observed (Fig. 6A, inset). We conclude that purified TRPV3 forms both  dimers and tetramers in solution and that these species are in equilibrium."|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2013/09/13	2014/10/16	rogid:YcUgNSSqbvmuBtg9g5CyJWACaGU9606	rogid:YcUgNSSqbvmuBtg9g5CyJWACaGU9606	intact-crc:FD48DF246E6FCDAA|rigid:JngxQPmvxvNv8pqXSrUcslU5MW4	false	-	-	4	0	psi-mi:"MI:0818"(molecular weight estimation by coomasie staining)	psi-mi:"MI:0818"(molecular weight estimation by coomasie staining)
uniprotkb:Q2M3L1	uniprotkb:Q2M3L1	intact:EBI-8760964	intact:EBI-8760964	psi-mi:q2m3l1_human(display_long)|uniprotkb:TRPV3(gene name)|psi-mi:TRPV3(display_short)	psi-mi:q2m3l1_human(display_long)|uniprotkb:TRPV3(gene name)|psi-mi:TRPV3(display_short)	psi-mi:"MI:0276"(blue native page)	Kol et al. (2013)	pubmed:24028292|imex:IM-21430	taxid:9606(human)|taxid:9606(Homo sapiens)	taxid:9606(human)|taxid:9606(Homo sapiens)	psi-mi:"MI:0407"(direct interaction)	psi-mi:"MI:0471"(MINT)	intact:EBI-8761079|imex:IM-21430-5	-	-	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)	interpro:IPR036770|interpro:IPR024862|interpro:IPR002110(Ankyrin)|interpro:IPR020683|interpro:IPR005821(Ion transport)|interpro:IPR008347(Vanilloid receptor)|interpro:IPR024866|go:"GO:0005216"(ion channel activity)|go:"GO:0009266"(response to temperature stimulus)|go:"GO:0016021"(integral component of membrane)|go:"GO:0042802"(identical protein binding)	interpro:IPR036770|interpro:IPR024862|interpro:IPR002110(Ankyrin)|interpro:IPR020683|interpro:IPR005821(Ion transport)|interpro:IPR008347(Vanilloid receptor)|interpro:IPR024866|go:"GO:0005216"(ion channel activity)|go:"GO:0009266"(response to temperature stimulus)|go:"GO:0016021"(integral component of membrane)|go:"GO:0042802"(identical protein binding)	-	-	-	figure legend:f6b|comment:"All TRP channels are thought to form tetrameric assemblies [25]. To establish whether purified TRPV3 is  correctly folded and form homo-oligomers, we decided to use native PAGE. As mentioned in the previous  section TRPV3 forms a high molecular weight shoulder when eluting from a Superdex 200 column (Fig. 6A).  We pooled and analyzed the TRPV3 shoulder and peak separately into a high (HMW) and a low (LMW)  molecular weight pool and analyzed them by native PAGE. Although dimers (denoted by an asterisk at circa  200 kDa) and tetramers (denoted by an arrow at circa 400 kDa) are detected in both pools, we found that  the HMW pool has a higher fraction of tetrameric assemblies and that the LMW pool has a higher fraction  of dimeric assemblies. No monomeric or trimeric species were detected. In addition, when the LMW pool is  collected conservatively avoiding any HMW material (Fig. 6A, shaded area), and reanalyzed by gel filtration,  the tetrameric shoulder is again observed (Fig. 6A, inset). We conclude that purified TRPV3 forms both  dimers and tetramers in solution and that these species are in equilibrium."|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2013/09/13	2014/10/16	rogid:YcUgNSSqbvmuBtg9g5CyJWACaGU9606	rogid:YcUgNSSqbvmuBtg9g5CyJWACaGU9606	intact-crc:073880F52959178C|rigid:JngxQPmvxvNv8pqXSrUcslU5MW4	false	-	-	2	0	psi-mi:"MI:0818"(molecular weight estimation by coomasie staining)	psi-mi:"MI:0818"(molecular weight estimation by coomasie staining)