#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:P10997	uniprotkb:P10997	intact:EBI-8526679|uniprotkb:Q14598|intact:MINT-8074874|uniprotkb:Q0ZD87|ensembl:ENSP00000240652|ensembl:ENSP00000437357	intact:EBI-8526679|uniprotkb:Q14598|intact:MINT-8074874|uniprotkb:Q0ZD87|ensembl:ENSP00000240652|ensembl:ENSP00000437357	psi-mi:iapp_human(display_long)|uniprotkb:IAPP(gene name)|psi-mi:IAPP(display_short)|uniprotkb:Amylin(gene name synonym)|uniprotkb:Diabetes-associated peptide(gene name synonym)|uniprotkb:Insulinoma amyloid peptide(gene name synonym)	psi-mi:iapp_human(display_long)|uniprotkb:IAPP(gene name)|psi-mi:IAPP(display_short)|uniprotkb:Amylin(gene name synonym)|uniprotkb:Diabetes-associated peptide(gene name synonym)|uniprotkb:Insulinoma amyloid peptide(gene name synonym)	psi-mi:"MI:0051"(fluorescence technology)	Peinado et al. (2013)	pubmed:24042052|imex:IM-21426	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-8755150|imex:IM-21426-1	-	-	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0326"(protein)	psi-mi:"MI:0326"(protein)	refseq:NP_000406.1|refseq:NP_001316130.1|dip:DIP-29913N|ensembl:ENSG00000121351(gene)|ensembl:ENST00000240652(transcript)|ensembl:ENST00000539393(transcript)|go:"GO:0001540"(amyloid-beta binding)|go:"GO:0005102"(signaling receptor binding)|go:"GO:0005179"(hormone activity)|go:"GO:0005576"(extracellular region)|go:"GO:0005615"(extracellular space)|go:"GO:0006915"(apoptotic process)|go:"GO:0007165"(signal transduction)|go:"GO:0007189"(adenylate cyclase-activating G protein-coupled receptor signaling pathway)|go:"GO:0007204"(positive regulation of cytosolic calcium ion concentration)|go:"GO:0007267"(cell-cell signaling)|go:"GO:0008285"(negative regulation of cell population proliferation)|go:"GO:0010628"(positive regulation of gene expression)|go:"GO:0010739"(positive regulation of protein kinase A signaling)|go:"GO:0010823"(negative regulation of mitochondrion organization)|go:"GO:0010942"(positive regulation of cell death)|go:"GO:0016234"(inclusion body)|go:"GO:0019233"(sensory perception of pain)|go:"GO:0031333"(negative regulation of protein-containing complex assembly)|go:"GO:0031648"(protein destabilization)|go:"GO:0033138"(positive regulation of peptidyl-serine phosphorylation)|go:"GO:0042755"(eating behavior)|go:"GO:0042802"(identical protein binding)|go:"GO:0043065"(positive regulation of apoptotic process)|go:"GO:0043410"(positive regulation of MAPK cascade)|go:"GO:0045596"(negative regulation of cell differentiation)|go:"GO:0045779"(negative regulation of bone resorption)|go:"GO:0051260"(protein homooligomerization)|go:"GO:0051897"(positive regulation of protein kinase B signaling)|go:"GO:0070374"(positive regulation of ERK1 and ERK2 cascade)|go:"GO:0097647"(amylin receptor signaling pathway)|go:"GO:1905665"(positive regulation of calcium ion import across plasma membrane)|go:"GO:1905907"(negative regulation of amyloid fibril formation)|go:"GO:1990000"(amyloid fibril formation)|interpro:IPR000443(Islet amyloid polypeptide)|interpro:IPR001693(Calcitonin-like)|interpro:IPR018360|interpro:IPR021116|interpro:IPR021117|rcsb pdb:1KUW|rcsb pdb:2G48|rcsb pdb:2KB8|rcsb pdb:2L86|rcsb pdb:3DG1|rcsb pdb:3FPO|rcsb pdb:3FR1|rcsb pdb:3FTH|rcsb pdb:3FTK|rcsb pdb:3FTL|rcsb pdb:3FTR|rcsb pdb:3G7V|rcsb pdb:3G7W|rcsb pdb:3HGZ|rcsb pdb:5K5G|rcsb pdb:5KNZ|rcsb pdb:5KO0|rcsb pdb:5MGQ|rcsb pdb:6UCJ|rcsb pdb:6UCK|rcsb pdb:6VW2|rcsb pdb:6Y1A|rcsb pdb:6ZRF|rcsb pdb:6ZRQ|rcsb pdb:6ZRR|reactome:R-HSA-210745|reactome:R-HSA-418555|reactome:R-HSA-419812|reactome:R-HSA-9660821|reactome:R-HSA-977225	refseq:NP_000406.1|refseq:NP_001316130.1|dip:DIP-29913N|ensembl:ENSG00000121351(gene)|ensembl:ENST00000240652(transcript)|ensembl:ENST00000539393(transcript)|go:"GO:0001540"(amyloid-beta binding)|go:"GO:0005102"(signaling receptor binding)|go:"GO:0005179"(hormone activity)|go:"GO:0005576"(extracellular region)|go:"GO:0005615"(extracellular space)|go:"GO:0006915"(apoptotic process)|go:"GO:0007165"(signal transduction)|go:"GO:0007189"(adenylate cyclase-activating G protein-coupled receptor signaling pathway)|go:"GO:0007204"(positive regulation of cytosolic calcium ion concentration)|go:"GO:0007267"(cell-cell signaling)|go:"GO:0008285"(negative regulation of cell population proliferation)|go:"GO:0010628"(positive regulation of gene expression)|go:"GO:0010739"(positive regulation of protein kinase A signaling)|go:"GO:0010823"(negative regulation of mitochondrion organization)|go:"GO:0010942"(positive regulation of cell death)|go:"GO:0016234"(inclusion body)|go:"GO:0019233"(sensory perception of pain)|go:"GO:0031333"(negative regulation of protein-containing complex assembly)|go:"GO:0031648"(protein destabilization)|go:"GO:0033138"(positive regulation of peptidyl-serine phosphorylation)|go:"GO:0042755"(eating behavior)|go:"GO:0042802"(identical protein binding)|go:"GO:0043065"(positive regulation of apoptotic process)|go:"GO:0043410"(positive regulation of MAPK cascade)|go:"GO:0045596"(negative regulation of cell differentiation)|go:"GO:0045779"(negative regulation of bone resorption)|go:"GO:0051260"(protein homooligomerization)|go:"GO:0051897"(positive regulation of protein kinase B signaling)|go:"GO:0070374"(positive regulation of ERK1 and ERK2 cascade)|go:"GO:0097647"(amylin receptor signaling pathway)|go:"GO:1905665"(positive regulation of calcium ion import across plasma membrane)|go:"GO:1905907"(negative regulation of amyloid fibril formation)|go:"GO:1990000"(amyloid fibril formation)|interpro:IPR000443(Islet amyloid polypeptide)|interpro:IPR001693(Calcitonin-like)|interpro:IPR018360|interpro:IPR021116|interpro:IPR021117|rcsb pdb:1KUW|rcsb pdb:2G48|rcsb pdb:2KB8|rcsb pdb:2L86|rcsb pdb:3DG1|rcsb pdb:3FPO|rcsb pdb:3FR1|rcsb pdb:3FTH|rcsb pdb:3FTK|rcsb pdb:3FTL|rcsb pdb:3FTR|rcsb pdb:3G7V|rcsb pdb:3G7W|rcsb pdb:3HGZ|rcsb pdb:5K5G|rcsb pdb:5KNZ|rcsb pdb:5KO0|rcsb pdb:5MGQ|rcsb pdb:6UCJ|rcsb pdb:6UCK|rcsb pdb:6VW2|rcsb pdb:6Y1A|rcsb pdb:6ZRF|rcsb pdb:6ZRQ|rcsb pdb:6ZRR|reactome:R-HSA-210745|reactome:R-HSA-418555|reactome:R-HSA-419812|reactome:R-HSA-9660821|reactome:R-HSA-977225	-	"mimix:comment":not sure about the protein origin|comment:mint	"mimix:comment":not sure about the protein origin|comment:mint	figure legend:f1 f2 f3|comment:"We investigated hIAPP fibrillation using an in vitro fluorescence assay using a ThT  assay. In our hands, concentrations ranging from 5 to 20 μM of hIAPP exhibited complete  fibrillation within an hour at 25 C and 10 μM was chosen for further assays (Fig. 1A). It has  been shown that fibrillation of hIAPP is inhibited by insulin [25]. In our assays 5 μM insulin  blocked 80% of hIAPP fibrillation, while an irrelevant control protein such as carbonic  anhydrase did not block fibrillation (Fig. 1B)."|comment:"We found 90% inhibition of hIAPP fibrillation with 10 μM 7B2, while 1 μM  resulted in 50% inhibition (Fig. 1C). ProSAAS is also abundant in the pancreas [27]; in order to  evaluate whether proSAAS also possesses anti-fibrillation ability, we carried out an assay using  proSAAS concentrations between 0.1 and 10 μM. Under these conditions 10 μM 21 kDa  proSAAS blocked hIAPP fibrillation completely and 0.1 μM still retained some inhibitory  activity on fibril formation (Fig. 1D)."|comment:"To elucidate the region within 7B2 responsible for the anti-fibrillation effect, we  performed in vitro fibrillation assays with N-terminally truncated proteins. Structure-function  analysis using truncated forms of 7B2 revealed that the anti-aggregation effect was greatest using  21-kDa 7B2 (Fig. 2A), although 10 μM 7B230-150 and 7B268-150 partially inhibited hIAPP  fibrillation by 30 and 20% respectively (Fig. 2B)."|comment:"two truncated peptides (Fig. 3A) were synthesized (proSAAS97-137  and proSAAS138-180, see Materials and Methods) to test whether α-helices II and III play a role  in proSAAS-induced inhibition of fibrillation. However, neither of these two peptides was able  to inhibit fibrillation in vitro (Fig. 3B). We conclude that residues 1-97 in the N-terminal domain  contain key determinants for the anti-fibrillation ability of proSAAS on hIAPP"|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2013/09/06	2014/10/16	rogid:96US2nyXcc+hMG9Y4+Be1pxnJgw9606	rogid:96US2nyXcc+hMG9Y4+Be1pxnJgw9606	intact-crc:D70DEB91610A95FE|rigid:BBjpAdBwRFIGXy/POxEfN3wMtAs	false	-	-	-	-	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)