MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it Molecular insight of DREAM and presenilin 1 C-terminal fragment interactions. Molecular insight of DREAM and presenilin 1 C-terminal fragment interactions. FEBS letters 2016 imex curation Pham K., Miksovska J. miksocsk@fiu.edu 17-Oct-2016: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Pham K., Miksovska J. miksocsk@fiu.edu Accepted 2016-OCT-03 AT 09:51 BST AT 09:51 BST by MARTA FEBS letters 2016 Only protein-protein interactions imex curation imex curation csen_mouse Calsenilin A-type potassium channel modulatory protein 3 Kcnip3 Csen Dream Kchip3 DRE-antagonist modulator Kv channel-interacting protein 3 protein protein mouse Mus musculus Mouse MQRTKEAVKASDGNLLGDPGRIPLSKRESIKWQRPRFTRQALMRCCLIKWILSSAAPQGSDSSDSELELSTVRHQPEGLDQLQAQTKFTKKELQSLYRGFKNECPTGLVDEDTFKLIYSQFFPQGDATTYAHFLFNAFDADGNGAIHFEDFVVGLSILLRGTVHEKLKWAFNLYDINKDGCITKEEMLAIMKSIYDMMGRHTYPILREDAPLEHVERFFQKMDRNQDGVVTIDEFLETCQKDENIMNSMQLFENVI 0F43D5F239D6378C psn1_human Presenilin-1 PSEN1 AD3 PS1 PSNL1 Protein S182 protein protein human Homo sapiens Human MTELPAPLSYFQNAQMSEDNHLSNTVRSQNDNRERQEHNDRRSLGHPEPLSNGRPQGNSRQVVEQDEEEDEELTLKYGAKHVIMLFVPVTLCMVVVVATIKSVSFYTRKDGQLIYTPFTEDTETVGQRALHSILNAAIMISVIVVMTILLVVLYKYRCYKVIHAWLIISSLLLLFFFSFIYLGEVFKTYNVAVDYITVALLIWNFGVVGMISIHWKGPLRLQQAYLIMISALMALVFIKYLPEWTAWLILAVISVYDLVAVLCPKGPLRMLVETAQERNETLFPALIYSSTMVWLVNMAEGDPEAQRRVSKNSKYNAESTERESQDTVAENDDGGFSEEWEAQRDSHLGPHRSTPESRAAVQELSSSILAGEDPEERGVKLGLGDFIFYSVLVGKASATASGDWNTTIACFVAILIGLCLTLLLLAIFKKALPALPISITFGLVFYFATDYLVQPFMDQLAFHQFYI DIP protein P49768 original sequence version: 106 DIP protein P49768-1 original sequence version: 144 DIP protein P49768 original sequence version: 186 5E0F451EF82BCF20 kcnip3-psen1-2 1 2 unspecified role unspecified role neutral component neutral component purified purified Q9QXT8:p.Glu234Gln mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain E Q Wed May 02 16:34:56 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu234gln' Tue Jun 30 18:19:24 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu234Gln' Q9QXT8:p.Glu186Gln mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain E Q Wed May 02 19:11:15 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu186gln' Tue Jun 30 16:47:58 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu186Gln' binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 3 unspecified role unspecified role neutral component neutral component purified purified range binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction t1 f2 HL9 binds to Ca2+DREAM and Mg2+Ca2+DREAM with a similar Kd of 0.6 μm. In the absence of Ca2+, a weak interaction was determined for binding of HL9 to ApoDREAM (Kd = 183 ± 12 μm), whereas the Kd value for HL9 association with Mg2+DREAM was found to be 29 ± 2 μm. To investigate the mechanism by which Ca2+ binding to EF-hands 3 and 4 in DREAM mediates DREAM and HL9 interactions, binding of HL9 to DREAM-E234Q and DREAM-E186Q were studied. Titration data demonstrate that HL9 binds to DREAM-E234Q in the presence of Ca2+ and Ca2+/Mg2+ with a Kd of 8 μm, whereas a weaker binding (Kd = 32 μm) was observed for DREAM-E186Q mutant (Table 1).