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 Calbindin-D28K dynamically controls TRPV5-mediated Ca2+ transport. Calbindin-D28K dynamically controls TRPV5-mediated Ca2+ transport. EMBO J. (0261-4189) 2006 imex curation Lambers TT., Mahieu F., Oancea E., Hoofd L., de Lange F., Mensenkamp AR., Voets T., Nilius B., Clapham DE., Hoenderop JG., Bindels RJ. 2009-01-08 Only protein-protein interactions human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. pull down pull down nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence Lambers TT., Mahieu F., Oancea E., Hoofd L., de Lange F., Mensenkamp AR., Voets T., Nilius B., Clapham DE., Hoenderop JG., Bindels RJ. EMBO J. (0261-4189) 2006 2009-01-08 Only protein-protein interactions imex curation Calbindin-D28K dynamically controls TRPV5-mediated Ca2+ transport. Calbindin-D28K dynamically controls TRPV5-mediated Ca2+ transport. EMBO J. (0261-4189) 2006 imex curation Lambers TT., Mahieu F., Oancea E., Hoofd L., de Lange F., Mensenkamp AR., Voets T., Nilius B., Clapham DE., Hoenderop JG., Bindels RJ. 2009-01-08 Only protein-protein interactions human-kidney Human kidney kidney kidney [Renal] imaging technique imaging technique microscopy experimental particp experimental participant identification experimental particp Lambers TT., Mahieu F., Oancea E., Hoofd L., de Lange F., Mensenkamp AR., Voets T., Nilius B., Clapham DE., Hoenderop JG., Bindels RJ. EMBO J. (0261-4189) 2006 2009-01-08 Only protein-protein interactions imex curation Calbindin-D28K dynamically controls TRPV5-mediated Ca2+ transport. Calbindin-D28K dynamically controls TRPV5-mediated Ca2+ transport. EMBO J. (0261-4189) 2006 imex curation Lambers TT., Mahieu F., Oancea E., Hoofd L., de Lange F., Mensenkamp AR., Voets T., Nilius B., Clapham DE., Hoenderop JG., Bindels RJ. 2009-01-08 Only protein-protein interactions in vitro In vitro pull down pull down nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence Lambers TT., Mahieu F., Oancea E., Hoofd L., de Lange F., Mensenkamp AR., Voets T., Nilius B., Clapham DE., Hoenderop JG., Bindels RJ. EMBO J. (0261-4189) 2006 2009-01-08 Only protein-protein interactions imex curation trpv5_human Transient receptor potential cation channel subfamily V member 5 TRPV5 ECAC1 Calcium transport protein 2 Epithelial calcium channel 1 Osm-9-like TRP channel 3 protein protein human Homo sapiens Human MGGFLPKAEGPGSQLQKLLPSFLVREQDWDQHLDKLHMLQQKRILESPLLRASKENDLSVLRQLLLDCTCDVRQRGALGETALHIAALYDNLEAALVLMEAAPELVFEPTTCEAFAGQTALHIAVVNQNVNLVRALLTRRASVSARATGTAFRRSPRNLIYFGEHPLSFAACVNSEEIVRLLIEHGADIRAQDSLGNTVLHILILQPNKTFACQMYNLLLSYDGHGDHLQPLDLVPNHQGLTPFKLAGVEGNTVMFQHLMQKRRHIQWTYGPLTSILYDLTEIDSWGEELSFLELVVSSDKREARQILEQTPVKELVSFKWNKYGRPYFCILAALYLLYMICFTTCCVYRPLKFRGGNRTHSRDITILQQKLLQEAYETREDIIRLVGELVSIVGAVIILLLEIPDIFRVGASRYFGKTILGGPFHVIIITYASLVLVTMVMRLTNTNGEVVPMSFALVLGWCSVMYFTRGFQMLGPFTIMIQKMIFGDLMRFCWLMAVVILGFASAFYIIFQTEDPTSLGQFYDYPMALFTTFELFLTVIDAPANYDVDLPFMFSIVNFAFAIIATLLMLNLFIAMMGDTHWRVAQERDELWRAQVVATTVMLERKLPRCLWPRSGICGCEFGLGDRWFLRVENHNDQNPLRVLRYVEVFKNSDKEDDQEHPSEKQPSGAESGTLARASLALPTSSLSRTASQSSSHRGWEILRQNTLGHLNLGLNLSEGDGEEVYHF A10FB80205FD0DBB trpv6_human Transient receptor potential cation channel subfamily V member 6 TRPV6 ECAC2 Epithelial calcium channel 2 Calcium transport protein 1 CaT-like protein protein human Homo sapiens Human MGPLQGDGGPALGGADVAPRLSPVRVWPRPQAPKEPALHPMGLSLPKEKGLILCLWSKFCRWFQRRESWAQSRDEQNLLQQKRIWESPLLLAAKDNDVQALNKLLKYEDCKVHQRGAMGETALHIAALYDNLEAAMVLMEAAPELVFEPMTSELYEGQTALHIAVVNQNMNLVRALLARRASVSARATGTAFRRSPCNLIYFGEHPLSFAACVNSEEIVRLLIEHGADIRAQDSLGNTVLHILILQPNKTFACQMYNLLLSYDRHGDHLQPLDLVPNHQGLTPFKLAGVEGNTVMFQHLMQKRKHTQWTYGPLTSTLYDLTEIDSSGDEQSLLELIITTKKREARQILDQTPVKELVSLKWKRYGRPYFCMLGAIYLLYIICFTMCCIYRPLKPRTNNRTSPRDNTLLQQKLLQEAYMTPKDDIRLVGELVTVIGAIIILLVEVPDIFRMGVTRFFGQTILGGPFHVLIITYAFMVLVTMVMRLISASGEVVPMSFALVLGWCNVMYFARGFQMLGPFTIMIQKMIFGDLMRFCWLMAVVILGFASAFYIIFQTEDPEELGHFYDYPMALFSTFELFLTIIDGPANYNVDLPFMYSITYAAFAIIATLLMLNLLIAMMGDTHWRVAHERDELWRAQIVATTVMLERKLPRCLWPRSGICGREYGLGDRWFLRVEDRQDLNRQRIQRYAQAFHTRGSEDLDKDSVEKLELGCPFSPHLSLPMPSVSRSTSRSSANWERLRQGTLRRDLRGIINRGLEDGESWEYQI Calcium selective cation channel probably involved in Ca(2+) uptake in various tissues, including Ca(2+) reabsorption in intestine. The channel is activated by low internal calcium level, probably including intracellular calcium store depletion, and the current exhibits an inward rectification. Inactivation includes both, a rapid Ca(2+)-dependent and a slower Ca(2+)-calmodulin-dependent mechanism, the latter may be regulated by phosphorylation. In vitro, is slowly inhibited by Mg(2+) in a voltage-independent manner. Heteromeric assembly with TRPV5 seems to modify channel properties. TRPV5-TRPV6 heteromultimeric concatemers exhibit voltage-dependent gating mint homomint 626D515E12112546 calb1_human Calbindin CALB1 CAB27 Calbindin D28 D-28K Vitamin D-dependent calcium-binding protein, avian-type protein protein human Homo sapiens Human MAESHLQSSLITASQFFEIWLHFDADGSGYLEGKELQNLIQELQQARKKAGLELSPEMKTFVDQYGQRDDGKIGIVELAHVLPTEENFLLLFRCQQLKSCEEFMKTWRKYDTDHSGFIETEELKNFLKDLLEKANKTVDDTKLAEYTDLMLKLFDSNNDGKLELTEMARLLPVQENFLLKFQGIKMCGKEFNKAFELYDQDGNGYIDENELDALLKDLCEKNKQDLDINNITTYKKNIMALSDGGKLYRTDLALILCAGDN 8ED7A09BCC5FE5E4 calb1-trpv5 2 4 experimental particp experimental participant identification experimental particp predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell Stoichiometry: 1.0 6 experimental particp experimental participant identification experimental particp predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell Stoichiometry: 1.0 colocalization colocalization F1A EMBO-Journal In kidney, CaBP28K and TRPV5 colocalized in the distal convoluted tubule (DCT) and the connecting tubule (CNT) (Figure 1A). homomint mint trpv5-calb1 3 4 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role bait bait purified purified gst tagged gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Stoichiometry: 1.0 6 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role prey prey in vitro translated in vitro translated protein in vitro translated Stoichiometry: 1.0 physical association physical association F1D F4B EMBO-Journal he binding was virtually abolished in the presence of Ca2+ while CaBP28KDeltaEF binds in the absence (5 mM EDTA) as well as presence (1 mM CaCl2) of Ca2+ . CaBP28K bound to both the N- and C-termini of TRPV5 and TRPV6 in the absence of Ca2+ (5 mM EDTA), whereas the binding was virtually abolished in the presence of Ca2+ (1 mM CaCl2) (Figure 1D). In addition, pull-down analysis demonstrated that CaBP28KDeltaEF binds in the absence (5 mM EDTA) as well as presence (1 mM CaCl2) of Ca2+ to the N- and C-terminus of both TRPV5 and TRPV6 (Figure 4B). homomint mint trpv5-calb1-1 3 4 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role bait bait purified purified gst tagged gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Stoichiometry: 1.0 6 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role prey prey in vitro translated in vitro translated protein in vitro translated Stoichiometry: 1.0 physical association physical association F4C EMBO-Journal To investigate whether CaBP28KDeltaEF competes with wild-type CaBP28K for TRPV5 binding, increasing amounts of non-radioactive in vitro-translated CaBP28KDeltaEF were added during the pull-down assay. This resulted in a dose-dependent reduction of CaBP28K binding, indicating that CaBP28KDeltaEF competed with wild-type CaBP28K for TRPV5 association (Figure 4C). homomint mint trpv6-calb1 3 5 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role bait bait purified purified gst tagged gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Stoichiometry: 1.0 6 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role prey prey in vitro translated in vitro translated protein in vitro translated Stoichiometry: 1.0 physical association physical association F1D F4B EMBO-Journal he binding was virtually abolished in the presence of Ca2+ while CaBP28KDeltaEF binds in the absence (5 mM EDTA) as well as presence (1 mM CaCl2) of Ca2+ . CaBP28K bound to both the N- and C-termini of TRPV5 and TRPV6 in the absence of Ca2+ (5 mM EDTA), whereas the binding was virtually abolished in the presence of Ca2+ (1 mM CaCl2) (Figure 1D). In addition, pull-down analysis demonstrated that CaBP28KDeltaEF binds in the absence (5 mM EDTA) as well as presence (1 mM CaCl2) of Ca2+ to the N- and C-terminus of both TRPV5 and TRPV6 (Figure 4B). homomint mint calb1-trpv5-1 1 6 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role bait bait over-expressed over expressed level over-expressed living cell living cell gst tagged gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Stoichiometry: 1.0 4 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role prey prey over-expressed over expressed level over-expressed living cell living cell gfp tagged gfp tag green fluorescent protein tag GFP green fluorescent protein GFP green fluorescent protein gfp tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Stoichiometry: 1.0 physical association physical association F1E EMBO-Journal TRPV5 co-precipitated with GST-CaBP28K in cells that were treated with BAPTA-AM, whereas the channel was not precipitated from non-treated cells (Figure 1E). TRPV5 co-precipitated with GST-CaBP28K only in cells that were treated with BAPTA-AM. homomint mint