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 Structural basis for the inhibition of activin signalling by follistatin. Structural basis for the inhibition of activin signalling by follistatin. EMBO J. (0261-4189) 2006 imex curation Harrington AE., Morris-Triggs SA., Ruotolo BT., Robinson CV., Ohnuma S., Hyvönen M. 2009-01-08 Only protein-protein interactions in vitro In vitro chromatography chromatography technology column chromatography chromatography nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence Harrington AE., Morris-Triggs SA., Ruotolo BT., Robinson CV., Ohnuma S., Hyvönen M. EMBO J. (0261-4189) 2006 2009-01-08 Only protein-protein interactions imex curation Structural basis for the inhibition of activin signalling by follistatin. Structural basis for the inhibition of activin signalling by follistatin. EMBO J. (0261-4189) 2006 imex curation Harrington AE., Morris-Triggs SA., Ruotolo BT., Robinson CV., Ohnuma S., Hyvönen M. 2009-01-08 Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence Harrington AE., Morris-Triggs SA., Ruotolo BT., Robinson CV., Ohnuma S., Hyvönen M. EMBO J. (0261-4189) 2006 2009-01-08 Only protein-protein interactions imex curation inhba_human Inhibin beta A chain INHBA Activin beta-A chain Erythroid differentiation protein protein protein human Homo sapiens Human MPLLWLRGFLLASCWIIVRSSPTPGSEGHSAAPDCPSCALAALPKDVPNSQPEMVEAVKKHILNMLHLKKRPDVTQPVPKAALLNAIRKLHVGKVGENGYVEIEDDIGRRAEMNELMEQTSEIITFAESGTARKTLHFEISKEGSDLSVVERAEVWLFLKVPKANRTRTKVTIRLFQQQKHPQGSLDTGEEAEEVGLKGERSELLLSEKVVDARKSTWHVFPVSSSIQRLLDQGKSSLDVRIACEQCQESGASLVLLGKKKKKEEEGEGKKKGGGEGGAGADEEKEQSHRPFLMLQARQSEDHPHRRRRRGLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, erythroid differentiation, insulin secretion, nerve cell survival, embryonic axial development or bone growth, depending on their subunit composition. Inhibins appear to oppose the functions of activins mint 201CDEDF99CB6919 fst_rat Follistatin Fst Activin-binding protein protein protein rat Rattus norvegicus (Rat) Rat MVCARHQPGGLCLLLLLLCQFMEDRSAQAGNCWLRQAKNGRCQVLYKTELSKEECCSTGRLSTSWTEEDVNDNTLFKWMIFNGGAPNCIPCKETCENVDCGPGKKCRMNKKNKPRCVCAPDCSNITWKGPVCGLDGKTYRNECALLKARCKEQPELEVQYQGKCKKTCRDVFCPGSSTCVVDQTNNAYCVTCNRICPEPSSSEQSLCGNDGVTYSSACHLRKATCLLGRSIGLAYEGKCIKAKSCEDIQCGGGKKCLWDFKVGRGRCSLCDELCPDSKSDEPVCASDNATYASECAMKEAACSSGVLLEVKHSGSCNSISEETEEEEEEEDQDYSFPISSTLEW 864244CF05436552 fst-inhba 1 3 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified undefined mutation mutation decreasing interaction mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain Wed Jul 06 16:50:04 BST 2016 Sequence change details about this feature cannot be ascertained or do not fit with the current version of the referenced protein, so they have been deleted as a result of our quality control procedures. The original label was 'mutation decreasing' Arg221Ala range MINT-1787094: original sequence: 221-221 : VDARKSTWHVFPVSSSIQRL binding site binding region binding-associated region binding region deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain range MINT-1787092: original sequence: 93-241 : GKVGENGYVEIEDDIGRRAEMNELMEQTSEIITFAESGTARKTLHFEISKEGSDLSVVERAEVWLFLKVPKANRTRTKVTIRLFQQQKHPQGSLDTGEEAEEVGLKGERSELLLSEKVVDARKSTWHVFPVSSSIQRLLDQGKSSLDV Stoichiometry: 1.0 4 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 direct interaction direct interaction F2B EMBO-Journal The complexes isolated by size exclusion chromatography were analysed using nondissociative mass spectrometry. Both complexes gave rise to two major ion series (Figure 2B and G); a complex between an activin dimer and one chain of the follistatin construct (1:1 complex; charge states labelled with underlined text), and a higher intensity 1:2 complex. Each of these complexes was independently identified using tandem mass spectrometry homomint mint fst-inhba-1 2 3 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain range MINT-1787168: original sequence: 93-241 : GKVGENGYVEIEDDIGRRAEMNELMEQTSEIITFAESGTARKTLHFEISKEGSDLSVVERAEVWLFLKVPKANRTRTKVTIRLFQQQKHPQGSLDTGEEAEEVGLKGERSELLLSEKVVDARKSTWHVFPVSSSIQRLLDQGKSSLDV Stoichiometry: 1.0 4 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 direct interaction direct interaction F2E EMBO-Journal kd 430 nanomolar Titration of the follistatin fragments into activin A indicated these two fragments had near-identical affinities with Kd of 430 nM for Fs12 and 420 nM for Fs123 (Figure 2E and J, respectively). homomint mint