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 Phosphorylation-regulated transitions in an oligomeric state control the activity of the Sae2 DNA repair enzyme. Phosphorylation-regulated transitions in an oligomeric state control the activity of the Sae2 DNA repair enzyme. Molecular and cellular biology 2014 imex curation Fu Q., Chow J., Bernstein KA., Makharashvili N., Arora S., Lee CF., Person MD., Rothstein R., Paull TT., Fu Q., Chow J., Bernstein KA., Makharashvili N., Arora S., Lee CF., Person MD., Rothstein R., Paull TT. tpaull@utexas.edu Only protein-protein interactions imex curation in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Fu Q., Chow J., Bernstein KA., Makharashvili N., Arora S., Lee CF., Person MD., Rothstein R., Paull TT., Fu Q., Chow J., Bernstein KA., Makharashvili N., Arora S., Lee CF., Person MD., Rothstein R., Paull TT. tpaull@utexas.edu Accepted 2015-APR-20 by LUANA Molecular and cellular biology 2014 Only protein-protein interactions imex curation imex curation com1_yeast DNA endonuclease SAE2 SAE2 YGL175C G1639 COM1 Completion of meiotic recombination protein 1 Sporulation in the absence of SPO11 protein 2 protein protein yeast Saccharomyces cerevisiae Baker's yeast MVTGEENVYLKSSLSILKELSLDELLNVQYDVTTLIAKRVQALQNRNKCVLEEPNSKLAEILCHEKNAPQQSSQTSAGPGEQDSEDFILTQFDEDIKKESAEVHYRNENKHTVQLPLVTMPPNRHKRKISEFSSPLNGLNNLSDLEDCSDTVIHEKDNDKENKTRKLLGIELENPESTSPNLYKNVKDNFLFDFNTNPLTKRAWILEDFRPNEDIAPVKRGRRKLERFYAQVGKPEDSKHRSLSVVIESQNSDYEFAFDNLRNRSKSPPGFGRLDFPSTQEGNEDKKKSQEIIRRKTKYRFLMASNNKIPPYEREYVFKREQLNQIVDDGCFFWSDKLLQIYARC 284D57A3C11DD92B 284D57A3C11DD92B sae2-1 1 2 unspecified role unspecified role neutral component neutral component purified purified his tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined mutation of all five putative Tel1 phosphorylation sites (14) to aspartic acid together with S267E (5D/S267E) caused the distribution of Sae2 to change dramatically: the multimer peak nearly disappeared, and the monomer- size protein species increased in abundance (quantified in Fig. 1C). direct interaction direct interaction f1b f1c sae2-2 1 2 unspecified role unspecified role neutral component neutral component purified purified his tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 2 unspecified role unspecified role neutral component neutral component purified purified his tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined mutation of all five putative Tel1 phosphorylation sites (14) to aspartic acid together with S267E (5D/S267E) caused the distribution of Sae2 to change dramatically: the multimer peak nearly disappeared, and the monomer- size protein species increased in abundance (quantified in Fig. 1C). direct interaction direct interaction f1b f1c