IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ http://www.ebi.ac.uk/ lehman-1999-2 A conserved domain of yeast RNA triphosphatase flanking the catalytic core regulates self-association and interaction with the guanylyltransferase component of the mRNA capping apparatus. in vitro In vitro density sedimentation cosedimentation through density gradient density sedimentation predetermined predetermined participant predetermined Lehman K., Schwer B., Ho CK., Rouzankina I., Shuman S. 15-30% glycerol gradient s-shuman@ski.mskcc.org J. Biol. Chem. (0021-9258) 1999 Only protein-protein interactions imex curation Triphosphatase activity was determined by assaying manganese-dependent 32P-labelled ATP hydrolysis. lehman-1999-1 A conserved domain of yeast RNA triphosphatase flanking the catalytic core regulates self-association and interaction with the guanylyltransferase component of the mRNA capping apparatus. in vitro In vitro enzymatic study enzymatic study predetermined predetermined participant predetermined Lehman K., Schwer B., Ho CK., Rouzankina I., Shuman S. Triphosphatase activity was determined by assaying manganese-dependent 32P-labelled ATP hydrolysis. s-shuman@ski.mskcc.org J. Biol. Chem. (0021-9258) 1999 Only protein-protein interactions imex curation cet1_yeast mRNA-capping enzyme subunit beta CET1 mRNA 5'-phosphatase mRNA 5'-triphosphate monophosphatase P1433 YPL228W protein protein yeast Saccharomyces cerevisiae Baker's yeast MSYTDNPPQTKRALSLDDLVNHDENEKVKLQKLSEAANGSRPFAENLESDINQTETGQAAPIDNYKESTGHGSHSQKPKSRKSSNDDEETDTDDEMGASGEINFDSEMDFDYDKQHRNLLSNGSPPMNDGSDANAKLEKPSDDSIHQNSKSDEEQRIPKQGNEGNIASNYITQVPLQKQKQTEKKIAGNAVGSVVKKEEEANAAVDNIFEEKATLQSKKNNIKRDLEVLNEISASSKPSKYRNVPIWAQKWKPTIKALQSINVKDLKIDPSFLNIIPDDDLTKSVQDWVYATIYSIAPELRSFIELEMKFGVIIDAKGPDRVNPPVSSQCVFTELDAHLTPNIDASLFKELSKYIRGISEVTENTGKFSIIESQTRDSVYRVGLSTQRPRFLRMSTDIKTGRVGQFIEKRHVAQLLLYSPKDSYDVKISLNLELPVPDNDPPEKYKSQSPISERTKDRVSYIHNDSCTRIDITKVENHNQNSKSRQSETTHEVELEINTPALLNAFDNITNDSKEYASLIRTFLNNGTIIRRKLSSLSYEIFEGSKKVM 2B946CC53D66F824 mce1_yeast mRNA-capping enzyme subunit alpha CEG1 YGL130W G2853 mRNA guanylyltransferase GTP--RNA guanylyltransferase protein protein yeast Saccharomyces cerevisiae Baker's yeast MVLAMESRVAPEIPGLIQPGNVTQDLKMMVCKLLNSPKPTKTFPGSQPVSFQHSDVEEKLLAHDYYVCEKTDGLRVLMFIVINPVTGEQGCFMIDRENNYYLVNGFRFPRLPQKKKEELLETLQDGTLLDGELVIQTNPMTKLQELRYLMFDCLAINGRCLTQSPTSSRLAHLGKEFFKPYFDLRAAYPNRCTTFPFKISMKHMDFSYQLVKVAKSLDKLPHLSDGLIFTPVKAPYTAGGKDSLLLKWKPEQENTVDFKLILDIPMVEDPSLPKDDRNRWYYNYDVKPVFSLYVWQGGADVNSRLKHFDQPFDRKEFEILERTYRKFAELSVSDEEWQNLKNLEQPLNGRIVECAKNQETGAWEMLRFRDDKLNGNHTSVVQKVLESINDSVSLEDLEEIVGDIKRCWDERRANMAGGSGRPLPSQSQNATLSTSKPVHSQPPSNDKEPKYVDEDDWSD F7F5A3E59EEFA15F atp ATP Adenosine 5'-triphosphate Adenosine triphosphate ADENOSINE-5'-TRIPHOSPHATE Adephos Adetol Adynol Atipi ATP Atriphos Cardenosine Fosfobion Glucobasin H4atp Myotriphos Triadenyl Triphosphaden adenosine 5'-(tetrahydrogen triphosphate) small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) cet1-2 Homodimerization of Cet1 606751 N/A 606753 unspecified role unspecified role neutral component neutral component n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range false region sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) Stoichiometry: 2.0 direct interaction direct interaction false false false 7A cet1-ceg1-1 Stoichiometry of the Cet1-Ceg1 complex 606751 N/A 606754 unspecified role unspecified role neutral component neutral component n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range false ecobb Escherichia coli (strain B / BL21) Stoichiometry: 1.0 N/A 606753 unspecified role unspecified role neutral component neutral component n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range false region sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) Stoichiometry: 2.0 physical association physical association false false false 7B, 9 The sedimentation coefficient of the Cet1(230-549)p-Ceg1p complex was 7.1. Further truncation of Cet1 to 245-549 resulted in the formation of a multimer, although some protein did still form the heterotrimer with Ceg1. cet1-1 ATPase activity of Cet1 606752 N/A 606753 enzyme enzyme unspecified role unspecified role n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range false region sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) N/A 606755 enzyme target enzyme target substrate substrate unspecified role unspecified role phosphotransfer phosphotransfer reaction phosphotransfer false false false 4B