DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ tooley-2010-1 in vitro In vitro methyltransferase as methyltransferase assay methyltransferase as predetermined predetermined participant predetermined Tooley CE., Petkowski JJ., Muratore-Schroeder TL., Balsbaugh JL., Shabanowitz J., Sabat M., Minor W., Hunt DF., Macara IG. DIP original experiment: DIP-219394X Nature 2010 IMEx NRMT is an alpha-N-methyltransferase that methylates RCC1 and retinoblastoma protein. Tooley CE., Petkowski JJ., Muratore-Schroeder TL., Balsbaugh JL., Shabanowitz J., Sabat M., Minor W., Hunt DF., Macara IG. Only protein-protein interactions imex curation tooley-2010-2 in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Tooley CE., Petkowski JJ., Muratore-Schroeder TL., Balsbaugh JL., Shabanowitz J., Sabat M., Minor W., Hunt DF., Macara IG. DIP original experiment: DIP-219392X Nature 2010 IMEx NRMT is an alpha-N-methyltransferase that methylates RCC1 and retinoblastoma protein. Tooley CE., Petkowski JJ., Muratore-Schroeder TL., Balsbaugh JL., Shabanowitz J., Sabat M., Minor W., Hunt DF., Macara IG. Only protein-protein interactions imex curation tooley-2010-3 in vitro In vitro methyltransferase as methyltransferase assay methyltransferase as western blot western blot Immuno blot Immuno blot Tooley CE., Petkowski JJ., Muratore-Schroeder TL., Balsbaugh JL., Shabanowitz J., Sabat M., Minor W., Hunt DF., Macara IG. DIP original experiment: DIP-219397X Nature 2010 IMEx NRMT is an alpha-N-methyltransferase that methylates RCC1 and retinoblastoma protein. Tooley CE., Petkowski JJ., Muratore-Schroeder TL., Balsbaugh JL., Shabanowitz J., Sabat M., Minor W., Hunt DF., Macara IG. Only protein-protein interactions imex curation tooley-2010-4 in vitro In vitro methyltransferase as methyltransferase assay methyltransferase as western blot western blot Immuno blot Immuno blot Tooley CE., Petkowski JJ., Muratore-Schroeder TL., Balsbaugh JL., Shabanowitz J., Sabat M., Minor W., Hunt DF., Macara IG. DIP original experiment: DIP-219395X Nature 2010 IMEx NRMT is an alpha-N-methyltransferase that methylates RCC1 and retinoblastoma protein. Tooley CE., Petkowski JJ., Muratore-Schroeder TL., Balsbaugh JL., Shabanowitz J., Sabat M., Minor W., Hunt DF., Macara IG. Only protein-protein interactions imex curation tooley-2010-5 in vitro In vitro methyltransferase as methyltransferase assay methyltransferase as western blot western blot Immuno blot Immuno blot Tooley CE., Petkowski JJ., Muratore-Schroeder TL., Balsbaugh JL., Shabanowitz J., Sabat M., Minor W., Hunt DF., Macara IG. DIP original experiment: DIP-219393X Nature 2010 IMEx NRMT is an alpha-N-methyltransferase that methylates RCC1 and retinoblastoma protein. Tooley CE., Petkowski JJ., Muratore-Schroeder TL., Balsbaugh JL., Shabanowitz J., Sabat M., Minor W., Hunt DF., Macara IG. Only protein-protein interactions imex curation tooley-2010-6 in vitro In vitro methyltransferase as methyltransferase assay methyltransferase as western blot western blot Immuno blot Immuno blot Tooley CE., Petkowski JJ., Muratore-Schroeder TL., Balsbaugh JL., Shabanowitz J., Sabat M., Minor W., Hunt DF., Macara IG. DIP original experiment: DIP-219396X Nature 2010 IMEx NRMT is an alpha-N-methyltransferase that methylates RCC1 and retinoblastoma protein. Tooley CE., Petkowski JJ., Muratore-Schroeder TL., Balsbaugh JL., Shabanowitz J., Sabat M., Minor W., Hunt DF., Macara IG. Only protein-protein interactions imex curation rcc1_human Regulator of chromosome condensation Chromosome condensation protein 1 Cell cycle regulatory protein RCC1 CHC1 protein protein human Homo sapiens Human MSPKRIAKRRSPPADAIPKSKKVKVSHRSHSTEPGLVLTLGQGDVGQLGLGENVMERKKPALVSIPEDVVQAEAGGMHTVCLSKSGQVYSFGCNDEGALGRDTSVEGSEMVPGKVELQEKVVQVSAGDSHTAALTDDGRVFLWGSFRDNNGVIGLLEPMKKSMVPVQVQLDVPVVKVASGNDHLVMLTADGDLYTLGCGEQGQLGRVPELFANRGGRQGLERLLVPKCVMLKSRGSRGHVRFQDAFCGAYFTFAISHEGHVYGFGLSNYHQLGTPGTESCFIPQNLTSFKNSTKSWVGFSGGQHHTVCMDSEGKAYSLGRAEYGRLGLGEGAEEKSIPTLISRLPAVSSVACGASVGYAVTKDGRVFAWGMGTNYQLGTGQDEDAWSPVEMMGKQLENRVVLSVSSGGQHTVLLVKDKEQS ntm1a_human N-terminal Xaa-Pro-Lys N-methyltransferase 1 NRMT1 NTMT1 Alpha N-terminal protein methyltransferase 1A C9orf32 METTL11A Methyltransferase-like protein 11A N-terminal RCC1 methyltransferase NRMT X-Pro-Lys N-terminal protein methyltransferase 1A AD-003 protein protein human Homo sapiens Human MTSEVIEDEKQFYSKAKTYWKQIPPTVDGMLGGYGHISSIDINSSRKFLQRFLREGPNKTGTSCALDCGAGIGRITKRLLLPLFREVDMVDITEDFLVQAKTYLGEEGKRVRNYFCCGLQDFTPEPDSYDVIWIQWVIGHLTDQHLAEFLRRCKGSLRPNGIIVIKDNMAQEGVILDDVDSSVCRDLDVVRRIICSAGLSLLAEERQENLPDEIYHVYSFALR rb_human Retinoblastoma-associated protein pRb pp110 p105-Rb RB1 p110-RB1 protein protein human Homo sapiens Human MPPKTPRKTAATAAAAAAEPPAPPPPPPPEEDPEQDSGPEDLPLVRLEFEETEEPDFTALCQKLKIPDHVRERAWLTWEKVSSVDGVLGGYIQKKKELWGICIFIAAVDLDEMSFTFTELQKNIEISVHKFFNLLKEIDTSTKVDNAMSRLLKKYDVLFALFSKLERTCELIYLTQPSSSISTEINSALVLKVSWITFLLAKGEVLQMEDDLVISFQLMLCVLDYFIKLSPPMLLKEPYKTAVIPINGSPRTPRRGQNRSARIAKQLENDTRIIEVLCKEHECNIDEVKNVYFKNFIPFMNSLGLVTSNGLPEVENLSKRYEEIYLKNKDLDARLFLDHDKTLQTDSIDSFETQRTPRKSNLDEEVNVIPPHTPVRTVMNTIQQLMMILNSASDQPSENLISYFNNCTVNPKESILKRVKDIGYIFKEKFAKAVGQGCVEIGSQRYKLGVRLYYRVMESMLKSEEERLSIQNFSKLLNDNIFHMSLLACALEVVMATYSRSTSQNLDSGTDLSFPWILNVLNLKAFDFYKVIESFIKAEGNLTREMIKHLERCEHRIMESLAWLSDSPLFDLIKQSKDREGPTDHLESACPLNLPLQNNHTAADMYLSPVRSPKKKGSTTRVNSTANAETQATSAFQTQKPLKSTSLSLFYKKVYRLAYLRLNTLCERLLSEHPELEHIIWTLFQHTLQNEYELMRDRHLDQIMMCSMYGICKVKNIDLKFKIIVTAYKDLPHAVQETFKRVLIKEEEYDSIIVFYNSVFMQRLKTNILQYASTRPPTLSPIPHIPRSPYKFPSSPLRIPGGNIYISPLKSPYKISEGLPTPTKMTPRSRILVSIGESFGTSEKFQKINQMVCNSDRVLKRSAEGSNPPKPLKKLRFDIEGSDEADGSKHLPGESKFQQKLAEMTSTRTRMQKQKMNDSMDTSNKEEK q01105-1 Protein SET TAF-I alpha SET HLA-DR-associated protein II Inhibitor of granzyme A-activated DNase PHAPII Phosphatase 2A inhibitor I2PP2A Template-activating factor I protein protein human Homo sapiens Human MAPKRQSPLPPQKKKPRPPPALGPEETSASAGLPKKGEKEQQEAIEHIDEVQNEIDRLNEQASEEILKVEQKYNKLRQPFFQKRSELIAKIPNFWVTTFVNHPQVSALLGEEDEEALHYLTRVEVTEFEDIKSGYRIDFYFDENPYFENKVLSKEFHLNESGDPSSKSTEIKWKSGKDLTKRSSQTQNKASRKRQHEEPESFFTWFTDHSDAGADELGEVIKDDIWPNPLQYYLVPDMDDEEGEGEEDDDDDEEEEGLEDIDEEGDEDEGEEDEDDDEGEEGEEDEGEDD ntmt1-rcc1-1 3211851 N/A 3211857 enzyme target enzyme target substrate substrate unspecified role unspecified role P18754:p.Ser2Leu S2L/I/W/D/E mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false P18754:p.Ser2Val S2V/F/K/N/Q/T/H mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false P18754:p.Ser2Phe mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain false P18754:p.Ser2Lys mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain false P18754:p.Ser2Asn mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain false P18754:p.Ser2Gln mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain false P18754:p.Ser2Thr mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain false P18754:p.Ser2His mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain false P18754:p.Ser2Ile mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate certain certain sequence position certain certain certain sequence position certain false P18754:p.Ser2Trp mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate certain certain sequence position certain certain certain sequence position certain false P18754:p.Ser2Asp mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength certain certain sequence position certain certain certain sequence position certain false P18754:p.Ser2Glu mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli N/A 3211858 enzyme enzyme unspecified role unspecified role ecolx Escherichia coli methylation methylation reaction methylation false false false ntmt1-rcc1-2 3211852 N/A 3211857 unspecified role unspecified role unspecified role unspecified role Region 2-13 Region 2-13 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false P18754:p.Lys4Gln K4Q mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false in vitro In vitro N/A 3211858 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction false false false ntmt1-rcc1-3 3211853 N/A 3211857 enzyme target enzyme target substrate substrate unspecified role unspecified role ecolx Escherichia coli N/A 3211858 enzyme enzyme unspecified role unspecified role Q9BV86:p.Asn168Lys N168K mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false Q9BV86:p.Asp180Lys D180K mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli methylation methylation reaction methylation false false false ntmt1-rb1-1 3211854 N/A 3211859 enzyme target enzyme target substrate substrate unspecified role unspecified role ecolx Escherichia coli N/A 3211858 enzyme enzyme unspecified role unspecified role ecolx Escherichia coli methylation methylation reaction methylation false false false ntmt1-rcc1-4 3211855 N/A 3211857 enzyme target enzyme target substrate substrate unspecified role unspecified role Region 2-13 Region 2-13 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false P18754:p.Lys4Gln K4Q mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false in vitro In vitro N/A 3211858 enzyme enzyme unspecified role unspecified role ecolx Escherichia coli methylation methylation reaction methylation false false false ntmt1-set-1 3211856 N/A 3211860 enzyme target enzyme target substrate substrate unspecified role unspecified role ecolx Escherichia coli N/A 3211858 enzyme enzyme unspecified role unspecified role ecolx Escherichia coli methylation methylation reaction methylation false false false