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/ A network of redundant bHLH proteins functions in all TTG1-dependent pathways of Arabidopsis. A network of redundant bHLH proteins functions in all TTG1-dependent pathways of Arabidopsis. Development (0950-1991) 2003 Zhang F., Gonzalez A., Zhao M., Payne CT., Lloyd A. lloyd@uts.cc.utexas.edu orchard yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 2 hybrid two hybrid 2H 2h Gal4 transcription regeneration two-hybrid yeast two hybrid 2-hybrid classical two hybrid classical two hybrid 2H two-hybrid 2-hybrid Gal4 transcription regeneration 2h yeast two hybrid Y2H Y-2H 2 hybrid predetermined predetermined participant predetermined Zhang F., Gonzalez A., Zhao M., Payne CT., Lloyd A. lloyd@uts.cc.utexas.edu Accepted 2007-DEC-20 by ORCHARD. Development (0950-1991) 2003 orchard myb90_arath Transcription factor MYB90 MYB90 PAP2 T27F4.14 At1g66390 Myb-related protein 90 Production of anthocyanin pigment 2 protein protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MEGSSKGLRKGAWTAEEDSLLRLCIDKYGEGKWHQVPLRAGLNRCRKSCRLRWLNYLKPSIKRGRLSNDEVDLLLRLHKLLGNRWSLIAGRLPGRTANDVKNYWNTHLSKKHESSCCKSKMKKKNIISPPTTPVQKIGVFKPRPRSFSVNNGCSHLNGLPEVDLIPSCLGLKKNNVCENSITCNKDDEKDDFVNNLMNGDNMWLENLLGENQEADAIVPEATTAEHGATLAFDVEQLWSLFDGETVELD 309024FD4103700A myb75_arath Transcription factor MYB75 MYB75 PAP1 SIAA1 F25P12.92 At1g56650 Myb-related protein 75 Production of anthocyanin pigment 1 protein Suc-induced anthocyanin accumulation locus 1 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MEGSSKGLRKGAWTTEEDSLLRQCINKYGEGKWHQVPVRAGLNRCRKSCRLRWLNYLKPSIKRGKLSSDEVDLLLRLHRLLGNRWSLIAGRLPGRTANDVKNYWNTHLSKKHEPCCKIKMKKRDITPIPTTPALKNNVYKPRPRSFTVNNDCNHLNAPPKVDVNPPCLGLNINNVCDNSIIYNKDKKKDQLVNNLIDGDNMWLEKFLEESQEVDILVPEATTTEKGDTLAFDVDQLWSLFDGETVKFD B86103A9AB5CF442 egl1_arath Transcription factor EGL1 Protein ENHANCER OF GLABRA 3 Basic helix-loop-helix protein 2 BHLH2 EGL3 EGL1 MYC146 At1g63650 F24D7.16 EN30 Transcription factor EN 30 bHLH transcription factor bHLH002 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MATGENRTVPDNLKKQLAVSVRNIQWSYGIFWSVSASQPGVLEWGDGYYNGDIKTRKTIQAAEVKIDQLGLERSEQLRELYESLSLAESSASGSSQVTRRASAAALSPEDLTDTEWYYLVCMSFVFNIGEGIPGGALSNGEPIWLCNAETADSKVFTRSLLAKSASLQTVVCFPFLGGVLEIGTTEHIKEDMNVIQSVKTLFLEAPPYTTISTRSDYQEIFDPLSDDKYTPVFITEAFPTTSTSGFEQEPEDHDSFINDGGASQVQSWQFVGEEISNCIHQSLNSSDCVSQTFVGTTGRLACDPRKSRIQRLGQIQEQSNHVNMDDDVHYQGVISTIFKTTHQLILGPQFQNFDKRSSFTRWKRSSSVKTLGEKSQKMIKKILFEVPLMNKKEELLPDTPEETGNHALSEKKRREKLNERFMTLRSIIPSISKIDKVSILDDTIEYLQDLQKRVQELESCRESADTETRITMMKRKKPDDEEERASANCMNSKRKGSDVNVGEDEPADIGYAGLTDNLRISSLGNEVVIELRCAWREGILLEIMDVISDLNLDSHSVQSSTGDGLLCLTVNCKHKGTKIATTGMIQEALQRVAWIC 6B934DFBE82AA102 gl3_arath Transcription factor GLABRA 3 Basic helix-loop-helix protein 1 Protein SHAPESHIFTER At5g41315 GL3 BHLH1 MYC6 SST MYC6.2 EN31 Transcription factor EN 31 bHLH transcription factor bHLH001 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MATGQNRTTVPENLKKHLAVSVRNIQWSYGIFWSVSASQSGVLEWGDGYYNGDIKTRKTIQASEIKADQLGLRRSEQLSELYESLSVAESSSSGVAAGSQVTRRASAAALSPEDLADTEWYYLVCMSFVFNIGEGMPGRTFANGEPIWLCNAHTADSKVFSRSLLAKSAAVKTVVCFPFLGGVVEIGTTEHITEDMNVIQCVKTSFLEAPDPYATILPARSDYHIDNVLDPQQILGDEIYAPMFSTEPFPTASPSRTTNGFDQEHEQVADDHDSFMTERITGGASQVQSWQLMDDELSNCVHQSLNSSDCVSQTFVEGAAGRVAYGARKSRVQRLGQIQEQQRNVKTLSFDPRNDDVHYQSVISTIFKTNHQLILGPQFRNCDKQSSFTRWKKSSSSSSGTATVTAPSQGMLKKIIFDVPRVHQKEKLMLDSPEARDETGNHAVLEKKRREKLNERFMTLRKIIPSINKIDKVSILDDTIEYLQELERRVQELESCRESTDTETRGTMTMKRKKPCDAGERTSANCANNETGNGKKVSVNNVGEAEPADTGFTGLTDNLRIGSFGNEVVIELRCAWREGVLLEIMDVISDLHLDSHSVQSSTGDGLLCLTVNCKHKGSKIATPGMIKEALQRVAWIC 5225EF0E9745CDB7 ttg1_arath Protein TRANSPARENT TESTA GLABRA 1 TTG1 At5g24520 T31K7.8 K18P6_4 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MDNSAPDSLSRSETAVTYDSPYPLYAMAFSSLRSSSGHRIAVGSFLEDYNNRIDILSFDSDSMTVKPLPNLSFEHPYPPTKLMFSPPSLRRPSSGDLLASSGDFLRLWEINEDSSTVEPISVLNNSKTSEFCAPLTSFDWNDVEPKRLGTCSIDTTCTIWDIEKSVVETQLIAHDKEVHDIAWGEARVFASVSADGSVRIFDLRDKEHSTIIYESPQPDTPLLRLAWNKQDLRYMATILMDSNKVVILDIRSPTMPVAELERHQASVNAIAWAPQSCKHICSGGDDTQALIWELPTVAGPNGIDPMSVYSAGSEINQLQWSSSQPDWIGIAFANKMQLLRV B247738AE41FEE38 cpc_arath Transcription factor CPC Protein CAPRICE At2g46410 CPC F11C10.10 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MFRSDKAEKMDKRRRRQSKAKASCSEEVSSIEWEAVKMSEEEEDLISRMYKLVGDRWELIAGRIPGRTPEEIERYWLMKHGVVFANRRRDFFRK 608B1C7B4BA48846 try_arath Transcription factor TRY TRY MFH8.14 Protein TRIPTYCHON At5g53200 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MDNTDRRRRRKQHKIALHDSEEVSSIEWEFINMTEQEEDLIFRMYRLVGDRWDLIAGRVPGRQPEEIERYWIMRNSEGFADKRRQLHSSSHKHTKPHRPRFSIYPS 2957DF51D3F86D86 gl1_arath Trichome differentiation protein GL1 GL1 MYB0 K16N12.17 At3g27920 Protein GLABROUS 1 Protein GLABRA 1 R2R3-MYB transcription factor GL1 Myb-related protein 0 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MRIRRRDEKENQEYKKGLWTVEEDNILMDYVLNHGTGQWNRIVRKTGLKRCGKSCRLRWMNYLSPNVNKGNFTEQEEDLIIRLHKLLGNRWSLIAKRVPGRTDNQVKNYWNTHLSKKLVGDYSSAVKTTGEDDDSPPSLFITAATPSSCHHQQENIYENIAKSFNGVVSASYEDKPKQELAQKDVLMATTNDPSHYYGNNALWVHDDDFELSSLVMMNFASGDVEYCL DIP protein P27900 original sequence version: 134 822A8646F446F6B9 gl1-gl3-1 1 5 unspecified role unspecified role prey prey n-terminal binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 9 unspecified role unspecified role bait bait n-terminal binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 12 14 physical association physical association Table 2 We previously found that GL3 had three distinct proteinprotein interaction domains (Payne et al., 2000). (1) The first 100 amino acids were required for interactions with myb proteins GL1, PAP1 and PAP2, CPC and TRY pap1-gl3-2 1 5 unspecified role unspecified role prey prey n-terminal binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 3 unspecified role unspecified role bait bait n-terminal binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain physical association physical association Table 2 We previously found that GL3 had three distinct proteinprotein interaction domains (Payne et al., 2000). (1) The first 100 amino acids were required for interactions with myb proteins GL1, PAP1 and PAP2, CPC and TRY pap2-gl3-3 1 5 unspecified role unspecified role prey prey n-terminal binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 2 unspecified role unspecified role bait bait n-terminal binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 22 24 physical association physical association Table 2 We previously found that GL3 had three distinct proteinprotein interaction domains (Payne et al., 2000). (1) The first 100 amino acids were required for interactions with myb proteins GL1, PAP1 and PAP2, CPC and TRY cpc-gl3 1 5 unspecified role unspecified role prey prey n-terminal binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 7 unspecified role unspecified role bait bait physical association physical association Table 2 We previously found that GL3 had three distinct proteinprotein interaction domains (Payne et al., 2000). (1) The first 100 amino acids were required for interactions with myb proteins GL1, PAP1 and PAP2, CPC and TRY try-gl3 1 5 unspecified role unspecified role prey prey n-terminal binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 8 unspecified role unspecified role bait bait physical association physical association Table 2 We previously found that GL3 had three distinct proteinprotein interaction domains (Payne et al., 2000). (1) The first 100 amino acids were required for interactions with myb proteins GL1, PAP1 and PAP2, CPC and TRY gl3-gl3-1 1 5 unspecified role unspecified role bait bait c-terminal binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 5 unspecified role unspecified role prey prey c-terminal binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 37 35 physical association physical association Table 2 We previously found that GL3 had three distinct proteinprotein interaction domains (Payne et al., 2000). (1) The first 100 amino acids were required for interactions with myb proteins GL1, PAP1 and PAP2, CPC and TRY. presented here; Table 2), (2) approximately amino acids 200-400 mediated interaction with TTG1, and (3) a carboxy end fragment including the bHLH domain was able to interact with itself (homodimerize). egl3-gl3 1 5 unspecified role unspecified role prey prey c-terminal binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 4 unspecified role unspecified role bait bait c-terminal binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain physical association physical association Table 2 Two-hybrid studies (Table 2) showed that the EGL3 amino fragment interacted with full-length TTG1 and the myb domains of GL1, PAP1 and PAP2, CPC and TRY. The EGL3 carboxy fragment interacted with itself and the full-length and bHLH end of GL3. All EGL3 interactions observed were consistent with a model where EGL3 and GL3 are able to form essentially the same protein-protein interactions. ttg1-gl3 1 6 unspecified role unspecified role bait bait 5 unspecified role unspecified role prey prey region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain physical association physical association Table 2 The first 100 amino acids were required for interactions with myb proteins GL1, PAP1 and PAP2, CPC and TRY (the latter fourpresented here; Table 2), (2) approximately amino acids 200-400 mediated interaction with TTG1, gl1-egl3 1 9 unspecified role unspecified role bait bait n-terminal binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 4 unspecified role unspecified role prey prey n-terminal binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain physical association physical association Table 2 Two-hybrid studies (Table 2) showed that the EGL3 amino fragment interacted with full-length TTG1 and the myb domains of GL1, PAP1 and PAP2, CPC and TRY. The EGL3 carboxy fragment interacted with itself and the full-length and bHLH end of GL3. All EGL3 interactions observed were consistent with a model where EGL3 and GL3 are able to form essentially the same protein-protein interactions. pap1-egl3-1 1 4 unspecified role unspecified role prey prey n-terminal binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 3 unspecified role unspecified role bait bait n-terminal binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 56 54 physical association physical association Table 2 Two-hybrid studies (Table 2) showed that the EGL3 amino fragment interacted with full-length TTG1 and the myb domains of GL1, PAP1 and PAP2, CPC and TRY. The EGL3 carboxy fragment interacted with itself and the full-length and bHLH end of GL3. All EGL3 interactions observed were consistent with a model where EGL3 and GL3 are able to form essentially the same protein-protein interactions. pap2-egl3 1 2 unspecified role unspecified role bait bait n-terminal binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 4 unspecified role unspecified role prey prey n-terminal binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain physical association physical association Table 2 Two-hybrid studies (Table 2) showed that the EGL3 amino fragment interacted with full-length TTG1 and the myb domains of GL1, PAP1 and PAP2, CPC and TRY. The EGL3 carboxy fragment interacted with itself and the full-length and bHLH end of GL3. All EGL3 interactions observed were consistent with a model where EGL3 and GL3 are able to form essentially the same protein-protein interactions. cpc-egl3 1 4 unspecified role unspecified role prey prey n-terminal binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 7 unspecified role unspecified role bait bait physical association physical association Table 2 Two-hybrid studies (Table 2) showed that the EGL3 amino fragment interacted with full-length TTG1 and the myb domains of GL1, PAP1 and PAP2, CPC and TRY. The EGL3 carboxy fragment interacted with itself and the full-length and bHLH end of GL3. All EGL3 interactions observed were consistent with a model where EGL3 and GL3 are able to form essentially the same protein-protein interactions. try-egl3 1 4 unspecified role unspecified role prey prey n-terminal binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 8 unspecified role unspecified role bait bait physical association physical association Table 2 Two-hybrid studies (Table 2) showed that the EGL3 amino fragment interacted with full-length TTG1 and the myb domains of GL1, PAP1 and PAP2, CPC and TRY. The EGL3 carboxy fragment interacted with itself and the full-length and bHLH end of GL3. All EGL3 interactions observed were consistent with a model where EGL3 and GL3 are able to form essentially the same protein-protein interactions. gl3-egl3-1 1 4 unspecified role unspecified role prey prey c-terminal binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 5 unspecified role unspecified role bait bait c-terminal binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain physical association physical association Table 2 Two-hybrid studies (Table 2) showed that the EGL3 amino fragment interacted with full-length TTG1 and the myb domains of GL1, PAP1 and PAP2, CPC and TRY. The EGL3 carboxy fragment interacted with itself and the full-length and bHLH end of GL3. All EGL3 interactions observed were consistent with a model where EGL3 and GL3 are able to form essentially the same protein-protein interactions. egl3-egl3 1 4 unspecified role unspecified role prey prey c-terminal binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 4 unspecified role unspecified role bait bait c-terminal binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain physical association physical association Table 2 Two-hybrid studies (Table 2) showed that the EGL3 amino fragment interacted with full-length TTG1 and the myb domains of GL1, PAP1 and PAP2, CPC and TRY. The EGL3 carboxy fragment interacted with itself and the full-length and bHLH end of GL3. All EGL3 interactions observed were consistent with a model where EGL3 and GL3 are able to form essentially the same protein-protein interactions. ttg1-egl3-1 1 4 unspecified role unspecified role prey prey n-terminal binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 6 unspecified role unspecified role bait bait physical association physical association Table 2 Two-hybrid studies (Table 2) showed that the EGL3 amino fragment interacted with full-length TTG1 and the myb domains of GL1, PAP1 and PAP2, CPC and TRY. The EGL3 carboxy fragment interacted with itself and the full-length and bHLH end of GL3. All EGL3 interactions observed were consistent with a model where EGL3 and GL3 are able to form essentially the same protein-protein interactions.