DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu SUMO protease SENP1 induces isomerization of the scissile peptide bond. SUMO protease SENP1 induces isomerization of the scissile peptide bond. Nature structural & molecular biology 2006 imex curation Shen L., Tatham MH., Dong C., Zagórska A., Naismith JH., Hay RT. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Shen L., Tatham MH., Dong C., Zagórska A., Naismith JH., Hay RT. DIP original experiment: DIP-66587X Nature structural & molecular biology 2006 IMEx SUMO protease SENP1 induces isomerization of the scissile peptide bond. SUMO protease SENP1 induces isomerization of the scissile peptide bond. SUMO protease SENP1 induces isomerization of the scissile peptide bond. Nature structural & molecular biology 2006 imex curation Shen L., Tatham MH., Dong C., Zagórska A., Naismith JH., Hay RT. Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Shen L., Tatham MH., Dong C., Zagórska A., Naismith JH., Hay RT. DIP original experiment: DIP-66582X Nature structural & molecular biology 2006 IMEx SUMO protease SENP1 induces isomerization of the scissile peptide bond. SUMO protease SENP1 induces isomerization of the scissile peptide bond. SUMO protease SENP1 induces isomerization of the scissile peptide bond. Nature structural & molecular biology 2006 imex curation Shen L., Tatham MH., Dong C., Zagórska A., Naismith JH., Hay RT. Only protein-protein interactions in vitro In vitro enzymatic study enzymatic study predetermined predetermined participant predetermined Shen L., Tatham MH., Dong C., Zagórska A., Naismith JH., Hay RT. DIP original experiment: DIP-66590X Nature structural & molecular biology 2006 IMEx SUMO protease SENP1 induces isomerization of the scissile peptide bond. SUMO protease SENP1 induces isomerization of the scissile peptide bond. SUMO protease SENP1 induces isomerization of the scissile peptide bond. Nature structural & molecular biology 2006 imex curation Shen L., Tatham MH., Dong C., Zagórska A., Naismith JH., Hay RT. Only protein-protein interactions in vitro In vitro fret fluorescent resonance energy transfer FRET RET FRET analysis FRET RET FRET analysis fret predetermined predetermined participant predetermined Shen L., Tatham MH., Dong C., Zagórska A., Naismith JH., Hay RT. DIP original experiment: DIP-66585X Nature structural & molecular biology 2006 IMEx SUMO protease SENP1 induces isomerization of the scissile peptide bond. SUMO protease SENP1 induces isomerization of the scissile peptide bond. SUMO protease SENP1 induces isomerization of the scissile peptide bond. Nature structural & molecular biology 2006 imex curation Shen L., Tatham MH., Dong C., Zagórska A., Naismith JH., Hay RT. Only protein-protein interactions in vitro In vitro enzymatic study enzymatic study predetermined predetermined participant predetermined Shen L., Tatham MH., Dong C., Zagórska A., Naismith JH., Hay RT. DIP original experiment: DIP-66591X Nature structural & molecular biology 2006 IMEx SUMO protease SENP1 induces isomerization of the scissile peptide bond. SUMO protease SENP1 induces isomerization of the scissile peptide bond. SUMO protease SENP1 induces isomerization of the scissile peptide bond. Nature structural & molecular biology 2006 imex curation Shen L., Tatham MH., Dong C., Zagórska A., Naismith JH., Hay RT. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Shen L., Tatham MH., Dong C., Zagórska A., Naismith JH., Hay RT. DIP original experiment: DIP-66588X Nature structural & molecular biology 2006 IMEx SUMO protease SENP1 induces isomerization of the scissile peptide bond. SUMO protease SENP1 induces isomerization of the scissile peptide bond. SUMO protease SENP1 induces isomerization of the scissile peptide bond. Nature structural & molecular biology 2006 imex curation Shen L., Tatham MH., Dong C., Zagórska A., Naismith JH., Hay RT. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Shen L., Tatham MH., Dong C., Zagórska A., Naismith JH., Hay RT. DIP original experiment: DIP-66586X Nature structural & molecular biology 2006 IMEx SUMO protease SENP1 induces isomerization of the scissile peptide bond. SUMO protease SENP1 induces isomerization of the scissile peptide bond. SUMO protease SENP1 induces isomerization of the scissile peptide bond. Nature structural & molecular biology 2006 imex curation Shen L., Tatham MH., Dong C., Zagórska A., Naismith JH., Hay RT. Only protein-protein interactions in vitro In vitro fret fluorescent resonance energy transfer FRET RET FRET analysis FRET RET FRET analysis fret predetermined predetermined participant predetermined Shen L., Tatham MH., Dong C., Zagórska A., Naismith JH., Hay RT. DIP original experiment: DIP-66584X Nature structural & molecular biology 2006 IMEx SUMO protease SENP1 induces isomerization of the scissile peptide bond. SUMO protease SENP1 induces isomerization of the scissile peptide bond. SUMO protease SENP1 induces isomerization of the scissile peptide bond. Nature structural & molecular biology 2006 imex curation Shen L., Tatham MH., Dong C., Zagórska A., Naismith JH., Hay RT. Only protein-protein interactions in vitro In vitro enzymatic study enzymatic study predetermined predetermined participant predetermined Shen L., Tatham MH., Dong C., Zagórska A., Naismith JH., Hay RT. DIP original experiment: DIP-66589X Nature structural & molecular biology 2006 IMEx SUMO protease SENP1 induces isomerization of the scissile peptide bond. SUMO protease SENP1 induces isomerization of the scissile peptide bond. SUMO protease SENP1 induces isomerization of the scissile peptide bond. Nature structural & molecular biology 2006 imex curation Shen L., Tatham MH., Dong C., Zagórska A., Naismith JH., Hay RT. Only protein-protein interactions in vitro In vitro enzymatic study enzymatic study predetermined predetermined participant predetermined Shen L., Tatham MH., Dong C., Zagórska A., Naismith JH., Hay RT. DIP original experiment: DIP-66592X Nature structural & molecular biology 2006 IMEx SUMO protease SENP1 induces isomerization of the scissile peptide bond. SUMO protease SENP1 induces isomerization of the scissile peptide bond. SUMO protease SENP1 induces isomerization of the scissile peptide bond. Nature structural & molecular biology 2006 imex curation Shen L., Tatham MH., Dong C., Zagórska A., Naismith JH., Hay RT. Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Shen L., Tatham MH., Dong C., Zagórska A., Naismith JH., Hay RT. DIP original experiment: DIP-66583X Nature structural & molecular biology 2006 IMEx SUMO protease SENP1 induces isomerization of the scissile peptide bond. sumo2_human Small ubiquitin-related modifier 2 SMT3 homolog 2 Sentrin-2 HSMT3 SUMO-3 SUMO2 SMT3H2 SMT3B Ubiquitin-like protein SMT3B protein protein human Homo sapiens Human MADEKPKEGVKTENNDHINLKVAGQDGSVVQFKIKRHTPLSKLMKAYCERQGLSMRQIRFRFDGQPINETDTPAQLEMEDEDTIDVFQQQTGGVY DIP protein P61956 original sequence version: 39 DIP protein P61956 original sequence version: 79 DIP protein P61956 original sequence version: 81 DIP protein P61956 original sequence version: 77 DIP protein P61956 original sequence version: 98 DIP protein P61956 original sequence version: 116 DIP protein P61956 original sequence version: 141 F8F0426849BEF08B senp1_human Sentrin-specific protease 1 SENP1 Sentrin/SUMO-specific protease SENP1 protein protein human Homo sapiens Human MDDIADRMRMDAGEVTLVNHNSVFKTHLLPQTGFPEDQLSLSDQQILSSRQGHLDRSFTCSTRSAAYNPSYYSDNPSSDSFLGSGDLRTFGQSANGQWRNSTPSSSSSLQKSRNSRSLYLETRKTSSGLSNSFAGKSNHHCHVSAYEKSFPIKPVPSPSWSGSCRRSLLSPKKTQRRHVSTAEETVQEEEREIYRQLLQMVTGKQFTIAKPTTHFPLHLSRCLSSSKNTLKDSLFKNGNSCASQIIGSDTSSSGSASILTNQEQLSHSVYSLSSYTPDVAFGSKDSGTLHHPHHHHSVPHQPDNLAASNTQSEGSDSVILLKVKDSQTPTPSSTFFQAELWIKELTSVYDSRARERLRQIEEQKALALQLQNQRLQEREHSVHDSVELHLRVPLEKEIPVTVVQETQKKGHKLTDSEDEFPEITEEMEKEIKNVFRNGNQDEVLSEAFRLTITRKDIQTLNHLNWLNDEIINFYMNMLMERSKEKGLPSVHAFNTFFFTKLKTAGYQAVKRWTKKVDVFSVDILLVPIHLGVHWCLAVVDFRKKNITYYDSMGGINNEACRILLQYLKQESIDKKRKEFDTNGWQLFSKKSQEIPQQMNGSDCGMFACKYADCITKDRPINFTQQHMPYFRKRMVWEILHRKLL DIP protein Q9P0U3 original sequence version: 45 941951A8B341EC64 sumo1_human Small ubiquitin-related modifier 1 SUMO1 Sentrin Ubiquitin-like protein SMT3C Ubiquitin-homology domain protein PIC1 Ubiquitin-like protein UBL1 GAP-modifying protein 1 SMT3 homolog 3 SMT3C SMT3H3 UBL1 OK/SW-cl.43 protein protein human Homo sapiens Human MSDQEAKPSTEDLGDKKEGEYIKLKVIGQDSSEIHFKVKMTTHLKKLKESYCQRQGVPMNSLRFLFEGQRIADNHTPKELGMEEEDVIEVYQEQTGGHSTV DIP protein P63165 original sequence version: 36 DIP protein P63165 original sequence version: 40 DIP protein P63165 original sequence version: 124 DIP protein P63165 original sequence version: 125 DIP protein P63165 original sequence version: 83 DIP protein P63165 original sequence version: 85 DIP protein P63165 original sequence version: 81 DIP protein P63165 original sequence version: 84 DIP protein P63165 original sequence version: 103 DIP protein P63165 original sequence version: 100 DIP protein P63165 original sequence version: 95 DIP protein P63165 original sequence version: 98 DIP protein P63165 original sequence version: 101 DIP protein P63165-1 original sequence version: 131 DIP protein P63165 original sequence version: 102 DIP protein P63165 original sequence version: 122 DIP protein P63165 original sequence version: 62 DIP protein P63165 original sequence version: 119 DIP protein P63165 original sequence version: 82 89BE97D2D054FB33 ragp1_human Ran GTPase-activating protein 1 RANGAP1 KIAA1835 SD protein protein human Homo sapiens Human MASEDIAKLAETLAKTQVAGGQLSFKGKSLKLNTAEDAKDVIKEIEDFDSLEALRLEGNTVGVEAARVIAKALEKKSELKRCHWSDMFTGRLRTEIPPALISLGEGLITAGAQLVELDLSDNAFGPDGVQGFEALLKSSACFTLQELKLNNCGMGIGGGKILAAALTECHRKSSAQGKPLALKVFVAGRNRLENDGATALAEAFRVIGTLEEVHMPQNGINHPGITALAQAFAVNPLLRVINLNDNTFTEKGAVAMAETLKTLRQVEVINFGDCLVRSKGAVAIADAIRGGLPKLKELNLSFCEIKRDAALAVAEAMADKAELEKLDLNGNTLGEEGCEQLQEVLEGFNMAKVLASLSDDEDEEEEEEGEEEEEEAEEEEEEDEEEEEEEEEEEEEEPQQRGQGEKSATPSRKILDPNTGEPAPVLSSPPPADVSTFLAFPSPEKLLRLGPKSSVLIAQQTDTSDPEKVVSAFLKVSSVFKDEATVRMAVQDAVDALMQKAFNSSSFNSNTFLTRLLVHMGLLKSEDKVKAIANLYGPLMALNHMVQQDYFPKALAPLLLAFVTKPNSALESCSFARHSLLQTLYKV DIP protein P46060 original sequence version: 74 DIP protein P46060 original sequence version: 77 DIP protein P46060 original sequence version: 120 DIP protein P46060 original sequence version: 147 3C18068AAC06B98F rangap1-senp1-1 2 13 unspecified role unspecified role neutral component neutral component 415-644 binding region 415-644 binding region sufficient to bind sufficient binding region sufficient to bind predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain Q9P0U3:p.Cys603Ala C603A mutation mutation mutation predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain C A This feature has been corrected as a result of our quality control procedures. The original label was 'C603A mutation'. Wed May 02 20:15:34 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys603ala' Tue Jun 30 18:08:12 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys603Ala' ecolx Escherichia coli 15 unspecified role unspecified role neutral component neutral component 418-587 binding region 418-587 binding region sufficient to bind sufficient binding region sufficient to bind predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 14 unspecified role unspecified role neutral component neutral component 1-97 binding region 1-97 binding region sufficient to bind sufficient binding region sufficient to bind predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli physical association physical association senp1-sumo1-5 11 13 unspecified role unspecified role neutral component neutral component 415-644 binding region 415-644 binding region sufficient to bind sufficient binding region sufficient to bind predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain Q9P0U3:p.Cys603Ala C603A mutation mutation mutation predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain C A This feature has been corrected as a result of our quality control procedures. The original label was 'C603A mutation'. Wed May 02 17:17:42 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys603ala' Wed May 02 20:29:25 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys603ala' Tue Jun 30 17:58:39 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys603Ala' ecolx Escherichia coli 14 unspecified role unspecified role neutral component neutral component ecolx Escherichia coli direct interaction direct interaction senp1-sumo1-6 8 13 unspecified role unspecified role unspecified role unspecified role 415-644 binding region 415-644 binding region sufficient to bind sufficient binding region sufficient to bind predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain Q9P0U3:p.Cys603Ala C603A mutation mutation mutation predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain C A This feature has been corrected as a result of our quality control procedures. The original label was 'C603A mutation'. Wed May 02 16:21:00 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys603ala' Tue Jun 30 15:49:59 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys603Ala' ecolx Escherichia coli 14 unspecified role unspecified role fret pair fluorescence acceptor donor pair fret pair YFP Tag YFP Tag yfp tag yellow fluorescent protein tag YFP yellow fluorescent protein yellow fluorescent protein YFP yfp tag predetermined featur predetermined feature predetermined featur c-term range C-terminal range c-term range c-term range C-terminal range c-term range CFP Tag CFP Tag cfp tag cyan fluorescent protein tag CFP cyan fluorescent protein cyan fluorescent protein CFP cfp tag predetermined featur predetermined feature predetermined featur n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli direct interaction direct interaction senp1-sumo2-5 4 12 unspecified role unspecified role fret pair fluorescence acceptor donor pair fret pair CFP Tag CFP Tag cfp tag cyan fluorescent protein tag CFP cyan fluorescent protein cyan fluorescent protein CFP cfp tag predetermined featur predetermined feature predetermined featur n-term range n-terminal range n-term range n-term range n-terminal range n-term range YFP Tag YFP Tag yfp tag yellow fluorescent protein tag YFP yellow fluorescent protein yellow fluorescent protein YFP yfp tag predetermined featur predetermined feature predetermined featur c-term range C-terminal range c-term range c-term range C-terminal range c-term range ecolx Escherichia coli 13 unspecified role unspecified role neutral component neutral component 415-644 binding region 415-644 binding region sufficient to bind sufficient binding region sufficient to bind predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain Q9P0U3:p.Cys603Ala C603A mutation mutation mutation predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain C A This feature has been corrected as a result of our quality control procedures. The original label was 'C603A mutation'. Wed May 02 16:16:22 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys603ala' Tue Jun 30 16:04:29 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys603Ala' ecolx Escherichia coli direct interaction direct interaction rangap1-senp1-2 7 13 unspecified role unspecified role neutral component neutral component 415-644 binding region 415-644 binding region sufficient to bind sufficient binding region sufficient to bind predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain Q9P0U3:p.Cys603Ala C603A mutation mutation mutation predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain C A This feature has been corrected as a result of our quality control procedures. The original label was 'C603A mutation'. Wed May 02 15:22:43 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys603ala' Tue Jun 30 18:01:08 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys603Ala' ecolx Escherichia coli 15 unspecified role unspecified role neutral component neutral component 418-587 binding region 418-587 binding region sufficient to bind sufficient binding region sufficient to bind predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 14 unspecified role unspecified role neutral component neutral component 1-97 binding region 1-97 binding region sufficient to bind sufficient binding region sufficient to bind predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli physical association physical association senp1-sumo1-7 1 13 unspecified role unspecified role neutral component neutral component 415-644 binding region 415-644 binding region sufficient to bind sufficient binding region sufficient to bind predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain Q9P0U3:p.Cys603Ala C603A mutation mutation mutation predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain C A This feature has been corrected as a result of our quality control procedures. The original label was 'C603A mutation'. Wed May 02 17:03:56 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys603ala' Tue Jun 30 19:17:41 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys603Ala' ecolx Escherichia coli 14 unspecified role unspecified role neutral component neutral component ecolx Escherichia coli direct interaction direct interaction senp1-sumo2-6 6 12 unspecified role unspecified role neutral component neutral component ecolx Escherichia coli 13 unspecified role unspecified role neutral component neutral component 415-644 binding region 415-644 binding region sufficient to bind sufficient binding region sufficient to bind predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain Q9P0U3:p.Cys603Ala C603A mutation mutation mutation predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain C A This feature has been corrected as a result of our quality control procedures. The original label was 'C603A mutation'. Wed May 02 15:17:06 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys603ala' Tue Jun 30 19:18:13 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys603Ala' ecolx Escherichia coli direct interaction direct interaction senp1-sumo1-8 9 13 enzyme enzyme unspecified role unspecified role region region sufficient to bind sufficient binding region sufficient to bind predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 14 enzyme target enzyme target substrate substrate fret pair fluorescence acceptor donor pair fret pair YFP Tag YFP Tag yfp tag yellow fluorescent protein tag YFP yellow fluorescent protein yellow fluorescent protein YFP yfp tag predetermined featur predetermined feature predetermined featur c-term range C-terminal range c-term range c-term range C-terminal range c-term range CFP Tag CFP Tag cfp tag cyan fluorescent protein tag CFP cyan fluorescent protein cyan fluorescent protein CFP cfp tag predetermined featur predetermined feature predetermined featur n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli direct interaction direct interaction senp1-sumo2-7 3 12 enzyme target enzyme target substrate substrate fret pair fluorescence acceptor donor pair fret pair CFP Tag CFP Tag cfp tag cyan fluorescent protein tag CFP cyan fluorescent protein cyan fluorescent protein CFP cfp tag predetermined featur predetermined feature predetermined featur n-term range n-terminal range n-term range n-term range n-terminal range n-term range YFP Tag YFP Tag yfp tag yellow fluorescent protein tag YFP yellow fluorescent protein yellow fluorescent protein YFP yfp tag predetermined featur predetermined feature predetermined featur c-term range C-terminal range c-term range c-term range C-terminal range c-term range ecolx Escherichia coli 13 enzyme enzyme neutral component neutral component 415-644 binding region 415-644 binding region sufficient to bind sufficient binding region sufficient to bind predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction sumo1-rangap1-2 5 13 enzyme enzyme neutral component neutral component 415-644 binding region 415-644 binding region sufficient to bind sufficient binding region sufficient to bind predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 15 enzyme target enzyme target substrate substrate fluorescence accept fluorescence acceptor fluorescence accept 418-587 binding region 418-587 binding region sufficient to bind sufficient binding region sufficient to bind predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain YFP Tag YFP Tag yfp tag yellow fluorescent protein tag YFP yellow fluorescent protein yellow fluorescent protein YFP yfp tag predetermined featur predetermined feature predetermined featur n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli 14 enzyme target enzyme target substrate substrate fluorescence donor fluorescence donor 1-97 binding region 1-97 binding region sufficient to bind sufficient binding region sufficient to bind predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain CFP Tag CFP Tag cfp tag cyan fluorescent protein tag CFP cyan fluorescent protein cyan fluorescent protein CFP cfp tag predetermined featur predetermined feature predetermined featur n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli physical association physical association sumo2-rangap1-1 10 12 enzyme target enzyme target substrate substrate fluorescence donor fluorescence donor CFP Tag CFP Tag cfp tag cyan fluorescent protein tag CFP cyan fluorescent protein cyan fluorescent protein CFP cfp tag predetermined featur predetermined feature predetermined featur n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli 13 enzyme enzyme neutral component neutral component 415-644 binding region 415-644 binding region sufficient to bind sufficient binding region sufficient to bind predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 15 enzyme target enzyme target substrate substrate fluorescence accept fluorescence acceptor fluorescence accept 418-587 binding region 418-587 binding region sufficient to bind sufficient binding region sufficient to bind predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain YFP Tag YFP Tag yfp tag yellow fluorescent protein tag YFP yellow fluorescent protein yellow fluorescent protein YFP yfp tag predetermined featur predetermined feature predetermined featur n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli physical association physical association