DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates. Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates. Nature structural & molecular biology 2006 imex curation Reverter D., Lima CD. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Reverter D., Lima CD. DIP original experiment: DIP-66595X Nature structural & molecular biology 2006 IMEx Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates. Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates. Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates. Nature structural & molecular biology 2006 imex curation Reverter D., Lima CD. Only protein-protein interactions in vitro In vitro enzymatic study enzymatic study predetermined predetermined participant predetermined Reverter D., Lima CD. DIP original experiment: DIP-66598X Nature structural & molecular biology 2006 IMEx Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates. Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates. Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates. Nature structural & molecular biology 2006 imex curation Reverter D., Lima CD. 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 Reverter D., Lima CD. DIP original experiment: DIP-66599X Nature structural & molecular biology 2006 IMEx Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates. Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates. Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates. Nature structural & molecular biology 2006 imex curation Reverter D., Lima CD. Only protein-protein interactions in vitro In vitro enzymatic study enzymatic study predetermined predetermined participant predetermined Reverter D., Lima CD. DIP original experiment: DIP-66601X Nature structural & molecular biology 2006 IMEx Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates. Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates. Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates. Nature structural & molecular biology 2006 imex curation Reverter D., Lima CD. Only protein-protein interactions in vitro In vitro enzymatic study enzymatic study predetermined predetermined participant predetermined Reverter D., Lima CD. DIP original experiment: DIP-66594X Nature structural & molecular biology 2006 IMEx Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates. Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates. Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates. Nature structural & molecular biology 2006 imex curation Reverter D., Lima CD. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Reverter D., Lima CD. DIP original experiment: DIP-66596X Nature structural & molecular biology 2006 IMEx Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates. Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates. Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates. Nature structural & molecular biology 2006 imex curation Reverter D., Lima CD. 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 Reverter D., Lima CD. DIP original experiment: DIP-66600X Nature structural & molecular biology 2006 IMEx Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates. Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates. Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates. Nature structural & molecular biology 2006 imex curation Reverter D., Lima CD. 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 Reverter D., Lima CD. DIP original experiment: DIP-66593X Nature structural & molecular biology 2006 IMEx Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates. Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates. Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates. Nature structural & molecular biology 2006 imex curation Reverter D., Lima CD. Only protein-protein interactions in vitro In vitro enzymatic study enzymatic study predetermined predetermined participant predetermined Reverter D., Lima CD. DIP original experiment: DIP-66603X Nature structural & molecular biology 2006 IMEx Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates. Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates. Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates. Nature structural & molecular biology 2006 imex curation Reverter D., Lima CD. Only protein-protein interactions in vitro In vitro enzymatic study enzymatic study predetermined predetermined participant predetermined Reverter D., Lima CD. DIP original experiment: DIP-66597X Nature structural & molecular biology 2006 IMEx Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates. Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates. Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates. Nature structural & molecular biology 2006 imex curation Reverter D., Lima CD. Only protein-protein interactions in vitro In vitro enzymatic study enzymatic study predetermined predetermined participant predetermined Reverter D., Lima CD. DIP original experiment: DIP-66602X Nature structural & molecular biology 2006 IMEx Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates. 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 sumo3_human Small ubiquitin-related modifier 3 SMT3 homolog 1 SUMO-2 SMT3H1 SUMO3 SMT3A Ubiquitin-like protein SMT3A protein protein human Homo sapiens Human MSEEKPKEGVKTENDHINLKVAGQDGSVVQFKIKRHTPLSKLMKAYCERQGLSMRQIRFRFDGQPINETDTPAQLEMEDEDTIDVFQQQTGGVPESSLAGHSF DIP protein P55854 original sequence version: 56 DIP protein P55854 original sequence version: 127 DIP protein P55854 original sequence version: 106 DIP protein P55854 original sequence version: 124 DIP protein P55854 original sequence version: 99 E337E34CB5B3B187 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 senp2_human Sentrin-specific protease 2 Sentrin/SUMO-specific protease SENP2 SMT3-specific isopeptidase 2 Axam2 SENP2 KIAA1331 protein protein human Homo sapiens Human MYRWLVRILGTIFRFCDRSVPPARALLKRRRSDSTLFSTVDTDEIPAKRPRLDCFIHQVKNSLYNAASLFGFPFQLTTKPMVTSACNGTRNVAPSGEVFSNSSSCELTGSGSWNNMLKLGNKSPNGISDYPKIRVTVTRDQPRRVLPSFGFTLNSEGCNRRPGGRRHSKGNPESSLMWKPQEQAVTEMISEESGKGLRRPHCTVEEGVQKEEREKYRKLLERLKESGHGNSVCPVTSNYHSSQRSQMDTLKTKGWGEEQNHGVKTTQFVPKQYRLVETRGPLCSLRSEKRCSKGKITDTETMVGIRFENESRRGYQLEPDLSEEVSARLRLGSGSNGLLRRKVSIIETKEKNCSGKERDRRTDDLLELTEDMEKEISNALGHGPQDEILSSAFKLRITRGDIQTLKNYHWLNDEVINFYMNLLVERNKKQGYPALHVFSTFFYPKLKSGGYQAVKRWTKGVNLFEQEIILVPIHRKVHWSLVVIDLRKKCLKYLDSMGQKGHRICEILLQYLQDESKTKRNSDLNLLEWTHHSMKPHEIPQQLNGSDCGMFTCKYADYISRDKPITFTQHQMPLFRKKMVWEILHQQLL DIP protein Q9HC62 original sequence version: 49 712707DCC2C5431C 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-senp2-1 8 16 unspecified role unspecified role neutral component neutral component 419-587 bindng region 419-587 bindng 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 18-97 binding region 18-97 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 15 unspecified role unspecified role neutral component neutral component 364-589 binding region 364-589 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 Q9HC62:p.Cys548Ser C548S mutation mutation mutation predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain C S This feature has been corrected as a result of our quality control procedures. The original label was 'C548S mutation'. Wed May 02 19:00:05 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys548ser' Tue Jun 30 17:00:32 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys548Ser' ecolx Escherichia coli physical association physical association rangap1-senp2-2 5 12 unspecified role unspecified role neutral component neutral component 14-93 binding region 14-93 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 16 unspecified role unspecified role neutral component neutral component 419-587 bindng region 419-587 bindng 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 unspecified role unspecified role neutral component neutral component 364-589 binding region 364-589 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 Q9HC62:p.Cys548Ser C548S mutation mutation mutation predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain C S This feature has been corrected as a result of our quality control procedures. The original label was 'C548S mutation'. Wed May 02 16:10:49 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys548ser' Tue Jun 30 18:26:44 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys548Ser' ecolx Escherichia coli physical association physical association rangap1-senp2-3 1 16 unspecified role unspecified role neutral component neutral component 419-587 bindng region 419-587 bindng 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 18-101 binding region 18-101 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 unspecified role unspecified role neutral component neutral component 364-589 binding region 364-589 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 Q9HC62:p.Cys548Ser C548S mutation mutation mutation predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain C S This feature has been corrected as a result of our quality control procedures. The original label was 'C548S mutation'. Wed May 02 19:52:58 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys548ser' Tue Jun 30 18:06:51 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys548Ser' ecolx Escherichia coli physical association physical association rangap1-senp2-4 6 12 unspecified role unspecified role neutral component neutral component 14-95 binding region 14-95 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 16 unspecified role unspecified role neutral component neutral component 419-587 bindng region 419-587 bindng 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 unspecified role unspecified role neutral component neutral component 364-589 binding region 364-589 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 Q9HC62:p.Cys548Ser C548S mutation mutation mutation predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain C S This feature has been corrected as a result of our quality control procedures. The original label was 'C548S mutation'. Wed May 02 16:41:33 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys548ser' Tue Jun 30 16:59:36 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys548Ser' ecolx Escherichia coli physical association physical association rangap1-senp2-5 10 16 enzyme target enzyme target substrate substrate neutral component neutral component 419-587 bindng region 419-587 bindng 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 neutral component neutral component 18-101 binding region 18-101 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 enzyme neutral component neutral component 364-589 binding region 364-589 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 rangap1-senp2-6 2 12 enzyme target enzyme target substrate substrate neutral component neutral component 14-95 binding region 14-95 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 16 enzyme target enzyme target substrate substrate neutral component neutral component 419-587 bindng region 419-587 bindng 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 enzyme neutral component neutral component 364-589 binding region 364-589 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 senp2-sumo2-3 3 12 unspecified role unspecified role neutral component neutral component 14-95 binding region 14-95 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 unspecified role unspecified role neutral component neutral component 364-589 binding region 364-589 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 Q9HC62:p.Cys548Ser C548S mutation mutation mutation predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain C S This feature has been corrected as a result of our quality control procedures. The original label was 'C548S mutation'. Wed May 02 20:19:18 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys548ser' Tue Jun 30 18:02:35 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys548Ser' ecolx Escherichia coli direct interaction direct interaction senp2-sumo3-6 7 13 unspecified role unspecified role neutral component neutral component 14-103 binding region 14-103 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 unspecified role unspecified role neutral component neutral component 364-589 binding region 364-589 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 Q9HC62:p.Cys548Ser C548S mutation mutation mutation predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain C S This feature has been corrected as a result of our quality control procedures. The original label was 'C548S mutation'. Wed May 02 20:11:07 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys548ser' Tue Jun 30 17:43:03 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys548Ser' ecolx Escherichia coli direct interaction direct interaction senp2-sumo2-4 4 12 enzyme target enzyme target substrate substrate neutral component neutral component 14-95 binding region 14-95 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 enzyme neutral component neutral component 364-589 binding region 364-589 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 senp2-sumo3-7 11 13 enzyme target enzyme target substrate substrate neutral component neutral component 14-103 binding region 14-103 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 enzyme neutral component neutral component 364-589 binding region 364-589 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 senp2-sumo1-2 9 14 enzyme target enzyme target substrate substrate unspecified role unspecified role 18-101 binding region 18-101 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 15 enzyme enzyme neutral component neutral component 364-589 binding region 364-589 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