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 and functional characterization of the phosphorylation-dependent interaction between PML and SUMO1. Structural and functional characterization of the phosphorylation-dependent interaction between PML and SUMO1. Structure (London, England : 1993) 2015 imex curation Cappadocia L., Mascle XH., Bourdeau V., Tremblay-Belzile S., Chaker-Margot M., Lussier-Price M., Wada J., Sakaguchi K., Aubry M., Ferbeyre G., Omichinski JG. Only protein-protein interactions human Homo sapiens Human bret bioluminescence resonance energy transfer BRET LRET LRET BRET bret predetermined predetermined participant predetermined Cappadocia L., Mascle XH., Bourdeau V., Tremblay-Belzile S., Chaker-Margot M., Lussier-Price M., Wada J., Sakaguchi K., Aubry M., Ferbeyre G., Omichinski JG. DIP original experiment: DIP-264704X Structure (London, England : 1993) 2015 IMEx Structural and functional characterization of the phosphorylation-dependent interaction between PML and SUMO1. Structural and functional characterization of the phosphorylation-dependent interaction between PML and SUMO1. Structural and functional characterization of the phosphorylation-dependent interaction between PML and SUMO1. Structure (London, England : 1993) 2015 imex curation Cappadocia L., Mascle XH., Bourdeau V., Tremblay-Belzile S., Chaker-Margot M., Lussier-Price M., Wada J., Sakaguchi K., Aubry M., Ferbeyre G., Omichinski JG. 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 Cappadocia L., Mascle XH., Bourdeau V., Tremblay-Belzile S., Chaker-Margot M., Lussier-Price M., Wada J., Sakaguchi K., Aubry M., Ferbeyre G., Omichinski JG. DIP original experiment: DIP-264702X Structure (London, England : 1993) 2015 IMEx Structural and functional characterization of the phosphorylation-dependent interaction between PML and SUMO1. Structural and functional characterization of the phosphorylation-dependent interaction between PML and SUMO1. Structural and functional characterization of the phosphorylation-dependent interaction between PML and SUMO1. Structure (London, England : 1993) 2015 imex curation Cappadocia L., Mascle XH., Bourdeau V., Tremblay-Belzile S., Chaker-Margot M., Lussier-Price M., Wada J., Sakaguchi K., Aubry M., Ferbeyre G., Omichinski JG. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Cappadocia L., Mascle XH., Bourdeau V., Tremblay-Belzile S., Chaker-Margot M., Lussier-Price M., Wada J., Sakaguchi K., Aubry M., Ferbeyre G., Omichinski JG. DIP original experiment: DIP-264705X Structure (London, England : 1993) 2015 IMEx Structural and functional characterization of the phosphorylation-dependent interaction between PML and SUMO1. Structural and functional characterization of the phosphorylation-dependent interaction between PML and SUMO1. Structural and functional characterization of the phosphorylation-dependent interaction between PML and SUMO1. Structure (London, England : 1993) 2015 imex curation Cappadocia L., Mascle XH., Bourdeau V., Tremblay-Belzile S., Chaker-Margot M., Lussier-Price M., Wada J., Sakaguchi K., Aubry M., Ferbeyre G., Omichinski JG. Only protein-protein interactions human Homo sapiens Human bret bioluminescence resonance energy transfer BRET LRET LRET BRET bret predetermined predetermined participant predetermined Cappadocia L., Mascle XH., Bourdeau V., Tremblay-Belzile S., Chaker-Margot M., Lussier-Price M., Wada J., Sakaguchi K., Aubry M., Ferbeyre G., Omichinski JG. DIP original experiment: DIP-264703X Structure (London, England : 1993) 2015 IMEx Structural and functional characterization of the phosphorylation-dependent interaction between PML and SUMO1. Structural and functional characterization of the phosphorylation-dependent interaction between PML and SUMO1. Structural and functional characterization of the phosphorylation-dependent interaction between PML and SUMO1. Structure (London, England : 1993) 2015 imex curation Cappadocia L., Mascle XH., Bourdeau V., Tremblay-Belzile S., Chaker-Margot M., Lussier-Price M., Wada J., Sakaguchi K., Aubry M., Ferbeyre G., Omichinski JG. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Cappadocia L., Mascle XH., Bourdeau V., Tremblay-Belzile S., Chaker-Margot M., Lussier-Price M., Wada J., Sakaguchi K., Aubry M., Ferbeyre G., Omichinski JG. DIP original experiment: DIP-264706X Structure (London, England : 1993) 2015 IMEx Structural and functional characterization of the phosphorylation-dependent interaction between PML and SUMO1. pml_human Protein PML PML MYL RNF71 TRIM19 Tripartite motif-containing protein 19 RING finger protein 71 Promyelocytic leukemia protein PP8675 E3 SUMO-protein ligase PML RING-type E3 SUMO transferase PML protein protein human Homo sapiens Human MEPAPARSPRPQQDPARPQEPTMPPPETPSEGRQPSPSPSPTERAPASEEEFQFLRCQQCQAEAKCPKLLPCLHTLCSGCLEASGMQCPICQAPWPLGADTPALDNVFFESLQRRLSVYRQIVDAQAVCTRCKESADFWCFECEQLLCAKCFEAHQWFLKHEARPLAELRNQSVREFLDGTRKTNNIFCSNPNHRTPTLTSIYCRGCSKPLCCSCALLDSSHSELKCDISAEIQQRQEELDAMTQALQEQDSAFGAVHAQMHAAVGQLGRARAETEELIRERVRQVVAHVRAQERELLEAVDARYQRDYEEMASRLGRLDAVLQRIRTGSALVQRMKCYASDQEVLDMHGFLRQALCRLRQEEPQSLQAAVRTDGFDEFKVRLQDLSSCITQGKDAAVSKKASPEAASTPRDPIDVDLPEEAERVKAQVQALGLAEAQPMAVVQSVPGAHPVPVYAFSIKGPSYGEDVSNTTTAQKRKCSQTQCPRKVIKMESEEGKEARLARSSPEQPRPSTSKAVSPPHLDGPPSPRSPVIGSEVFLPNSNHVASGAGEAEERVVVISSSEDSDAENSSSRELDDSSSESSDLQLEGPSTLRVLDENLADPQAEDRPLVFFDLKIDNETQKISQLAAVNRESKFRVVIQPEAFFSIYSKAVSLEVGLQHFLSFLSSMRRPILACYKLWGPGLPNFFRALEDINRLWEFQEAISGFLAALPLIRERVPGASSFKLKNLAQTYLARNMSERSAMAAVLAMRDLCRLLEVSPGPQLAQHVYPFSSLQCFASLQPLVQAAVLPRAEARLLALHNVSFMELLSAHRRDRQGGLKKYSRYLSLQTTTLPPAQPAFNLQALGTYFEGLLEGPALARAEGVSTPLAGRGLAERASQQS DIP protein P29590 original sequence version: 188 DIP protein P29590 original sequence version: 195 DIP protein P29590-1 original sequence version: 187 D50968A977E34287 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 p29590-9 Protein PML PML-III PML MYL PP8675 RNF71 TRIM19 Promyelocytic leukemia protein RING finger protein 71 Tripartite motif-containing protein 19 E3 SUMO-protein ligase PML RING-type E3 SUMO transferase PML protein protein human Homo sapiens Human MEPAPARSPRPQQDPARPQEPTMPPPETPSEGRQPSPSPSPTERAPASEEEFQFLRCQQCQAEAKCPKLLPCLHTLCSGCLEASGMQCPICQAPWPLGADTPALDNVFFESLQRRLSVYRQIVDAQAVCTRCKESADFWCFECEQLLCAKCFEAHQWFLKHEARPLAELRNQSVREFLDGTRKTNNIFCSNPNHRTPTLTSIYCRGCSKPLCCSCALLDSSHSELKCDISAEIQQRQEELDAMTQALQEQDSAFGAVHAQMHAAVGQLGRARAETEELIRERVRQVVAHVRAQERELLEAVDARYQRDYEEMASRLGRLDAVLQRIRTGSALVQRMKCYASDQEVLDMHGFLRQALCRLRQEEPQSLQAAVRTDGFDEFKVRLQDLSSCITQGKDAAVSKKASPEAASTPRDPIDVDLPEEAERVKAQVQALGLAEAQPMAVVQSVPGAHPVPVYAFSIKGPSYGEDVSNTTTAQKRKCSQTQCPRKVIKMESEEGKEARLARSSPEQPRPSTSKAVSPPHLDGPPSPRSPVIGSEVFLPNSNHVASGAGEAEERVVVISSSEDSDAENSVSSSPQSEVLYWKVHGAHGDRRATVLASPLLASPLLASPLLASPVSAESTRSLQPALWHIPPPSLASPPAR 8262393E2B00CBC7 pml-sumo1-2 2 6 unspecified role unspecified role unspecified role unspecified role Region 547-573 Region 547-573 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 7 unspecified role unspecified role unspecified role unspecified role Region 17-97 Region 17-97 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction pml-sumo1-3 1 7 unspecified role unspecified role fluorescence accept fluorescence acceptor fluorescence accept GFP-tag GFP-tag gfp tag green fluorescent protein tag GFP green fluorescent protein GFP green fluorescent protein gfp tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range P63165:p.[Lys37Ala;Lys39Ala;Lys45_Lys46delinsAlaAla] K36A/K39A/K45A/K46A mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain KK AA certain certain sequence position certain certain certain sequence position certain K A certain certain sequence position certain certain certain sequence position certain K A Fri Jul 28 10:55:55 BST 2017 This feature has been corrected as a result of our quality control procedures. The original label was 'lys37ala,lys39ala,lys45-46ala_ala' Wed May 02 17:32:09 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys37ala,lys39ala,lys_lys45-46ala_ala' Tue Jun 30 18:41:27 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Lys37Ala;Lys39Ala;Lys45_Lys46delinsAlaAla]' human Homo sapiens Human 8 unspecified role unspecified role fluorescence donor fluorescence donor Rluc-tag Rluc-tag renilla luciferase renilla luciferase protein tag renilla luciferase undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined human Homo sapiens Human proximity proximity close-contact colocalization neighbourhood interaction pml-sumo1-4 5 6 unspecified role unspecified role unspecified role unspecified role Region 547-573 Region 547-573 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain pSer pSer opser O-phospho-L-serine (2S)-2-amino-3-(phosphonooxy)propanoic acid 2-amino-3-hydroxypropanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)propanoic acid ACT_SITE Phosphoserine intermediate MOD_RES Phosphoserine O-phospho-L-serine O-phosphonoserine O-phosphorylated L-serine O3-phosphoserine serine phosphate ester OPSer Phospho Phospho Seryl Phosphorylation phosphorylations certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain increasing-ptm ptm increasing an interaction increasing-ptm ecolx Escherichia coli 7 unspecified role unspecified role unspecified role unspecified role Region 2-97 Region 2-97 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction pml-sumo1-5 4 7 unspecified role unspecified role fluorescence accept fluorescence acceptor fluorescence accept GFP-tag GFP-tag gfp tag green fluorescent protein tag GFP green fluorescent protein GFP green fluorescent protein gfp tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range human Homo sapiens Human 8 unspecified role unspecified role fluorescence donor fluorescence donor Rluc-tag Rluc-tag renilla luciferase renilla luciferase protein tag renilla luciferase undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined P29590-9:p.[Ser560Ala;Ser561Ala;Ser562Ala;Ser565Ala] S560A/S561A/S562A/S565A mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain S A certain certain sequence position certain certain certain sequence position certain S A certain certain sequence position certain certain certain sequence position certain S A certain certain sequence position certain certain certain sequence position certain S A This feature has been corrected as a result of our quality control procedures. The original label was 'S560A/S561A/S562A/S565A'. Wed May 02 15:55:06 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser560ala,ser561ala,ser562ala,ser565ala' Tue Jun 30 19:27:57 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Ser560Ala;Ser561Ala;Ser562Ala;Ser565Ala]' human Homo sapiens Human proximity proximity close-contact colocalization neighbourhood interaction pml-sumo1-6 3 6 unspecified role unspecified role unspecified role unspecified role Region 547-573 Region 547-573 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain pSer pSer opser O-phospho-L-serine (2S)-2-amino-3-(phosphonooxy)propanoic acid 2-amino-3-hydroxypropanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)propanoic acid ACT_SITE Phosphoserine intermediate MOD_RES Phosphoserine O-phospho-L-serine O-phosphonoserine O-phosphorylated L-serine O3-phosphoserine serine phosphate ester OPSer Phospho Phospho Seryl Phosphorylation phosphorylations certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain increasing-ptm ptm increasing an interaction increasing-ptm ecolx Escherichia coli 7 unspecified role unspecified role unspecified role unspecified role Region 2-97 Region 2-97 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction