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/ Structural framework of the GABARAP-calreticulin interface--implications for substrate binding to endoplasmic reticulum chaperones. Structural framework of the GABARAP-calreticulin interface--implications for substrate binding to endoplasmic reticulum chaperones. FEBS J. (1742-464X) 2009 imex curation Thielmann Y., Weiergräber O.H., Mohrlüder J., Willbold D. d.willbold@fz-juelich.de 11-Jun-2014: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Thielmann Y., Weiergräber O.H., Mohrlüder J., Willbold D. d.willbold@fz-juelich.de Accepted 2014-MAY-30 by MGT FEBS J. (1742-464X) 2009 imex curation Structural framework of the GABARAP-calreticulin interface--implications for substrate binding to endoplasmic reticulum chaperones. Structural framework of the GABARAP-calreticulin interface--implications for substrate binding to endoplasmic reticulum chaperones. FEBS J. (1742-464X) 2009 imex curation Thielmann Y., Weiergräber O.H., Mohrlüder J., Willbold D. d.willbold@fz-juelich.de 11-Jun-2014: Contacted by IntAct-Help. 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 Thielmann Y., Weiergräber O.H., Mohrlüder J., Willbold D. d.willbold@fz-juelich.de Accepted 2014-MAY-30 by MGT FEBS J. (1742-464X) 2009 imex curation Structural framework of the GABARAP-calreticulin interface--implications for substrate binding to endoplasmic reticulum chaperones. Structural framework of the GABARAP-calreticulin interface--implications for substrate binding to endoplasmic reticulum chaperones. FEBS J. (1742-464X) 2009 imex curation Thielmann Y., Weiergräber O.H., Mohrlüder J., Willbold D. d.willbold@fz-juelich.de 11-Jun-2014: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro spr surface plasmon resonance Optical biosensor BIAcore(r) BIAcore(r) Optical biosensor spr predetermined predetermined participant predetermined Thielmann Y., Weiergräber O.H., Mohrlüder J., Willbold D. d.willbold@fz-juelich.de Accepted 2014-MAY-30 by MGT FEBS J. (1742-464X) 2009 imex curation calr_human Calreticulin CRP55 Calregulin HACBP Endoplasmic reticulum resident protein 60 grp60 CALR CRTC protein protein human Homo sapiens Human MLLSVPLLLGLLGLAVAEPAVYFKEQFLDGDGWTSRWIESKHKSDFGKFVLSSGKFYGDEEKDKGLQTSQDARFYALSASFEPFSNKGQTLVVQFTVKHEQNIDCGGGYVKLFPNSLDQTDMHGDSEYNIMFGPDICGPGTKKVHVIFNYKGKNVLINKDIRCKDDEFTHLYTLIVRPDNTYEVKIDNSQVESGSLEDDWDFLPPKKIKDPDASKPEDWDERAKIDDPTDSKPEDWDKPEHIPDPDAKKPEDWDEEMDGEWEPPVIQNPEYKGEWKPRQIDNPDYKGTWIHPEIDNPEYSPDPSIYAYDNFGVLGLDLWQVKSGTIFDNFLITNDEAYAEEFGNETWGVTKAAEKQMKDKQDEEQRLKEEEEDKKRKEEEEAEDKEDDEDKDEDEEDEEDKEEDEEEDVPGQAKDEL BC37C3C0F1054FB2 gbrap_human Gamma-aminobutyric acid receptor-associated protein GABA(A) receptor-associated protein MM46 GABARAP FLC3B HT004 protein protein human Homo sapiens Human MKFVYKEEHPFEKRRSEGEKIRKKYPDRVPVIVEKAPKARIGDLDKKKYLVPSDLTVGQFYFLIRKRIHLRAEDALFFFVNNVIPPTSATMGQLYQEHHEEDFFLYIAYSDESVYGL DIP protein O95166 original sequence version: 109 DIP protein O95166 original sequence version: 112 DIP protein O95166 original sequence version: 128 DIP protein O95166 original sequence version: 132 BC0B84B8A51C1E32 gabarap-calr 3 5 unspecified role unspecified role bait bait ubiquitin-related domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecobb Escherichia coli (strain B / BL21) 4 unspecified role unspecified role prey prey lig_lir_gen_1 motif sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain chemical synthesis Chemical synthesis (Chemical synthesis) direct interaction direct interaction Fig. 1 Temp = 21.5C A construct of calreticulin containing the P-domain (residues 194-305) binds gabarap with Kd = (930 +/- 120) x 10-9 molar. A shorter synthetic calreticulin peptide (residues 195-205) supports binding to gabarap with Kd = (11.5 +/- 1.1) x 10-6 molar. calr-gabarap 1 4 unspecified role unspecified role neutral component neutral component lig_lir_gen_1 motif sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain P27797:p.Trp200Ala mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain W A Wed May 02 14:32:10 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'trp200ala' Tue Jun 30 19:04:28 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Trp200Ala' chemical synthesis Chemical synthesis (Chemical synthesis) 5 unspecified role unspecified role neutral component neutral component ubiquitin-related domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecobb Escherichia coli (strain B / BL21) direct interaction direct interaction Fig. 2 calr-gabarap-1 2 4 unspecified role unspecified role neutral component neutral component lig_lir_gen_1 motif sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain chemical synthesis Chemical synthesis (Chemical synthesis) 5 unspecified role unspecified role neutral component neutral component ubiquitin-related domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecobb Escherichia coli (strain B / BL21) direct interaction direct interaction Table 2 working 23.2%, free 27.0% 2.30A