MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it Binding determinants of the small heat shock protein, αB-crystallin: recognition of the 'IxI' motif. Binding determinants of the small heat shock protein, αB-crystallin: recognition of the 'IxI' motif. EMBO J. (0261-4189) 2012 imex curation Delbecq SP., Jehle S., Klevit R. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr experimental particp experimental participant identification experimental particp Delbecq SP., Jehle S., Klevit R. EMBO J. (0261-4189) 2012 Only protein-protein interactions imex curation hspb1_human Heat shock protein beta-1 HSPB1 HSP27 HSP28 Heat shock 27 kDa protein Stress-responsive protein 27 Estrogen-regulated 24 kDa protein 28 kDa heat shock protein protein protein human Homo sapiens Human MTERRVPFSLLRGPSWDPFRDWYPHSRLFDQAFGLPRLPEEWSQWLGGSSWPGYVRPLPPAAIESPAVAAPAYSRALSRQLSSGVSEIRHTADRWRVSLDVNHFAPDELTVKTKDGVVEITGKHEERQDEHGYISRCFTRKYTLPPGVDPTQVSSSLSPEGTLTVEAPMPKLATQSNEITIPVTFESRAQLGGPEAAKSDETAAK 1B4DC44A6F6606D5 1B4DC44A6F6606D5 cryab_human Alpha-crystallin B chain CRYAB CRYA2 Renal carcinoma antigen NY-REN-27 Alpha(B)-crystallin Rosenthal fiber component Heat shock protein beta-5 HSPB5 protein protein human Homo sapiens Human MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFPTSTSLSPFYLRPPSFLRAPSWFDTGLSEMRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYRIPADVDPLTITSSLSSDGVLTVNGPRKQVSGPERTIPITREEKPAVTAAPKK DIP protein P02511 original sequence version: null AE08BED46B7849CB DIP protein P02511 original sequence version: 195 DIP protein P02511 original sequence version: 130 DIP protein P02511 original sequence version: 131 DIP protein P02511 original sequence version: 151 DIP protein P02511 original sequence version: 167 DIP protein P02511 original sequence version: 154 DIP protein P02511 original sequence version: 146 AE08BED46B7849CB cryaa_human Alpha-crystallin A chain CRYAA CRYA1 HSPB4 Heat shock protein beta-4 protein protein human Homo sapiens Human MDVTIQHPWFKRTLGPFYPSRLFDQFFGEGLFEYDLLPFLSSTISPYYRQSLFRTVLDSGISEVRSDRDKFVIFLDVKHFSPEDLTVKVQDDFVEIHGKHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSADGMLTFCGPKIQTGLDATHAERAIPVSREEKPTSAPSS DIP protein P02489 original sequence version: 121 DIP protein P02489 original sequence version: 131 81804A8439837D50 hspb2_human Heat shock protein beta-2 HSPB2 DMPK-binding protein protein protein human Homo sapiens Human MSGRSVPHAHPATAEYEFANPSRLGEQRFGEGLLPEEILTPTLYHGYYVRPRAAPAGEGSRAGASELRLSEGKFQAFLDVSHFTPDEVTVRTVDNLLEVSARHPQRLDRHGFVSREFCRTYVLPADVDPWRVRAALSHDGILNLEAPRGGRHLDTEVNEVYISLLPAPPDPEEEEEAAIVEP DIP protein Q16082 original sequence version: null 7586DCE8FBD19F6D cryab-cryab-5 1 alphaB-ACD 3 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified P02511:p.Ser135Gln mutation decreasing interaction mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain S Q Tue Jul 12 10:21:30 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation decreasing' Wed May 02 16:18:02 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser135gln' Tue Jun 30 18:49:27 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser135Gln' binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Stoichiometry: 2.1 alphaB-lxl 3 peptide synthesis peptide synthesis experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Stoichiometry: 1.2 9 11 direct interaction direct interaction homomint mint NMR binding experiments were performed by titrating peptides with sequences containing the C-terminal IxI motif of aB or other human sHSPs into NMR samples of 15N-aBACD. The effect of peptide addition was monitored in the 1H 15N HSQC NMR spectra of aB-ACD collected at 221C. As illustrated in Figure 1, significant changes in specific peak positions are observed as a consequence of addition of C-terminal aB-IxI peptide (Ac-PERTIPITREEK-NH2). Thus, the spectra confirm that isolated ACD dimers in solution can interact with a C-terminal sequence outside an oligomeric context. f1 sf2 f2 f3 f4 f5 cryab-hspb2 1 HSPB2-Vxl 5 peptide synthesis peptide synthesis experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Stoichiometry: 1.2 alphaB-ACD 3 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Stoichiometry: 2.1 16 14 direct interaction direct interaction homomint mint NMR binding experiments were performed by titrating peptides with sequences containing the C-terminal IxI motif of aB or other human sHSPs into NMR samples of 15N-aBACD. The effect of peptide addition was monitored in the 1H 15N HSQC NMR spectra of aB-ACD collected at 221C. sf2 f2 t1 sf4 cryaa-cryab-7 1 alphaA-lxV 4 peptide synthesis peptide synthesis experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Stoichiometry: 1.2 alphaB-ACD 3 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Stoichiometry: 2.1 19 21 direct interaction direct interaction homomint mint NMR binding experiments were performed by titrating peptides with sequences containing the C-terminal IxI motif of aB or other human sHSPs into NMR samples of 15N-aBACD. The effect of peptide addition was monitored in the 1H 15N HSQC NMR spectra of aB-ACD collected at 221C. sf2 t1 cryab-hspb1-2 1 HSPB1 2 peptide synthesis peptide synthesis experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Stoichiometry: 1.2 alphaB-ACD 3 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Stoichiometry: 2.1 24 26 direct interaction direct interaction t1 homomint mint NMR binding experiments were performed by titrating peptides with sequences containing the C-terminal IxI motif of aB or other human sHSPs into NMR samples of 15N-aBACD. The effect of peptide addition was monitored in the 1H 15N HSQC NMR spectra of aB-ACD collected at 221C.