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 A highly conserved tryptophan in the N-terminal variable domain regulates disulfide bond formation and oligomeric assembly of adiponectin. A highly conserved tryptophan in the N-terminal variable domain regulates disulfide bond formation and oligomeric assembly of adiponectin. FEBS J. (1742-464X) 2012 Radjainia M., Huang B., Bai B., Schmitz M., Yang SH., Harris PW., Griffin MD., Brimble MA., Wang Y., Mitra AK. in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Radjainia M., Huang B., Bai B., Schmitz M., Yang SH., Harris PW., Griffin MD., Brimble MA., Wang Y., Mitra AK. FEBS J. (1742-464X) 2012 A highly conserved tryptophan in the N-terminal variable domain regulates disulfide bond formation and oligomeric assembly of adiponectin. A highly conserved tryptophan in the N-terminal variable domain regulates disulfide bond formation and oligomeric assembly of adiponectin. FEBS J. (1742-464X) 2012 Radjainia M., Huang B., Bai B., Schmitz M., Yang SH., Harris PW., Griffin MD., Brimble MA., Wang Y., Mitra AK. human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. anti tag coip anti tag coimmunoprecipitation anti tag coip western blot western blot Immuno blot Immuno blot Radjainia M., Huang B., Bai B., Schmitz M., Yang SH., Harris PW., Griffin MD., Brimble MA., Wang Y., Mitra AK. FEBS J. (1742-464X) 2012 A highly conserved tryptophan in the N-terminal variable domain regulates disulfide bond formation and oligomeric assembly of adiponectin. A highly conserved tryptophan in the N-terminal variable domain regulates disulfide bond formation and oligomeric assembly of adiponectin. FEBS J. (1742-464X) 2012 Radjainia M., Huang B., Bai B., Schmitz M., Yang SH., Harris PW., Griffin MD., Brimble MA., Wang Y., Mitra AK. in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Radjainia M., Huang B., Bai B., Schmitz M., Yang SH., Harris PW., Griffin MD., Brimble MA., Wang Y., Mitra AK. FEBS J. (1742-464X) 2012 A highly conserved tryptophan in the N-terminal variable domain regulates disulfide bond formation and oligomeric assembly of adiponectin. A highly conserved tryptophan in the N-terminal variable domain regulates disulfide bond formation and oligomeric assembly of adiponectin. FEBS J. (1742-464X) 2012 Radjainia M., Huang B., Bai B., Schmitz M., Yang SH., Harris PW., Griffin MD., Brimble MA., Wang Y., Mitra AK. in vitro In vitro solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Radjainia M., Huang B., Bai B., Schmitz M., Yang SH., Harris PW., Griffin MD., Brimble MA., Wang Y., Mitra AK. FEBS J. (1742-464X) 2012 A highly conserved tryptophan in the N-terminal variable domain regulates disulfide bond formation and oligomeric assembly of adiponectin. A highly conserved tryptophan in the N-terminal variable domain regulates disulfide bond formation and oligomeric assembly of adiponectin. FEBS J. (1742-464X) 2012 Radjainia M., Huang B., Bai B., Schmitz M., Yang SH., Harris PW., Griffin MD., Brimble MA., Wang Y., Mitra AK. in vitro In vitro tem transmission electron microscopy tem predetermined predetermined participant predetermined Radjainia M., Huang B., Bai B., Schmitz M., Yang SH., Harris PW., Griffin MD., Brimble MA., Wang Y., Mitra AK. FEBS J. (1742-464X) 2012 adipo_mouse Adiponectin Apm1 Adipocyte, C1q and collagen domain-containing protein 30 kDa adipocyte complement-related protein Adipocyte complement-related 30 kDa protein Adipocyte-specific protein AdipoQ Adipoq Acdc Acrp30 protein protein mouse Mus musculus Mouse MLLLQALLFLLILPSHAEDDVTTTEELAPALVPPPKGTCAGWMAGIPGHPGHNGTPGRDGRDGTPGEKGEKGDAGLLGPKGETGDVGMTGAEGPRGFPGTPGRKGEPGEAAYVYRSAFSVGLETRVTVPNVPIRFTKIFYNQQNHYDGSTGKFYCNIPGLYYFSYHITVYMKDVKVSLFKKDKAVLFTYDQYQEKNVDQASGSVLLHLEVGDQVWLQVYGDGDHNGLYADNVNDSTFTGFLLYHDTN DIP protein Q60994 original sequence version: 102 mint Important adipokine involved in the control of fat metabolism and insulin sensitivity, with direct anti-diabetic, anti-atherogenic and anti-inflammatory activities. Stimulates AMPK phosphorylation and activation in the liver and the skeletal muscle, enhancing glucose utilization and fatty-acid combustion. Antagonizes TNF-alpha by negatively regulating its expression in various tissues such as liver and macrophages, and also by counteracting its effects. Inhibits endothelial NF-kappa-B signaling through a cAMP-dependent pathway. May play a role in cell growth, angiogenesis and tissue remodeling by binding and sequestering various growth factors with distinct binding affinities, depending on the type of complex, LMW, MMW or HMW 0ECC687D9A8E8123 gstk1_human Glutathione S-transferase kappa 1 Glutathione S-transferase subunit 13 GST 13-13 GST class-kappa GSTK1-1 GSTK1 HDCMD47P protein protein human Homo sapiens Human MGPLPRTVELFYDVLSPYSWLGFEILCRYQNIWNINLQLRPSLITGIMKDSGNKPPGLLPRKGLYMANDLKLLRHHLQIPIHFPKDFLSVMLEKGSLSAMRFLTAVNLEHPEMLEKASRELWMRVWSRNEDITEPQSILAAAEKAGMSAEQAQGLLEKIATPKVKNQLKETTEAACRYGAFGLPITVAHVDGQTHMLFGSDRMELLAHLLGEKWMGPIPPAVNARL DIP protein Q9Y2Q3 original sequence version: 88 D3FDAFD1533B58A4 erp44_human Endoplasmic reticulum resident protein 44 ERP44 UNQ532/PRO1075 TXNDC4 Thioredoxin domain-containing protein 4 KIAA0573 protein protein human Homo sapiens Human MHPAVFLSLPDLRCSLLLLVTWVFTPVTTEITSLDTENIDEILNNADVALVNFYADWCRFSQMLHPIFEEASDVIKEEFPNENQVVFARVDCDQHSDIAQRYRISKYPTLKLFRNGMMMKREYRGQRSVKALADYIRQQKSDPIQEIRDLAEITTLDRSKRNIIGYFEQKDSDNYRVFERVANILHDDCAFLSAFGDVSKPERYSGDNIIYKPPGHSAPDMVYLGAMTNFDVTYNWIQDKCVPLVREITFENGEELTEEGLPFLILFHMKEDTESLEIFQNEVARQLISEKGTINFLHADCDKFRHPLLHIQKTPADCPVIAIDSFRHMYVFGDFKDVLIPGKLKQFVFDLHSGKLHREFHHGPDPTDTAPGEQAQDVASSPPESSFQKLAPSEYRYTLLRDRDEL 3865DCF3811BC263 adipoq-1 3 Adiponectin 6 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified flag tag flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Q60994:p.Trp42Ala mutation increasing mutation increasing interaction mutation increasing certain certain sequence position certain certain certain sequence position certain W A Tue Jul 12 10:24:24 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation increasing' Wed May 02 14:53:43 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'trp42ala' Tue Jun 30 19:26:19 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Trp42Ala' Stoichiometry: 3.0 direct interaction direct interaction f2c mint Non-reducing SDS-PAGE and gel filtration chromatographic analysis demonstrated that the amount of the HMW form is significantly reduced for the W42A mutant compared to the WT. On the other hand, the amount of trimer was significantly elevated for the W42A mutant (Fig. 2B). adipoq-1 3 Adiponectin 6 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified flag tag flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Stoichiometry: 6.0 direct interaction direct interaction f2c mint Non-reducing SDS-PAGE and gel filtration chromatographic analysis demonstrated that the amount of the HMW form is significantly reduced for the W42A mutant compared to the WT. On the other hand, the amount of trimer was significantly elevated for the W42A mutant (Fig. 2B). adipoq-adipoq 3 Adiponectin 6 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Q60994:p.Trp42Ala mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain W A Tue Jul 12 10:59:11 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation increasing' Wed May 02 17:12:22 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'trp42ala' Tue Jun 30 19:42:17 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Trp42Ala' flag tag flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Adiponectin 6 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified flag tag flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Q60994:p.Trp42Ala mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain W A Tue Jul 12 10:24:06 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation decreasing' Wed May 02 20:29:56 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'trp42ala' Tue Jun 30 16:29:21 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Trp42Ala' direct interaction direct interaction f2c mint Similarly, gel-filtration analysis revealed that W42A protein samples contained only ~3% of the HMW adiponectin oligomers, compared to ~26% in WT samples. On the other hand, the LMW fraction of W42A mutant was significantly higher than that of wild type adiponectin (Fig. 2C). adipoq-1 3 Adiponectin 6 peptide synthesis peptide synthesis predetermined predetermined participant predetermined 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 Q60994:p.Trp42Ala mutation increasing mutation increasing interaction mutation increasing certain certain sequence position certain certain certain sequence position certain W A Tue Jul 12 10:21:24 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation increasing' Wed May 02 20:22:07 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'trp42ala' Tue Jun 30 17:26:45 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Trp42Ala' Stoichiometry: 2.0 direct interaction direct interaction mint f6 sf3 adipoq-1 3 Adiponectin 6 peptide synthesis peptide synthesis predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Q60994:p.Trp42Ala mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain W A Tue Jul 12 10:21:28 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation increasing' Wed May 02 15:49:17 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'trp42ala' Tue Jun 30 15:42:10 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Trp42Ala' binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Stoichiometry: 2.0 direct interaction direct interaction sf1 mint Similar to 1844 WT, 3744 WT is initially monomeric and dimerize through disulfide bonding over time. This conversion occurs at a considerably faster rate in the case of 3744 WT compared to 1844 WT. Conversion of W3744 W42A monomers to dimers occurs at a slower rate compared to 3744 WT adipoq-1 5 Adiponectin 6 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Q60994:p.Trp42Ala mutation increasing mutation increasing interaction mutation increasing certain certain sequence position certain certain certain sequence position certain W A Tue Jul 12 10:22:23 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation increasing' Wed May 02 18:10:53 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'trp42ala' Tue Jun 30 17:45:14 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Trp42Ala' flag tag flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Stoichiometry: 3.0 direct interaction direct interaction f3 mint In a typical wild-type adiponectin preparation, ~35% of the species are comprised of 18mers, ~22% are 3mers, ~10% 6mers, and the rest distributed in 9mers, 12mers and 15mers (Fig. 3) Thus, the effect of W42A mutation primarily manifests itself in the trimer pool (LMW), which is enhanced at the expense of HMW pool; with somewhat less pronounced alteration in the hexamer population, which shows an increase. Within the HMW population, we observe that the relative distributions of 12mers, 15mers and 18mers are also markedly altered. In the wild type, the majority is in the form of 18mers and the rest distributed amongst 12mers and 15mers. In W42A, all these subspecies were uniformly low. adipoq-erp44 2 Adiponectin 6 western blot western blot Immuno blot Immuno blot predetermined predetermined participant predetermined unspecified role unspecified role bait bait over-expressed over expressed level over-expressed living cell living cell flag tag flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Q60994:p.Trp42Ala mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain W A Tue Jul 12 10:06:28 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation decreasing' Wed May 02 19:49:09 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'trp42ala' Tue Jun 30 18:54:19 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Trp42Ala' DsbA-L 7 western blot western blot Immuno blot Immuno blot predetermined predetermined participant predetermined unspecified role unspecified role prey prey living cell living cell physiological level physiological level endogenous level endogenous endogenous endogenous level ERP44 8 western blot western blot Immuno blot Immuno blot predetermined predetermined participant predetermined unspecified role unspecified role prey prey living cell living cell physiological level physiological level endogenous level endogenous endogenous endogenous level association association f4c mint adipoq-1 4 Adiponectin 6 peptide synthesis peptide synthesis predetermined predetermined participant predetermined 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: 2.0 direct interaction direct interaction sf4 mint Analytical ultracentrifugation (AUC) analysis for the peptide construct 1844 C39S, which only forms the smaller species in SEC experiments, established that the species of larger mass for 1844 WT is a dimer (see S4 and supplementary text) generated through the spontaneous formation of disulfide bond over time adipoq-1 1 Adiponectin 6 peptide synthesis peptide synthesis predetermined predetermined participant predetermined 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: 2.0 direct interaction direct interaction sf2 mint