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 http://mint.bio.uniroma2.it/mint boisram_-1998-1 Interaction of Kar2p and Sls1p is required for efficient co-translational translocation of secreted proteins in the yeast Yarrowia lipolytica. in vivo in vivo 2 hybrid two hybrid 2H 2h Gal4 transcription regeneration two-hybrid yeast two hybrid 2-hybrid classical two hybrid classical two hybrid 2H two-hybrid 2-hybrid Gal4 transcription regeneration 2h yeast two hybrid Y2H Y-2H 2 hybrid predetermined predetermined participant predetermined Boisramé A., Kabani M., Beckerich JM., Hartmann E., Gaillardin C. boisrame@cardere.grignon.inra.fr J. Biol. Chem. (0021-9258) 1998 sil1_yarli Nucleotide exchange factor SIL1 SIL1 SLS1 YALI0E32703g Protein SLS1 protein protein yarli Yarrowia lipolytica (strain CLIB 122 / E 150) Yeast Candida lipolytica MKFSKTLLLALVAGALAKGEDEICRVEKNSGKEICYPKVFVPTEEWQVVWPDQVIPAGLHVRMDYENGVKEAKINDPNEEVEGVAVAVGEEVPEGEVVIEDLTEENGDEGISANEKVQRAIEKAIKEKRIKEGHKPNPNIPESDHQTFSDAVAALRDYKVNGQAAMLPIALSQLEELSHEIDFGIALSDVDPLNALLQILEDAKVDVESKIMAARTIGASLRNNPHALDKVINSKVDLVKSLLDDLAQSSKEKADKLSSSLVYALSAVLKTPETVTRFVDLHGGDTLRQLYETGSDDVKGRVSTLIEDVLATPDLHNDFSSITGAVKKRSANWWEDELKEWSGVFQRSLPSKLSSKVKSKVYTSLAAIRRNFRESVDVSEEFLEWLDHPKKAAAEIGDDLVKLIKQDRGELWGNAKARKYDARDEL mint Required for protein translocation and folding in the endoplasmic reticulum (ER). Probably functions as a nucleotide exchange factor for the ER lumenal chaperone KAR2. It is not required for viability but is essential for optimal growth at elevated temperatures bip_yarli Endoplasmic reticulum chaperone BiP KAR2 YALI0E13706g Immunoglobulin heavy chain-binding protein homolog protein protein yarli Yarrowia lipolytica (strain CLIB 122 / E 150) Yeast Candida lipolytica MKFSMPSWGVVFYALLVCLLPFLSKAGVQADDVDSYGTVIGIDLGTTYSCVGVMKGGRVEILANDQGSRITPSYVAFTEDERLVGDAAKNQAANNPFNTIFDIKRLIGLKYKDESVQRDIKHFPYKVKNKDGKPVVVVETKGEKKTYTPEEISAMILTKMKDIAQDYLGKKVTHAVVTVPAYFNDAQRQATKDAGIIAGLNVLRIVNEPTAAAIAYGLDHTDDEKQIVVYDLGGGTFDVSLLSIESGVFEVLATAGDTHLGGEDFDYRVIKHFVKQYNKKHDVDITKNAKTIGKLKREVEKAKRTLSSQMSTRIEIESFFDGEDFSETLTRAKFEELNIDLFKRTLKPVEQVLKDSGVKKEDVHDIVLVGGSTRIPKVQELLEKFFDGKKASKGINPDEAVAYGAAVQAGVLSGEDGVEDIVLLDVNPLTLGIETTGGVMTKLINRNTNIPTKKSQIFSTAVDNQSTVLIQVFEGERTMSKDNNLLGKFELKGIPPAPRGVPQIEVTFELDANGILRVTAHDKGTGKSETITITNDKGRLSKDEIERMVEEAERFAEEDALIRETIEAKNSLENYAHSLRNQVADKSGLGGKISADDKEALNDAVTETLEWLEANSVSATKEDFEEKKEALSAIAYPITSKIYEGGEGGDESNDGGFYADDDEAPFHDEL Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis mint kar2-sil1 981 sil1_yarli 982 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence unspecified role unspecified role prey prey over-expressed over expressed level over-expressed tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false Stoichiometry: 1.0 grp78_yarli 983 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence unspecified role unspecified role bait bait over-expressed over expressed level over-expressed tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false Stoichiometry: 1.0 physical association physical association false false false mint