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 AlFx affects the formation of focal complexes by stabilizing the Arf-GAP ASAP1 in a complex with Arf1. AlFx affects the formation of focal complexes by stabilizing the Arf-GAP ASAP1 in a complex with Arf1. FEBS Lett. (0014-5793) 2005 imex curation Klein S., Franco M., Chardin P., Luton F. no In vitro complex formation on liposomes. Purified proteins were incubated in presence of a sucrose-loaded phospholipid liposome preparation. After liposome sedimentation, the fraction bound to liposomes were quantified after SDS-PAGE and sypro staining by densitometry. Negative control corresponds to proteins incubated alone. fig 1 luton@ipmc.cnrs.fr Only protein-protein interactions in vitro In vitro cosedimentation cosedimentation predetermined predetermined participant predetermined Klein S., Franco M., Chardin P., Luton F. no In vitro complex formation on liposomes. Purified proteins were incubated in presence of a sucrose-loaded phospholipid liposome preparation. After liposome sedimentation, the fraction bound to liposomes were quantified after SDS-PAGE and sypro staining by densitometry. Negative control corresponds to proteins incubated alone. fig 1 luton@ipmc.cnrs.fr Annotation to indicate that this entry has been checked and accepted by a senior curator. FEBS Lett. (0014-5793) 2005 Only protein-protein interactions imex curation AlFx affects the formation of focal complexes by stabilizing the Arf-GAP ASAP1 in a complex with Arf1. AlFx affects the formation of focal complexes by stabilizing the Arf-GAP ASAP1 in a complex with Arf1. FEBS Lett. (0014-5793) 2005 imex curation Klein S., Franco M., Chardin P., Luton F. no In vitro complex formation on liposomes. Purified proteins were incubated in presence of a sucrose-loaded phospholipid liposome preparation. After liposome sedimentation, the fraction bound to liposomes were quantified after SDS-PAGE and sypro staining by densitometry. Negative control corresponds to proteins incubated alone. fig 1 luton@ipmc.cnrs.fr Only protein-protein interactions crisp-kidney Cricetidae sp. kidney kidney [Renal] anti tag coip anti tag coimmunoprecipitation anti tag coip western blot western blot Immuno blot Immuno blot Klein S., Franco M., Chardin P., Luton F. no In vitro complex formation on liposomes. Purified proteins were incubated in presence of a sucrose-loaded phospholipid liposome preparation. After liposome sedimentation, the fraction bound to liposomes were quantified after SDS-PAGE and sypro staining by densitometry. Negative control corresponds to proteins incubated alone. fig 1 luton@ipmc.cnrs.fr Annotation to indicate that this entry has been checked and accepted by a senior curator. FEBS Lett. (0014-5793) 2005 Only protein-protein interactions imex curation asap1_mouse Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 PIP2-dependent ARF1 GAP ADP-ribosylation factor-directed GTPase-activating protein 1 Development and differentiation-enhancing factor 1 Asap1 Ddef1 Kiaa1249 Shag1 130 kDa phosphatidylinositol 4,5-bisphosphate-dependent ARF1 GTPase-activating protein protein protein mouse Mus musculus Mouse MRSSASRLSSFSSRDSLWNRMPDQISVSEFIAETTEDYNSPTTSSFTTRLHNCRNTVTLLEEALDQDRTALQKVKKSVKAIYNSGQDHVQNEENYAQVLDKFGSNFLSRDNPDLGTAFVKFSTLTKELSTLLKNLLQGLSHNVIFTLDSLLKGDLKGVKGDLKKPFDKAWKDYETKFTKIEKEKREHAKQHGMIRTEITGAEIAEEMEKERRLFQLQMCEYLIKVNEIKTKKGVDLLQNLIKYYHAQCNFFQDGLKTADKLKQYIEKLAADLYNIKQTQDEEKKQLTALRDLIKSSLQLDPKEVGGLYVASRANSSRRDSQSRQGGYSMHQLQGNKEYGSEKKGFLLKKSDGIRKVWQRRKCAVKNGILTISHATSNRQPAKLNLLTCQVKPNAEDKKSFDLISHNRTYHFQAEDEQDYIAWISVLTNSKEEALTMAFRGEQSTGENSLEDLTKAIIEDVQRLPGNDICCDCGSSEPTWLSTNLGILTCIECSGIHREMGVHISRIQSLELDKLGTSELLLAKNVGNNSFNDIMEANLPSPSPKPTPSSDMTVRKEYITAKYVDHRFSRKTCASSSAKLNELLEAIKSRDLLALIQVYAEGVELMEPLLEPGQELGETALHLAVRTADQTSLHLVDFLVQNCGNLDKQTSVGNTVLHYCSMYGKPECLKLLLRSKPTVDIVNQNGETALDIAKRLKATQCEDLLSQAKSGKFNPHVHVEYEWNLRQDEMDESDDDLDDKPSPIKKERSPRPQSFCHSSSISPQDKLALPGFSTPRDKQRLSYGAFTNQIFASTSTDLPTSPTSEAPPLPPRNAGKGPTGPPSTLPLGTQTSSGSSTLSKKRPPPPPPGHKRTLSDPPSPLPHGPPNKGAIPWGNDVGPLSSSKTANKFEGLSQQASTSSAKTALGPRVLPKLPQKVALRKTETSHHLSLDRTNIPPETFQKSSQLTELPQKPPLGELPPKPVELAPKPQVGELPPKPGELPPKPQLGDLPPKPQLSDLPPKPQMKDLPPKPQLGDLLAKSQAGDVSAKVQPPSEVTQRSHTGDLSPNVQSRDAIQKQASEDSNDLTPTLPETPVPLPRKINTGKNKVRRVKTIYDCQADNDDELTFIEGEVIIVTGEEDQEWWIGHIEGQPERKGVFPVSFVHILSD 12950D1C4F49A909 arf1_bovin ADP-ribosylation factor 1 ARF1 protein protein bovin Bos taurus (Bovine) Bovine MGNIFANLFKGLFGKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERVNEAREELMRMLAEDELRDAVLLVFANKQDLPNAMNAAEITDKLGLHSLRHRNWYIQATCATSGDGLYEGLDWLSNQLRNQK AAC773D4A60186B6 arf1-ddef1-1 1 3 unspecified role unspecified role neutral component neutral component pza fragment sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecobb Escherichia coli (strain B / BL21) 4 unspecified role unspecified role neutral component neutral component myristoylglycine required nmyrgly N-myristoylglycine (tetradecanoylamino)ethanoic acid LIPID N-myristoyl glycine N-(1-oxotetradecyl)glycine N-(C14:0 aliphatic acyl)glycine N-myristoyl-glycine N-myristoylated glycine N-myristylglycine N-tetradecanoylglycine Myristoyl Myristoylation NMyrGly ntermpepmyristoylationg certain certain sequence position certain certain certain sequence position certain ecobb Escherichia coli (strain B / BL21) direct interaction direct interaction liposome sedimentation: only 27% of myr-Arf1 GDP and 34% of ASAP1 PZA fragment were recovered in the pelleted membrane fraction if alone. The addition of AlFx did not change the sedimentation properties of each proteins. When mixed together in presence of AlFx, both PZA and and myr-Arf1 translocated to membrane fraction within the same proportion 74% and 83% respectively. AlFx (Aluminum fluoride) stabilize the complex formation between Arf1-GDP and PZA fragment of ASAP1 by mimicking activated form of Arf1, Arf1-GDP-AlFx. Both proteins are purified to homogeneity. Myristoylated Arf1 was produced by co-expressing in E. coli the yeast N-myristoyl-transferase. arf1-ddef1-2 2 3 unspecified role unspecified role bait bait n-terminal flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged n-term range n-terminal range n-term range n-term range n-terminal range n-term range 4 unspecified role unspecified role prey prey n-terminal ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range direct interaction direct interaction AlFx (Aluminum fluoride) stabilize the complex formation between Arf1-GDP and ASAP1 by mimicking activated form of Arf1, Arf1-GDP-AlFx.