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 The PDZ domain protein PICK1 and the sodium channel BNaC1 interact and localize at mechanosensory terminals of dorsal root ganglion neurons and dendrites of central neurons. The PDZ domain protein PICK1 and the sodium channel BNaC1 interact and localize at mechanosensory terminals of dorsal root ganglion neurons and dendrites of central neurons. J. Biol. Chem. (0021-9258) 2002 Duggan A., Garcia-Anoveros J., Corey DP. no chlae-cos_7 Cercopithecus aethiops simian cells transformed with SV40 Grivet cos_7 cercopithecus aethiops, by transformation with SV40 anti tag coip anti tag coimmunoprecipitation anti tag coip nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence Duggan A., Garcia-Anoveros J., Corey DP. no J. Biol. Chem. (0021-9258) 2002 The PDZ domain protein PICK1 and the sodium channel BNaC1 interact and localize at mechanosensory terminals of dorsal root ganglion neurons and dendrites of central neurons. The PDZ domain protein PICK1 and the sodium channel BNaC1 interact and localize at mechanosensory terminals of dorsal root ganglion neurons and dendrites of central neurons. J. Biol. Chem. (0021-9258) 2002 Duggan A., Garcia-Anoveros J., Corey DP. no chlae-cos_7 Cercopithecus aethiops simian cells transformed with SV40 Grivet cos_7 cercopithecus aethiops, by transformation with SV40 pull down pull down predetermined predetermined participant predetermined Duggan A., Garcia-Anoveros J., Corey DP. no J. Biol. Chem. (0021-9258) 2002 The PDZ domain protein PICK1 and the sodium channel BNaC1 interact and localize at mechanosensory terminals of dorsal root ganglion neurons and dendrites of central neurons. The PDZ domain protein PICK1 and the sodium channel BNaC1 interact and localize at mechanosensory terminals of dorsal root ganglion neurons and dendrites of central neurons. J. Biol. Chem. (0021-9258) 2002 Duggan A., Garcia-Anoveros J., Corey DP. no rat Rattus norvegicus (Rat) Rat coip coimmunoprecipitation co-immunoprecipitation CoIp immunoprecipitation Co-IP co-immunoprecipitation CoIp immunoprecipitation Co-IP coip predetermined predetermined participant predetermined Duggan A., Garcia-Anoveros J., Corey DP. no J. Biol. Chem. (0021-9258) 2002 The PDZ domain protein PICK1 and the sodium channel BNaC1 interact and localize at mechanosensory terminals of dorsal root ganglion neurons and dendrites of central neurons. The PDZ domain protein PICK1 and the sodium channel BNaC1 interact and localize at mechanosensory terminals of dorsal root ganglion neurons and dendrites of central neurons. J. Biol. Chem. (0021-9258) 2002 Duggan A., Garcia-Anoveros J., Corey DP. no yeast Saccharomyces cerevisiae Baker's yeast 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 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence Duggan A., Garcia-Anoveros J., Corey DP. no J. Biol. Chem. (0021-9258) 2002 asic2_mouse Acid-sensing ion channel 2 Asic2 Accn1 Amiloride-sensitive brain sodium channel Amiloride-sensitive cation channel 1, neuronal Bnac1 Brain sodium channel 1 protein protein mouse Mus musculus Mouse MDLKESPSEGSLQPSSIQIFANTSTLHGIRHIFVYGPLTIRRVLWAVAFVGSLGLLLVESSERVSYYFSYQHVTKVDEVVAQSLVFPAVTLCNLNGFRFSRLTTNDLYHAGELLALLDVNLQIPDPHLADPTVLEALRQKANFKHYKPKQFSMLEFLHRVGHDLKDMMLYCKFKGQECGHQDFTTVFTKYGKCYMFNSGEDGKPLLTTVKGGTGNGLEIMLDIQQDEYLPIWGETEETTFEAGVKVQIHSQSEPPFIQELGFGVAPGFQTFVATQEQRLTYLPPPWGECRSSEMGLDFFPVYSITACRIDCETRYIVENCNCRMVHMPGDAPFCTPEQHKECAEPALGLLAEKDSNYCLCRTPCNLTRYNKELSMVKIPSKTSAKYLEKKFNKSEKYISENILVLDIFFEALNYETIEQKKAYEVAALLGDIGGQMGLFIGASILTILELFDYIYELIKEKLLDLLGKEEEEGSHDENMSTCDTMPNHSETISHTVNVPLQTALGTLEEIAC mint Cation channel with high affinity for sodium, which is gated by extracellular protons and inhibited by the diuretic amiloride. Also permeable for Li(+) and K(+). Generates a biphasic current with a fast inactivating and a slow sustained phase. Heteromeric channel assembly seems to modulate 7D81A77C3B347B04 asic1_rat Acid-sensing ion channel 1 Asic1 Accn2 Amiloride-sensitive cation channel 2, neuronal Bnac2 Brain sodium channel 2 protein protein rat Rattus norvegicus (Rat) Rat MELKTEEEEVGGVQPVSIQAFASSSTLHGLAHIFSYERLSLKRALWALCFLGSLAVLLCVCTERVQYYFCYHHVTKLDEVAASQLTFPAVTLCNLNEFRFSQVSKNDLYHAGELLALLNNRYEIPDTQMADEKQLEILQDKANFRSFKPKPFNMREFYDRAGHDIRDMLLSCHFRGEACSAEDFKVVFTRYGKCYTFNSGQDGRPRLKTMKGGTGNGLEIMLDIQQDEYLPVWGETDETSFEAGIKVQIHSQDEPPFIDQLGFGVAPGFQTFVSCQEQRLIYLPSPWGTCNAVTMDSDFFDSYSITACRIDCETRYLVENCNCRMVHMPGDAPYCTPEQYKECADPALDFLVEKDQEYCVCEMPCNLTRYGKELSMVKIPSKASAKYLAKKFNKSEQYIGENILVLDIFFEVLNYETIEQKKAYEIAGLLGDIGGQMGLFIGASILTVLELFDYAYEVIKHRLCRRGKCQKEAKRSSADKGVALSLDDVKRHNPCESLRGHPAGMTYAANILPHHPARGTFEDFTC mint Cation channel with high affinity for sodium, which is gated by extracellular protons and inhibited by the diuretic amiloride. Also permeable for Ca(2+), Li(+) and K(+). Generates a biphasic current with a fast inactivating and a slow sustained phase. Isoform 3 discrimates stronger than isoform 1 between monovalent cations. Isoform 3 can flux Ca(2+) while isoform 1 cannot. Heteromeric channels composed of isoform 2 and isoform 3 are active but have a lower pH-sensitivity. Mediates glutamate-independent Ca(2+) entry into neurons upon acidosis. This Ca(2+) overloading is toxic for cortical neurons and may be in part responsible for ischemic brain injury. Heteromeric channel assembly seems to modulate channel properties 5462A7786E2A1726 pick1_mouse PRKCA-binding protein Pick1 Prkcabp Protein kinase C-alpha-binding protein Protein interacting with C kinase 1 protein protein mouse Mus musculus Mouse MFADLDYDIEEDKLGIPTVPGKVTLQKDAQNLIGISIGGGAQYCPCLYIVQVFDNTPAALDGTVAAGDEITGVNGKSIKGKTKVEVAKMIQEVKGEVTIHYNKLQADPKQGMSLDIVLKKVKHRLVENMSSGTADALGLSRAILCNDGLVKRLEELERTAELYKGMTEHTKNLLRAFYELSQTHRAFGDVFSVIGVREPQPAASEAFVKFADAHRSIEKFGIRLLKTIKPMLTDLNTYLNKAIPDTRLTIKKYLDVKFEYLSYCLKVKEMDDEEYSCIGPRRALYRVSTGNYEYRLILRCRQEARARFSQMRKDVLEKMELLDQKHVQDIVFQLQRFVSTMSKYYNDCYAVLQDADVFPIEVDLAHTTLAYGPNQGSFTDGEEEDEEEEDGAAREVSKDACGATGPTDKGGSWCDS DIP protein Q62083 original sequence version: 125 DIP protein Q62083 original sequence version: 118 437369D0AB7DCE7B asic2_rat Acid-sensing ion channel 2 Asic2 Accn1 Amiloride-sensitive brain sodium channel Amiloride-sensitive brain sodium channel 2 Amiloride-sensitive cation channel 1, neuronal Amiloride-sensitive cation channel neuronal 1 Bnac1 Brain sodium channel 1 Mammalian degenerin homolog Mdeg protein protein rat Rattus norvegicus (Rat) Rat MDLKESPSEGSLQPSSIQIFANTSTLHGIRHIFVYGPLTIRRVLWAVAFVGSLGLLLVESSERVSYYFSYQHVTKVDEVVAQSLVFPAVTLCNLNGFRFSRLTTNDLYHAGELLALLDVNLQIPDPHLADPTVLEALRQKANFKHYKPKQFSMLEFLHRVGHDLKDMMLYCKFKGQECGHQDFTTVFTKYGKCYMFNSGEDGKPLLTTVKGGTGNGLEIMLDIQQDEYLPIWGETEETTFEAGVKVQIHSQSEPPFIQELGFGVAPGFQTFVATQEQRLTYLPPPWGECRSSEMGLDFFPVYSITACRIDCETRYIVENCNCRMVHMPGDAPFCTPEQHKECAEPALGLLAEKDSNYCLCRTPCNLTRYNKELSMVKIPSKTSAKYLEKKFNKSEKYISENILVLDIFFEALNYETIEQKKAYEVAALLGDIGGQMGLFIGASLLTILELFDYIYELIKEKLLDLLGKEEEEGSHDENMSTCDTMPNHSETISHTVNVPLQTALGTLEEIAC mint Cation channel with high affinity for sodium, which is gated by extracellular protons and inhibited by the diuretic amiloride. Also permeable for Li(+) and K(+). Activation by an extracellular pH drop is followed by a rapid pH-independent inactivation. Heteromeric channel assembly seems to modulate channel properties 38D0A77C3C430B03 asic2_human Acid-sensing ion channel 2 ASIC2 ACCN ACCN1 Amiloride-sensitive brain sodium channel Amiloride-sensitive cation channel 1, neuronal Amiloride-sensitive cation channel neuronal 1 BNAC1 Brain sodium channel 1 MDEG Mammalian degenerin homolog protein protein human Homo sapiens Human MDLKESPSEGSLQPSSIQIFANTSTLHGIRHIFVYGPLTIRRVLWAVAFVGSLGLLLVESSERVSYYFSYQHVTKVDEVVAQSLVFPAVTLCNLNGFRFSRLTTNDLYHAGELLALLDVNLQIPDPHLADPSVLEALRQKANFKHYKPKQFSMLEFLHRVGHDLKDMMLYCKFKGQECGHQDFTTVFTKYGKCYMFNSGEDGKPLLTTVKGGTGNGLEIMLDIQQDEYLPIWGETEETTFEAGVKVQIHSQSEPPFIQELGFGVAPGFQTFVATQEQRLTYLPPPWGECRSSEMGLDFFPVYSITACRIDCETRYIVENCNCRMVHMPGDAPFCTPEQHKECAEPALGLLAEKDSNYCLCRTPCNLTRYNKELSMVKIPSKTSAKYLEKKFNKSEKYISENILVLDIFFEALNYETIEQKKAYEVAALLGDIGGQMGLFIGASILTILELFDYIYELIKEKLLDLLGKEEDEGSHDENVSTCDTMPNHSETISHTVNVPLQTTLGTLEEIAC 7C95B0B32EFF2814 pick1_rat PRKCA-binding protein Pick1 Prkcabp Protein kinase C-alpha-binding protein Protein interacting with C kinase 1 protein protein rat Rattus norvegicus (Rat) Rat MFADLDYDIEEDKLGIPTVPGKVTLQKDAQNLIGISIGGGAQYCPCLYIVQVFDNTPAALDGTVAAGDEITGVNGRSIKGKTKVEVAKMIQEVKGEVTIHYNKLQADPKQGMSLDIVLKKVKHRLVENMSSGTADALGLSRAILCNDGLVKRLEELERTAELYKGMTEHTKNLLRAFYELSQTHRAFGDVFSVIGVREPQPAASEAFVKFADAHRSIEKFGIRLLKTIKPMLTDLNTYLNKAIPDTRLTIKKYLDVKFEYLSYCLKVKEMDDEEYSCIALGEPLYRVSTGNYEYRLILRCRQEARARFSQMRKDVLEKMELLDQKHVQDIVFQLQRFVSTMSKYYNDCYAVLRDADVFPIEVDLAHTTLAYGPNQGGFTDGEDEEEEEEDGAAREVSKDARGATGPTDKGGSWCDS DIP protein Q9EP80 original sequence version: 84 DIP protein Q9EP80 original sequence version: 104 DIP protein Q9EP80 original sequence version: 122 8FDE0D78BB26C006 asic2-pick1 2 5 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role bait bait purified purified binding site binding region binding-associated region binding region deletion analysis deletion analysis certain certain sequence position certain c-terminal c-terminal position c-term carboxy-terminus c-terminus c-term c-terminus carboxy-terminus c-terminal range MINT-595710: original sequence: 481-512 : TCDTMPNHSETISHTVNVPLQTALGTLEEIA undefined mutation mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain Wed Jul 06 16:34:35 BST 2016 Sequence change details about this feature cannot be ascertained or do not fit with the current version of the referenced protein, so they have been deleted as a result of our quality control procedures. The original label was 'mutation decreasing ' range MINT-595713: original sequence: 508-512 : VPLQTALGTLEEIA tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Stoichiometry: 1.0 7 polyclonal western polyclonal antibody western blot polyclonal western predetermined predetermined participant predetermined 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 undefined mutation mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain Wed Jul 06 16:34:33 BST 2016 Sequence change details about this feature cannot be ascertained or do not fit with the current version of the referenced protein, so they have been deleted as a result of our quality control procedures. The original label was 'mutation decreasing ' range MINT-595701: original sequence: 27-27 : PTVPGKVTLQKDAQNLIGIS range MINT-595702: original sequence: 28-28 : TVPGKVTLQKDAQNLIGISI Stoichiometry: 1.0 physical association physical association F2 PDZ addition of a tyrosine to the C terminus, in ctBNaC1-(481-512)+Y, disrupts the interaction. homomint mint pick1-asic2 4 5 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined 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 binding site binding region binding-associated region binding region deletion analysis deletion analysis certain certain sequence position certain c-terminal c-terminal position c-term carboxy-terminus c-terminus c-term c-terminus carboxy-terminus c-terminal range MINT-595862: original sequence: 481-512 : TCDTMPNHSETISHTVNVPLQTALGTLEEIA Stoichiometry: 1.0 7 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined 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 undefined mutation mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain Wed Jul 06 16:30:38 BST 2016 Sequence change details about this feature cannot be ascertained or do not fit with the current version of the referenced protein, so they have been deleted as a result of our quality control procedures. The original label was 'mutation decreasing ' range MINT-595853: original sequence: 27-27 : PTVPGKVTLQKDAQNLIGIS range MINT-595854: original sequence: 28-28 : TVPGKVTLQKDAQNLIGISI binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain INFERRED range MINT-595849: original sequence: 22-105 : KVTLQKDAQNLIGISIGGGAQYCPCLYIVQVFDNTPAALDGTVAAGDEITGVNGKSIKGKTKVEVAKMIQEVKGEVTIHYNKL Stoichiometry: 1.0 physical association physical association PDZ F1A F1B Deletion of the last four amino acids of BNaC1, or addition of a tyrosine to the C terminus, in ctBNaC1-(481-512)+Y, disrupts the interaction. homomint domino mint pick1-asic1 4 6 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined 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 binding site binding region binding-associated region binding region deletion analysis deletion analysis certain certain sequence position certain c-terminal c-terminal position c-term carboxy-terminus c-terminus c-term c-terminus carboxy-terminus c-terminal range MINT-595787: original sequence: 477-526 : SADKGVALSLDDVKRHNPCESLRGHPAGMTYAANILPHHPARGTFEDFT Stoichiometry: 1.0 7 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role bait bait over-expressed over expressed level over-expressed undefined mutation mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain Wed Jul 06 16:32:04 BST 2016 Sequence change details about this feature cannot be ascertained or do not fit with the current version of the referenced protein, so they have been deleted as a result of our quality control procedures. The original label was 'mutation decreasing ' range MINT-595778: original sequence: 27-27 : PTVPGKVTLQKDAQNLIGIS range MINT-595779: original sequence: 28-28 : TVPGKVTLQKDAQNLIGISI binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain INFERRED range MINT-595774: original sequence: 22-105 : KVTLQKDAQNLIGISIGGGAQYCPCLYIVQVFDNTPAALDGTVAAGDEITGVNGKSIKGKTKVEVAKMIQEVKGEVTIHYNKL tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Stoichiometry: 1.0 physical association physical association PDZ F1A F1B homomint domino mint asic2-pick1-1 1 7 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role prey prey over-expressed over expressed level over-expressed undefined mutation mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain Wed Jul 06 16:28:33 BST 2016 Sequence change details about this feature cannot be ascertained or do not fit with the current version of the referenced protein, so they have been deleted as a result of our quality control procedures. The original label was 'mutation decreasing ' range MINT-595802: original sequence: 27-27 : PTVPGKVTLQKDAQNLIGIS range MINT-595803: original sequence: 28-28 : TVPGKVTLQKDAQNLIGISI tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Stoichiometry: 1.0 9 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined 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 binding site binding region binding-associated region binding region certain certain sequence position certain c-terminal c-terminal position c-term carboxy-terminus c-terminus c-term c-terminus carboxy-terminus c-terminal range MINT-595811: original sequence: 481-512 : TCDTMPNHSETISHTVNVPLQTTLGTLEEIA Stoichiometry: 1.0 physical association physical association F3A PDZ homomint mint pick1-asic2-1 3 8 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role prey prey physiological level physiological level endogenous level endogenous endogenous endogenous level Stoichiometry: 1.0 10 monoclonal western monoclonal antibody western blot monoclonal western predetermined predetermined participant predetermined unspecified role unspecified role bait bait physiological level physiological level endogenous level endogenous endogenous endogenous level tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Stoichiometry: 1.0 deformylation deformylation reaction deformylation F3B PDZ The authors were unable to demonstrate coimmunoprecipitation of PICK1 from cerebellar membrane extracts using a BNaC1 antibody; coimmunoprecipitation may be obscured in this case, because the precipitating antibody migrates with a mobility similar to that of PICK1 and is recognized at a low level by the secondary antibody used for immunoblotting. homomint mint