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 chen-2018-12 mouse_sn4741 mouse_sn4741 sn4741 SN4741 Cell line from substantia nigra dopaminergic cells derived from transgenic mouse embryos. anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Chen J., Ren Y., Gui C., Zhao M., Wu X., Mao K., Li W., Zou F., Chen J., Ren Y., Gui C., Zhao M., Wu X., Mao K., Li W., Zou F. cjlwj@smu.edu.cn Cell death & disease 2018 Only protein-protein interactions imex curation imex curation chen-2018-13 mouse_sn4741 mouse_sn4741 sn4741 SN4741 Cell line from substantia nigra dopaminergic cells derived from transgenic mouse embryos. confocal microscopy confocal microscopy immunostaining immunostaining Chen J., Ren Y., Gui C., Zhao M., Wu X., Mao K., Li W., Zou F., Chen J., Ren Y., Gui C., Zhao M., Wu X., Mao K., Li W., Zou F. cjlwj@smu.edu.cn Cell death & disease 2018 Only protein-protein interactions imex curation imex curation chen-2018-14 mouse_sn4741 mouse_sn4741 sn4741 SN4741 Cell line from substantia nigra dopaminergic cells derived from transgenic mouse embryos. anti tag coip anti tag coimmunoprecipitation anti tag coip western blot western blot Immuno blot Immuno blot Chen J., Ren Y., Gui C., Zhao M., Wu X., Mao K., Li W., Zou F., Chen J., Ren Y., Gui C., Zhao M., Wu X., Mao K., Li W., Zou F. cjlwj@smu.edu.cn Cell death & disease 2018 Only protein-protein interactions imex curation imex curation prkn_mouse E3 ubiquitin-protein ligase parkin Prkn Park2 Parkin RBR E3 ubiquitin-protein ligase protein protein mouse Mus musculus Mouse MIVFVRFNSSYGFPVEVDSDTSILQLKEVVAKRQGVPADQLRVIFAGKELPNHLTVQNCDLEQQSIVHIVQRPRRRSHETNASGGDEPQSTSEGSIWESRSLTRVDLSSHTLPVDSVGLAVILDTDSKRDSEAARGPVKPTYNSFFIYCKGPCHKVQPGKLRVQCGTCKQATLTLAQGPSCWDDVLIPNRMSGECQSPDCPGTRAEFFFKCGAHPTSDKDTSVALNLITSNRRSIPCIACTDVRSPVLVFQCNHRHVICLDCFHLYCVTRLNDRQFVHDAQLGYSLPCVAGCPNSLIKELHHFRILGEEQYTRYQQYGAEECVLQMGGVLCPRPGCGAGLLPEQGQRKVTCEGGNGLGCGFVFCRDCKEAYHEGDCDSLLEPSGATSQAYRVDKRAAEQARWEEASKETIKKTTKPCPRCNVPIEKNGGCMHMKCPQPQCKLEWCWNCGCEWNRACMGDHWFDV pink1_mouse Serine/threonine-protein kinase PINK1, mitochondrial Pink1 PTEN-induced putative kinase protein 1 BRPK protein protein mouse Mus musculus Mouse MAVRQALGRGLQLGRALLLRFAPKPGPLFGWGKPGPAAAWGRGERPGQVVSPGAQPRPVGLPLPDRYRFFRQSVAGLAARIQRQFMVRARGGAGPCGRAVFLAFGLGLGLIEEKQAEGRRAASACQEIQAIFTQKTKRVSDPLDTRCWQGFRLEDYLIGQAIGKGCNAAVYEATMPTLPQHLEKAKHLGLIGKGPDVVLKGADGEQAPGTPTFPFAIKMMWNISAGSSSEAILSKMSQELVPASRVALAGEYGAVTYRRSRDGPKQLAPHPNIIRVFRAFTSSVPLLPGALADYPDMLPPHYYPEGLGHGRTLFLVMKNYPCTLRQYLEEQTPSSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDGCPWLVISDFGCCLADQHVGLRLPFNSSSVERGGNGSLMAPEVSTAHSGPSAVIDYSKADTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQEAQLPEMPESVPPEARRLVRSLLQREASKRPSARLAANVLHLSLWGEHLLALKNLKLDKMIAWLLQQSAATLLADRLREKSCVETKLQMLFLANLECEALCQAALLLSSWRAAP mk14_mouse Mitogen-activated protein kinase 14 Mapk14 Crk1 Csbp1 Csbp2 Mitogen-activated protein kinase p38 alpha CRK1 protein protein mouse Mus musculus Mouse MSQERPTFYRQELNKTIWEVPERYQNLSPVGSGAYGSVCAAFDTKTGHRVAVKKLSRPFQSIIHAKRTYRELRLLKHMKHENVIGLLDVFTPARSLEEFNDVYLVTHLMGADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHTDDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRLVGTPGAELLKKISSESARNYIQSLAQMPKMNFANVFIGANPLAVDLLEKMLVLDSDKRITAAQALAHAYFAQYHDPDDEPVADPYDQSFESRDLLIDEWKSLTYDEVISFVPPPLDQEEMES prkn_human E3 ubiquitin-protein ligase parkin PRKN PARK2 Parkin RBR E3 ubiquitin-protein ligase Parkinson juvenile disease protein 2 protein protein human Homo sapiens Human MIVFVRFNSSHGFPVEVDSDTSIFQLKEVVAKRQGVPADQLRVIFAGKELRNDWTVQNCDLDQQSIVHIVQRPWRKGQEMNATGGDDPRNAAGGCEREPQSLTRVDLSSSVLPGDSVGLAVILHTDSRKDSPPAGSPAGRSIYNSFYVYCKGPCQRVQPGKLRVQCSTCRQATLTLTQGPSCWDDVLIPNRMSGECQSPHCPGTSAEFFFKCGAHPTSDKETSVALHLIATNSRNITCITCTDVRSPVLVFQCNSRHVICLDCFHLYCVTRLNDRQFVHDPQLGYSLPCVAGCPNSLIKELHHFRILGEEQYNRYQQYGAEECVLQMGGVLCPRPGCGAGLLPEPDQRKVTCEGGNGLGCGFAFCRECKEAYHEGECSAVFEASGTTTQAYRVDERAAEQARWEAASKETIKKTTKPCPRCHVPVEKNGGCMHMKCPQPQCRLEWCWNCGCEWNRVCMGDHWFDV pink1-1 3980131 N/A 3980134 unspecified role unspecified role bait bait physiological level physiological level endogenous level endogenous endogenous endogenous level phosres phosres phosphorylated residue PhosRes Phospho Phosphorylation Phosphorylation (O of Serine, Threonine, Tyrosine and Aspartate, N epsilon of Lysine) certain certain sequence position certain certain certain sequence position certain false N/A 3980135 unspecified role unspecified role prey prey physiological level physiological level endogenous level endogenous endogenous endogenous level physical association physical association false false false F4C Furthermore, we measured the interaction between PINK1 and Parkin as well as Parkin phosphorylation at serine 65 in SN4741 cells. As expected, we observed that SB203580 restored the reduction of PINK1-Parkin interaction and co-localization (Fig. 4c–f) prkn-mapk14-1 3980131 N/A 3980134 unspecified role unspecified role bait bait physiological level physiological level endogenous level endogenous endogenous endogenous level N/A 3980136 unspecified role unspecified role prey prey physiological level physiological level endogenous level endogenous endogenous endogenous level physical association physical association false false false F5A we first detected the interaction between p38 MAPK and Parkin by performing co-immunoprecipitation experiments and immunofluorescence microscopy. It revealed that SB203580 decreased the interaction and co-localization that enhanced by α-synucleinA53T aggregation (Fig. 5a-e). prkn-mapk14-2 3980131 N/A 3980134 unspecified role unspecified role prey prey physiological level physiological level endogenous level endogenous endogenous endogenous level N/A 3980136 unspecified role unspecified role bait bait physiological level physiological level endogenous level endogenous endogenous endogenous level physical association physical association false false false F5B we first detected the interaction between p38 MAPK and Parkin by performing co-immunoprecipitation experiments and immunofluorescence microscopy. It revealed that SB203580 decreased the interaction and co-localization that enhanced by α-synucleinA53T aggregation (Fig. 5a-e). pink1-prkn-1 3980132 N/A 3980134 unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell N/A 3980135 unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell colocalization colocalization false false false F4E Furthermore, we measured the interaction between PINK1 and Parkin as well as Parkin phosphorylation at serine 65 in SN4741 cells. As expected, we observed that SB203580 restored the reduction of PINK1–Parkin interaction and co-localization (Fig. 4c–f) mapk14-prkn-1 3980132 N/A 3980134 unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell N/A 3980136 unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell colocalization colocalization false false false F5D we first detected the interaction between p38 MAPK and Parkin by performing co-immunoprecipitation experiments and immunofluorescence microscopy. It revealed that SB203580 decreased the interaction and co-localization that enhanced by α-synucleinA53T aggregation (Fig. 5a–e). prkn-pink1-1 3980133 N/A 3980137 unspecified role unspecified role bait bait over-expressed over expressed level over-expressed O60260:p.Ser131Ala mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain false gfp tag gfp tag gfp tag green fluorescent protein tag GFP green fluorescent protein GFP green fluorescent protein gfp tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range false N/A 3980135 unspecified role unspecified role prey prey physiological level physiological level endogenous level endogenous endogenous endogenous level physical association physical association false false false F7C Furthermore, we measured the interaction between PINK1 and Parkin as well as Parkin phosphorylation at serine 65 in SN4741 cells. As expected, we observed that SB203580 restored the reduction of PINK1–Parkin interaction and co-localization (Fig. 4c–f)