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 novel bipartite UNC-101/AP-1 μ1 binding signal mediates KVS-4/Kv2.1 somatodendritic distribution in Caenorhabditis elegans. A novel bipartite UNC-101/AP-1 μ1 binding signal mediates KVS-4/Kv2.1 somatodendritic distribution in Caenorhabditis elegans. FEBS letters 2016 imex curation Zhou X., Zeng J., Ouyang C., Luo Q., Yu M., Yang Z., Wang H., Shen K., Shi A. ashi@hust.edu.cn 11-Apr-2016: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro pull down pull down anti tag western anti tag western blot anti tag western Zhou X., Zeng J., Ouyang C., Luo Q., Yu M., Yang Z., Wang H., Shen K., Shi A. ashi@hust.edu.cn Accepted 2016-MAR-03 AT 11:39 GMT AT 11:39 GMT by MARTA FEBS letters 2016 Only protein-protein interactions imex curation imex curation kvs4_caeel Probable voltage-gated potassium channel subunit kvs-4 kvs-4 Y48A6B.6 protein protein caeel Caenorhabditis elegans MNSAIMQGAAMATSHGIARLNRHNAQRNHFHIPTANRLFYQLQTPCTSTEEERRTVQTDDVAEIGMQRPDYQMYCGEEEISEQFVKLNVGGQRFMLRKDTIRRRGVGRLLDLINKPVADSNADAFFSSTSEFYFERPPSLFHIVYQFYLNGVIHQPSNLCPVDIIEELEYWRIIPDQYLASCCCAQQIDDDDEEVEEQDKPNLFKTLRFGEIRRCVWNIIEEPASSGKAQAFAVCSVVFVLISISGLVLGSLPELQVATKQRNNLTGEEFTEMEPMPILGYIEYVCIVWFTMEYGLKMLVSAERSKTFRQLLNIIDLLAILPFIIEMLLLIFGISTEQLRDLKGAFLVIRILRVLRVIRVLKLGRYSSGLQMFGKTLKASFRQLGMMAMVVMTGVIFFSTLVYFLEKDEPASKFHSIPAACWWCIVTMTTVGYGDLTPVTVPGKLVATGAIACGVLVLALPITIIVDNFMKVAETERPAGGNRYRTSQYPKATKSEQMILKVT 1611A5E0417E016C ap1m_caeel AP-1 complex subunit mu-1-I unc-101 K11D2.3 Mu1-I-adaptin Golgi adaptor AP-1 47 kDa protein HA1 47 kDa subunit Clathrin coat assembly protein AP47 Clathrin coat-associated protein AP47 Uncoordinated protein 101 Clathrin assembly protein complex 1 mu-1-I medium chain protein protein caeel Caenorhabditis elegans MATSAMFILDLKGKTIISRNYRGDIDMTAIDKFIHLLMEKEEEGSAAPVLTYQDTNFVFIKHTNIYLVSACRSNVNVTMILSFLYKCVEVFSEYFKDVEEESVRDNFVVIYELLDEMMDFGFPQTTESRILQEYITQEGQKLISAPRPPMAVTNAVSWRSEGIKYRKNEVFLDVIESVNMLASANGTVLQSEIVGSVKMRVYLTGMPELRLGLNDKVLFEGSGRGKSKSVELEDVKFHQCVRLSRFDTDRTISFIPPDGAFELMSYRLTTVVKPLIWIETSIERHSHSRVSFIIKAKSQFKRRSTANNVEIIIPVPSDADSPKFKTSIGSVKYTPEQSAFVWTIKNFPGGKEYLLTAHLSLPSVMSEESEGRPPIKVKFEIPYFTTSGIQVRYLKIIEKSGYQALPWVRYITQNGEYEMRMK 947BF5D1EF496C8B kvs_4-1 1 2 unspecified role unspecified role prey prey in vitro translated in vitro translated protein in vitro translated ha tag ha tag ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined range binding region binding region binding-associated region binding region deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain 3 unspecified role unspecified role bait bait purified purified range binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain gst tag gst tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined direct interaction direct interaction f5b f5c f6 Compared to that of KVS-4, significantly decreased pull-down of KVS-4ΔEQMIL (~ 40% down) and KVS-4ΔWNIIE (~ 45% down) by GST-UNC-101 were detected (Fig. 5C,F). Removal of both EQMIL and WNIIE motifs did not cause significantly weaker interactions than those caused by the individual loss of either of them (Fig. 5D,F), which is consistent with the idea that motifs within the bipartite signal function together as a unit. Next, we introduced the N-terminal WNIIE motif to the C-terminus of KVS-4ΔWNIIE and assayed its ability to recover the interaction between KVS-4 and UNC-101. Notably, KVS-4ΔWNIIE-WNIIE displayed a significant level of interaction with GST-UNC-101 (Fig. 5C,F).