UniProt UniProt http://www.uniprot.org Control of lipid droplet size in budding yeast requires the collaboration between Fld1 and Ldb16. Control of lipid droplet size in budding yeast requires the collaboration between Fld1 and Ldb16. Journal of cell science 2014 imex curation Wang CW., Miao YH., Chang YS. cwwang02@gate.sinica.edu.tw 15-Nov-2017: Contacted by IntAct-Help. Only protein-protein interactions imex curation 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 predetermined predetermined participant predetermined Wang CW., Miao YH., Chang YS. cwwang02@gate.sinica.edu.tw Accepted 2017-NOV-02 AT 12:26 GMT AT 12:26 GMT by MGT Journal of cell science 2014 imex curation I know, but as 21-275 and 21-275 both bind, I inferred a minimum binding region from them. Control of lipid droplet size in budding yeast requires the collaboration between Fld1 and Ldb16. Control of lipid droplet size in budding yeast requires the collaboration between Fld1 and Ldb16. Journal of cell science 2014 imex curation Wang CW., Miao YH., Chang YS. cwwang02@gate.sinica.edu.tw 15-Nov-2017: Contacted by IntAct-Help. Only protein-protein interactions imex curation yeast Saccharomyces cerevisiae Baker's yeast affinity chrom affinity chromatography technology Affinity purification Affinity purification affinity chrom anti tag western anti tag western blot anti tag western Wang CW., Miao YH., Chang YS. cwwang02@gate.sinica.edu.tw Accepted 2017-NOV-02 AT 12:26 GMT AT 12:26 GMT by MGT Journal of cell science 2014 imex curation I know, but as 21-275 and 21-275 both bind, I inferred a minimum binding region from them. Control of lipid droplet size in budding yeast requires the collaboration between Fld1 and Ldb16. Control of lipid droplet size in budding yeast requires the collaboration between Fld1 and Ldb16. Journal of cell science 2014 imex curation Wang CW., Miao YH., Chang YS. cwwang02@gate.sinica.edu.tw 15-Nov-2017: Contacted by IntAct-Help. Only protein-protein interactions imex curation yeast Saccharomyces cerevisiae Baker's yeast fluorescence imaging fluorescence microscopy fluorescence imaging tag fluorescence tag visualisation by fluorescence tag fluorescence Wang CW., Miao YH., Chang YS. cwwang02@gate.sinica.edu.tw Accepted 2017-NOV-02 AT 12:26 GMT AT 12:26 GMT by MGT Journal of cell science 2014 imex curation I know, but as 21-275 and 21-275 both bind, I inferred a minimum binding region from them. sei1_yeast Seipin SEI1 FLD1 Few lipid droplets protein 1 YLR404W protein protein yeast Saccharomyces cerevisiae Baker's yeast MKINVSRPLQFLQWSSYIVVAFLIQLLIILPLSILIYHDFYLRLLPADSSNVVPLNTFNILNGVQFGTKFFQSIKSIPVGTDLPQTIDNGLSQLIPMRDNMEYKLDLNLQLYCQSKTDHLNLDNLLIDVYRGPGPLLGAPGGSNSKDEKIFHTSRPIVCLALTDSMSPQEIEQLGPSRLDVYDEEWLNTIRIEDKISLESSYETISVFLKTEIAQRNLIIHPESGIKFRMNFEQGLRNLMLRKRFLSYIIGISIFHCIICVLFFITGCTAFIFVRKGQEKSKKHS 3966CB0967B7B62B ldb16_yeast Protein LDB16 YCL005W YCL5W LDB16 Low dye-binding protein 16 protein protein yeast Saccharomyces cerevisiae Baker's yeast MFVVDWSVQLCMGVISPLFRALVQLPLSIFVWNGFQLVALPINIPLRLFLGTSLSRLVAQTSTLDFYVVLTLFQYFAVLCAFGSIIGLIFGFILGVFHSICGVPSVYISLEWKRWFAPIRTVLERASTSIVNIMRGQTIAPIPMPKPNPTHISKPNMKKFHDEPGADDMTITHDVNCYITPCQTPTNEKIQHYNNDSFNTTTTDDEPTDIWDRSDTYQNSFVTNETLMSLSNRAKLRRNASDADIVNIKILRRNSR 49C8084FFCAF50E3 ldb16-sei1-1 2 4 unspecified role unspecified role prey prey Q06058:p.Gly225Pro mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength certain certain sequence position certain certain certain sequence position certain G P Wed May 02 18:27:19 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly225pro' Tue Jun 30 17:02:14 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly225Pro' region myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 5 unspecified role unspecified role bait bait region tap tagged calmodulin binding peptide plus protein a tag CBP-ProtA tagged CBP-ProtA tagged tap tagged undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined physical association physical association Fig. 3C, 8C in addition, using Fld1 as bait in tandem affinity purification (Fld1-TAP) pulled down Ldb16–13×Myc and vice versa, sei1-ldb16-1 2 4 unspecified role unspecified role bait bait region tap tagged calmodulin binding peptide plus protein a tag CBP-ProtA tagged CBP-ProtA tagged tap tagged undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 5 unspecified role unspecified role prey prey region myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined physical association physical association Fig. 3C in addition, using Fld1 as bait in tandem affinity purification (Fld1-TAP) pulled down Ldb16–13×Myc and vice versa, ldb16-sei1-2 1 4 unspecified role unspecified role prey prey 5 unspecified role unspecified role bait bait region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain physical association physical association Fig. 3D, 4B Yeast two-hybrid assay further confirmed the Fld1–Ldb16 interaction and Fld1 self-interaction (Fig. 3D). sei1-sei1-1 1 4 unspecified role unspecified role prey prey region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 4 unspecified role unspecified role bait bait physical association physical association Fig. 3D, 5B, 5F Yeast two-hybrid assay further confirmed the Fld1–Ldb16 interaction and Fld1 self-interaction (Fig. 3D). The affinity of SEI1–SEI1 reduced in ldb16-/- cells ldb16-sei1-3 3 4 unspecified role unspecified role neutral component neutral component region mcherry mcherry fluorescent protein tag mcherry undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 5 unspecified role unspecified role neutral component neutral component region gfp tag green fluorescent protein tag GFP green fluorescent protein GFP green fluorescent protein gfp tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined colocalization colocalization Fig. 3E The quantified data indicated that ∼50% of the Fld1 and Ldb16 puncta colocalized ldb16-sei1-4 2 4 unspecified role unspecified role bait bait region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain region protein a tag protein a tag protein A protein A undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 5 unspecified role unspecified role prey prey region myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined physical association physical association Fig. 5C using pulldown assays, we found that Fld1 self-interaction, and interaction with Ldb16, ldb16-sei1-5 1 5 unspecified role unspecified role bait bait 4 unspecified role unspecified role prey prey region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain physical association physical association Fig. 5B Yeast two-hybrid assay further confirmed the Fld1–Ldb16 interaction and Fld1 self-interaction (Fig. 3D). sei1-sei1-2 2 4 unspecified role unspecified role bait bait region tap tagged calmodulin binding peptide plus protein a tag CBP-ProtA tagged CBP-ProtA tagged tap tagged undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 4 unspecified role unspecified role prey prey region myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined physical association physical association Fig. 5F using pulldown assays, we found that Fld1 self-interaction, and interaction with Ldb16, The affinity of Fld1–Fld1 reduced in ldb16-/- cells ldb16-sei1-6 2 5 unspecified role unspecified role bait bait region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain region protein a tag protein a tag protein A protein A undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 4 unspecified role unspecified role prey prey region myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined physical association physical association Fig. 4C in addition, using Fld1 as bait in tandem affinity purification (Fld1-TAP) pulled down Ldb16–13×Myc and vice versa,