##gff-version 3 P50570 UniProtKB Chain 1 870 . . . ID=PRO_0000206570;Note=Dynamin-2 P50570 UniProtKB Domain 28 294 . . . Note=Dynamin-type G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01055 P50570 UniProtKB Domain 519 625 . . . Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145 P50570 UniProtKB Domain 653 744 . . . Note=GED;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00720 P50570 UniProtKB Region 38 45 . . . Note=G1 motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01055 P50570 UniProtKB Region 64 66 . . . Note=G2 motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01055 P50570 UniProtKB Region 136 139 . . . Note=G3 motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01055 P50570 UniProtKB Region 205 208 . . . Note=G4 motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01055 P50570 UniProtKB Region 235 238 . . . Note=G5 motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01055 P50570 UniProtKB Region 741 870 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P50570 UniProtKB Compositional bias 755 770 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P50570 UniProtKB Compositional bias 771 796 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P50570 UniProtKB Compositional bias 828 859 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P50570 UniProtKB Binding site 41 41 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q05193 P50570 UniProtKB Binding site 43 43 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q05193 P50570 UniProtKB Binding site 44 44 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q05193 P50570 UniProtKB Binding site 45 45 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q05193 P50570 UniProtKB Binding site 46 46 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q05193 P50570 UniProtKB Binding site 59 59 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q05193 P50570 UniProtKB Binding site 60 60 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q05193 P50570 UniProtKB Binding site 206 206 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q05193 P50570 UniProtKB Binding site 208 208 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q05193 P50570 UniProtKB Binding site 211 211 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q05193 P50570 UniProtKB Binding site 236 236 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q05193 P50570 UniProtKB Binding site 237 237 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q05193 P50570 UniProtKB Binding site 239 239 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q05193 P50570 UniProtKB Modified residue 231 231 . . . Note=Phosphotyrosine%3B by SRC;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P39052,ECO:0000305|PubMed:34744632;Dbxref=PMID:34744632 P50570 UniProtKB Modified residue 299 299 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P39054 P50570 UniProtKB Modified residue 597 597 . . . Note=Phosphotyrosine%3B by SRC;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P39052,ECO:0000305|PubMed:34744632;Dbxref=PMID:34744632 P50570 UniProtKB Modified residue 598 598 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 P50570 UniProtKB Modified residue 755 755 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569 P50570 UniProtKB Modified residue 764 764 . . . Note=Phosphoserine%3B by CDK1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P39052 P50570 UniProtKB Modified residue 848 848 . . . Note=Phosphoserine%3B by GSK3-alpha;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:36445308;Dbxref=PMID:36445308 P50570 UniProtKB Alternative sequence 407 444 . . . ID=VSP_044280;Note=In isoform 3 and isoform 4. LAFEAIVKKQVVKLKEPCLKCVDLVIQELINTVRQCTS->MAFEAIVKKQIVKLKEPSLKCVDLVVSELATVIKKCAE;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 P50570 UniProtKB Alternative sequence 516 519 . . . ID=VSP_001325;Note=In isoform 2 and isoform 3. Missing;Ontology_term=ECO:0000303,ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:14702039,ECO:0000303|PubMed:15489334,ECO:0000303|PubMed:7590285;Dbxref=PMID:14702039,PMID:15489334,PMID:7590285 P50570 UniProtKB Alternative sequence 848 848 . . . ID=VSP_047534;Note=In isoform 5. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 P50570 UniProtKB Natural variant 263 263 . . . ID=VAR_031961;Note=P->L;Dbxref=dbSNP:rs3745674 P50570 UniProtKB Natural variant 358 358 . . . ID=VAR_068425;Note=In CMT2M. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18560793;Dbxref=dbSNP:rs267606772,PMID:18560793 P50570 UniProtKB Natural variant 368 368 . . . ID=VAR_031962;Note=In CNM1. E->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16227997,ECO:0000269|PubMed:20227276;Dbxref=dbSNP:rs121909092,PMID:16227997,PMID:20227276 P50570 UniProtKB Natural variant 368 368 . . . ID=VAR_068365;Note=In CNM1. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17825552;Dbxref=PMID:17825552 P50570 UniProtKB Natural variant 369 369 . . . ID=VAR_031963;Note=In CNM1. R->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16227997;Dbxref=dbSNP:rs121909089,PMID:16227997 P50570 UniProtKB Natural variant 369 369 . . . ID=VAR_031964;Note=In CNM1%3B reduced association with the centrosome. R->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16227997;Dbxref=dbSNP:rs121909090,PMID:16227997 P50570 UniProtKB Natural variant 379 379 . . . ID=VAR_070163;Note=In LCCS5%3B hypomorphic mutation impacting on endocytosis. F->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23092955;Dbxref=dbSNP:rs397514735,PMID:23092955 P50570 UniProtKB Natural variant 465 465 . . . ID=VAR_031965;Note=In CNM1%3B reduced association with the centrosome%3B COS7 cells show a reduced uptake of transferrin and low-density lipoprotein complex%3B decreases autophagosome maturation%3B does not affect endocytosis%3B does not affect the trafficking of ATG9A and ATG16L1%3B does not affect SNX18 interaction%3B increases cell membrane localization%3B increases interaction with ITSN1%3B impairs recruitment to phagophore assembly site%3B increases GTPase-mediated membrane fission%3B inhibits GTPase-mediated membrane fission by BIN1 in a dose-dependent manner. R->W;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16227997,ECO:0000269|PubMed:19623537,ECO:0000269|PubMed:20227276,ECO:0000269|PubMed:32315611,ECO:0000269|PubMed:36445308;Dbxref=dbSNP:rs121909091,PMID:16227997,PMID:19623537,PMID:20227276,PMID:32315611,PMID:36445308 P50570 UniProtKB Natural variant 522 522 . . . ID=VAR_068366;Note=In CNM1. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22396310;Dbxref=dbSNP:rs2072577342,PMID:22396310 P50570 UniProtKB Natural variant 522 522 . . . ID=VAR_068367;Note=In CNM1. R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20227276;Dbxref=dbSNP:rs587783595,PMID:20227276 P50570 UniProtKB Natural variant 523 523 . . . ID=VAR_068368;Note=In CNM1. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22396310;Dbxref=dbSNP:rs587783596,PMID:22396310 P50570 UniProtKB Natural variant 537 537 . . . ID=VAR_062574;Note=In CMT2M. G->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17636067;Dbxref=dbSNP:rs121909093,PMID:17636067 P50570 UniProtKB Natural variant 555 557 . . . ID=VAR_031966;Note=In CMTDIB and CNM1%3B may affect binding to vesicles and membranes in favor of binding to microtubules%3B may affect receptor-mediated endocytosis%3B does not affect binding to vesicles composed of 1-phosphatidyl-1D-myo-inositol 4%2C5-bisphosphate%2C stabilizes polymers%3B increases GTPase activity%3B becomes resistant to disassembly%3B does not induce the formation of high-order oligomers%3B increases tyrosine phosphorylation. Missing;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15731758,ECO:0000269|PubMed:34744632;Dbxref=PMID:15731758,PMID:34744632 P50570 UniProtKB Natural variant 560 560 . . . ID=VAR_068369;Note=In CNM1. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19122038;Dbxref=dbSNP:rs879254086,PMID:19122038 P50570 UniProtKB Natural variant 562 562 . . . ID=VAR_031967;Note=In CMTDIB and CNM1%3B with neutropenia%3B COS7 cells show a reduced uptake of transferrin and low-density lipoprotein complex%3B impairs PHD domain binding to vesicles composed of 1-phosphatidyl-1D-myo-inositol 4%2C5-bisphosphate%3B does not affect GTP- and salt-induced disassembly%3B does not induce the formation of high-order oligomers%3B does not affect phosphorylation. K->E;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15731758,ECO:0000269|PubMed:19623537,ECO:0000269|PubMed:34744632;Dbxref=dbSNP:rs121909088,PMID:15731758,PMID:19623537,PMID:34744632 P50570 UniProtKB Natural variant 562 562 . . . ID=VAR_070164;Note=In CMTDIB. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15731758;Dbxref=dbSNP:rs1599620408,PMID:15731758 P50570 UniProtKB Natural variant 570 570 . . . ID=VAR_062575;Note=In CMT2M. L->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17636067;Dbxref=dbSNP:rs121909094,PMID:17636067 P50570 UniProtKB Natural variant 618 618 . . . ID=VAR_068370;Note=In CNM1. A->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19932619;Dbxref=dbSNP:rs1555715869,PMID:19932619 P50570 UniProtKB Natural variant 618 618 . . . ID=VAR_039041;Note=In CNM1%3B severe%3B does not affect PHD domain binding to vesicles composed of and 1-phosphatidyl-1D-myo-inositol 4%2C5-bisphosphate%3B induces the formation of high-order oligomers%3B does not affect phosphorylation%3B increases GTPase-mediated membrane fission%3B inhibits GTPase-mediated membrane fission by BIN1 in a dose-dependent manner. A->T;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17932957,ECO:0000269|PubMed:20227276,ECO:0000269|PubMed:34744632,ECO:0000269|PubMed:36445308;Dbxref=dbSNP:rs773598203,PMID:17932957,PMID:20227276,PMID:34744632,PMID:36445308 P50570 UniProtKB Natural variant 619 619 . . . ID=VAR_039042;Note=In CNM1%3B severe%3B impairs BIN1-dependent T-tubule formation%2C zebrafish larval muscle show alteration of T-tubule organization%3B increases GTPase-mediated membrane fission%3B inhibits GTPase-mediated membrane fission by BIN1 in a dose-dependent manner. S->L;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17932957,ECO:0000269|PubMed:20227276,ECO:0000269|PubMed:24135484,ECO:0000269|PubMed:36445308;Dbxref=dbSNP:rs121909095,PMID:17932957,PMID:20227276,PMID:24135484,PMID:36445308 P50570 UniProtKB Natural variant 619 619 . . . ID=VAR_039043;Note=In CNM1%3B severe. S->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17932957;Dbxref=dbSNP:rs121909095,PMID:17932957 P50570 UniProtKB Natural variant 621 621 . . . ID=VAR_068371;Note=In CNM1%3B centronuclear myopathy with cataracts. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19932620;Dbxref=dbSNP:rs587783597,PMID:19932620 P50570 UniProtKB Natural variant 625 625 . . . ID=VAR_039044;Note=In CNM1%3B severe%3B COS7 cells show a reduced uptake of transferrin and low-density lipoprotein complex%3B increases GTPase-mediated membrane fission%3B inhibits GTPase-mediated membrane fission by BIN1 in a dose-dependent manner. Missing;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17932957,ECO:0000269|PubMed:19623537,ECO:0000269|PubMed:36445308;Dbxref=PMID:17932957,PMID:19623537,PMID:36445308 P50570 UniProtKB Natural variant 627 627 . . . ID=VAR_068372;Note=In CNM1. P->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20227276;Dbxref=PMID:20227276 P50570 UniProtKB Natural variant 627 627 . . . ID=VAR_068373;Note=In CNM1. P->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22396310;Dbxref=dbSNP:rs587783598,PMID:22396310 P50570 UniProtKB Natural variant 650 650 . . . ID=VAR_062576;Note=In CNM1%3B COS7 cells show a reduced uptake of transferrin and low-density lipoprotein complex. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19623537;Dbxref=PMID:19623537 P50570 UniProtKB Mutagenesis 44 44 . . . Note=Inhibits receptor-mediated endocytosis. Inhibits EGF-induced MAPK3 and MAPK1 activation. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19623537;Dbxref=PMID:19623537 P50570 UniProtKB Mutagenesis 231 231 . . . Note=Greatly reduces tyrosine phosphorylation%3B when associated with F-597. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:34744632;Dbxref=PMID:34744632 P50570 UniProtKB Mutagenesis 525 525 . . . Note=Abolishes interaction with MAP1LC3B. Does not affect interaction with ITSN1. Affects nascent autophagosome membranes. Does not affect the trafficking of ATG9A and ATG16L1. Does not affect SNX18 interaction. Decreases autophagosome maturation. W->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32315611;Dbxref=PMID:32315611 P50570 UniProtKB Mutagenesis 597 597 . . . Note=Greatly reduces tyrosine phosphorylation%3B when associated with F-231. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:34744632;Dbxref=PMID:34744632 P50570 UniProtKB Mutagenesis 848 848 . . . Note=Decreases receptor internalization. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:36445308;Dbxref=PMID:36445308 P50570 UniProtKB Mutagenesis 848 848 . . . Note=Decreases binding affinity to BIN1. Increases GTPase mediated-membrane fission activity by BIN1. Decreases cell surface expression of SLC2A4. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:36445308;Dbxref=PMID:36445308 P50570 UniProtKB Sequence conflict 155 156 . . . Note=QI->RV;Ontology_term=ECO:0000305;evidence=ECO:0000305 P50570 UniProtKB Sequence conflict 207 207 . . . Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 P50570 UniProtKB Sequence conflict 316 316 . . . Note=N->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 P50570 UniProtKB Sequence conflict 324 324 . . . Note=R->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 P50570 UniProtKB Sequence conflict 475 475 . . . Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 P50570 UniProtKB Beta strand 522 530 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YS1 P50570 UniProtKB Beta strand 533 535 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YS1 P50570 UniProtKB Beta strand 540 545 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YS1 P50570 UniProtKB Beta strand 550 555 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YS1 P50570 UniProtKB Beta strand 560 565 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YS1 P50570 UniProtKB Beta strand 567 573 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YS1 P50570 UniProtKB Beta strand 585 590 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YS1 P50570 UniProtKB Beta strand 596 599 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YS1 P50570 UniProtKB Beta strand 601 606 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YS1 P50570 UniProtKB Helix 610 623 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YS1