ID DYN2_HUMAN Reviewed; 870 AA. AC P50570; A8K1B6; E7EV30; E9PEQ4; K7ESI9; Q5I0Y0; Q7Z5S3; Q9UPH4; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 10-MAY-2004, sequence version 2. DT 27-MAR-2024, entry version 232. DE RecName: Full=Dynamin-2 {ECO:0000303|PubMed:29437695}; DE EC=3.6.5.5 {ECO:0000269|PubMed:34744632}; DE AltName: Full=Dynamin 2 {ECO:0000303|PubMed:17676042}; DE AltName: Full=Dynamin II {ECO:0000303|PubMed:7590285}; GN Name=DNM2 {ECO:0000312|HGNC:HGNC:2974}; Synonyms=DYN2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY. RX PubMed=7590285; DOI=10.1016/0378-1119(95)00275-b; RA Diatloff-Zito C., Gordon A.J.E., Duchaud E., Merlin G.; RT "Isolation of an ubiquitously expressed cDNA encoding human dynamin II, a RT member of the large GTP-binding protein family."; RL Gene 163:301-306(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5). RC TISSUE=Astrocyte, and Brain; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Ovary, and Uterus; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP INTERACTION WITH SHANK PROTEINS. RX PubMed=11583995; DOI=10.1074/jbc.m104927200; RA Okamoto P.M., Gamby C., Wells D., Fallon J., Vallee R.B.; RT "Dynamin isoform-specific interaction with the shank/ProSAP scaffolding RT proteins of the postsynaptic density and actin cytoskeleton."; RL J. Biol. Chem. 276:48458-48465(2001). RN [6] RP SUBCELLULAR LOCATION. RX PubMed=15048127; DOI=10.1038/ncb1112; RA Thompson H.M., Cao H., Chen J., Euteneuer U., McNiven M.A.; RT "Dynamin 2 binds gamma-tubulin and participates in centrosome cohesion."; RL Nat. Cell Biol. 6:335-342(2004). RN [7] RP INTERACTION WITH SH3BP4. RX PubMed=16325581; DOI=10.1016/j.cell.2005.10.021; RA Tosoni D., Puri C., Confalonieri S., Salcini A.E., De Camilli P., RA Tacchetti C., Di Fiore P.P.; RT "TTP specifically regulates the internalization of the transferrin RT receptor."; RL Cell 123:875-888(2005). RN [8] RP SUBCELLULAR LOCATION, AND INTERACTION WITH SNX9. RX PubMed=15703209; DOI=10.1091/mbc.e04-11-1016; RA Soulet F., Yarar D., Leonard M., Schmid S.L.; RT "SNX9 regulates dynamin assembly and is required for efficient clathrin- RT mediated endocytosis."; RL Mol. Biol. Cell 16:2058-2067(2005). RN [9] RP INTERACTION WITH MYO1E. RX PubMed=17257598; DOI=10.1016/j.febslet.2007.01.021; RA Krendel M., Osterweil E.K., Mooseker M.S.; RT "Myosin 1E interacts with synaptojanin-1 and dynamin and is involved in RT endocytosis."; RL FEBS Lett. 581:644-650(2007). RN [10] RP INTERACTION WITH BIN1. RX PubMed=17676042; DOI=10.1038/ng2086; RA Nicot A.-S., Toussaint A., Tosch V., Kretz C., Wallgren-Pettersson C., RA Iwarsson E., Kingston H., Garnier J.-M., Biancalana V., Oldfors A., RA Mandel J.-L., Laporte J.; RT "Mutations in amphiphysin 2 (BIN1) disrupt interaction with dynamin 2 and RT cause autosomal recessive centronuclear myopathy."; RL Nat. Genet. 39:1134-1139(2007). RN [11] RP INTERACTION WITH SNX33. RX PubMed=18353773; DOI=10.1074/jbc.m801531200; RA Schobel S., Neumann S., Hertweck M., Dislich B., Kuhn P.H., Kremmer E., RA Seed B., Baumeister R., Haass C., Lichtenthaler S.F.; RT "A novel sorting nexin modulates endocytic trafficking and alpha-secretase RT cleavage of the amyloid precursor protein."; RL J. Biol. Chem. 283:14257-14268(2008). RN [12] RP INTERACTION WITH PSTPIP1, AND SUBCELLULAR LOCATION. RX PubMed=18480402; DOI=10.1091/mbc.e08-02-0225; RA Cooper K.M., Bennin D.A., Huttenlocher A.; RT "The PCH family member proline-serine-threonine phosphatase-interacting RT protein 1 targets to the leukocyte uropod and regulates directed cell RT migration."; RL Mol. Biol. Cell 19:3180-3191(2008). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [14] RP FUNCTION. RX PubMed=19605363; DOI=10.1074/jbc.m109.024398; RA Mooren O.L., Kotova T.I., Moore A.J., Schafer D.A.; RT "Dynamin2 GTPase and cortactin remodel actin filaments."; RL J. Biol. Chem. 284:23995-24005(2009). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-598, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [17] RP PHOSPHORYLATION AT SER-764. RX PubMed=20496096; DOI=10.1007/s00018-010-0401-z; RA Chircop M., Malladi C.S., Lian A.T., Page S.L., Zavortink M., Gordon C.P., RA McCluskey A., Robinson P.J.; RT "Calcineurin activity is required for the completion of cytokinesis."; RL Cell. Mol. Life Sci. 67:3725-3737(2010). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [19] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [20] RP INTERACTION WITH CTNND2. RX PubMed=22022388; DOI=10.1371/journal.pone.0025379; RA Koutras C., Levesque G.; RT "Identification of novel NPRAP/delta-catenin-interacting proteins and the RT direct association of NPRAP with dynamin 2."; RL PLoS ONE 6:E25379-E25379(2011). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-755, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [22] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [23] RP FUNCTION, AND INTERACTION WITH SNX18. RX PubMed=29437695; DOI=10.15252/embr.201744837; RA Soereng K., Munson M.J., Lamb C.A., Bjoerndal G.T., Pankiv S., RA Carlsson S.R., Tooze S.A., Simonsen A.; RT "SNX18 regulates ATG9A trafficking from recycling endosomes by recruiting RT Dynamin-2."; RL EMBO Rep. 19:0-0(2018). RN [24] RP FUNCTION. RX PubMed=33713620; DOI=10.1016/j.cell.2021.02.053; RA Yeung M.L., Teng J.L.L., Jia L., Zhang C., Huang C., Cai J.P., Zhou R., RA Chan K.H., Zhao H., Zhu L., Siu K.L., Fung S.Y., Yung S., Chan T.M., RA To K.K., Chan J.F., Cai Z., Lau S.K.P., Chen Z., Jin D.Y., Woo P.C.Y., RA Yuen K.Y.; RT "Soluble ACE2-mediated cell entry of SARS-CoV-2 via interaction with RT proteins related to the renin-angiotensin system."; RL Cell 0:0-0(2021). RN [25] RP FUNCTION, INTERACTION WITH BIN1, SUBUNIT, VARIANTS CNM1 TRP-465; THR-618; RP LEU-619 AND VAL-625 DEL, CHARACTERIZATION OF VARIANTS CNM1 TRP-465; RP THR-618; LEU-619 AND VAL-625 DEL, MUTAGENESIS OF SER-848, AND RP PHOSPHORYLATION AT SER-848. RX PubMed=36445308; DOI=10.1083/jcb.202102119; RA Laiman J., Hsu Y.J., Loh J., Tang W.C., Chuang M.C., Liu H.K., Yang W.S., RA Chen B.C., Chuang L.M., Chang Y.C., Liu Y.W.; RT "GSK3alpha phosphorylates dynamin-2 to promote GLUT4 endocytosis in muscle RT cells."; RL J. Cell Biol. 222:0-0(2023). RN [26] RP STRUCTURE BY NMR OF 514-625. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the PH domain of dynamin-2 from human."; RL Submitted (APR-2008) to the PDB data bank. RN [27] RP VARIANTS CMTDIB 555-ASP--GLU-557 DEL; LYS-562 DEL AND GLU-562, RP CHARACTERIZATION OF VARIANT CMTDIB 555-ASP--GLU-557 DEL, SUBCELLULAR RP LOCATION, AND FUNCTION. RX PubMed=15731758; DOI=10.1038/ng1514; RA Zuechner S., Noureddine M., Kennerson M., Verhoeven K., Claeys K., RA De Jonghe P., Merory J., Oliveira S.A., Speer M.C., Stenger J.E., RA Walizada G., Zhu D., Pericak-Vance M.A., Nicholson G., Timmerman V., RA Vance J.M.; RT "Mutations in the pleckstrin homology domain of dynamin 2 cause dominant RT intermediate Charcot-Marie-Tooth disease."; RL Nat. Genet. 37:289-294(2005). RN [28] RP VARIANTS CNM1 LYS-368; TRP-369; GLN-369 AND TRP-465, CHARACTERIZATION OF RP VARIANTS CNM1 TRP-369 AND TRP-465, AND SUBCELLULAR LOCATION. RX PubMed=16227997; DOI=10.1038/ng1657; RA Bitoun M., Maugenre S., Jeannet P.-Y., Lacene E., Ferrer X., Laforet P., RA Martin J.-J., Laporte J., Lochmueller H., Beggs A.H., Fardeau M., RA Eymard B., Romero N.B., Guicheney P.; RT "Mutations in dynamin 2 cause dominant centronuclear myopathy."; RL Nat. Genet. 37:1207-1209(2005). RN [29] RP VARIANTS CNM1 THR-618; LEU-619; TRP-619 AND VAL-625 DEL. RX PubMed=17932957; DOI=10.1002/ana.21235; RA Bitoun M., Bevilacqua J.A., Prudhon B., Maugenre S., Taratuto A.L., RA Monges S., Lubieniecki F., Cances C., Uro-Coste E., Mayer M., Fardeau M., RA Romero N.B., Guicheney P.; RT "Dynamin 2 mutations cause sporadic centronuclear myopathy with neonatal RT onset."; RL Ann. Neurol. 62:666-670(2007). RN [30] RP VARIANTS CMT2M CYS-537 AND HIS-570. RX PubMed=17636067; DOI=10.1212/01.wnl.0000265820.51075.61; RA Fabrizi G.M., Ferrarini M., Cavallaro T., Cabrini I., Cerini R., RA Bertolasi L., Rizzuto N.; RT "Two novel mutations in dynamin-2 cause axonal Charcot-Marie-Tooth RT disease."; RL Neurology 69:291-295(2007). RN [31] RP VARIANT CNM1 GLN-368. RX PubMed=17825552; DOI=10.1016/j.nmd.2007.06.467; RA Echaniz-Laguna A., Nicot A.S., Carre S., Franques J., Tranchant C., RA Dondaine N., Biancalana V., Mandel J.L., Laporte J.; RT "Subtle central and peripheral nervous system abnormalities in a family RT with centronuclear myopathy and a novel dynamin 2 gene mutation."; RL Neuromuscul. Disord. 17:955-959(2007). RN [32] RP VARIANT CMT2M ARG-358. RX PubMed=18560793; DOI=10.1007/s00415-008-0808-8; RA Gallardo E., Claeys K.G., Nelis E., Garcia A., Canga A., Combarros O., RA Timmerman V., De Jonghe P., Berciano J.; RT "Magnetic resonance imaging findings of leg musculature in Charcot-Marie- RT Tooth disease type 2 due to dynamin 2 mutation."; RL J. Neurol. 255:986-992(2008). RN [33] RP VARIANT CNM1 LYS-650, CHARACTERIZATION OF VARIANTS CNM1 TRP-465; VAL-625 RP DEL AND LYS-650, CHARACTERIZATION OF VARIANT CMTDIB GLU-562, RP PATHOPHYSIOLOGICAL PATHWAY IN THE AUTOSOMAL FORMS OF CNM AND DNM2-CMT RP NEUROPATHY, FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF LYS-44. RX PubMed=19623537; DOI=10.1002/humu.21086; RA Bitoun M., Durieux A.-C., Prudhon B., Bevilacqua J.A., Herledan A., RA Sakanyan V., Urtizberea A., Cartier L., Romero N.B., Guicheney P.; RT "Dynamin 2 mutations associated with human diseases impair clathrin- RT mediated receptor endocytosis."; RL Hum. Mutat. 30:1419-1427(2009). RN [34] RP VARIANT CNM1 LYS-560. RX PubMed=19122038; DOI=10.1212/01.wnl.0000338624.25852.12; RA Bitoun M., Bevilacqua J.A., Eymard B., Prudhon B., Fardeau M., RA Guicheney P., Romero N.B.; RT "A new centronuclear myopathy phenotype due to a novel dynamin 2 RT mutation."; RL Neurology 72:93-95(2009). RN [35] RP VARIANT CNM1 PRO-621. RX PubMed=19932620; DOI=10.1016/j.nmd.2009.10.005; RA Jungbluth H., Cullup T., Lillis S., Zhou H., Abbs S., Sewry C., Muntoni F.; RT "Centronuclear myopathy with cataracts due to a novel dynamin 2 (DNM2) RT mutation."; RL Neuromuscul. Disord. 20:49-52(2010). RN [36] RP VARIANT CNM1 ASP-618. RX PubMed=19932619; DOI=10.1016/j.nmd.2009.10.006; RA Melberg A., Kretz C., Kalimo H., Wallgren-Pettersson C., Toussaint A., RA Bohm J., Stalberg E., Laporte J.; RT "Adult course in dynamin 2 dominant centronuclear myopathy with neonatal RT onset."; RL Neuromuscul. Disord. 20:53-56(2010). RN [37] RP VARIANTS CNM1 LYS-368; TRP-465; HIS-522; THR-618; LEU-619 AND HIS-627. RX PubMed=20227276; DOI=10.1016/j.nmd.2010.02.016; RA Susman R.D., Quijano-Roy S., Yang N., Webster R., Clarke N.F., Dowling J., RA Kennerson M., Nicholson G., Biancalana V., Ilkovski B., Flanigan K.M., RA Arbuckle S., Malladi C., Robinson P., Vucic S., Mayer M., Romero N.B., RA Urtizberea J.A., Garcia-Bragado F., Guicheney P., Bitoun M., Carlier R.Y., RA North K.N.; RT "Expanding the clinical, pathological and MRI phenotype of DNM2-related RT centronuclear myopathy."; RL Neuromuscul. Disord. 20:229-237(2010). RN [38] RP VARIANTS CNM1 CYS-522; GLY-523 AND ARG-627. RX PubMed=22396310; DOI=10.1002/humu.22067; RA Bohm J., Biancalana V., Dechene E.T., Bitoun M., Pierson C.R., Schaefer E., RA Karasoy H., Dempsey M.A., Klein F., Dondaine N., Kretz C., Haumesser N., RA Poirson C., Toussaint A., Greenleaf R.S., Barger M.A., Mahoney L.J., RA Kang P.B., Zanoteli E., Vissing J., Witting N., Echaniz-Laguna A., RA Wallgren-Pettersson C., Dowling J., Merlini L., Oldfors A., RA Bomme Ousager L., Melki J., Krause A., Jern C., Oliveira A.S., Petit F., RA Jacquette A., Chaussenot A., Mowat D., Leheup B., Cristofano M., RA Poza Aldea J.J., Michel F., Furby A., Llona J.E., Van Coster R., RA Bertini E., Urtizberea J.A., Drouin-Garraud V., Beroud C., Prudhon B., RA Bedford M., Mathews K., Erby L.A., Smith S.A., Roggenbuck J., Crowe C.A., RA Brennan Spitale A., Johal S.C., Amato A.A., Demmer L.A., Jonas J., RA Darras B.T., Bird T.D., Laurino M., Welt S.I., Trotter C., Guicheney P., RA Das S., Mandel J.L., Beggs A.H., Laporte J.; RT "Mutation spectrum in the large GTPase dynamin 2, and genotype-phenotype RT correlation in autosomal dominant centronuclear myopathy."; RL Hum. Mutat. 33:949-959(2012). RN [39] RP VARIANT LCCS5 VAL-379. RX PubMed=23092955; DOI=10.1038/ejhg.2012.226; RA Koutsopoulos O.S., Kretz C., Weller C.M., Roux A., Mojzisova H., Boehm J., RA Koch C., Toussaint A., Heckel E., Stemkens D., Ter Horst S.A., Thibault C., RA Koch M., Mehdi S.Q., Bijlsma E.K., Mandel J.L., Vermot J., Laporte J.; RT "Dynamin 2 homozygous mutation in humans with a lethal congenital RT syndrome."; RL Eur. J. Hum. Genet. 21:637-642(2013). RN [40] RP VARIANT CNM1 LEU-619, CHARACTERIZATION OF VARIANT CNM1 LEU-619, AND RP FUNCTION. RX PubMed=24135484; DOI=10.1242/dmm.012286; RA Gibbs E.M., Davidson A.E., Telfer W.R., Feldman E.L., Dowling J.J.; RT "The myopathy-causing mutation DNM2-S619L leads to defective tubulation in RT vitro and in developing zebrafish."; RL Dis. Model. Mech. 7:157-161(2014). RN [41] RP VARIANT CNM1 TRP-465, CHARACTERIZATION OF VARIANT CNM1 TRP-465, FUNCTION, RP SUBCELLULAR LOCATION, INTERACTION WITH SNX18; ITSN1; MAP1LC3B; GABARAP; RP GABARAPL1 AND GABARAPL2, AND MUTAGENESIS OF TRP-525. RX PubMed=32315611; DOI=10.1016/j.devcel.2020.03.018; RA Puri C., Manni M.M., Vicinanza M., Hilcenko C., Zhu Y., Runwal G., RA Stamatakou E., Menzies F.M., Mamchaoui K., Bitoun M., Rubinsztein D.C.; RT "A DNM2 Centronuclear Myopathy Mutation Reveals a Link between Recycling RT Endosome Scission and Autophagy."; RL Dev. Cell 53:154.e6-168.e6(2020). RN [42] RP VARIANTS CNM1 555-ASP--GLU-557 DEL; GLU-562 AND THR-618, CHARACTERIZATION RP OF VARIANTS CNM1 555-ASP--GLU-557 DEL; GLU-562 AND THR-618, FUNCTION, RP CATALYTIC ACTIVITY, SUBUNIT, DOMAIN, PHOSPHORYLATION AT TYR-231 AND RP TYR-597, AND MUTAGENESIS OF TYR-231 AND TYR-597. RX PubMed=34744632; DOI=10.3389/fncel.2021.745940; RA Tassin T.C., Barylko B., Hedde P.N., Chen Y., Binns D.D., James N.G., RA Mueller J.D., Jameson D.M., Taussig R., Albanesi J.P.; RT "Gain-of-Function Properties of a Dynamin 2 Mutant Implicated in Charcot- RT Marie-Tooth Disease."; RL Front. Cell. Neurosci. 15:745940-745940(2021). CC -!- FUNCTION: Catalyzes the hydrolysis of GTP and utilizes this energy to CC mediate vesicle scission at plasma membrane during endocytosis and CC filament remodeling at many actin structures during organization of the CC actin cytoskeleton (PubMed:33713620, PubMed:15731758, PubMed:19623537, CC PubMed:34744632, PubMed:19605363). Plays an important role in vesicular CC trafficking processes, namely clathrin-mediated endocytosis (CME), CC exocytic and clathrin-coated vesicle from the trans-Golgi network, and CC PDGF stimulated macropinocytosis (PubMed:33713620, PubMed:15731758, CC PubMed:19623537). During vesicular trafficking process, associates to CC the membrane, through lipid binding, and self-assembles into ring-like CC structure through oligomerization to form a helical polymer around the CC vesicle membrane and leading to vesicle scission (PubMed:17636067, CC PubMed:34744632, PubMed:36445308). Plays a role in organization of the CC actin cytoskeleton by mediating arrangement of stress fibers and actin CC bundles in podocytes (By similarity). During organization of the actin CC cytoskeleton, self-assembles into ring-like structure that directly CC bundles actin filaments to form typical membrane tubules decorated with CC dynamin spiral polymers (By similarity). Self-assembly increases GTPase CC activity and the GTP hydrolysis causes the rapid depolymerization of CC dynamin spiral polymers, and results in dispersion of actin bundles (By CC similarity). Remodels, through its interaction with CTTN, bundled actin CC filaments in a GTPase-dependent manner and plays a role in CC orchestrating the global actomyosin cytoskeleton (PubMed:19605363). The CC interaction with CTTN stabilizes the interaction of DNM2 and actin CC filaments and stimulates the intrinsic GTPase activity that results in CC actin filament-barbed ends and increases the sensitivity of filaments CC in bundles to the actin depolymerizing factor, CFL1 (By similarity). CC Plays a role in the autophagy process, by participating in the CC formation of ATG9A vesicles destined for the autophagosomes through its CC interaction with SNX18 (PubMed:29437695), by mediating recycling CC endosome scission leading to autophagosome release through MAP1LC3B CC interaction (PubMed:32315611, PubMed:29437695). Also regulates CC maturation of apoptotic cell corpse-containing phagosomes by recruiting CC PIK3C3 to the phagosome membrane (By similarity). Also plays a role in CC cytokinesis (By similarity). May participate in centrosome cohesion CC through its interaction with TUBG1 (By similarity). Plays a role in the CC regulation of neuron morphology, axon growth and formation of neuronal CC growth cones (By similarity). Involved in membrane tubulation CC (PubMed:24135484). {ECO:0000250|UniProtKB:P39052, CC ECO:0000250|UniProtKB:P39054, ECO:0000269|PubMed:15731758, CC ECO:0000269|PubMed:17636067, ECO:0000269|PubMed:19605363, CC ECO:0000269|PubMed:19623537, ECO:0000269|PubMed:24135484, CC ECO:0000269|PubMed:29437695, ECO:0000269|PubMed:32315611, CC ECO:0000269|PubMed:33713620, ECO:0000269|PubMed:34744632, CC ECO:0000269|PubMed:36445308}. CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.5; CC Evidence={ECO:0000269|PubMed:34744632}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; CC Evidence={ECO:0000269|PubMed:34744632}; CC -!- SUBUNIT: Oligomerizes into a helical polymer that self-assembles around CC the vesicle membrane, when associated to the menbrane through lipid CC binding (PubMed:34744632, PubMed:36445308). Interacts with SHANK1 and CC SHANK2 (PubMed:11583995). Interacts with SNX9 (PubMed:15703209). CC Interacts (via C-terminal proline-rich domain (PRD)) with SNX18 (via CC SH3 domain); this interaction regulates ATG9A and ATG16L1 trafficking CC from recycling endosomes to sites of autophagosome formation CC (PubMed:29437695, PubMed:32315611). Interacts with SNX33 (via SH3 CC domain) (PubMed:18353773). Interacts with MYO1E (via SH3 domain) CC (PubMed:17257598). Interacts with PSTPIP1 (via SH3 domain) CC (PubMed:18480402). Interacts with CTNND2 (PubMed:22022388). Interacts CC (via C-terminal proline-rich domain (PRD)) with BIN1 (via SH3 domain); CC this interaction allows the recruitment of DNM2 to the membrane tubules CC and inhibits self-assembly-stimulated GTPase activity on the membrane CC (PubMed:17676042, PubMed:36445308). Interacts with GABARAP, GABARAPL1 CC and GABARAPL2 (PubMed:32315611). Interacts with MAP1LC3B (the lipidate CC and non-lipidated LC3 form); this interaction mediates recycling CC endosome scission leading to autophagosome release (PubMed:32315611). CC Interacts with ITSN1 (PubMed:32315611). Interacts (via C-terminal CC proline-rich domain (PRD)) with SH3BP4 (via SH3 domain); this CC interaction controls the GTPase activity and is prevented by EGFR- CC induced tyrosine phosphorylation of either DNM2 or SH3BP4 CC (PubMed:16325581). May interact with PIK3C3. May be a component of a CC complex composed of RAB5A (in GDP-bound form), DYN2 and PIK3C3. CC Interacts with SDC4; this interaction is markedly enhanced at focal CC ahesion site upon induction of focal adhesions and stress-fiber CC formation (By similarity). Interacts with ACTN1. Interacts with CTTN; CC this interaction stimulates the intrinsic GTPase activity of DNM2 and CC stabilizes the association of DNM2 and actin filaments; in addition CC this interaction is stimulated by ligand binding to the receptor, CC leading to the recruitment of the DNM2-CTTN complex to the sequestered CC receptor-ligand complex to its internalization. Interacts with NOSTRIN CC (via SH3 domain); this interaction allows the recruitment of NOS3 to CC dynamin-positive structures.Interacts with TUBG1; this interaction may CC participate in centrosome cohesion (By similarity). CC {ECO:0000250|UniProtKB:P39052, ECO:0000250|UniProtKB:P39054, CC ECO:0000269|PubMed:11583995, ECO:0000269|PubMed:15703209, CC ECO:0000269|PubMed:16325581, ECO:0000269|PubMed:17257598, CC ECO:0000269|PubMed:17676042, ECO:0000269|PubMed:18353773, CC ECO:0000269|PubMed:18480402, ECO:0000269|PubMed:22022388, CC ECO:0000269|PubMed:29437695, ECO:0000269|PubMed:32315611, CC ECO:0000269|PubMed:34744632, ECO:0000269|PubMed:36445308}. CC -!- INTERACTION: CC P50570; Q8N157: AHI1; NbExp=2; IntAct=EBI-346547, EBI-1049056; CC P50570; O95817: BAG3; NbExp=3; IntAct=EBI-346547, EBI-747185; CC P50570; Q14247: CTTN; NbExp=5; IntAct=EBI-346547, EBI-351886; CC P50570; Q8NFF5-2: FLAD1; NbExp=3; IntAct=EBI-346547, EBI-11526128; CC P50570; P62993: GRB2; NbExp=8; IntAct=EBI-346547, EBI-401755; CC P50570; Q15811: ITSN1; NbExp=2; IntAct=EBI-346547, EBI-602041; CC P50570; Q12965: MYO1E; NbExp=2; IntAct=EBI-346547, EBI-4279548; CC P50570; P22392: NME2; NbExp=2; IntAct=EBI-346547, EBI-713693; CC P50570; Q9UNF0: PACSIN2; NbExp=4; IntAct=EBI-346547, EBI-742503; CC P50570; P54646: PRKAA2; NbExp=3; IntAct=EBI-346547, EBI-1383852; CC P50570; P47897: QARS1; NbExp=3; IntAct=EBI-346547, EBI-347462; CC P50570; O76064: RNF8; NbExp=3; IntAct=EBI-346547, EBI-373337; CC P50570; O00560: SDCBP; NbExp=3; IntAct=EBI-346547, EBI-727004; CC P50570; Q15436: SEC23A; NbExp=3; IntAct=EBI-346547, EBI-81088; CC P50570; Q9P0V3: SH3BP4; NbExp=3; IntAct=EBI-346547, EBI-1049513; CC P50570; Q99962: SH3GL2; NbExp=2; IntAct=EBI-346547, EBI-77938; CC P50570; Q96B97: SH3KBP1; NbExp=5; IntAct=EBI-346547, EBI-346595; CC P50570; Q9Y5X1: SNX9; NbExp=4; IntAct=EBI-346547, EBI-77848; CC P50570; Q9BUZ4: TRAF4; NbExp=3; IntAct=EBI-346547, EBI-3650647; CC P50570; P57075-2: UBASH3A; NbExp=3; IntAct=EBI-346547, EBI-7353612; CC P50570; Q9QPN3: nef; Xeno; NbExp=4; IntAct=EBI-346547, EBI-7355146; CC P50570-2; Q9H7C9: AAMDC; NbExp=3; IntAct=EBI-10968534, EBI-10308705; CC P50570-2; Q6PCB6: ABHD17C; NbExp=3; IntAct=EBI-10968534, EBI-22011868; CC P50570-2; Q9NP61: ARFGAP3; NbExp=3; IntAct=EBI-10968534, EBI-2875816; CC P50570-2; Q86TN1: ARNT2; NbExp=3; IntAct=EBI-10968534, EBI-25844820; CC P50570-2; Q9NWX5-2: ASB6; NbExp=3; IntAct=EBI-10968534, EBI-25838672; CC P50570-2; Q96FT7-4: ASIC4; NbExp=3; IntAct=EBI-10968534, EBI-9089489; CC P50570-2; Q8WXF7: ATL1; NbExp=3; IntAct=EBI-10968534, EBI-2410266; CC P50570-2; Q9UII2: ATP5IF1; NbExp=3; IntAct=EBI-10968534, EBI-718459; CC P50570-2; P54252: ATXN3; NbExp=3; IntAct=EBI-10968534, EBI-946046; CC P50570-2; Q9UQB8-6: BAIAP2; NbExp=3; IntAct=EBI-10968534, EBI-9092016; CC P50570-2; Q9UMX3: BOK; NbExp=3; IntAct=EBI-10968534, EBI-7105206; CC P50570-2; Q8WUW1: BRK1; NbExp=3; IntAct=EBI-10968534, EBI-2837444; CC P50570-2; P83916: CBX1; NbExp=3; IntAct=EBI-10968534, EBI-78129; CC P50570-2; Q53EZ4: CEP55; NbExp=3; IntAct=EBI-10968534, EBI-747776; CC P50570-2; Q96FZ7: CHMP6; NbExp=3; IntAct=EBI-10968534, EBI-1049648; CC P50570-2; Q9NSE2: CISH; NbExp=3; IntAct=EBI-10968534, EBI-617866; CC P50570-2; Q92478: CLEC2B; NbExp=3; IntAct=EBI-10968534, EBI-13350535; CC P50570-2; Q16740: CLPP; NbExp=3; IntAct=EBI-10968534, EBI-1056029; CC P50570-2; P04141: CSF2; NbExp=3; IntAct=EBI-10968534, EBI-1809826; CC P50570-2; Q9NR90-2: DAZ3; NbExp=3; IntAct=EBI-10968534, EBI-25830216; CC P50570-2; Q9H816: DCLRE1B; NbExp=3; IntAct=EBI-10968534, EBI-3508943; CC P50570-2; Q9UHI6: DDX20; NbExp=3; IntAct=EBI-10968534, EBI-347658; CC P50570-2; Q14154: DELE1; NbExp=3; IntAct=EBI-10968534, EBI-2805660; CC P50570-2; Q9H147: DNTTIP1; NbExp=3; IntAct=EBI-10968534, EBI-2795449; CC P50570-2; Q9UI08-2: EVL; NbExp=3; IntAct=EBI-10968534, EBI-6448852; CC P50570-2; Q99504: EYA3; NbExp=3; IntAct=EBI-10968534, EBI-9089567; CC P50570-2; Q6SJ93: FAM111B; NbExp=3; IntAct=EBI-10968534, EBI-6309082; CC P50570-2; Q9UKA2: FBXL4; NbExp=3; IntAct=EBI-10968534, EBI-2869903; CC P50570-2; Q6P3S6: FBXO42; NbExp=3; IntAct=EBI-10968534, EBI-2506081; CC P50570-2; Q9UHY8: FEZ2; NbExp=3; IntAct=EBI-10968534, EBI-396453; CC P50570-2; Q9Y261-2: FOXA2; NbExp=3; IntAct=EBI-10968534, EBI-25830360; CC P50570-2; Q6PIV2: FOXR1; NbExp=3; IntAct=EBI-10968534, EBI-10253815; CC P50570-2; P02792: FTL; NbExp=3; IntAct=EBI-10968534, EBI-713279; CC P50570-2; P06241-3: FYN; NbExp=3; IntAct=EBI-10968534, EBI-10691738; CC P50570-2; Q9ULV1: FZD4; NbExp=3; IntAct=EBI-10968534, EBI-2466380; CC P50570-2; Q9H4A5: GOLPH3L; NbExp=3; IntAct=EBI-10968534, EBI-4403434; CC P50570-2; Q13588: GRAP; NbExp=3; IntAct=EBI-10968534, EBI-2847510; CC P50570-2; P0C0S5: H2AZ1; NbExp=3; IntAct=EBI-10968534, EBI-1199859; CC P50570-2; P68431: H3C12; NbExp=3; IntAct=EBI-10968534, EBI-79722; CC P50570-2; P52790: HK3; NbExp=3; IntAct=EBI-10968534, EBI-2965780; CC P50570-2; Q8WVV9-3: HNRNPLL; NbExp=3; IntAct=EBI-10968534, EBI-25845242; CC P50570-2; P09017: HOXC4; NbExp=3; IntAct=EBI-10968534, EBI-3923226; CC P50570-2; P42858: HTT; NbExp=6; IntAct=EBI-10968534, EBI-466029; CC P50570-2; Q6DN90-2: IQSEC1; NbExp=3; IntAct=EBI-10968534, EBI-21911304; CC P50570-2; Q8NA54: IQUB; NbExp=3; IntAct=EBI-10968534, EBI-10220600; CC P50570-2; Q92993: KAT5; NbExp=3; IntAct=EBI-10968534, EBI-399080; CC P50570-2; Q92993-2: KAT5; NbExp=3; IntAct=EBI-10968534, EBI-20795332; CC P50570-2; A1A512: KIAA0355; NbExp=3; IntAct=EBI-10968534, EBI-25844799; CC P50570-2; Q3SY46: KRTAP13-3; NbExp=3; IntAct=EBI-10968534, EBI-10241252; CC P50570-2; Q8IUB9: KRTAP19-1; NbExp=3; IntAct=EBI-10968534, EBI-12811111; CC P50570-2; Q3LI72: KRTAP19-5; NbExp=3; IntAct=EBI-10968534, EBI-1048945; CC P50570-2; Q3SYF9: KRTAP19-7; NbExp=3; IntAct=EBI-10968534, EBI-10241353; CC P50570-2; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-10968534, EBI-10261141; CC P50570-2; Q6DKI2: LGALS9C; NbExp=3; IntAct=EBI-10968534, EBI-9088829; CC P50570-2; A2RU56: LOC401296; NbExp=3; IntAct=EBI-10968534, EBI-9088215; CC P50570-2; Q4G0S1: LOC730441; NbExp=3; IntAct=EBI-10968534, EBI-10241801; CC P50570-2; P07948: LYN; NbExp=3; IntAct=EBI-10968534, EBI-79452; CC P50570-2; Q9UI95: MAD2L2; NbExp=3; IntAct=EBI-10968534, EBI-77889; CC P50570-2; Q9UDY8-2: MALT1; NbExp=3; IntAct=EBI-10968534, EBI-12056869; CC P50570-2; Q99683: MAP3K5; NbExp=3; IntAct=EBI-10968534, EBI-476263; CC P50570-2; Q15759: MAPK11; NbExp=3; IntAct=EBI-10968534, EBI-298304; CC P50570-2; Q8TDB4: MGARP; NbExp=3; IntAct=EBI-10968534, EBI-4397720; CC P50570-2; P41218: MNDA; NbExp=3; IntAct=EBI-10968534, EBI-2829677; CC P50570-2; Q9Y605: MRFAP1; NbExp=3; IntAct=EBI-10968534, EBI-995714; CC P50570-2; O43196-2: MSH5; NbExp=3; IntAct=EBI-10968534, EBI-25844576; CC P50570-2; Q99457: NAP1L3; NbExp=3; IntAct=EBI-10968534, EBI-8645631; CC P50570-2; O76041: NEBL; NbExp=3; IntAct=EBI-10968534, EBI-2880203; CC P50570-2; Q15466: NR0B2; NbExp=3; IntAct=EBI-10968534, EBI-3910729; CC P50570-2; Q9NPJ8-3: NXT2; NbExp=3; IntAct=EBI-10968534, EBI-10698339; CC P50570-2; Q16625: OCLN; NbExp=3; IntAct=EBI-10968534, EBI-2903088; CC P50570-2; Q96CV9-2: OPTN; NbExp=3; IntAct=EBI-10968534, EBI-9091423; CC P50570-2; Q96FW1: OTUB1; NbExp=3; IntAct=EBI-10968534, EBI-1058491; CC P50570-2; O15460-2: P4HA2; NbExp=3; IntAct=EBI-10968534, EBI-10182841; CC P50570-2; Q99497: PARK7; NbExp=3; IntAct=EBI-10968534, EBI-1164361; CC P50570-2; Q13113: PDZK1IP1; NbExp=3; IntAct=EBI-10968534, EBI-716063; CC P50570-2; O14813: PHOX2A; NbExp=3; IntAct=EBI-10968534, EBI-25844430; CC P50570-2; P27986-2: PIK3R1; NbExp=3; IntAct=EBI-10968534, EBI-9090282; CC P50570-2; P12273: PIP; NbExp=3; IntAct=EBI-10968534, EBI-1049746; CC P50570-2; Q96J94: PIWIL1; NbExp=3; IntAct=EBI-10968534, EBI-527417; CC P50570-2; O75626-3: PRDM1; NbExp=3; IntAct=EBI-10968534, EBI-25829882; CC P50570-2; Q15286: RAB35; NbExp=3; IntAct=EBI-10968534, EBI-722275; CC P50570-2; P57729: RAB38; NbExp=3; IntAct=EBI-10968534, EBI-6552718; CC P50570-2; Q96QF0-7: RAB3IP; NbExp=3; IntAct=EBI-10968534, EBI-11984839; CC P50570-2; Q9NS23-4: RASSF1; NbExp=3; IntAct=EBI-10968534, EBI-438710; CC P50570-2; Q9GZR2: REXO4; NbExp=3; IntAct=EBI-10968534, EBI-2856313; CC P50570-2; Q96D59: RNF183; NbExp=3; IntAct=EBI-10968534, EBI-743938; CC P50570-2; Q9BY12-3: SCAPER; NbExp=3; IntAct=EBI-10968534, EBI-25837959; CC P50570-2; Q2NKQ1-4: SGSM1; NbExp=3; IntAct=EBI-10968534, EBI-10182463; CC P50570-2; Q9NQ40: SLC52A3; NbExp=3; IntAct=EBI-10968534, EBI-25845274; CC P50570-2; Q12824: SMARCB1; NbExp=3; IntAct=EBI-10968534, EBI-358419; CC P50570-2; Q12824-2: SMARCB1; NbExp=3; IntAct=EBI-10968534, EBI-358436; CC P50570-2; Q16637-3: SMN2; NbExp=3; IntAct=EBI-10968534, EBI-395447; CC P50570-2; O60749: SNX2; NbExp=3; IntAct=EBI-10968534, EBI-1046690; CC P50570-2; Q8WV41: SNX33; NbExp=3; IntAct=EBI-10968534, EBI-2481535; CC P50570-2; Q05C28: SPACA3; NbExp=3; IntAct=EBI-10968534, EBI-25845337; CC P50570-2; Q7Z6I5: SPATA12; NbExp=3; IntAct=EBI-10968534, EBI-10696971; CC P50570-2; Q7Z698: SPRED2; NbExp=3; IntAct=EBI-10968534, EBI-7082156; CC P50570-2; O75558: STX11; NbExp=3; IntAct=EBI-10968534, EBI-714135; CC P50570-2; Q8N4C7: STX19; NbExp=3; IntAct=EBI-10968534, EBI-8484990; CC P50570-2; P37802: TAGLN2; NbExp=3; IntAct=EBI-10968534, EBI-1056740; CC P50570-2; O95551: TDP2; NbExp=3; IntAct=EBI-10968534, EBI-2819865; CC P50570-2; P28347-2: TEAD1; NbExp=3; IntAct=EBI-10968534, EBI-12151837; CC P50570-2; Q10587: TEF; NbExp=3; IntAct=EBI-10968534, EBI-2796967; CC P50570-2; Q03403: TFF2; NbExp=3; IntAct=EBI-10968534, EBI-4314702; CC P50570-2; P21980-2: TGM2; NbExp=3; IntAct=EBI-10968534, EBI-25842075; CC P50570-2; Q53EQ6-2: TIGD5; NbExp=3; IntAct=EBI-10968534, EBI-10242213; CC P50570-2; Q12888: TP53BP1; NbExp=3; IntAct=EBI-10968534, EBI-396540; CC P50570-2; Q9BUZ4: TRAF4; NbExp=3; IntAct=EBI-10968534, EBI-3650647; CC P50570-2; Q9NX07-2: TRNAU1AP; NbExp=3; IntAct=EBI-10968534, EBI-21894090; CC P50570-2; Q5W5X9-3: TTC23; NbExp=3; IntAct=EBI-10968534, EBI-9090990; CC P50570-2; P10599: TXN; NbExp=3; IntAct=EBI-10968534, EBI-594644; CC P50570-2; P58304: VSX2; NbExp=3; IntAct=EBI-10968534, EBI-6427899; CC P50570-2; O00308: WWP2; NbExp=3; IntAct=EBI-10968534, EBI-743923; CC P50570-2; Q8NAP3: ZBTB38; NbExp=3; IntAct=EBI-10968534, EBI-5235984; CC P50570-2; Q8IUH5: ZDHHC17; NbExp=3; IntAct=EBI-10968534, EBI-524753; CC P50570-2; Q05CR2: ZNF248; NbExp=3; IntAct=EBI-10968534, EBI-25835471; CC P50570-2; Q8N895: ZNF366; NbExp=3; IntAct=EBI-10968534, EBI-2813661; CC P50570-2; Q14966-2: ZNF638; NbExp=3; IntAct=EBI-10968534, EBI-25845021; CC P50570-2; Q5TEC3: ZNF697; NbExp=3; IntAct=EBI-10968534, EBI-25845217; CC P50570-2; Q5JTY5: ZNG1C; NbExp=3; IntAct=EBI-10968534, EBI-723434; CC P50570-2; B7Z3E8; NbExp=3; IntAct=EBI-10968534, EBI-25831617; CC P50570-2; Q99KR7: Ppif; Xeno; NbExp=3; IntAct=EBI-10968534, EBI-6455001; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:15731758}. Cytoplasmic vesicle, clathrin-coated CC vesicle {ECO:0000269|PubMed:15731758}. Cell projection, uropodium CC {ECO:0000269|PubMed:18480402}. Endosome {ECO:0000269|PubMed:15731758}. CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome CC {ECO:0000269|PubMed:16227997}. Cytoplasm, cytoskeleton, microtubule CC organizing center, centrosome, centriole {ECO:0000269|PubMed:15048127}. CC Recycling endosome {ECO:0000269|PubMed:32315611}. Cell projection, CC phagocytic cup {ECO:0000250|UniProtKB:P39054}. Cytoplasmic vesicle, CC phagosome membrane {ECO:0000250|UniProtKB:P39054}; Peripheral membrane CC protein {ECO:0000250|UniProtKB:P39054}. Cell projection, podosome CC {ECO:0000250|UniProtKB:P39054}. Cytoplasm CC {ECO:0000250|UniProtKB:P39052}. Cell junction CC {ECO:0000250|UniProtKB:P39052}. Postsynaptic density CC {ECO:0000250|UniProtKB:P39052}. Synapse, synaptosome CC {ECO:0000250|UniProtKB:P39052}. Midbody {ECO:0000250|UniProtKB:P39052}. CC Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:P39052}. CC Note=Localized in recycling endosomes fragment to release nascent CC autophagosomes (PubMed:32315611). Co-localizes with PIK3C3 and RAB5A to CC the nascent phagosome. Localized at focal ahesion site upon induction CC of focal adhesions and stress-fiber formation, when interacts with SDC4 CC (By similarity). Exists as a dynamic component of the centrosome. CC Associates with clathrin-coated vesicles at both the plasma membrane CC and the trans-Golgi network (TGN) (By similarity). CC {ECO:0000250|UniProtKB:P39052, ECO:0000250|UniProtKB:P39054, CC ECO:0000269|PubMed:32315611}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=P50570-1; Sequence=Displayed; CC Name=2; CC IsoId=P50570-2; Sequence=VSP_001325; CC Name=3; CC IsoId=P50570-3; Sequence=VSP_044280, VSP_001325; CC Name=4; CC IsoId=P50570-4; Sequence=VSP_044280; CC Name=5; CC IsoId=P50570-5; Sequence=VSP_047534; CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:7590285). Expressed in CC skeletal muscle and the peripheral nerve (PubMed:19623537). CC {ECO:0000269|PubMed:19623537, ECO:0000269|PubMed:7590285}. CC -!- PTM: Phosphorylation at Ser-848 by GSK3-alpha relieves the inhibition CC of BIN1 and promotes endocytosis (PubMed:36445308). Phosphorylation at CC Ser-764 by CDK1 is greatly increased upon mitotic entry CC (PubMed:20496096). It regulates cytokinesis downstream of calcineurin, CC and does not affect clathrin-mediated endocytosis (By similarity). CC Dephosphorylated by calcineurin/PP2 during cytokinesis in a Ca(2+)- and CC calmodulin-dependent manner (PubMed:20496096). Phosphorylated on CC tyrosine residues by EGFR and after activation of SRC (By similarity). CC {ECO:0000250|UniProtKB:P39052, ECO:0000250|UniProtKB:P39054, CC ECO:0000269|PubMed:20496096, ECO:0000269|PubMed:36445308}. CC -!- DISEASE: Myopathy, centronuclear, 1 (CNM1) [MIM:160150]: A congenital CC muscle disorder characterized by progressive muscular weakness and CC wasting involving mainly limb girdle, trunk, and neck muscles. It may CC also affect distal muscles. Weakness may be present during childhood or CC adolescence or may not become evident until the third decade of life. CC Ptosis is a frequent clinical feature. The most prominent CC histopathologic features include high frequency of centrally located CC nuclei in muscle fibers not secondary to regeneration, radial CC arrangement of sarcoplasmic strands around the central nuclei, and CC predominance and hypotrophy of type 1 fibers. CC {ECO:0000269|PubMed:16227997, ECO:0000269|PubMed:17825552, CC ECO:0000269|PubMed:17932957, ECO:0000269|PubMed:19122038, CC ECO:0000269|PubMed:19623537, ECO:0000269|PubMed:19932619, CC ECO:0000269|PubMed:19932620, ECO:0000269|PubMed:20227276, CC ECO:0000269|PubMed:22396310, ECO:0000269|PubMed:24135484, CC ECO:0000269|PubMed:32315611, ECO:0000269|PubMed:34744632, CC ECO:0000269|PubMed:36445308}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Lethal congenital contracture syndrome 5 (LCCS5) [MIM:615368]: CC A form of lethal congenital contracture syndrome, an autosomal CC recessive disorder characterized by degeneration of anterior horn CC neurons, extreme skeletal muscle atrophy and congenital non-progressive CC joint contractures. The contractures can involve the upper or lower CC limbs and/or the vertebral column, leading to various degrees of CC flexion or extension limitations evident at birth. CC {ECO:0000269|PubMed:23092955}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Charcot-Marie-Tooth disease, dominant intermediate B (CMTDIB) CC [MIM:606482]: A form of Charcot-Marie-Tooth disease, a disorder of the CC peripheral nervous system, characterized by progressive weakness and CC atrophy, initially of the peroneal muscles and later of the distal CC muscles of the arms. The dominant intermediate type B is characterized CC by clinical and pathologic features intermediate between demyelinating CC and axonal peripheral neuropathies, and motor median nerve conduction CC velocities ranging from 25 to 45 m/sec. {ECO:0000269|PubMed:15731758, CC ECO:0000269|PubMed:19623537}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Charcot-Marie-Tooth disease, axonal, 2M (CMT2M) [MIM:606482]: CC An axonal form of Charcot-Marie-Tooth disease, a disorder of the CC peripheral nervous system, characterized by progressive weakness and CC atrophy, initially of the peroneal muscles and later of the distal CC muscles of the arms. Charcot-Marie-Tooth disease is classified in two CC main groups on the basis of electrophysiologic properties and CC histopathology: primary peripheral demyelinating neuropathies CC (designated CMT1 when they are dominantly inherited) and primary CC peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group CC are characterized by signs of axonal degeneration in the absence of CC obvious myelin alterations, normal or slightly reduced nerve conduction CC velocities, and progressive distal muscle weakness and atrophy. CC {ECO:0000269|PubMed:17636067, ECO:0000269|PubMed:18560793}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- MISCELLANEOUS: Overexpression of CNM- and CMT-related DNM2 mutants in CC COS7 cells, whatever the mutated domain, led to a reduction in CC clathrin-mediated receptor endocytosis associated with MAPK ERK-1 and CC ERK-2 impairment. The membrane trafficking impairment process may CC represent a common pathophysiological pathway in the autosomal forms of CC CNM DNM2-CMT neuropathy. CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase CC superfamily. Dynamin/Fzo/YdjA family. {ECO:0000255|PROSITE- CC ProRule:PRU01055}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L36983; AAA88025.1; -; mRNA. DR EMBL; AK289831; BAF82520.1; -; mRNA. DR EMBL; AK312260; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AC007229; AAD23604.1; -; Genomic_DNA. DR EMBL; AC011475; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC011552; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC011554; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC112707; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC039596; AAH39596.1; -; mRNA. DR EMBL; BC054501; AAH54501.1; -; mRNA. DR CCDS; CCDS32907.1; -. [P50570-2] DR CCDS; CCDS32908.1; -. [P50570-3] DR CCDS; CCDS45968.1; -. [P50570-1] DR CCDS; CCDS45969.1; -. [P50570-4] DR CCDS; CCDS59351.1; -. [P50570-5] DR PIR; JC4305; JC4305. DR RefSeq; NP_001005360.1; NM_001005360.2. [P50570-1] DR RefSeq; NP_001005361.1; NM_001005361.2. [P50570-4] DR RefSeq; NP_001005362.1; NM_001005362.2. [P50570-3] DR RefSeq; NP_001177645.1; NM_001190716.1. [P50570-5] DR RefSeq; NP_004936.2; NM_004945.3. [P50570-2] DR PDB; 2YS1; NMR; -; A=520-625. DR PDBsum; 2YS1; -. DR AlphaFoldDB; P50570; -. DR BMRB; P50570; -. DR SMR; P50570; -. DR BioGRID; 108122; 278. DR CORUM; P50570; -. DR DIP; DIP-31244N; -. DR ELM; P50570; -. DR IntAct; P50570; 251. DR MINT; P50570; -. DR STRING; 9606.ENSP00000373905; -. DR BindingDB; P50570; -. DR ChEMBL; CHEMBL5812; -. DR MoonDB; P50570; Curated. DR TCDB; 1.R.1.1.1; the membrane contact site (mcs) family. DR TCDB; 8.A.34.1.4; the endophilin (endophilin) family. DR GlyGen; P50570; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P50570; -. DR MetOSite; P50570; -. DR PhosphoSitePlus; P50570; -. DR SwissPalm; P50570; -. DR BioMuta; DNM2; -. DR DMDM; 47117856; -. DR EPD; P50570; -. DR jPOST; P50570; -. DR MassIVE; P50570; -. DR MaxQB; P50570; -. DR PaxDb; 9606-ENSP00000373905; -. DR PeptideAtlas; P50570; -. DR ProteomicsDB; 1845; -. DR ProteomicsDB; 19939; -. DR ProteomicsDB; 56250; -. [P50570-1] DR ProteomicsDB; 56251; -. [P50570-2] DR Pumba; P50570; -. DR Antibodypedia; 25505; 300 antibodies from 34 providers. DR DNASU; 1785; -. DR Ensembl; ENST00000355667.11; ENSP00000347890.6; ENSG00000079805.19. [P50570-1] DR Ensembl; ENST00000359692.10; ENSP00000352721.6; ENSG00000079805.19. [P50570-2] DR Ensembl; ENST00000389253.9; ENSP00000373905.4; ENSG00000079805.19. [P50570-4] DR Ensembl; ENST00000408974.8; ENSP00000386192.3; ENSG00000079805.19. [P50570-3] DR Ensembl; ENST00000585892.5; ENSP00000468734.1; ENSG00000079805.19. [P50570-5] DR GeneID; 1785; -. DR KEGG; hsa:1785; -. DR MANE-Select; ENST00000389253.9; ENSP00000373905.4; NM_001005361.3; NP_001005361.1. [P50570-4] DR UCSC; uc002mps.3; human. [P50570-1] DR AGR; HGNC:2974; -. DR CTD; 1785; -. DR DisGeNET; 1785; -. DR GeneCards; DNM2; -. DR HGNC; HGNC:2974; DNM2. DR HPA; ENSG00000079805; Low tissue specificity. DR MalaCards; DNM2; -. DR MIM; 160150; phenotype. DR MIM; 602378; gene. DR MIM; 606482; phenotype. DR MIM; 615368; phenotype. DR neXtProt; NX_P50570; -. DR OpenTargets; ENSG00000079805; -. DR Orphanet; 169189; Autosomal dominant centronuclear myopathy. DR Orphanet; 228179; Autosomal dominant Charcot-Marie-Tooth disease type 2M. DR Orphanet; 100044; Autosomal dominant intermediate Charcot-Marie-Tooth disease type B. DR Orphanet; 363409; Fetal akinesia-cerebral and retinal hemorrhage syndrome. DR PharmGKB; PA27442; -. DR VEuPathDB; HostDB:ENSG00000079805; -. DR eggNOG; KOG0446; Eukaryota. DR GeneTree; ENSGT00940000155764; -. DR HOGENOM; CLU_008964_1_1_1; -. DR InParanoid; P50570; -. DR OMA; FIGFANM; -. DR OrthoDB; 1052588at2759; -. DR PhylomeDB; P50570; -. DR TreeFam; TF300362; -. DR BRENDA; 3.6.5.5; 2681. DR PathwayCommons; P50570; -. DR Reactome; R-HSA-166016; Toll Like Receptor 4 (TLR4) Cascade. DR Reactome; R-HSA-177504; Retrograde neurotrophin signalling. DR Reactome; R-HSA-190873; Gap junction degradation. DR Reactome; R-HSA-196025; Formation of annular gap junctions. DR Reactome; R-HSA-203641; NOSTRIN mediated eNOS trafficking. DR Reactome; R-HSA-2132295; MHC class II antigen presentation. DR Reactome; R-HSA-432720; Lysosome Vesicle Biogenesis. DR Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis. DR Reactome; R-HSA-437239; Recycling pathway of L1. DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis. DR Reactome; R-HSA-9031628; NGF-stimulated transcription. DR SignaLink; P50570; -. DR SIGNOR; P50570; -. DR BioGRID-ORCS; 1785; 748 hits in 1175 CRISPR screens. DR ChiTaRS; DNM2; human. DR EvolutionaryTrace; P50570; -. DR GeneWiki; DNM2; -. DR GenomeRNAi; 1785; -. DR Pharos; P50570; Tchem. DR PRO; PR:P50570; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; P50570; Protein. DR Bgee; ENSG00000079805; Expressed in metanephros cortex and 154 other cell types or tissues. DR ExpressionAtlas; P50570; baseline and differential. DR GO; GO:0005814; C:centriole; IDA:UniProtKB. DR GO; GO:0005813; C:centrosome; IDA:UniProtKB. DR GO; GO:0005905; C:clathrin-coated pit; ISS:UniProtKB. DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0005768; C:endosome; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0005874; C:microtubule; IDA:UniProtKB. DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell. DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB. DR GO; GO:0001891; C:phagocytic cup; IEA:UniProtKB-SubCell. DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0002102; C:podosome; IEA:UniProtKB-SubCell. DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB. DR GO; GO:0045211; C:postsynaptic membrane; IDA:UniProtKB. DR GO; GO:0098793; C:presynapse; IEA:GOC. DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB. DR GO; GO:0045202; C:synapse; IBA:GO_Central. DR GO; GO:0001931; C:uropod; IDA:UniProtKB. DR GO; GO:0019899; F:enzyme binding; NAS:UniProtKB. DR GO; GO:0005525; F:GTP binding; NAS:UniProtKB. DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB. DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central. DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB. DR GO; GO:0043621; F:protein self-association; ISS:UniProtKB. DR GO; GO:0017124; F:SH3 domain binding; IDA:UniProtKB. DR GO; GO:0061572; P:actin filament bundle organization; IMP:UniProtKB. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome. DR GO; GO:0006914; P:autophagy; IDA:UniProtKB. DR GO; GO:0007098; P:centrosome cycle; ISS:UniProtKB. DR GO; GO:0006897; P:endocytosis; IDA:UniProtKB. DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; NAS:UniProtKB. DR GO; GO:0061024; P:membrane organization; TAS:Reactome. DR GO; GO:0097749; P:membrane tubulation; IDA:UniProtKB. DR GO; GO:1903526; P:negative regulation of membrane tubulation; IDA:UniProtKB. DR GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB. DR GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW. DR GO; GO:0043065; P:positive regulation of apoptotic process; NAS:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; NAS:UniProtKB. DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; TAS:Reactome. DR GO; GO:0051258; P:protein polymerization; IDA:UniProtKB. DR GO; GO:0031623; P:receptor internalization; IMP:BHF-UCL. DR GO; GO:0006898; P:receptor-mediated endocytosis; IDA:UniProtKB. DR GO; GO:0030516; P:regulation of axon extension; ISS:UniProtKB. DR GO; GO:0006355; P:regulation of DNA-templated transcription; NAS:UniProtKB. DR GO; GO:0007165; P:signal transduction; NAS:UniProtKB. DR GO; GO:0043149; P:stress fiber assembly; ISS:UniProtKB. DR GO; GO:0048488; P:synaptic vesicle endocytosis; IBA:GO_Central. DR GO; GO:0048489; P:synaptic vesicle transport; NAS:UniProtKB. DR GO; GO:0033572; P:transferrin transport; IMP:BHF-UCL. DR GO; GO:0099050; P:vesicle scission; IDA:UniProtKB. DR CDD; cd08771; DLP_1; 1. DR CDD; cd01256; PH_dynamin; 1. DR Gene3D; 1.20.120.1240; Dynamin, middle domain; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR InterPro; IPR022812; Dynamin. DR InterPro; IPR001401; Dynamin_GTPase. DR InterPro; IPR019762; Dynamin_GTPase_CS. DR InterPro; IPR045063; Dynamin_N. DR InterPro; IPR000375; Dynamin_stalk. DR InterPro; IPR030381; G_DYNAMIN_dom. DR InterPro; IPR003130; GED. DR InterPro; IPR020850; GED_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR001849; PH_domain. DR PANTHER; PTHR11566; DYNAMIN; 1. DR PANTHER; PTHR11566:SF23; DYNAMIN-2; 1. DR Pfam; PF01031; Dynamin_M; 1. DR Pfam; PF00350; Dynamin_N; 1. DR Pfam; PF02212; GED; 1. DR Pfam; PF00169; PH; 1. DR PRINTS; PR00195; DYNAMIN. DR SMART; SM00053; DYNc; 1. DR SMART; SM00302; GED; 1. DR SMART; SM00233; PH; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR PROSITE; PS00410; G_DYNAMIN_1; 1. DR PROSITE; PS51718; G_DYNAMIN_2; 1. DR PROSITE; PS51388; GED; 1. DR PROSITE; PS50003; PH_DOMAIN; 1. DR Genevisible; P50570; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cell junction; KW Cell projection; Charcot-Marie-Tooth disease; Coated pit; Cytoplasm; KW Cytoplasmic vesicle; Cytoskeleton; Disease variant; Endocytosis; Endosome; KW GTP-binding; Hydrolase; Membrane; Microtubule; Motor protein; KW Neurodegeneration; Neuropathy; Nucleotide-binding; Phagocytosis; KW Phosphoprotein; Reference proteome; Synapse; Synaptosome. FT CHAIN 1..870 FT /note="Dynamin-2" FT /id="PRO_0000206570" FT DOMAIN 28..294 FT /note="Dynamin-type G" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055" FT DOMAIN 519..625 FT /note="PH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145" FT DOMAIN 653..744 FT /note="GED" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00720" FT REGION 38..45 FT /note="G1 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055" FT REGION 64..66 FT /note="G2 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055" FT REGION 136..139 FT /note="G3 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055" FT REGION 205..208 FT /note="G4 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055" FT REGION 235..238 FT /note="G5 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055" FT REGION 741..870 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 755..770 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 771..796 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 828..859 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 41 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0000250|UniProtKB:Q05193" FT BINDING 43 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0000250|UniProtKB:Q05193" FT BINDING 44 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0000250|UniProtKB:Q05193" FT BINDING 45 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0000250|UniProtKB:Q05193" FT BINDING 46 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0000250|UniProtKB:Q05193" FT BINDING 59 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0000250|UniProtKB:Q05193" FT BINDING 60 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0000250|UniProtKB:Q05193" FT BINDING 206 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0000250|UniProtKB:Q05193" FT BINDING 208 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0000250|UniProtKB:Q05193" FT BINDING 211 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0000250|UniProtKB:Q05193" FT BINDING 236 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0000250|UniProtKB:Q05193" FT BINDING 237 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0000250|UniProtKB:Q05193" FT BINDING 239 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0000250|UniProtKB:Q05193" FT MOD_RES 231 FT /note="Phosphotyrosine; by SRC" FT /evidence="ECO:0000250|UniProtKB:P39052, FT ECO:0000305|PubMed:34744632" FT MOD_RES 299 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P39054" FT MOD_RES 597 FT /note="Phosphotyrosine; by SRC" FT /evidence="ECO:0000250|UniProtKB:P39052, FT ECO:0000305|PubMed:34744632" FT MOD_RES 598 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 755 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 764 FT /note="Phosphoserine; by CDK1" FT /evidence="ECO:0000250|UniProtKB:P39052" FT MOD_RES 848 FT /note="Phosphoserine; by GSK3-alpha" FT /evidence="ECO:0000269|PubMed:36445308" FT VAR_SEQ 407..444 FT /note="LAFEAIVKKQVVKLKEPCLKCVDLVIQELINTVRQCTS -> MAFEAIVKKQ FT IVKLKEPSLKCVDLVVSELATVIKKCAE (in isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_044280" FT VAR_SEQ 516..519 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:7590285" FT /id="VSP_001325" FT VAR_SEQ 848 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_047534" FT VARIANT 263 FT /note="P -> L (in dbSNP:rs3745674)" FT /id="VAR_031961" FT VARIANT 358 FT /note="G -> R (in CMT2M; dbSNP:rs267606772)" FT /evidence="ECO:0000269|PubMed:18560793" FT /id="VAR_068425" FT VARIANT 368 FT /note="E -> K (in CNM1; dbSNP:rs121909092)" FT /evidence="ECO:0000269|PubMed:16227997, FT ECO:0000269|PubMed:20227276" FT /id="VAR_031962" FT VARIANT 368 FT /note="E -> Q (in CNM1)" FT /evidence="ECO:0000269|PubMed:17825552" FT /id="VAR_068365" FT VARIANT 369 FT /note="R -> Q (in CNM1; dbSNP:rs121909089)" FT /evidence="ECO:0000269|PubMed:16227997" FT /id="VAR_031963" FT VARIANT 369 FT /note="R -> W (in CNM1; reduced association with the FT centrosome; dbSNP:rs121909090)" FT /evidence="ECO:0000269|PubMed:16227997" FT /id="VAR_031964" FT VARIANT 379 FT /note="F -> V (in LCCS5; hypomorphic mutation impacting on FT endocytosis; dbSNP:rs397514735)" FT /evidence="ECO:0000269|PubMed:23092955" FT /id="VAR_070163" FT VARIANT 465 FT /note="R -> W (in CNM1; reduced association with the FT centrosome; COS7 cells show a reduced uptake of transferrin FT and low-density lipoprotein complex; decreases FT autophagosome maturation; does not affect endocytosis; does FT not affect the trafficking of ATG9A and ATG16L1; does not FT affect SNX18 interaction; increases cell membrane FT localization; increases interaction with ITSN1; impairs FT recruitment to phagophore assembly site; increases FT GTPase-mediated membrane fission; inhibits GTPase-mediated FT membrane fission by BIN1 in a dose-dependent manner; FT dbSNP:rs121909091)" FT /evidence="ECO:0000269|PubMed:16227997, FT ECO:0000269|PubMed:19623537, ECO:0000269|PubMed:20227276, FT ECO:0000269|PubMed:32315611, ECO:0000269|PubMed:36445308" FT /id="VAR_031965" FT VARIANT 522 FT /note="R -> C (in CNM1; dbSNP:rs2072577342)" FT /evidence="ECO:0000269|PubMed:22396310" FT /id="VAR_068366" FT VARIANT 522 FT /note="R -> H (in CNM1; dbSNP:rs587783595)" FT /evidence="ECO:0000269|PubMed:20227276" FT /id="VAR_068367" FT VARIANT 523 FT /note="R -> G (in CNM1; dbSNP:rs587783596)" FT /evidence="ECO:0000269|PubMed:22396310" FT /id="VAR_068368" FT VARIANT 537 FT /note="G -> C (in CMT2M; dbSNP:rs121909093)" FT /evidence="ECO:0000269|PubMed:17636067" FT /id="VAR_062574" FT VARIANT 555..557 FT /note="Missing (in CMTDIB and CNM1; may affect binding to FT vesicles and membranes in favor of binding to microtubules; FT may affect receptor-mediated endocytosis; does not affect FT binding to vesicles composed of FT 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate, stabilizes FT polymers; increases GTPase activity; becomes resistant to FT disassembly; does not induce the formation of high-order FT oligomers; increases tyrosine phosphorylation)" FT /evidence="ECO:0000269|PubMed:15731758, FT ECO:0000269|PubMed:34744632" FT /id="VAR_031966" FT VARIANT 560 FT /note="E -> K (in CNM1; dbSNP:rs879254086)" FT /evidence="ECO:0000269|PubMed:19122038" FT /id="VAR_068369" FT VARIANT 562 FT /note="K -> E (in CMTDIB and CNM1; with neutropenia; COS7 FT cells show a reduced uptake of transferrin and low-density FT lipoprotein complex; impairs PHD domain binding to vesicles FT composed of 1-phosphatidyl-1D-myo-inositol FT 4,5-bisphosphate; does not affect GTP- and salt-induced FT disassembly; does not induce the formation of high-order FT oligomers; does not affect phosphorylation; FT dbSNP:rs121909088)" FT /evidence="ECO:0000269|PubMed:15731758, FT ECO:0000269|PubMed:19623537, ECO:0000269|PubMed:34744632" FT /id="VAR_031967" FT VARIANT 562 FT /note="Missing (in CMTDIB; dbSNP:rs1599620408)" FT /evidence="ECO:0000269|PubMed:15731758" FT /id="VAR_070164" FT VARIANT 570 FT /note="L -> H (in CMT2M; dbSNP:rs121909094)" FT /evidence="ECO:0000269|PubMed:17636067" FT /id="VAR_062575" FT VARIANT 618 FT /note="A -> D (in CNM1; dbSNP:rs1555715869)" FT /evidence="ECO:0000269|PubMed:19932619" FT /id="VAR_068370" FT VARIANT 618 FT /note="A -> T (in CNM1; severe; does not affect PHD domain FT binding to vesicles composed of and FT 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate; induces FT the formation of high-order oligomers; does not affect FT phosphorylation; increases GTPase-mediated membrane FT fission; inhibits GTPase-mediated membrane fission by BIN1 FT in a dose-dependent manner; dbSNP:rs773598203)" FT /evidence="ECO:0000269|PubMed:17932957, FT ECO:0000269|PubMed:20227276, ECO:0000269|PubMed:34744632, FT ECO:0000269|PubMed:36445308" FT /id="VAR_039041" FT VARIANT 619 FT /note="S -> L (in CNM1; severe; impairs BIN1-dependent FT T-tubule formation, zebrafish larval muscle show alteration FT of T-tubule organization; increases GTPase-mediated FT membrane fission; inhibits GTPase-mediated membrane fission FT by BIN1 in a dose-dependent manner; dbSNP:rs121909095)" FT /evidence="ECO:0000269|PubMed:17932957, FT ECO:0000269|PubMed:20227276, ECO:0000269|PubMed:24135484, FT ECO:0000269|PubMed:36445308" FT /id="VAR_039042" FT VARIANT 619 FT /note="S -> W (in CNM1; severe; dbSNP:rs121909095)" FT /evidence="ECO:0000269|PubMed:17932957" FT /id="VAR_039043" FT VARIANT 621 FT /note="L -> P (in CNM1; centronuclear myopathy with FT cataracts; dbSNP:rs587783597)" FT /evidence="ECO:0000269|PubMed:19932620" FT /id="VAR_068371" FT VARIANT 625 FT /note="Missing (in CNM1; severe; COS7 cells show a reduced FT uptake of transferrin and low-density lipoprotein complex; FT increases GTPase-mediated membrane fission; inhibits FT GTPase-mediated membrane fission by BIN1 in a FT dose-dependent manner)" FT /evidence="ECO:0000269|PubMed:17932957, FT ECO:0000269|PubMed:19623537, ECO:0000269|PubMed:36445308" FT /id="VAR_039044" FT VARIANT 627 FT /note="P -> H (in CNM1)" FT /evidence="ECO:0000269|PubMed:20227276" FT /id="VAR_068372" FT VARIANT 627 FT /note="P -> R (in CNM1; dbSNP:rs587783598)" FT /evidence="ECO:0000269|PubMed:22396310" FT /id="VAR_068373" FT VARIANT 650 FT /note="E -> K (in CNM1; COS7 cells show a reduced uptake of FT transferrin and low-density lipoprotein complex)" FT /evidence="ECO:0000269|PubMed:19623537" FT /id="VAR_062576" FT MUTAGEN 44 FT /note="K->A: Inhibits receptor-mediated endocytosis. FT Inhibits EGF-induced MAPK3 and MAPK1 activation." FT /evidence="ECO:0000269|PubMed:19623537" FT MUTAGEN 231 FT /note="Y->F: Greatly reduces tyrosine phosphorylation; when FT associated with F-597." FT /evidence="ECO:0000269|PubMed:34744632" FT MUTAGEN 525 FT /note="W->L: Abolishes interaction with MAP1LC3B. Does not FT affect interaction with ITSN1. Affects nascent FT autophagosome membranes. Does not affect the trafficking of FT ATG9A and ATG16L1. Does not affect SNX18 interaction. FT Decreases autophagosome maturation." FT /evidence="ECO:0000269|PubMed:32315611" FT MUTAGEN 597 FT /note="Y->F: Greatly reduces tyrosine phosphorylation; when FT associated with F-231." FT /evidence="ECO:0000269|PubMed:34744632" FT MUTAGEN 848 FT /note="S->A: Decreases receptor internalization." FT /evidence="ECO:0000269|PubMed:36445308" FT MUTAGEN 848 FT /note="S->E: Decreases binding affinity to BIN1. Increases FT GTPase mediated-membrane fission activity by BIN1. FT Decreases cell surface expression of SLC2A4." FT /evidence="ECO:0000269|PubMed:36445308" FT CONFLICT 155..156 FT /note="QI -> RV (in Ref. 1; AAA88025)" FT /evidence="ECO:0000305" FT CONFLICT 207 FT /note="L -> P (in Ref. 2; AK312260)" FT /evidence="ECO:0000305" FT CONFLICT 316 FT /note="N -> I (in Ref. 1; AAA88025)" FT /evidence="ECO:0000305" FT CONFLICT 324 FT /note="R -> P (in Ref. 1; AAA88025)" FT /evidence="ECO:0000305" FT CONFLICT 475 FT /note="I -> T (in Ref. 2; AK312260)" FT /evidence="ECO:0000305" FT STRAND 522..530 FT /evidence="ECO:0007829|PDB:2YS1" FT STRAND 533..535 FT /evidence="ECO:0007829|PDB:2YS1" FT STRAND 540..545 FT /evidence="ECO:0007829|PDB:2YS1" FT STRAND 550..555 FT /evidence="ECO:0007829|PDB:2YS1" FT STRAND 560..565 FT /evidence="ECO:0007829|PDB:2YS1" FT STRAND 567..573 FT /evidence="ECO:0007829|PDB:2YS1" FT STRAND 585..590 FT /evidence="ECO:0007829|PDB:2YS1" FT STRAND 596..599 FT /evidence="ECO:0007829|PDB:2YS1" FT STRAND 601..606 FT /evidence="ECO:0007829|PDB:2YS1" FT HELIX 610..623 FT /evidence="ECO:0007829|PDB:2YS1" SQ SEQUENCE 870 AA; 98064 MW; 2F4567B75980935D CRC64; MGNRGMEELI PLVNKLQDAF SSIGQSCHLD LPQIAVVGGQ SAGKSSVLEN FVGRDFLPRG SGIVTRRPLI LQLIFSKTEH AEFLHCKSKK FTDFDEVRQE IEAETDRVTG TNKGISPVPI NLRVYSPHVL NLTLIDLPGI TKVPVGDQPP DIEYQIKDMI LQFISRESSL ILAVTPANMD LANSDALKLA KEVDPQGLRT IGVITKLDLM DEGTDARDVL ENKLLPLRRG YIGVVNRSQK DIEGKKDIRA ALAAERKFFL SHPAYRHMAD RMGTPHLQKT LNQQLTNHIR ESLPALRSKL QSQLLSLEKE VEEYKNFRPD DPTRKTKALL QMVQQFGVDF EKRIEGSGDQ VDTLELSGGA RINRIFHERF PFELVKMEFD EKDLRREISY AIKNIHGVRT GLFTPDLAFE AIVKKQVVKL KEPCLKCVDL VIQELINTVR QCTSKLSSYP RLREETERIV TTYIREREGR TKDQILLLID IEQSYINTNH EDFIGFANAQ QRSTQLNKKR AIPNQGEILV IRRGWLTINN ISLMKGGSKE YWFVLTAESL SWYKDEEEKE KKYMLPLDNL KIRDVEKGFM SNKHVFAIFN TEQRNVYKDL RQIELACDSQ EDVDSWKASF LRAGVYPEKD QAENEDGAQE NTFSMDPQLE RQVETIRNLV DSYVAIINKS IRDLMPKTIM HLMINNTKAF IHHELLAYLY SSADQSSLME ESADQAQRRD DMLRMYHALK EALNIIGDIS TSTVSTPVPP PVDDTWLQSA SSHSPTPQRR PVSSIHPPGR PPAVRGPTPG PPLIPVPVGA AASFSAPPIP SRPGPQSVFA NSDLFPAPPQ IPSRPVRIPP GIPPGVPSRR PPAAPSRPTI IRPAEPSLLD //