ID DNM1L_HUMAN Reviewed; 736 AA. AC O00429; A8K4X9; B4DGC9; B4DSU8; J3KPI2; O14541; O60709; Q59GN9; AC Q7L6B3; Q8TBT7; Q9BWM1; Q9Y5J2; DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 2. DT 24-JUN-2015, entry version 136. DE RecName: Full=Dynamin-1-like protein; DE EC=3.6.5.5; DE AltName: Full=Dnm1p/Vps1p-like protein; DE Short=DVLP; DE AltName: Full=Dynamin family member proline-rich carboxyl-terminal domain less; DE Short=Dymple; DE AltName: Full=Dynamin-like protein; DE AltName: Full=Dynamin-like protein 4; DE AltName: Full=Dynamin-like protein IV; DE Short=HdynIV; DE AltName: Full=Dynamin-related protein 1; GN Name=DNM1L; Synonyms=DLP1, DRP1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION. RC TISSUE=Hepatoma; RX PubMed=9348079; DOI=10.1093/oxfordjournals.jbchem.a021784; RA Shin H.-W., Shinotsuka C., Torii S., Murakami K., Nakayama K.; RT "Identification and subcellular localization of a novel mammalian RT dynamin-related protein homologous to yeast Vps1p and Dnm1p."; RL J. Biochem. 122:525-530(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), VARIANT THR-71, TISSUE RP SPECIFICITY, AND INTERACTION WITH GSK3B. RC TISSUE=Liver; RX PubMed=9731200; DOI=10.1006/bbrc.1998.9253; RA Hong Y.-R., Chen C.-H., Cheng D.-S., Howng S.-L., Chow C.-C.; RT "Human dynamin-like protein interacts with the glycogen synthase RT kinase 3beta."; RL Biochem. Biophys. Res. Commun. 249:697-703(1998). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT THR-71, TISSUE RP SPECIFICITY, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-38, AND RP FUNCTION. RC TISSUE=Brain; RX PubMed=9570752; RA Imoto M., Tachibana I., Urrutia R.; RT "Identification and functional characterization of a novel human RT protein highly related to the yeast dynamin-like GTPase Vps1p."; RL J. Cell Sci. 111:1341-1349(1998). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3; 4 AND 5), VARIANT THR-71, RP TISSUE SPECIFICITY, AND INTERACTION WITH GSK3B. RC TISSUE=Brain; RX PubMed=10749171; DOI=10.1089/104454900314573; RA Chen C.-H., Howng S.-L., Hwang S.-L., Chou C.-K., Liao C.-H., RA Hong Y.-R.; RT "Differential expression of four human dynamin-like protein variants RT in brain tumors."; RL DNA Cell Biol. 19:189-194(2000). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 6 AND 7). RC TISSUE=Amygdala, 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8). RC TISSUE=Brain; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno R.F.; RT "Homo sapiens protein coding cDNA."; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., RA Kucherlapati R., Weinstock G., Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 27-736 (ISOFORM 1). RC TISSUE=Lung; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP MUTAGENESIS OF SER-39, TISSUE SPECIFICITY, CATALYTIC ACTIVITY, AND RP SUBCELLULAR LOCATION. RX PubMed=9422767; DOI=10.1074/jbc.273.2.1044; RA Kamimoto T., Nagai Y., Onogi H., Muro Y., Wakabayashi T., Hagiwara M.; RT "Dymple, a novel dynamin-like high molecular weight GTPase lacking a RT proline-rich carboxyl-terminal domain in mammalian cells."; RL J. Biol. Chem. 273:1044-1051(1998). RN [10] RP SUBCELLULAR LOCATION. RX PubMed=9472031; DOI=10.1083/jcb.140.4.779; RA Yoon Y., Pitts K.R., Dahan S., McNiven M.A.; RT "A novel dynamin-like protein associates with cytoplasmic vesicles and RT tubules of the endoplasmic reticulum in mammalian cells."; RL J. Cell Biol. 140:779-793(1998). RN [11] RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND FUNCTION. RX PubMed=9786947; DOI=10.1083/jcb.143.2.351; RA Smirnova E., Shurland D.-L., Ryazantsev S.N., van der Bliek A.M.; RT "A human dynamin-related protein controls the distribution of RT mitochondria."; RL J. Cell Biol. 143:351-358(1998). RN [12] RP OLIGOMERIZATION. RX PubMed=9915810; DOI=10.1074/jbc.274.5.2780; RA Shin H.-W., Takatsu H., Mukai H., Munekata E., Murakami K., RA Nakayama K.; RT "Intermolecular and interdomain interactions of a dynamin-related GTP- RT binding protein, Dnm1p/Vps1p-like protein."; RL J. Biol. Chem. 274:2780-2785(1999). RN [13] RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-38; VAL-41; THR-59 RP AND GLY-281, AND OLIGOMERIZATION. RX PubMed=11514614; DOI=10.1091/mbc.12.8.2245; RA Smirnova E., Griparic L., Shurland D.-L., van der Bliek A.M.; RT "Dynamin-related protein Drp1 is required for mitochondrial division RT in mammalian cells."; RL Mol. Biol. Cell 12:2245-2256(2001). RN [14] RP MUTAGENESIS OF LYS-38, SUBCELLULAR LOCATION, AND FUNCTION. RX PubMed=12499366; DOI=10.1074/jbc.M211761200; RA Koch A., Thiemann M., Grabenbauer M., Yoon Y., McNiven M.A., RA Schrader M.; RT "Dynamin-like protein 1 is involved in peroxisomal fission."; RL J. Biol. Chem. 278:8597-8605(2003). RN [15] RP MUTAGENESIS OF SER-39 AND THR-59, FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=12618434; DOI=10.1074/jbc.M212031200; RA Li X., Gould S.J.; RT "The dynamin-like GTPase DLP1 is essential for peroxisome division and RT is recruited to peroxisomes in part by PEX11."; RL J. Biol. Chem. 278:17012-17020(2003). RN [16] RP FUNCTION OF STRUCTURAL DOMAINS, OLIGOMERIZATION, SUBCELLULAR LOCATION, RP AND MUTAGENESIS OF LYS-38 AND LYS-679. RX PubMed=15208300; DOI=10.1074/jbc.M404105200; RA Zhu P.P., Patterson A., Stadler J., Seeburg D.P., Sheng M., RA Blackstone C.; RT "Intra- and intermolecular domain interactions of the C-terminal RT GTPase effector domain of the multimeric dynamin-like GTPase Drp1."; RL J. Biol. Chem. 279:35967-35974(2004). RN [17] RP UBIQUITINATION BY MARCH5, AND INTERACTION WITH MARCH5. RX PubMed=16874301; DOI=10.1038/sj.emboj.7601249; RA Yonashiro R., Ishido S., Kyo S., Fukuda T., Goto E., Matsuki Y., RA Ohmura-Hoshino M., Sada K., Hotta H., Yamamura H., Inatome R., RA Yanagi S.; RT "A novel mitochondrial ubiquitin ligase plays a critical role in RT mitochondrial dynamics."; RL EMBO J. 25:3618-3626(2006). RN [18] RP UBIQUITINATION BY MARCH5, AND INTERACTION WITH MARCH5. RX PubMed=16936636; DOI=10.1038/sj.embor.7400790; RA Nakamura N., Kimura Y., Tokuda M., Honda S., Hirose S.; RT "MARCH-V is a novel mitofusin 2- and Drp1-binding protein able to RT change mitochondrial morphology."; RL EMBO Rep. 7:1019-1022(2006). RN [19] RP FUNCTION. RX PubMed=17015472; DOI=10.1128/MCB.02282-05; RA Parone P.A., James D.I., Da Cruz S., Mattenberger Y., Donze O., RA Barja F., Martinou J.C.; RT "Inhibiting the mitochondrial fission machinery does not prevent RT Bax/Bak-dependent apoptosis."; RL Mol. Cell. Biol. 26:7397-7408(2006). RN [20] RP PHOSPHORYLATION, AND FUNCTION. RX PubMed=17301055; DOI=10.1074/jbc.M607279200; RA Taguchi N., Ishihara N., Jofuku A., Oka T., Mihara K.; RT "Mitotic phosphorylation of dynamin-related GTPase Drp1 participates RT in mitochondrial fission."; RL J. Biol. Chem. 282:11521-11529(2007). RN [21] RP PHOSPHORYLATION AT SER-637, FUNCTION, SUBUNIT, AND MUTAGENESIS OF RP SER-637. RX PubMed=17553808; DOI=10.1074/jbc.C700083200; RA Chang C.R., Blackstone C.; RT "Cyclic AMP-dependent protein kinase phosphorylation of Drp1 regulates RT its GTPase activity and mitochondrial morphology."; RL J. Biol. Chem. 282:21583-21587(2007). RN [22] RP SUBCELLULAR LOCATION. RX PubMed=17606867; DOI=10.1083/jcb.200611064; RA Karbowski M., Neutzner A., Youle R.J.; RT "The mitochondrial E3 ubiquitin ligase MARCH5 is required for Drp1 RT dependent mitochondrial division."; RL J. Cell Biol. 178:71-84(2007). RN [23] RP FUNCTION, VARIANT EMPF ASP-395, AND CHARACTERIZATION OF VARIANT EMPF RP ASP-395. RX PubMed=17460227; DOI=10.1056/NEJMoa064436; RA Waterham H.R., Koster J., van Roermund C.W., Mooyer P.A., RA Wanders R.J., Leonard J.V.; RT "A lethal defect of mitochondrial and peroxisomal fission."; RL N. Engl. J. Med. 356:1736-1741(2007). RN [24] RP PHOSPHORYLATION AT SER-637, FUNCTION, INTERACTION WITH FIS1, AND RP MUTAGENESIS OF SER-637. RX PubMed=18695047; DOI=10.1083/jcb.200802164; RA Han X.J., Lu Y.F., Li S.A., Kaitsuka T., Sato Y., Tomizawa K., RA Nairn A.C., Takei K., Matsui H., Matsushita M.; RT "CaM kinase I alpha-induced phosphorylation of Drp1 regulates RT mitochondrial morphology."; RL J. Cell Biol. 182:573-585(2008). RN [25] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-616, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [26] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-548; SER-607 AND RP SER-616, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [27] RP PHOSPHORYLATION AT SER-616 AND SER-637, INTERACTION WITH PPP3CA, RP DEPHOSPHORYLATION, FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF RP SER-616 AND SER-637. RX PubMed=18838687; DOI=10.1073/pnas.0808249105; RA Cereghetti G.M., Stangherlin A., Martins de Brito O., Chang C.R., RA Blackstone C., Bernardi P., Scorrano L.; RT "Dephosphorylation by calcineurin regulates translocation of Drp1 to RT mitochondria."; RL Proc. Natl. Acad. Sci. U.S.A. 105:15803-15808(2008). RN [28] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [29] RP SUMOYLATION BY MUL1. RX PubMed=19407830; DOI=10.1038/embor.2009.86; RA Braschi E., Zunino R., McBride H.M.; RT "MAPL is a new mitochondrial SUMO E3 ligase that regulates RT mitochondrial fission."; RL EMBO Rep. 10:748-754(2009). RN [30] RP SUMOYLATION AT LYS-532; LYS-535; LYS-558; LYS-568; LYS-594; LYS-597; RP LYS-606 AND LYS-608, INTERACTION WITH UBE2I, FUNCTION, AND MUTAGENESIS RP OF LYS-38; LYS-532; LYS-535; LYS-558; LYS-568; LYS-594; LYS-597; RP LYS-606 AND LYS-608. RX PubMed=19638400; DOI=10.1096/fj.09-136630; RA Figueroa-Romero C., Iniguez-Lluhi J.A., Stadler J., Chang C.R., RA Arnoult D., Keller P.J., Hong Y., Blackstone C., Feldman E.L.; RT "SUMOylation of the mitochondrial fission protein Drp1 occurs at RT multiple nonconsensus sites within the B domain and is linked to its RT activity cycle."; RL FASEB J. 23:3917-3927(2009). RN [31] RP SUMOYLATION, DESUMOYLATION, AND FUNCTION. RX PubMed=19411255; DOI=10.1074/jbc.M901902200; RA Zunino R., Braschi E., Xu L., McBride H.M.; RT "Translocation of SenP5 from the nucleoli to the mitochondria RT modulates DRP1-dependent fission during mitosis."; RL J. Biol. Chem. 284:17783-17795(2009). RN [32] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-616, AND IDENTIFICATION RP 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 [33] RP S-NITROSYLATION AT CYS-644, FUNCTION, ASSOCIATION WITH ALZHEIMER RP DISEASE, AND MUTAGENESIS OF CYS-300; CYS-345; CYS-361; CYS-367; RP CYS-431; CYS-446; CYS-470; CYS-505 AND CYS-644. RX PubMed=19342591; DOI=10.1126/science.1171091; RA Cho D.H., Nakamura T., Fang J., Cieplak P., Godzik A., Gu Z., RA Lipton S.A.; RT "S-nitrosylation of Drp1 mediates beta-amyloid-related mitochondrial RT fission and neuronal injury."; RL Science 324:102-105(2009). RN [34] RP POSSIBLE FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=20688057; DOI=10.1016/j.yexcr.2010.07.020; RA Bonekamp N.A., Vormund K., Jacob R., Schrader M.; RT "Dynamin-like protein 1 at the Golgi complex: A novel component of the RT sorting/targeting machinery en route to the plasma membrane."; RL Exp. Cell Res. 316:3454-3467(2010). RN [35] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-616, AND IDENTIFICATION RP 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., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [36] 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., RA Buerckstuemmer T., 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 [37] RP INTERACTION WITH MIEF2 AND MIEF1. RX PubMed=21508961; DOI=10.1038/embor.2011.54; RA Palmer C.S., Osellame L.D., Laine D., Koutsopoulos O.S., Frazier A.E., RA Ryan M.T.; RT "MiD49 and MiD51, new components of the mitochondrial fission RT machinery."; RL EMBO Rep. 12:565-573(2011). RN [38] RP INTERACTION WITH MIEF1. RX PubMed=21701560; DOI=10.1038/emboj.2011.198; RA Zhao J., Liu T., Jin S., Wang X., Qu M., Uhlen P., Tomilin N., RA Shupliakov O., Lendahl U., Nister M.; RT "Human MIEF1 recruits Drp1 to mitochondrial outer membranes and RT promotes mitochondrial fusion rather than fission."; RL EMBO J. 30:2762-2778(2011). RN [39] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-616, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [40] RP INTERACTION WITH PGAM5, AND SUBCELLULAR LOCATION. RX PubMed=22265414; DOI=10.1016/j.cell.2011.11.030; RA Wang Z., Jiang H., Chen S., Du F., Wang X.; RT "The mitochondrial phosphatase PGAM5 functions at the convergence RT point of multiple necrotic death pathways."; RL Cell 148:228-243(2012). RN [41] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.M111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., RA Meinnel T., Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [42] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=23921378; DOI=10.1074/jbc.M113.479873; RA Palmer C.S., Elgass K.D., Parton R.G., Osellame L.D., Stojanovski D., RA Ryan M.T.; RT "MiD49 and MiD51 can act independently of Mff and Fis1 in Drp1 RT recruitment and are specific for mitochondrial fission."; RL J. Biol. Chem. 288:27584-27593(2013). RN [43] RP FUNCTION, INTERACTION WITH MIEF2 AND MIEF1, PHOSPHORYLATION AT RP SER-637, AND MUTAGENESIS OF SER-637. RX PubMed=23283981; DOI=10.1091/mbc.E12-10-0721; RA Loson O.C., Song Z., Chen H., Chan D.C.; RT "Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial RT fission."; RL Mol. Biol. Cell 24:659-667(2013). RN [44] RP INTERACTION WITH BCL2L1. RX PubMed=23792689; DOI=10.1038/ncb2791; RA Li H., Alavian K.N., Lazrove E., Mehta N., Jones A., Zhang P., RA Licznerski P., Graham M., Uo T., Guo J., Rahner C., Duman R.S., RA Morrison R.S., Jonas E.A.; RT "A Bcl-xL-Drp1 complex regulates synaptic vesicle membrane dynamics RT during endocytosis."; RL Nat. Cell Biol. 15:773-785(2013). RN [45] RP FUNCTION, INTERACTION WITH MIEF2, AND SUBUNIT. RX PubMed=23530241; DOI=10.1073/pnas.1300855110; RA Koirala S., Guo Q., Kalia R., Bui H.T., Eckert D.M., Frost A., RA Shaw J.M.; RT "Interchangeable adaptors regulate mitochondrial dynamin assembly for RT membrane scission."; RL Proc. Natl. Acad. Sci. U.S.A. 110:E1342-E1351(2013). RN [46] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-616, AND IDENTIFICATION RP BY 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [47] RP X-RAY CRYSTALLOGRAPHY (3.48 ANGSTROMS), FUNCTION, SUBUNIT, SUBCELLULAR RP LOCATION, MUTAGENESIS OF 401-GLY--PRO-404; GLU-490 AND LYS-668, AND RP LIPID-BINDING. RX PubMed=23584531; DOI=10.1038/emboj.2013.74; RA Frohlich C., Grabiger S., Schwefel D., Faelber K., Rosenbaum E., RA Mears J., Rocks O., Daumke O.; RT "Structural insights into oligomerization and mitochondrial RT remodelling of dynamin 1-like protein."; RL EMBO J. 32:1280-1292(2013). RN [48] RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-327 AND 711-736 IN COMPLEX RP WITH GTP ANALOGS, CATALYTIC ACTIVITY, MUTAGENESIS OF GLN-34; LYS-38; RP SER-39; THR-59; ASP-146; GLY-149; LYS-216 AND ASP-218, ENZYME RP REGULATION, AND SUBUNIT. RX PubMed=23977156; DOI=10.1371/journal.pone.0071835; RA Wenger J., Klinglmayr E., Frohlich C., Eibl C., Gimeno A., RA Hessenberger M., Puehringer S., Daumke O., Goettig P.; RT "Functional mapping of human dynamin-1-like GTPase domain based on x- RT ray structure analyses."; RL PLoS ONE 8:E71835-E71835(2013). CC -!- FUNCTION: Functions in mitochondrial and peroxisomal division. CC Mediates membrane fission through oligomerization into membrane- CC associated tubular structures that wrap around the scission site CC to constrict and sever the mitochondrial membrane through a GTP CC hydrolysis-dependent mechanism. Through its function in CC mitochondrial division, ensures the survival of at least some CC types of postmitotic neurons, including Purkinje cells, by CC suppressing oxidative damage. Required for normal brain CC development, including that of cerebellum. Facilitates CC developmentally regulated apoptosis during neural tube formation. CC Required for a normal rate of cytochrome c release and caspase CC activation during apoptosis; this requirement may depend upon the CC cell type and the physiological apoptotic cues. Also required for CC mitochondrial fission during mitosis. Required for formation of CC endocytic vesicles. Proposed to regulate synaptic vesicle membrane CC dynamics through association with BCL2L1 isoform Bcl-X(L) which CC stimulates its GTPase activity in synaptic vesicles; the function CC may require its recruitment by MFF to clathrin-containing CC vesicles. Required for programmed necrosis execution. CC -!- FUNCTION: Isoform 1 and isoform 4 inhibit peroxisomal division CC when overexpressed. CC -!- CATALYTIC ACTIVITY: GTP + H(2)O = GDP + phosphate. CC {ECO:0000269|PubMed:23977156, ECO:0000269|PubMed:9422767}. CC -!- ENZYME REGULATION: GTPase activity is increased by binding to CC phospholipid membranes. {ECO:0000269|PubMed:23977156}. CC -!- SUBUNIT: Homotetramer; dimerizes through the N-terminal GTP-middle CC region of one molecule binding to the GED domain of another DNM1L CC molecule. Oligomerizes in a GTP-dependent manner to form membrane- CC associated tubules with a spiral pattern. Can also oligomerize to CC form multimeric ring-like structures. Interacts with GSK3B and CC MARCH5. Interacts (via the GTPase and B domains) with UBE2I; the CC interaction promotes sumoylation of DNM1L, mainly in its B domain. CC Interacts with PPP3CA; the interaction dephosphorylates DNM1L and CC regulates its transition to mitochondria. Interacts with BCL2L1 CC isoform BCL-X(L) and CLTA; DNM1L and BCL2L1 isoform BCL-X(L) may CC form a complex in synaptic vesicles that also contains clathrin CC and MFF. Interacts with FIS1. Interacts with MIEF2 and MIEF1; this CC regulates GTP hydrolysis and DNM1L oligomerization. Interacts with CC PGAM5; this interaction leads to dephosphorylation at Ser-656 and CC activation of GTPase activity and eventually to mitochondria CC fragmentation. {ECO:0000269|PubMed:10749171, CC ECO:0000269|PubMed:16874301, ECO:0000269|PubMed:16936636, CC ECO:0000269|PubMed:17553808, ECO:0000269|PubMed:18695047, CC ECO:0000269|PubMed:18838687, ECO:0000269|PubMed:19638400, CC ECO:0000269|PubMed:21508961, ECO:0000269|PubMed:21701560, CC ECO:0000269|PubMed:22265414, ECO:0000269|PubMed:23283981, CC ECO:0000269|PubMed:23530241, ECO:0000269|PubMed:23584531, CC ECO:0000269|PubMed:23792689, ECO:0000269|PubMed:23977156, CC ECO:0000269|PubMed:9731200}. CC -!- INTERACTION: CC P03372:ESR1; NbExp=2; IntAct=EBI-724571, EBI-78473; CC Q5S007:LRRK2; NbExp=11; IntAct=EBI-724571, EBI-5323863; CC Q9NQG6:MIEF1; NbExp=9; IntAct=EBI-724571, EBI-740987; CC Q96C03:MIEF2; NbExp=3; IntAct=EBI-724571, EBI-750153; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Golgi apparatus. CC Endomembrane system; Peripheral membrane protein. Mitochondrion CC outer membrane; Peripheral membrane protein. Peroxisome. Membrane, CC clathrin-coated pit {ECO:0000250}. Cytoplasmic vesicle, secretory CC vesicle, synaptic vesicle membrane {ECO:0000250}. Note=Mainly CC cytosolic. Translocated to the mitochondrial membrane through O- CC GlcNAcylation and interaction with FIS1. Recruited to the CC mitochondrial outer membrane by interaction with MIEF1. CC Colocalized with MARCH5 at mitochondrial membrane. Localizes to CC mitochondria at sites of division. Localizes to mitochondria CC following necrosis induction. Associated with peroxisomal CC membranes, partly recruited there by PEX11B. May also be CC associated with endoplasmic reticulum tubules and cytoplasmic CC vesicles and found to be perinuclear. In some cell types, CC localizes to the Golgi complex. Binds to phospholipid membranes. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=8; CC Name=1; Synonyms=HdynIV-WT, DLP1F; CC IsoId=O00429-1; Sequence=Displayed; CC Name=4; Synonyms=HdynIV-11, DLP1c; CC IsoId=O00429-2; Sequence=VSP_013688; CC Name=2; Synonyms=DLP1a; CC IsoId=O00429-3; Sequence=VSP_013686; CC Name=3; Synonyms=HdynIV-37, DLP1b; CC IsoId=O00429-4; Sequence=VSP_013685; CC Name=5; Synonyms=HdynIV-26; CC IsoId=O00429-5; Sequence=VSP_013687; CC Note=No experimental confirmation available.; CC Name=6; CC IsoId=O00429-6; Sequence=VSP_039097; CC Name=7; CC IsoId=O00429-7; Sequence=VSP_054544, VSP_054545; CC Note=No experimental confirmation available.; CC Name=8; CC IsoId=O00429-8; Sequence=VSP_039097, VSP_013688; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with highest levels CC found in skeletal muscles, heart, kidney and brain. Isoform 1 is CC brain-specific. Isoform 2 and isoform 3 are predominantly CC expressed in testis and skeletal muscles respectively. Isoform 4 CC is weakly expressed in brain, heart and kidney. Isoform 5 is CC dominantly expressed in liver, heart and kidney. Isoform 6 is CC expressed in neurons. {ECO:0000269|PubMed:10749171, CC ECO:0000269|PubMed:9422767, ECO:0000269|PubMed:9570752, CC ECO:0000269|PubMed:9731200, ECO:0000269|PubMed:9786947}. CC -!- DOMAIN: The GED domain folds back to interact, in cis, with the CC GTP-binding domain and middle domain, and interacts, in trans, CC with the GED domains of other DNM1L molecules, and is thus CC critical for activating GTPase activity and for DNM1L CC dimerization. CC -!- PTM: Phosphorylation/dephosphorylation events on two sites near CC the GED domain regulate mitochondrial fission. Phosphorylation on CC Ser-637 inhibits mitochondrial fission probably through preventing CC intramolecular interaction. Dephosphorylated on this site by CC PPP3CA which promotes mitochondrial fission. Phosphorylation on CC Ser-616 also promotes mitochondrial fission. CC {ECO:0000269|PubMed:17301055, ECO:0000269|PubMed:17553808, CC ECO:0000269|PubMed:18695047, ECO:0000269|PubMed:18838687, CC ECO:0000269|PubMed:23283981}. CC -!- PTM: Sumoylated on various lysine residues within the B domain, CC probably by MUL1. Sumoylation positively regulates mitochondrial CC fission. Desumoylated by SENP5 during G2/M transition of mitosis. CC Appears to be linked to its catalytic activity. CC {ECO:0000269|PubMed:19407830, ECO:0000269|PubMed:19411255, CC ECO:0000269|PubMed:19638400}. CC -!- PTM: S-nitrosylation increases DNM1L dimerization, mitochondrial CC fission and causes neuronal damage. {ECO:0000269|PubMed:19342591}. CC -!- PTM: Ubiquitination by MARCH5 affects mitochondrial morphology. CC {ECO:0000269|PubMed:16874301, ECO:0000269|PubMed:16936636}. CC -!- PTM: O-GlcNAcylation augments the level of the GTP-bound active CC form of DRP1 and induces translocation from the cytoplasm to CC mitochondria in cardiomyocytes. It also decreases phosphorylation CC at Ser-637 (By similarity). {ECO:0000250}. CC -!- DISEASE: Note=May be associated with Alzheimer disease through CC beta-amyloid-induced increased S-nitrosylation of DNM1L, which CC triggers, directly or indirectly, excessive mitochondrial fission, CC synaptic loss and neuronal damage. CC -!- DISEASE: Encephalopathy, lethal, due to defective mitochondrial CC and peroxisomal fission (EMPF) [MIM:614388]: A rare autosomal CC dominant systemic disorder resulting in lack of neurologic CC development and death in infancy. After birth, infants present in CC the first week of life with poor feeding and neurologic CC impairment, including hypotonia, little spontaneous movement, no CC tendon reflexes, no response to light stimulation, and poor visual CC fixation. Other features include mildly elevated plasma CC concentration of very-long-chain fatty acids, lactic acidosis, CC microcephaly, deep-set eyes, optic atrophy and hypoplasia, and an CC abnormal gyral pattern in both frontal lobes associated with CC dysmyelination. {ECO:0000269|PubMed:17460227}. Note=The disease is CC caused by mutations affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase CC superfamily. Dynamin/Fzo/YdjA family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 dynamin-type G (guanine nucleotide-binding) CC domain. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 GED domain. {ECO:0000255|PROSITE- CC ProRule:PRU00720}. CC -!- SEQUENCE CAUTION: CC Sequence=BAD92307.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; 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; AB006965; BAA22193.1; -; mRNA. DR EMBL; AF061795; AAC35283.1; -; mRNA. DR EMBL; AF000430; AAC23724.1; -; mRNA. DR EMBL; AF151685; AAD39541.1; -; mRNA. DR EMBL; AK299926; BAG61760.1; -; mRNA. DR EMBL; AK291094; BAF83783.1; -; mRNA. DR EMBL; AK294533; BAG57740.1; -; mRNA. DR EMBL; AB209070; BAD92307.1; ALT_INIT; mRNA. DR EMBL; AC084824; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC087588; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC024590; AAH24590.1; -; mRNA. DR CCDS; CCDS61095.1; -. [O00429-6] DR CCDS; CCDS61096.1; -. [O00429-8] DR CCDS; CCDS61098.1; -. [O00429-2] DR CCDS; CCDS61099.1; -. [O00429-7] DR CCDS; CCDS8728.1; -. [O00429-4] DR CCDS; CCDS8729.1; -. [O00429-1] DR CCDS; CCDS8730.1; -. [O00429-3] DR PIR; JC5695; JC5695. DR RefSeq; NP_001265392.1; NM_001278463.1. [O00429-2] DR RefSeq; NP_001265393.1; NM_001278464.1. [O00429-6] DR RefSeq; NP_001265394.1; NM_001278465.1. [O00429-8] DR RefSeq; NP_001265395.1; NM_001278466.1. [O00429-7] DR RefSeq; NP_005681.2; NM_005690.4. [O00429-4] DR RefSeq; NP_036192.2; NM_012062.4. [O00429-1] DR RefSeq; NP_036193.2; NM_012063.3. [O00429-3] DR UniGene; Hs.556296; -. DR PDB; 3W6N; X-ray; 2.00 A; A/B=1-329, A/B=709-736. DR PDB; 3W6O; X-ray; 1.90 A; A/B=1-329, A/B=709-736. DR PDB; 3W6P; X-ray; 1.70 A; A/B=1-329, A/B=709-736. DR PDB; 4BEJ; X-ray; 3.48 A; A/B/C/D=1-736. DR PDB; 4H1U; X-ray; 2.30 A; A=1-327, A=711-736. DR PDB; 4H1V; X-ray; 2.30 A; A=1-327, A=711-736. DR PDBsum; 3W6N; -. DR PDBsum; 3W6O; -. DR PDBsum; 3W6P; -. DR PDBsum; 4BEJ; -. DR PDBsum; 4H1U; -. DR PDBsum; 4H1V; -. DR ProteinModelPortal; O00429; -. DR SMR; O00429; 1-731. DR BioGrid; 115370; 47. DR DIP; DIP-42704N; -. DR IntAct; O00429; 12. DR MINT; MINT-1394198; -. DR STRING; 9606.ENSP00000450399; -. DR PhosphoSite; O00429; -. DR MaxQB; O00429; -. DR PaxDb; O00429; -. DR PRIDE; O00429; -. DR DNASU; 10059; -. DR Ensembl; ENST00000266481; ENSP00000266481; ENSG00000087470. [O00429-4] DR Ensembl; ENST00000381000; ENSP00000370388; ENSG00000087470. [O00429-8] DR Ensembl; ENST00000414834; ENSP00000404160; ENSG00000087470. [O00429-7] DR Ensembl; ENST00000452533; ENSP00000415131; ENSG00000087470. [O00429-3] DR Ensembl; ENST00000547312; ENSP00000448610; ENSG00000087470. [O00429-2] DR Ensembl; ENST00000549701; ENSP00000450399; ENSG00000087470. [O00429-1] DR Ensembl; ENST00000553257; ENSP00000449089; ENSG00000087470. [O00429-6] DR GeneID; 10059; -. DR KEGG; hsa:10059; -. DR UCSC; uc001rld.2; human. [O00429-1] DR UCSC; uc001rle.2; human. [O00429-3] DR UCSC; uc001rlf.2; human. [O00429-4] DR UCSC; uc010ski.1; human. DR CTD; 10059; -. DR GeneCards; GC12P032832; -. DR H-InvDB; HIX0010537; -. DR HGNC; HGNC:2973; DNM1L. DR HPA; CAB009952; -. DR HPA; HPA039324; -. DR MIM; 603850; gene. DR MIM; 614388; phenotype. DR neXtProt; NX_O00429; -. DR Orphanet; 330050; Lethal encephalopathy due to mitochondrial and peroxisomal fission defect. DR PharmGKB; PA27441; -. DR eggNOG; COG0699; -. DR GeneTree; ENSGT00760000119213; -. DR HOGENOM; HOG000161068; -. DR HOVERGEN; HBG107833; -. DR InParanoid; O00429; -. DR KO; K17065; -. DR OMA; ASHEDQH; -. DR OrthoDB; EOG7GJ6CB; -. DR PhylomeDB; O00429; -. DR TreeFam; TF352031; -. DR Reactome; REACT_995; Apoptotic execution phase. DR ChiTaRS; DNM1L; human. DR GeneWiki; DNM1L; -. DR GenomeRNAi; 10059; -. DR NextBio; 35471718; -. DR PMAP-CutDB; O00429; -. DR PRO; PR:O00429; -. DR Proteomes; UP000005640; Chromosome 12. DR Bgee; O00429; -. DR CleanEx; HS_DNM1L; -. DR ExpressionAtlas; O00429; baseline and differential. DR Genevisible; O00429; HS. DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW. DR GO; GO:0005905; C:coated pit; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0005874; C:microtubule; IDA:UniProtKB. DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB. DR GO; GO:0043234; C:protein complex; IDA:UniProtKB. DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB. DR GO; GO:0006915; P:apoptotic process; TAS:Reactome. DR GO; GO:0006921; P:cellular component disassembly involved in execution phase of apoptosis; TAS:Reactome. DR GO; GO:0003374; P:dynamin polymerization involved in mitochondrial fission; IDA:UniProtKB. DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW. DR GO; GO:0061025; P:membrane fusion; IDA:UniProtKB. DR GO; GO:0008152; P:metabolic process; IDA:GOC. DR GO; GO:0000266; P:mitochondrial fission; IDA:UniProtKB. DR GO; GO:0043653; P:mitochondrial fragmentation involved in apoptotic process; IMP:UniProtKB. DR GO; GO:0090149; P:mitochondrial membrane fission; IDA:UniProtKB. DR GO; GO:0070584; P:mitochondrion morphogenesis; IMP:MGI. DR GO; GO:0070266; P:necroptotic process; IMP:UniProtKB. DR GO; GO:0016559; P:peroxisome fission; IDA:UniProtKB. DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB. DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB. DR GO; GO:0090141; P:positive regulation of mitochondrial fission; IMP:ParkinsonsUK-UCL. DR GO; GO:0050714; P:positive regulation of protein secretion; IDA:UniProtKB. DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; IMP:UniProtKB. DR GO; GO:0012501; P:programmed cell death; TAS:Reactome. DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB. DR GO; GO:0070585; P:protein localization to mitochondrion; IEA:Ensembl. DR GO; GO:1903146; P:regulation of mitochondrion degradation; IGI:ParkinsonsUK-UCL. DR GO; GO:0010821; P:regulation of mitochondrion organization; IMP:UniProtKB. DR GO; GO:1900063; P:regulation of peroxisome organization; IMP:UniProtKB. DR GO; GO:0032459; P:regulation of protein oligomerization; IDA:UniProtKB. DR GO; GO:0001836; P:release of cytochrome c from mitochondria; IMP:UniProtKB. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR030556; DNM1L. DR InterPro; IPR000375; Dynamin_central. DR InterPro; IPR001401; Dynamin_GTPase. DR InterPro; IPR019762; Dynamin_GTPase_CS. DR InterPro; IPR022812; Dynamin_SF. DR InterPro; IPR030381; G_DYNAMIN_dom. DR InterPro; IPR003130; GED. DR InterPro; IPR020850; GTPase_effector_domain_GED. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR11566; PTHR11566; 1. DR PANTHER; PTHR11566:SF39; PTHR11566:SF39; 1. DR Pfam; PF01031; Dynamin_M; 1. DR Pfam; PF02212; GED; 1. DR PRINTS; PR00195; DYNAMIN. DR SMART; SM00053; DYNc; 1. DR SMART; SM00302; GED; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00410; G_DYNAMIN_1; 1. DR PROSITE; PS51718; G_DYNAMIN_2; 1. DR PROSITE; PS51388; GED; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cell junction; KW Coated pit; Complete proteome; Cytoplasm; Cytoplasmic vesicle; KW Disease mutation; Endocytosis; Glycoprotein; Golgi apparatus; KW GTP-binding; Hydrolase; Isopeptide bond; Lipid-binding; Membrane; KW Mitochondrion; Mitochondrion outer membrane; Necrosis; KW Nucleotide-binding; Peroxisome; Phosphoprotein; Polymorphism; KW Reference proteome; S-nitrosylation; Synapse; Ubl conjugation. FT CHAIN 1 736 Dynamin-1-like protein. FT /FTId=PRO_0000206566. FT DOMAIN 22 302 Dynamin-type G. FT DOMAIN 644 735 GED. {ECO:0000255|PROSITE- FT ProRule:PRU00720}. FT NP_BIND 32 39 GTP. FT NP_BIND 146 150 GTP. FT NP_BIND 215 218 GTP. FT NP_BIND 246 249 GTP. FT REGION 1 343 GTPase domain. FT REGION 344 489 Middle domain. FT REGION 448 685 Interaction with GSK3B. FT REGION 502 569 B domain. FT REGION 654 668 Important for homodimerization. FT MOD_RES 1 1 N-acetylmethionine. FT {ECO:0000269|PubMed:19413330, FT ECO:0000269|PubMed:22223895}. FT MOD_RES 548 548 Phosphoserine. FT {ECO:0000269|PubMed:18669648}. FT MOD_RES 597 597 N6-acetyllysine; alternate. FT {ECO:0000250|UniProtKB:Q8K1M6}. FT MOD_RES 607 607 Phosphoserine. FT {ECO:0000269|PubMed:18669648}. FT MOD_RES 616 616 Phosphoserine; by CDK1. FT {ECO:0000269|PubMed:18088087, FT ECO:0000269|PubMed:18669648, FT ECO:0000269|PubMed:18838687, FT ECO:0000269|PubMed:19690332, FT ECO:0000269|PubMed:20068231, FT ECO:0000269|PubMed:21406692, FT ECO:0000269|PubMed:24275569}. FT MOD_RES 637 637 Phosphoserine; by CAMK1 and PKA. FT {ECO:0000269|PubMed:17553808, FT ECO:0000269|PubMed:18695047, FT ECO:0000269|PubMed:18838687, FT ECO:0000269|PubMed:23283981}. FT MOD_RES 644 644 S-nitrosocysteine. FT {ECO:0000269|PubMed:19342591}. FT CARBOHYD 585 585 O-linked (GlcNAc). {ECO:0000250}. FT CARBOHYD 586 586 O-linked (GlcNAc). {ECO:0000250}. FT CROSSLNK 532 532 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO). FT CROSSLNK 535 535 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO). FT CROSSLNK 558 558 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO). FT CROSSLNK 568 568 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO). FT CROSSLNK 594 594 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO). FT {ECO:0000305}. FT CROSSLNK 597 597 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO); FT alternate. FT CROSSLNK 606 606 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO). FT {ECO:0000305}. FT CROSSLNK 608 608 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO). FT VAR_SEQ 1 43 MEALIPVINKLQDVFNTVGADIIQLPQIVVVGTQSSGKSSV FT LE -> MFHKKINGKQQEKKMTLLHGKTQDTFLKGWKQKNG FT VNFFTPKI (in isoform 7). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_054544. FT VAR_SEQ 44 246 Missing (in isoform 7). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_054545. FT VAR_SEQ 83 83 N -> NDPATWKNSRHLSK (in isoform 6 and FT isoform 8). {ECO:0000303|PubMed:14702039, FT ECO:0000303|Ref.6}. FT /FTId=VSP_039097. FT VAR_SEQ 533 569 Missing (in isoform 3). FT {ECO:0000303|PubMed:10749171, FT ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:9731200}. FT /FTId=VSP_013685. FT VAR_SEQ 533 558 Missing (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_013686. FT VAR_SEQ 544 569 Missing (in isoform 5). FT {ECO:0000303|PubMed:10749171}. FT /FTId=VSP_013687. FT VAR_SEQ 559 569 Missing (in isoform 4 and isoform 8). FT {ECO:0000303|PubMed:10749171, FT ECO:0000303|Ref.6}. FT /FTId=VSP_013688. FT VARIANT 71 71 S -> T (in dbSNP:rs1064610). FT {ECO:0000269|PubMed:10749171, FT ECO:0000269|PubMed:9570752, FT ECO:0000269|PubMed:9731200}. FT /FTId=VAR_022446. FT VARIANT 395 395 A -> D (in EMPF; the mutation acts in a FT dominant-negative manner; defects FT observed in both mitochondrial and FT peroxisomal fission). FT {ECO:0000269|PubMed:17460227}. FT /FTId=VAR_063704. FT VARIANT 426 426 E -> D (in dbSNP:rs2389105). FT /FTId=VAR_030489. FT MUTAGEN 34 34 Q->A: Abolishes GTP hydrolysis. FT {ECO:0000269|PubMed:23977156}. FT MUTAGEN 38 38 K->A: Loss of GTPase activity. Impairs FT mitochondrial division and induces FT changes in peroxisome morphology. No FT effect on oligomerization. Increase in FT sumoylation by SUMO3. FT {ECO:0000269|PubMed:11514614, FT ECO:0000269|PubMed:12499366, FT ECO:0000269|PubMed:15208300, FT ECO:0000269|PubMed:19638400, FT ECO:0000269|PubMed:23977156, FT ECO:0000269|PubMed:9570752}. FT MUTAGEN 38 38 K->E: Overexpression delays protein FT secretion. {ECO:0000269|PubMed:11514614, FT ECO:0000269|PubMed:12499366, FT ECO:0000269|PubMed:15208300, FT ECO:0000269|PubMed:19638400, FT ECO:0000269|PubMed:23977156, FT ECO:0000269|PubMed:9570752}. FT MUTAGEN 39 39 S->A: Abolishes GTP hydrolysis. FT {ECO:0000269|PubMed:12618434, FT ECO:0000269|PubMed:23977156, FT ECO:0000269|PubMed:9422767}. FT MUTAGEN 39 39 S->I: Decreased localization to the FT perinuclear region. FT {ECO:0000269|PubMed:12618434, FT ECO:0000269|PubMed:23977156, FT ECO:0000269|PubMed:9422767}. FT MUTAGEN 39 39 S->N: Reduces peroxisomal abundance. FT {ECO:0000269|PubMed:12618434, FT ECO:0000269|PubMed:23977156, FT ECO:0000269|PubMed:9422767}. FT MUTAGEN 41 41 V->F: Temperature-sensitive. Impairs FT mitochondrial division. FT {ECO:0000269|PubMed:11514614}. FT MUTAGEN 59 59 T->A: Abolishes GTP hydrolysis. Impairs FT mitochondrial division. Reduces FT peroxisomal abundance. FT {ECO:0000269|PubMed:11514614, FT ECO:0000269|PubMed:12618434, FT ECO:0000269|PubMed:23977156}. FT MUTAGEN 146 146 D->A: Abolishes GTP hydrolysis. FT {ECO:0000269|PubMed:23977156}. FT MUTAGEN 149 149 G->A: Abolishes GTP hydrolysis. FT {ECO:0000269|PubMed:23977156}. FT MUTAGEN 216 216 K->A: Abolishes GTP hydrolysis. FT {ECO:0000269|PubMed:23977156}. FT MUTAGEN 218 218 D->A: Abolishes GTP hydrolysis. FT {ECO:0000269|PubMed:23977156}. FT MUTAGEN 281 281 G->D: Temperature-sensitive. Impairs FT mitochondrial division. FT {ECO:0000269|PubMed:11514614}. FT MUTAGEN 300 300 C->A: No effect on S-nitrosylation. FT {ECO:0000269|PubMed:19342591}. FT MUTAGEN 345 345 C->A: No effect on S-nitrosylation. FT {ECO:0000269|PubMed:19342591}. FT MUTAGEN 361 361 C->A: No effect on S-nitrosylation. FT {ECO:0000269|PubMed:19342591}. FT MUTAGEN 367 367 C->A: No effect on S-nitrosylation. FT {ECO:0000269|PubMed:19342591}. FT MUTAGEN 401 404 GPRP->AAAA: Impairs formation of higher FT order oligomers, but not FT homodimerization. FT {ECO:0000269|PubMed:23584531}. FT MUTAGEN 431 431 C->A: No effect on S-nitrosylation. FT {ECO:0000269|PubMed:19342591}. FT MUTAGEN 446 446 C->A: No effect on S-nitrosylation. FT {ECO:0000269|PubMed:19342591}. FT MUTAGEN 470 470 C->A: No effect on S-nitrosylation. FT {ECO:0000269|PubMed:19342591}. FT MUTAGEN 490 490 E->A: Does not impair homodimerization FT and formation of higher order oligomers. FT {ECO:0000269|PubMed:23584531}. FT MUTAGEN 490 490 E->R: Impairs homodimerization and FT formation of higher order oligomers. FT {ECO:0000269|PubMed:23584531}. FT MUTAGEN 505 505 C->A: No effect on S-nitrosylation. FT {ECO:0000269|PubMed:19342591}. FT MUTAGEN 532 532 K->R: Some loss of sumoylation in B FT domain. Complete loss of sumoylation in B FT domain; when associated with R-535; R-558 FT and R-568. {ECO:0000269|PubMed:19638400}. FT MUTAGEN 535 535 K->R: Some loss of sumoylation in B FT domain. Complete loss of sumoylation in B FT domain; when associated with R-532; R-558 FT and R-568. {ECO:0000269|PubMed:19638400}. FT MUTAGEN 558 558 K->R: Some loss of sumoylation in B FT domain. Complete loss of sumoylation in B FT domain; when associated with R-532; R-535 FT and R-568. {ECO:0000269|PubMed:19638400}. FT MUTAGEN 568 568 K->R: Some loss of sumoylation in B FT domain. Complete loss of sumoylation in B FT domain; when associated with R-532; R-535 FT and R-558. {ECO:0000269|PubMed:19638400}. FT MUTAGEN 594 594 K->R: Some loss of sumoylation in the GED FT domain; Complete loss of sumoylation in FT the GED domain; when associated with R- FT 597; R-606 and R-608. FT {ECO:0000269|PubMed:19638400}. FT MUTAGEN 597 597 K->R: Some loss of sumoylation in the GED FT domain; Complete loss of sumoylation in FT the GED domain; when associated with R- FT 594; R-606 and R-608. FT {ECO:0000269|PubMed:19638400}. FT MUTAGEN 606 606 K->R: Some loss of sumoylation in the GED FT domain; Complete loss of sumoylation in FT the GED domain; when associated with R- FT 594; R-597 and R-608. FT {ECO:0000269|PubMed:19638400}. FT MUTAGEN 608 608 K->R: Some loss of sumoylation in the GED FT domain; Complete loss of sumoylation in FT the GED domain; when associated with R- FT 594; R-597 and R-606. FT {ECO:0000269|PubMed:19638400}. FT MUTAGEN 616 616 S->A: Little effect on mitochondrial FT morphology. Translocated to mitochondria. FT {ECO:0000269|PubMed:18838687}. FT MUTAGEN 637 637 S->A: Abolishes phosphorylation. Reduces FT interaction with MIEF1 and MIEF2. FT Promotes mitochondrial fission and cell FT vulnerability to apoptotic insults. FT Mostly mitochondrial. Disrupts, in vitro, FT binding to FIS1. FT {ECO:0000269|PubMed:17553808, FT ECO:0000269|PubMed:18695047, FT ECO:0000269|PubMed:18838687, FT ECO:0000269|PubMed:23283981}. FT MUTAGEN 637 637 S->D: Impairs intramolecular, but not FT intermolecular interactions. Slight FT reduction in GTPase activity. Does not FT reduce interaction with MIEF1 and MIEF2. FT Inhibits mitochondrial fission. Retained FT in cytoplasm. FT {ECO:0000269|PubMed:17553808, FT ECO:0000269|PubMed:18695047, FT ECO:0000269|PubMed:18838687, FT ECO:0000269|PubMed:23283981}. FT MUTAGEN 644 644 C->A: Abolishes S-nitrosylation. Reduced FT dimerization and no enhancement of GTPase FT activity. {ECO:0000269|PubMed:19342591}. FT MUTAGEN 668 668 K->A: Abolishes homodimerization and FT formation of higher order oligomers. FT {ECO:0000269|PubMed:23584531}. FT MUTAGEN 679 679 K->A: Diminishes intermolecular FT interaction between GTP-middle domain and FT GED domain but no effect on FT oligomerization. Marked reduction in FT GTPase activity, in vitro. Decreased FT mitochondrial division. FT {ECO:0000269|PubMed:15208300}. FT CONFLICT 208 208 R -> C (in Ref. 2; AAC35283 and 4; FT AAD39541). {ECO:0000305}. FT HELIX 5 18 {ECO:0000244|PDB:3W6P}. FT TURN 21 23 {ECO:0000244|PDB:4H1U}. FT STRAND 27 31 {ECO:0000244|PDB:3W6P}. FT HELIX 34 36 {ECO:0000244|PDB:4BEJ}. FT HELIX 38 44 {ECO:0000244|PDB:3W6P}. FT STRAND 55 57 {ECO:0000244|PDB:3W6P}. FT STRAND 63 69 {ECO:0000244|PDB:3W6P}. FT STRAND 86 88 {ECO:0000244|PDB:4H1U}. FT STRAND 90 93 {ECO:0000244|PDB:3W6P}. FT HELIX 94 96 {ECO:0000244|PDB:3W6P}. FT HELIX 104 119 {ECO:0000244|PDB:3W6P}. FT STRAND 121 123 {ECO:0000244|PDB:3W6P}. FT STRAND 130 136 {ECO:0000244|PDB:3W6P}. FT STRAND 141 146 {ECO:0000244|PDB:3W6P}. FT HELIX 155 157 {ECO:0000244|PDB:4H1U}. FT HELIX 162 174 {ECO:0000244|PDB:3W6P}. FT STRAND 179 186 {ECO:0000244|PDB:3W6P}. FT HELIX 191 193 {ECO:0000244|PDB:3W6P}. FT HELIX 195 203 {ECO:0000244|PDB:3W6P}. FT STRAND 205 207 {ECO:0000244|PDB:4H1U}. FT STRAND 210 215 {ECO:0000244|PDB:3W6P}. FT HELIX 217 219 {ECO:0000244|PDB:3W6P}. FT STRAND 222 225 {ECO:0000244|PDB:4BEJ}. FT HELIX 227 230 {ECO:0000244|PDB:3W6P}. FT STRAND 233 235 {ECO:0000244|PDB:3W6P}. FT STRAND 237 239 {ECO:0000244|PDB:4H1V}. FT STRAND 241 243 {ECO:0000244|PDB:3W6P}. FT HELIX 249 253 {ECO:0000244|PDB:3W6P}. FT HELIX 258 272 {ECO:0000244|PDB:3W6P}. FT TURN 274 276 {ECO:0000244|PDB:3W6P}. FT HELIX 277 279 {ECO:0000244|PDB:3W6P}. FT HELIX 282 317 {ECO:0000244|PDB:3W6P}. FT HELIX 329 349 {ECO:0000244|PDB:4BEJ}. FT HELIX 363 371 {ECO:0000244|PDB:4BEJ}. FT HELIX 373 380 {ECO:0000244|PDB:4BEJ}. FT HELIX 389 399 {ECO:0000244|PDB:4BEJ}. FT HELIX 409 420 {ECO:0000244|PDB:4BEJ}. FT HELIX 421 424 {ECO:0000244|PDB:4BEJ}. FT HELIX 425 440 {ECO:0000244|PDB:4BEJ}. FT TURN 441 443 {ECO:0000244|PDB:4BEJ}. FT HELIX 444 446 {ECO:0000244|PDB:4BEJ}. FT HELIX 458 493 {ECO:0000244|PDB:4BEJ}. FT HELIX 501 504 {ECO:0000244|PDB:4BEJ}. FT HELIX 633 673 {ECO:0000244|PDB:4BEJ}. FT HELIX 675 690 {ECO:0000244|PDB:4BEJ}. FT HELIX 693 699 {ECO:0000244|PDB:4BEJ}. FT HELIX 710 731 {ECO:0000244|PDB:3W6P}. SQ SEQUENCE 736 AA; 81877 MW; F9521A376B785B71 CRC64; MEALIPVINK LQDVFNTVGA DIIQLPQIVV VGTQSSGKSS VLESLVGRDL LPRGTGIVTR RPLILQLVHV SQEDKRKTTG EENGVEAEEW GKFLHTKNKL YTDFDEIRQE IENETERISG NNKGVSPEPI HLKIFSPNVV NLTLVDLPGM TKVPVGDQPK DIELQIRELI LRFISNPNSI ILAVTAANTD MATSEALKIS REVDPDGRRT LAVITKLDLM DAGTDAMDVL MGRVIPVKLG IIGVVNRSQL DINNKKSVTD SIRDEYAFLQ KKYPSLANRN GTKYLARTLN RLLMHHIRDC LPELKTRINV LAAQYQSLLN SYGEPVDDKS ATLLQLITKF ATEYCNTIEG TAKYIETSEL CGGARICYIF HETFGRTLES VDPLGGLNTI DILTAIRNAT GPRPALFVPE VSFELLVKRQ IKRLEEPSLR CVELVHEEMQ RIIQHCSNYS TQELLRFPKL HDAIVEVVTC LLRKRLPVTN EMVHNLVAIE LAYINTKHPD FADACGLMNN NIEEQRRNRL ARELPSAVSR DKSSKVPSAL APASQEPSPA ASAEADGKLI QDSRRETKNV ASGGGGVGDG VQEPTTGNWR GMLKTSKAEE LLAEEKSKPI PIMPASPQKG HAVNLLDVPV PVARKLSARE QRDCEVIERL IKSYFLIVRK NIQDSVPKAV MHFLVNHVKD TLQSELVGQL YKSSLLDDLL TESEDMAQRR KEAADMLKAL QGASQIIAEI RETHLW //