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Dynamin-1-like protein (EC 3.6.5.5) (Dnm1p/Vps1p-like protein) (DVLP) (Dynamin family member proline-rich carboxyl-terminal domain less) (Dymple) (Dynamin-like protein) (Dynamin-like protein 4) (Dynamin-like protein IV) (HdynIV) (Dynamin-related protein 1)

 DNM1L_HUMAN             Reviewed;         736 AA.
O00429; A8K4X9; B4DGC9; B4DSU8; J3KPI2; O14541; O60709; Q59GN9;
Q7L6B3; Q8TBT7; Q9BWM1; Q9Y5J2;
10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
06-FEB-2007, sequence version 2.
27-SEP-2017, entry version 161.
RecName: Full=Dynamin-1-like protein;
EC=3.6.5.5;
AltName: Full=Dnm1p/Vps1p-like protein;
Short=DVLP;
AltName: Full=Dynamin family member proline-rich carboxyl-terminal domain less;
Short=Dymple;
AltName: Full=Dynamin-like protein;
AltName: Full=Dynamin-like protein 4;
AltName: Full=Dynamin-like protein IV;
Short=HdynIV;
AltName: Full=Dynamin-related protein 1;
Name=DNM1L; Synonyms=DLP1, DRP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION.
TISSUE=Hepatoma;
PubMed=9348079; DOI=10.1093/oxfordjournals.jbchem.a021784;
Shin H.-W., Shinotsuka C., Torii S., Murakami K., Nakayama K.;
"Identification and subcellular localization of a novel mammalian
dynamin-related protein homologous to yeast Vps1p and Dnm1p.";
J. Biochem. 122:525-530(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), VARIANT THR-71, TISSUE
SPECIFICITY, AND INTERACTION WITH GSK3B.
TISSUE=Liver;
PubMed=9731200; DOI=10.1006/bbrc.1998.9253;
Hong Y.-R., Chen C.-H., Cheng D.-S., Howng S.-L., Chow C.-C.;
"Human dynamin-like protein interacts with the glycogen synthase
kinase 3beta.";
Biochem. Biophys. Res. Commun. 249:697-703(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT THR-71, TISSUE
SPECIFICITY, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-38, AND
FUNCTION.
TISSUE=Brain;
PubMed=9570752;
Imoto M., Tachibana I., Urrutia R.;
"Identification and functional characterization of a novel human
protein highly related to the yeast dynamin-like GTPase Vps1p.";
J. Cell Sci. 111:1341-1349(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3; 4 AND 5), VARIANT THR-71,
TISSUE SPECIFICITY, AND INTERACTION WITH GSK3B.
TISSUE=Brain;
PubMed=10749171; DOI=10.1089/104454900314573;
Chen C.-H., Howng S.-L., Hwang S.-L., Chou C.-K., Liao C.-H.,
Hong Y.-R.;
"Differential expression of four human dynamin-like protein variants
in brain tumors.";
DNA Cell Biol. 19:189-194(2000).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 6 AND 7).
TISSUE=Amygdala, and Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8).
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
"Homo sapiens protein coding cDNA.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 27-736 (ISOFORM 1).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
MUTAGENESIS OF SER-39, TISSUE SPECIFICITY, CATALYTIC ACTIVITY, AND
SUBCELLULAR LOCATION.
PubMed=9422767; DOI=10.1074/jbc.273.2.1044;
Kamimoto T., Nagai Y., Onogi H., Muro Y., Wakabayashi T., Hagiwara M.;
"Dymple, a novel dynamin-like high molecular weight GTPase lacking a
proline-rich carboxyl-terminal domain in mammalian cells.";
J. Biol. Chem. 273:1044-1051(1998).
[10]
SUBCELLULAR LOCATION.
PubMed=9472031; DOI=10.1083/jcb.140.4.779;
Yoon Y., Pitts K.R., Dahan S., McNiven M.A.;
"A novel dynamin-like protein associates with cytoplasmic vesicles and
tubules of the endoplasmic reticulum in mammalian cells.";
J. Cell Biol. 140:779-793(1998).
[11]
TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=9786947; DOI=10.1083/jcb.143.2.351;
Smirnova E., Shurland D.-L., Ryazantsev S.N., van der Bliek A.M.;
"A human dynamin-related protein controls the distribution of
mitochondria.";
J. Cell Biol. 143:351-358(1998).
[12]
OLIGOMERIZATION.
PubMed=9915810; DOI=10.1074/jbc.274.5.2780;
Shin H.-W., Takatsu H., Mukai H., Munekata E., Murakami K.,
Nakayama K.;
"Intermolecular and interdomain interactions of a dynamin-related GTP-
binding protein, Dnm1p/Vps1p-like protein.";
J. Biol. Chem. 274:2780-2785(1999).
[13]
FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-38; VAL-41; THR-59
AND GLY-281, AND OLIGOMERIZATION.
PubMed=11514614; DOI=10.1091/mbc.12.8.2245;
Smirnova E., Griparic L., Shurland D.-L., van der Bliek A.M.;
"Dynamin-related protein Drp1 is required for mitochondrial division
in mammalian cells.";
Mol. Biol. Cell 12:2245-2256(2001).
[14]
MUTAGENESIS OF LYS-38, SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=12499366; DOI=10.1074/jbc.M211761200;
Koch A., Thiemann M., Grabenbauer M., Yoon Y., McNiven M.A.,
Schrader M.;
"Dynamin-like protein 1 is involved in peroxisomal fission.";
J. Biol. Chem. 278:8597-8605(2003).
[15]
MUTAGENESIS OF SER-39 AND THR-59, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12618434; DOI=10.1074/jbc.M212031200;
Li X., Gould S.J.;
"The dynamin-like GTPase DLP1 is essential for peroxisome division and
is recruited to peroxisomes in part by PEX11.";
J. Biol. Chem. 278:17012-17020(2003).
[16]
FUNCTION OF STRUCTURAL DOMAINS, OLIGOMERIZATION, SUBCELLULAR LOCATION,
AND MUTAGENESIS OF LYS-38 AND LYS-679.
PubMed=15208300; DOI=10.1074/jbc.M404105200;
Zhu P.P., Patterson A., Stadler J., Seeburg D.P., Sheng M.,
Blackstone C.;
"Intra- and intermolecular domain interactions of the C-terminal
GTPase effector domain of the multimeric dynamin-like GTPase Drp1.";
J. Biol. Chem. 279:35967-35974(2004).
[17]
UBIQUITINATION BY MARCH5, AND INTERACTION WITH MARCH5.
PubMed=16874301; DOI=10.1038/sj.emboj.7601249;
Yonashiro R., Ishido S., Kyo S., Fukuda T., Goto E., Matsuki Y.,
Ohmura-Hoshino M., Sada K., Hotta H., Yamamura H., Inatome R.,
Yanagi S.;
"A novel mitochondrial ubiquitin ligase plays a critical role in
mitochondrial dynamics.";
EMBO J. 25:3618-3626(2006).
[18]
UBIQUITINATION BY MARCH5, AND INTERACTION WITH MARCH5.
PubMed=16936636; DOI=10.1038/sj.embor.7400790;
Nakamura N., Kimura Y., Tokuda M., Honda S., Hirose S.;
"MARCH-V is a novel mitofusin 2- and Drp1-binding protein able to
change mitochondrial morphology.";
EMBO Rep. 7:1019-1022(2006).
[19]
FUNCTION.
PubMed=17015472; DOI=10.1128/MCB.02282-05;
Parone P.A., James D.I., Da Cruz S., Mattenberger Y., Donze O.,
Barja F., Martinou J.C.;
"Inhibiting the mitochondrial fission machinery does not prevent
Bax/Bak-dependent apoptosis.";
Mol. Cell. Biol. 26:7397-7408(2006).
[20]
PHOSPHORYLATION, AND FUNCTION.
PubMed=17301055; DOI=10.1074/jbc.M607279200;
Taguchi N., Ishihara N., Jofuku A., Oka T., Mihara K.;
"Mitotic phosphorylation of dynamin-related GTPase Drp1 participates
in mitochondrial fission.";
J. Biol. Chem. 282:11521-11529(2007).
[21]
PHOSPHORYLATION AT SER-637, FUNCTION, SUBUNIT, AND MUTAGENESIS OF
SER-637.
PubMed=17553808; DOI=10.1074/jbc.C700083200;
Chang C.R., Blackstone C.;
"Cyclic AMP-dependent protein kinase phosphorylation of Drp1 regulates
its GTPase activity and mitochondrial morphology.";
J. Biol. Chem. 282:21583-21587(2007).
[22]
SUBCELLULAR LOCATION.
PubMed=17606867; DOI=10.1083/jcb.200611064;
Karbowski M., Neutzner A., Youle R.J.;
"The mitochondrial E3 ubiquitin ligase MARCH5 is required for Drp1
dependent mitochondrial division.";
J. Cell Biol. 178:71-84(2007).
[23]
FUNCTION, VARIANT EMPF1 ASP-395, AND CHARACTERIZATION OF VARIANT EMPF1
ASP-395.
PubMed=17460227; DOI=10.1056/NEJMoa064436;
Waterham H.R., Koster J., van Roermund C.W., Mooyer P.A.,
Wanders R.J., Leonard J.V.;
"A lethal defect of mitochondrial and peroxisomal fission.";
N. Engl. J. Med. 356:1736-1741(2007).
[24]
PHOSPHORYLATION AT SER-637, FUNCTION, INTERACTION WITH FIS1, AND
MUTAGENESIS OF SER-637.
PubMed=18695047; DOI=10.1083/jcb.200802164;
Han X.J., Lu Y.F., Li S.A., Kaitsuka T., Sato Y., Tomizawa K.,
Nairn A.C., Takei K., Matsui H., Matsushita M.;
"CaM kinase I alpha-induced phosphorylation of Drp1 regulates
mitochondrial morphology.";
J. Cell Biol. 182:573-585(2008).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-616, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-548; SER-607 AND
SER-616, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[27]
PHOSPHORYLATION AT SER-616 AND SER-637, INTERACTION WITH PPP3CA,
DEPHOSPHORYLATION, FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
SER-616 AND SER-637.
PubMed=18838687; DOI=10.1073/pnas.0808249105;
Cereghetti G.M., Stangherlin A., Martins de Brito O., Chang C.R.,
Blackstone C., Bernardi P., Scorrano L.;
"Dephosphorylation by calcineurin regulates translocation of Drp1 to
mitochondria.";
Proc. Natl. Acad. Sci. U.S.A. 105:15803-15808(2008).
[28]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[29]
SUMOYLATION BY MUL1.
PubMed=19407830; DOI=10.1038/embor.2009.86;
Braschi E., Zunino R., McBride H.M.;
"MAPL is a new mitochondrial SUMO E3 ligase that regulates
mitochondrial fission.";
EMBO Rep. 10:748-754(2009).
[30]
SUMOYLATION AT LYS-532; LYS-535; LYS-558; LYS-568; LYS-594; LYS-597;
LYS-606 AND LYS-608, INTERACTION WITH UBE2I, FUNCTION, AND MUTAGENESIS
OF LYS-38; LYS-532; LYS-535; LYS-558; LYS-568; LYS-594; LYS-597;
LYS-606 AND LYS-608.
PubMed=19638400; DOI=10.1096/fj.09-136630;
Figueroa-Romero C., Iniguez-Lluhi J.A., Stadler J., Chang C.R.,
Arnoult D., Keller P.J., Hong Y., Blackstone C., Feldman E.L.;
"SUMOylation of the mitochondrial fission protein Drp1 occurs at
multiple nonconsensus sites within the B domain and is linked to its
activity cycle.";
FASEB J. 23:3917-3927(2009).
[31]
SUMOYLATION, DESUMOYLATION, AND FUNCTION.
PubMed=19411255; DOI=10.1074/jbc.M901902200;
Zunino R., Braschi E., Xu L., McBride H.M.;
"Translocation of SenP5 from the nucleoli to the mitochondria
modulates DRP1-dependent fission during mitosis.";
J. Biol. Chem. 284:17783-17795(2009).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-616, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[33]
S-NITROSYLATION AT CYS-644, FUNCTION, ASSOCIATION WITH ALZHEIMER
DISEASE, AND MUTAGENESIS OF CYS-300; CYS-345; CYS-361; CYS-367;
CYS-431; CYS-446; CYS-470; CYS-505 AND CYS-644.
PubMed=19342591; DOI=10.1126/science.1171091;
Cho D.H., Nakamura T., Fang J., Cieplak P., Godzik A., Gu Z.,
Lipton S.A.;
"S-nitrosylation of Drp1 mediates beta-amyloid-related mitochondrial
fission and neuronal injury.";
Science 324:102-105(2009).
[34]
POSSIBLE FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=20688057; DOI=10.1016/j.yexcr.2010.07.020;
Bonekamp N.A., Vormund K., Jacob R., Schrader M.;
"Dynamin-like protein 1 at the Golgi complex: A novel component of the
sorting/targeting machinery en route to the plasma membrane.";
Exp. Cell Res. 316:3454-3467(2010).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-616, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[36]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[37]
INTERACTION WITH MIEF2 AND MIEF1.
PubMed=21508961; DOI=10.1038/embor.2011.54;
Palmer C.S., Osellame L.D., Laine D., Koutsopoulos O.S., Frazier A.E.,
Ryan M.T.;
"MiD49 and MiD51, new components of the mitochondrial fission
machinery.";
EMBO Rep. 12:565-573(2011).
[38]
INTERACTION WITH MIEF1.
PubMed=21701560; DOI=10.1038/emboj.2011.198;
Zhao J., Liu T., Jin S., Wang X., Qu M., Uhlen P., Tomilin N.,
Shupliakov O., Lendahl U., Nister M.;
"Human MIEF1 recruits Drp1 to mitochondrial outer membranes and
promotes mitochondrial fusion rather than fission.";
EMBO J. 30:2762-2778(2011).
[39]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-616, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[40]
INTERACTION WITH PGAM5, AND SUBCELLULAR LOCATION.
PubMed=22265414; DOI=10.1016/j.cell.2011.11.030;
Wang Z., Jiang H., Chen S., Du F., Wang X.;
"The mitochondrial phosphatase PGAM5 functions at the convergence
point of multiple necrotic death pathways.";
Cell 148:228-243(2012).
[41]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[42]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=23921378; DOI=10.1074/jbc.M113.479873;
Palmer C.S., Elgass K.D., Parton R.G., Osellame L.D., Stojanovski D.,
Ryan M.T.;
"MiD49 and MiD51 can act independently of Mff and Fis1 in Drp1
recruitment and are specific for mitochondrial fission.";
J. Biol. Chem. 288:27584-27593(2013).
[43]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-529 AND SER-616, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[44]
FUNCTION, INTERACTION WITH MIEF2 AND MIEF1, PHOSPHORYLATION AT
SER-637, AND MUTAGENESIS OF SER-637.
PubMed=23283981; DOI=10.1091/mbc.E12-10-0721;
Loson O.C., Song Z., Chen H., Chan D.C.;
"Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial
fission.";
Mol. Biol. Cell 24:659-667(2013).
[45]
INTERACTION WITH BCL2L1.
PubMed=23792689; DOI=10.1038/ncb2791;
Li H., Alavian K.N., Lazrove E., Mehta N., Jones A., Zhang P.,
Licznerski P., Graham M., Uo T., Guo J., Rahner C., Duman R.S.,
Morrison R.S., Jonas E.A.;
"A Bcl-xL-Drp1 complex regulates synaptic vesicle membrane dynamics
during endocytosis.";
Nat. Cell Biol. 15:773-785(2013).
[46]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-616, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[47]
SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-616 AND SER-637.
PubMed=26122121; DOI=10.1093/brain/awv182;
Shahni R., Cale C.M., Anderson G., Osellame L.D., Hambleton S.,
Jacques T.S., Wedatilake Y., Taanman J.W., Chan E., Qasim W.,
Plagnol V., Chalasani A., Duchen M.R., Gilmour K.C., Rahman S.;
"Signal transducer and activator of transcription 2 deficiency is a
novel disorder of mitochondrial fission.";
Brain 138:2834-2846(2015).
[48]
FUNCTION, INTERACTION WITH MIEF2, AND SUBUNIT.
PubMed=23530241; DOI=10.1073/pnas.1300855110;
Koirala S., Guo Q., Kalia R., Bui H.T., Eckert D.M., Frost A.,
Shaw J.M.;
"Interchangeable adaptors regulate mitochondrial dynamin assembly for
membrane scission.";
Proc. Natl. Acad. Sci. U.S.A. 110:E1342-E1351(2013).
[49]
X-RAY CRYSTALLOGRAPHY (3.48 ANGSTROMS), FUNCTION, SUBUNIT, SUBCELLULAR
LOCATION, MUTAGENESIS OF 401-GLY--PRO-404; GLU-490 AND LYS-668, AND
LIPID-BINDING.
PubMed=23584531; DOI=10.1038/emboj.2013.74;
Frohlich C., Grabiger S., Schwefel D., Faelber K., Rosenbaum E.,
Mears J., Rocks O., Daumke O.;
"Structural insights into oligomerization and mitochondrial
remodelling of dynamin 1-like protein.";
EMBO J. 32:1280-1292(2013).
[50]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-327 AND 711-736 IN COMPLEX
WITH GTP ANALOGS, CATALYTIC ACTIVITY, MUTAGENESIS OF GLN-34; LYS-38;
SER-39; THR-59; ASP-146; GLY-149; LYS-216 AND ASP-218, ENZYME
REGULATION, AND SUBUNIT.
PubMed=23977156; DOI=10.1371/journal.pone.0071835;
Wenger J., Klinglmayr E., Frohlich C., Eibl C., Gimeno A.,
Hessenberger M., Puehringer S., Daumke O., Goettig P.;
"Functional mapping of human dynamin-1-like GTPase domain based on x-
ray structure analyses.";
PLoS ONE 8:E71835-E71835(2013).
[51]
VARIANT EMPF1 ASP-362, AND CHARACTERIZATION OF VARIANT EMPF1 ASP-362.
PubMed=26604000; DOI=10.1038/ejhg.2015.243;
Care4Rare Consortium;
Vanstone J.R., Smith A.M., McBride S., Naas T., Holcik M., Antoun G.,
Harper M.E., Michaud J., Sell E., Chakraborty P., Tetreault M.,
Majewski J., Baird S., Boycott K.M., Dyment D.A., MacKenzie A.,
Lines M.A.;
"DNM1L-related mitochondrial fission defect presenting as refractory
epilepsy.";
Eur. J. Hum. Genet. 24:1084-1088(2016).
[52]
VARIANT EMPF1 CYS-403, CHARACTERIZATION OF VARIANTS EMPF1 ASP-395 AND
CYS-403, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=27145208; DOI=10.1002/ajmg.a.37721;
Fahrner J.A., Liu R., Perry M.S., Klein J., Chan D.C.;
"A novel de novo dominant negative mutation in DNM1L impairs
mitochondrial fission and presents as childhood epileptic
encephalopathy.";
Am. J. Med. Genet. A 170:2002-2011(2016).
[53]
VARIANT EMPF1 SER-362, CHARACTERIZATION OF VARIANT EMPF1 SER-362, AND
FUNCTION.
PubMed=26992161; DOI=10.1002/ajmg.a.37624;
Sheffer R., Douiev L., Edvardson S., Shaag A., Tamimi K.,
Soiferman D., Meiner V., Saada A.;
"Postnatal microcephaly and pain insensitivity due to a de novo
heterozygous DNM1L mutation causing impaired mitochondrial fission and
function.";
Am. J. Med. Genet. A 170:1603-1607(2016).
-!- FUNCTION: Functions in mitochondrial and peroxisomal division.
Mediates membrane fission through oligomerization into membrane-
associated tubular structures that wrap around the scission site
to constrict and sever the mitochondrial membrane through a GTP
hydrolysis-dependent mechanism. Through its function in
mitochondrial division, ensures the survival of at least some
types of postmitotic neurons, including Purkinje cells, by
suppressing oxidative damage. Required for normal brain
development, including that of cerebellum. Facilitates
developmentally regulated apoptosis during neural tube formation.
Required for a normal rate of cytochrome c release and caspase
activation during apoptosis; this requirement may depend upon the
cell type and the physiological apoptotic cues. Plays an important
role in mitochondrial fission during mitosis (PubMed:26992161).
Required for formation of endocytic vesicles. Proposed to regulate
synaptic vesicle membrane dynamics through association with BCL2L1
isoform Bcl-X(L) which stimulates its GTPase activity in synaptic
vesicles; the function may require its recruitment by MFF to
clathrin-containing vesicles. Required for programmed necrosis
execution. {ECO:0000269|PubMed:11514614,
ECO:0000269|PubMed:12499366, ECO:0000269|PubMed:17015472,
ECO:0000269|PubMed:17301055, ECO:0000269|PubMed:17460227,
ECO:0000269|PubMed:17553808, ECO:0000269|PubMed:18695047,
ECO:0000269|PubMed:18838687, ECO:0000269|PubMed:19342591,
ECO:0000269|PubMed:19411255, ECO:0000269|PubMed:19638400,
ECO:0000269|PubMed:20688057, ECO:0000269|PubMed:23283981,
ECO:0000269|PubMed:23530241, ECO:0000269|PubMed:23584531,
ECO:0000269|PubMed:23921378, ECO:0000269|PubMed:26992161,
ECO:0000269|PubMed:27145208, ECO:0000269|PubMed:9570752,
ECO:0000269|PubMed:9786947}.
-!- FUNCTION: Isoform 1: Inhibits peroxisomal division when
overexpressed. {ECO:0000269|PubMed:12618434}.
-!- FUNCTION: Isoform 4: Inhibits peroxisomal division when
overexpressed. {ECO:0000269|PubMed:12618434}.
-!- CATALYTIC ACTIVITY: GTP + H(2)O = GDP + phosphate.
{ECO:0000269|PubMed:23977156, ECO:0000269|PubMed:9422767}.
-!- ENZYME REGULATION: GTPase activity is increased by binding to
phospholipid membranes. {ECO:0000269|PubMed:23977156}.
-!- SUBUNIT: Homotetramer; dimerizes through the N-terminal GTP-middle
region of one molecule binding to the GED domain of another DNM1L
molecule. Oligomerizes in a GTP-dependent manner to form membrane-
associated tubules with a spiral pattern. Can also oligomerize to
form multimeric ring-like structures. Interacts with GSK3B and
MARCH5. Interacts (via the GTPase and B domains) with UBE2I; the
interaction promotes sumoylation of DNM1L, mainly in its B domain.
Interacts with PPP3CA; the interaction dephosphorylates DNM1L and
regulates its transition to mitochondria. Interacts with BCL2L1
isoform BCL-X(L) and CLTA; DNM1L and BCL2L1 isoform BCL-X(L) may
form a complex in synaptic vesicles that also contains clathrin
and MFF. Interacts with FIS1. Interacts with MIEF2 and MIEF1; this
regulates GTP hydrolysis and DNM1L oligomerization. Interacts with
PGAM5; this interaction leads to dephosphorylation at Ser-656 and
activation of GTPase activity and eventually to mitochondria
fragmentation. {ECO:0000269|PubMed:10749171,
ECO:0000269|PubMed:16874301, ECO:0000269|PubMed:16936636,
ECO:0000269|PubMed:17553808, ECO:0000269|PubMed:18695047,
ECO:0000269|PubMed:18838687, ECO:0000269|PubMed:19638400,
ECO:0000269|PubMed:21508961, ECO:0000269|PubMed:21701560,
ECO:0000269|PubMed:22265414, ECO:0000269|PubMed:23283981,
ECO:0000269|PubMed:23530241, ECO:0000269|PubMed:23584531,
ECO:0000269|PubMed:23792689, ECO:0000269|PubMed:23977156,
ECO:0000269|PubMed:27145208, ECO:0000269|PubMed:9731200}.
-!- INTERACTION:
P03372:ESR1; NbExp=2; IntAct=EBI-724571, EBI-78473;
Q5S007:LRRK2; NbExp=11; IntAct=EBI-724571, EBI-5323863;
Q9NQG6:MIEF1; NbExp=9; IntAct=EBI-724571, EBI-740987;
Q96C03:MIEF2; NbExp=3; IntAct=EBI-724571, EBI-750153;
Q9Y512:SAMM50; NbExp=3; IntAct=EBI-724571, EBI-748409;
Q14160:SCRIB; NbExp=2; IntAct=EBI-724571, EBI-357345;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Golgi apparatus.
Endomembrane system; Peripheral membrane protein. Mitochondrion
outer membrane {ECO:0000269|PubMed:26122121,
ECO:0000269|PubMed:27145208}; Peripheral membrane protein.
Peroxisome. Membrane, clathrin-coated pit {ECO:0000250}.
Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane
{ECO:0000250}. Note=Mainly cytosolic. Translocated to the
mitochondrial membrane through O-GlcNAcylation and interaction
with FIS1. Recruited to the mitochondrial outer membrane by
interaction with MIEF1. Colocalized with MARCH5 at mitochondrial
membrane. Localizes to mitochondria at sites of division.
Localizes to mitochondria following necrosis induction. Associated
with peroxisomal membranes, partly recruited there by PEX11B. May
also be associated with endoplasmic reticulum tubules and
cytoplasmic vesicles and found to be perinuclear. In some cell
types, localizes to the Golgi complex. Binds to phospholipid
membranes.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=8;
Name=1; Synonyms=HdynIV-WT, DLP1F;
IsoId=O00429-1; Sequence=Displayed;
Name=4; Synonyms=HdynIV-11, DLP1c;
IsoId=O00429-2; Sequence=VSP_013688;
Name=2; Synonyms=DLP1a;
IsoId=O00429-3; Sequence=VSP_013686;
Name=3; Synonyms=HdynIV-37, DLP1b;
IsoId=O00429-4; Sequence=VSP_013685;
Name=5; Synonyms=HdynIV-26;
IsoId=O00429-5; Sequence=VSP_013687;
Note=No experimental confirmation available.;
Name=6;
IsoId=O00429-6; Sequence=VSP_039097;
Name=7;
IsoId=O00429-7; Sequence=VSP_054544, VSP_054545;
Note=No experimental confirmation available.;
Name=8;
IsoId=O00429-8; Sequence=VSP_039097, VSP_013688;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed with highest levels
found in skeletal muscles, heart, kidney and brain. Isoform 1 is
brain-specific. Isoform 2 and isoform 3 are predominantly
expressed in testis and skeletal muscles respectively. Isoform 4
is weakly expressed in brain, heart and kidney. Isoform 5 is
dominantly expressed in liver, heart and kidney. Isoform 6 is
expressed in neurons. {ECO:0000269|PubMed:10749171,
ECO:0000269|PubMed:9422767, ECO:0000269|PubMed:9570752,
ECO:0000269|PubMed:9731200, ECO:0000269|PubMed:9786947}.
-!- DOMAIN: The GED domain folds back to interact, in cis, with the
GTP-binding domain and middle domain, and interacts, in trans,
with the GED domains of other DNM1L molecules, and is thus
critical for activating GTPase activity and for DNM1L
dimerization.
-!- PTM: Phosphorylation/dephosphorylation events on two sites near
the GED domain regulate mitochondrial fission. Phosphorylation on
Ser-637 inhibits the GTPase activity, leading to a defect in
mitochondrial fission promoting mitochondrial elongation.
Dephosphorylated on this site by PPP3CA which promotes
mitochondrial fission. Phosphorylation on Ser-616 activates the
GTPase activity and promotes mitochondrial fission.
{ECO:0000269|PubMed:17301055, ECO:0000269|PubMed:17553808,
ECO:0000269|PubMed:18695047, ECO:0000269|PubMed:18838687,
ECO:0000269|PubMed:23283981, ECO:0000269|PubMed:26122121}.
-!- PTM: Sumoylated on various lysine residues within the B domain,
probably by MUL1. Sumoylation positively regulates mitochondrial
fission. Desumoylated by SENP5 during G2/M transition of mitosis.
Appears to be linked to its catalytic activity.
{ECO:0000269|PubMed:19407830, ECO:0000269|PubMed:19411255,
ECO:0000269|PubMed:19638400}.
-!- PTM: S-nitrosylation increases DNM1L dimerization, mitochondrial
fission and causes neuronal damage. {ECO:0000269|PubMed:19342591}.
-!- PTM: Ubiquitination by MARCH5 affects mitochondrial morphology.
{ECO:0000269|PubMed:16874301, ECO:0000269|PubMed:16936636}.
-!- PTM: O-GlcNAcylation augments the level of the GTP-bound active
form of DRP1 and induces translocation from the cytoplasm to
mitochondria in cardiomyocytes. It also decreases phosphorylation
at Ser-637 (By similarity). {ECO:0000250}.
-!- DISEASE: Note=May be associated with Alzheimer disease through
amyloid-beta-induced increased S-nitrosylation of DNM1L, which
triggers, directly or indirectly, excessive mitochondrial fission,
synaptic loss and neuronal damage. {ECO:0000269|PubMed:19342591}.
-!- DISEASE: Encephalopathy due to defective mitochondrial and
peroxisomal fission 1 (EMPF1) [MIM:614388]: A rare autosomal
dominant systemic disorder resulting in lack of neurologic
development and death in infancy. After birth, infants present in
the first week of life with poor feeding and neurologic
impairment, including hypotonia, little spontaneous movement, no
tendon reflexes, no response to light stimulation, and poor visual
fixation. Other features include mildly elevated plasma
concentration of very-long-chain fatty acids, lactic acidosis,
microcephaly, deep-set eyes, optic atrophy and hypoplasia, and an
abnormal gyral pattern in both frontal lobes associated with
dysmyelination. {ECO:0000269|PubMed:17460227,
ECO:0000269|PubMed:26604000, ECO:0000269|PubMed:26992161,
ECO:0000269|PubMed:27145208}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
superfamily. Dynamin/Fzo/YdjA family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAD92307.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AB006965; BAA22193.1; -; mRNA.
EMBL; AF061795; AAC35283.1; -; mRNA.
EMBL; AF000430; AAC23724.1; -; mRNA.
EMBL; AF151685; AAD39541.1; -; mRNA.
EMBL; AK299926; BAG61760.1; -; mRNA.
EMBL; AK291094; BAF83783.1; -; mRNA.
EMBL; AK294533; BAG57740.1; -; mRNA.
EMBL; AB209070; BAD92307.1; ALT_INIT; mRNA.
EMBL; AC084824; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC087588; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC024590; AAH24590.1; -; mRNA.
CCDS; CCDS61095.1; -. [O00429-6]
CCDS; CCDS61096.1; -. [O00429-8]
CCDS; CCDS61098.1; -. [O00429-2]
CCDS; CCDS61099.1; -. [O00429-7]
CCDS; CCDS8728.1; -. [O00429-4]
CCDS; CCDS8729.1; -. [O00429-1]
CCDS; CCDS8730.1; -. [O00429-3]
PIR; JC5695; JC5695.
RefSeq; NP_001265392.1; NM_001278463.1. [O00429-2]
RefSeq; NP_001265393.1; NM_001278464.1. [O00429-6]
RefSeq; NP_001265394.1; NM_001278465.1. [O00429-8]
RefSeq; NP_001265395.1; NM_001278466.1. [O00429-7]
RefSeq; NP_001317309.1; NM_001330380.1.
RefSeq; NP_005681.2; NM_005690.4. [O00429-4]
RefSeq; NP_036192.2; NM_012062.4. [O00429-1]
RefSeq; NP_036193.2; NM_012063.3. [O00429-3]
UniGene; Hs.556296; -.
PDB; 3W6N; X-ray; 2.00 A; A/B=1-329, A/B=709-736.
PDB; 3W6O; X-ray; 1.90 A; A/B=1-329, A/B=709-736.
PDB; 3W6P; X-ray; 1.70 A; A/B=1-329, A/B=709-736.
PDB; 4BEJ; X-ray; 3.48 A; A/B/C/D=1-736.
PDB; 4H1U; X-ray; 2.30 A; A=1-327, A=711-736.
PDB; 4H1V; X-ray; 2.30 A; A=1-327, A=711-736.
PDBsum; 3W6N; -.
PDBsum; 3W6O; -.
PDBsum; 3W6P; -.
PDBsum; 4BEJ; -.
PDBsum; 4H1U; -.
PDBsum; 4H1V; -.
ProteinModelPortal; O00429; -.
SMR; O00429; -.
BioGrid; 115370; 64.
CORUM; O00429; -.
DIP; DIP-42704N; -.
IntAct; O00429; 23.
MINT; MINT-1394198; -.
STRING; 9606.ENSP00000450399; -.
iPTMnet; O00429; -.
PhosphoSitePlus; O00429; -.
SwissPalm; O00429; -.
EPD; O00429; -.
MaxQB; O00429; -.
PaxDb; O00429; -.
PeptideAtlas; O00429; -.
PRIDE; O00429; -.
DNASU; 10059; -.
Ensembl; ENST00000266481; ENSP00000266481; ENSG00000087470. [O00429-4]
Ensembl; ENST00000381000; ENSP00000370388; ENSG00000087470. [O00429-8]
Ensembl; ENST00000414834; ENSP00000404160; ENSG00000087470. [O00429-7]
Ensembl; ENST00000452533; ENSP00000415131; ENSG00000087470. [O00429-3]
Ensembl; ENST00000547312; ENSP00000448610; ENSG00000087470. [O00429-2]
Ensembl; ENST00000549701; ENSP00000450399; ENSG00000087470. [O00429-1]
Ensembl; ENST00000553257; ENSP00000449089; ENSG00000087470. [O00429-6]
GeneID; 10059; -.
KEGG; hsa:10059; -.
UCSC; uc001rld.4; human. [O00429-1]
CTD; 10059; -.
DisGeNET; 10059; -.
EuPathDB; HostDB:ENSG00000087470.17; -.
GeneCards; DNM1L; -.
H-InvDB; HIX0010537; -.
HGNC; HGNC:2973; DNM1L.
HPA; CAB009952; -.
HPA; HPA039324; -.
MalaCards; DNM1L; -.
MIM; 603850; gene.
MIM; 614388; phenotype.
neXtProt; NX_O00429; -.
OpenTargets; ENSG00000087470; -.
Orphanet; 330050; Lethal encephalopathy due to mitochondrial and peroxisomal fission defect.
PharmGKB; PA27441; -.
eggNOG; KOG0446; Eukaryota.
eggNOG; COG0699; LUCA.
GeneTree; ENSGT00760000119213; -.
HOGENOM; HOG000161068; -.
HOVERGEN; HBG107833; -.
InParanoid; O00429; -.
KO; K17065; -.
OMA; HHIPNRR; -.
OrthoDB; EOG091G02TQ; -.
PhylomeDB; O00429; -.
TreeFam; TF352031; -.
Reactome; R-HSA-75153; Apoptotic execution phase.
SIGNOR; O00429; -.
ChiTaRS; DNM1L; human.
GeneWiki; DNM1L; -.
GenomeRNAi; 10059; -.
PMAP-CutDB; O00429; -.
PRO; PR:O00429; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000087470; -.
CleanEx; HS_DNM1L; -.
ExpressionAtlas; O00429; baseline and differential.
Genevisible; O00429; HS.
GO; GO:0005903; C:brush border; IEA:Ensembl.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:ParkinsonsUK-UCL.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IEA:Ensembl.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005874; C:microtubule; IDA:UniProtKB.
GO; GO:0015630; C:microtubule cytoskeleton; IEA:Ensembl.
GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0051433; F:BH2 domain binding; IEA:Ensembl.
GO; GO:0030276; F:clathrin binding; IEA:Ensembl.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0030742; F:GTP-dependent protein binding; IDA:ParkinsonsUK-UCL.
GO; GO:0005096; F:GTPase activator activity; IC:ParkinsonsUK-UCL.
GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0017137; F:Rab GTPase binding; IDA:ParkinsonsUK-UCL.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0090650; P:cellular response to oxygen-glucose deprivation; IEA:Ensembl.
GO; GO:1904579; P:cellular response to thapsigargin; IEA:Ensembl.
GO; GO:0003374; P:dynamin family protein polymerization involved in mitochondrial fission; IDA:UniProtKB.
GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
GO; GO:0097194; P:execution phase of apoptosis; TAS:Reactome.
GO; GO:0060047; P:heart contraction; IEA:Ensembl.
GO; GO:0048312; P:intracellular distribution of mitochondria; IMP:ParkinsonsUK-UCL.
GO; GO:0061025; P:membrane fusion; IDA:UniProtKB.
GO; GO:0000266; P:mitochondrial fission; IDA:UniProtKB.
GO; GO:0043653; P:mitochondrial fragmentation involved in apoptotic process; IMP:UniProtKB.
GO; GO:0090149; P:mitochondrial membrane fission; IDA:UniProtKB.
GO; GO:0070584; P:mitochondrion morphogenesis; IMP:MGI.
GO; GO:0007005; P:mitochondrion organization; IMP:ParkinsonsUK-UCL.
GO; GO:0070266; P:necroptotic process; IMP:UniProtKB.
GO; GO:0010637; P:negative regulation of mitochondrial fusion; IEA:Ensembl.
GO; GO:0016559; P:peroxisome fission; IDA:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; IEA:Ensembl.
GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB.
GO; GO:0090141; P:positive regulation of mitochondrial fission; IMP:ParkinsonsUK-UCL.
GO; GO:0050714; P:positive regulation of protein secretion; IDA:UniProtKB.
GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; IMP:UniProtKB.
GO; GO:1900244; P:positive regulation of synaptic vesicle endocytosis; IEA:Ensembl.
GO; GO:2000302; P:positive regulation of synaptic vesicle exocytosis; IEA:Ensembl.
GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
GO; GO:0070585; P:protein localization to mitochondrion; IEA:Ensembl.
GO; GO:0051259; P:protein oligomerization; IMP:UniProtKB.
GO; GO:1903578; P:regulation of ATP metabolic process; IEA:Ensembl.
GO; GO:0010821; P:regulation of mitochondrion organization; IMP:UniProtKB.
GO; GO:1903146; P:regulation of mitophagy; IGI:ParkinsonsUK-UCL.
GO; GO:1900063; P:regulation of peroxisome organization; IMP:UniProtKB.
GO; GO:0032459; P:regulation of protein oligomerization; IDA:UniProtKB.
GO; GO:0001836; P:release of cytochrome c from mitochondria; IMP:UniProtKB.
GO; GO:1905395; P:response to flavonoid; IEA:Ensembl.
GO; GO:1990910; P:response to hypobaric hypoxia; IEA:Ensembl.
GO; GO:0036466; P:synaptic vesicle recycling via endosome; IEA:Ensembl.
InterPro; IPR030556; DNM1L.
InterPro; IPR000375; Dynamin_central.
InterPro; IPR001401; Dynamin_GTPase.
InterPro; IPR019762; Dynamin_GTPase_CS.
InterPro; IPR022812; Dynamin_SF.
InterPro; IPR030381; G_DYNAMIN_dom.
InterPro; IPR003130; GED.
InterPro; IPR020850; GED_dom.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR11566; PTHR11566; 1.
PANTHER; PTHR11566:SF127; PTHR11566:SF127; 1.
Pfam; PF01031; Dynamin_M; 1.
Pfam; PF00350; Dynamin_N; 1.
Pfam; PF02212; GED; 1.
PRINTS; PR00195; DYNAMIN.
SMART; SM00053; DYNc; 1.
SMART; SM00302; GED; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS00410; G_DYNAMIN_1; 1.
PROSITE; PS51718; G_DYNAMIN_2; 1.
PROSITE; PS51388; GED; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cell junction;
Coated pit; Complete proteome; Cytoplasm; Cytoplasmic vesicle;
Disease mutation; Endocytosis; Glycoprotein; Golgi apparatus;
GTP-binding; Hydrolase; Isopeptide bond; Lipid-binding; Membrane;
Mitochondrion; Mitochondrion outer membrane; Necrosis;
Nucleotide-binding; Peroxisome; Phosphoprotein; Polymorphism;
Reference proteome; S-nitrosylation; Synapse; Ubl conjugation.
CHAIN 1 736 Dynamin-1-like protein.
/FTId=PRO_0000206566.
DOMAIN 22 302 Dynamin-type G.
DOMAIN 644 735 GED. {ECO:0000255|PROSITE-
ProRule:PRU00720}.
NP_BIND 32 40 GTP. {ECO:0000305|PubMed:23977156}.
NP_BIND 215 221 GTP. {ECO:0000305|PubMed:23977156}.
NP_BIND 246 249 GTP. {ECO:0000305|PubMed:23977156}.
REGION 1 343 GTPase domain.
REGION 344 489 Middle domain.
REGION 448 685 Interaction with GSK3B.
REGION 502 569 B domain.
REGION 654 668 Important for homodimerization.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895}.
MOD_RES 529 529 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 548 548 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 597 597 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8K1M6}.
MOD_RES 607 607 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 616 616 Phosphoserine; by CDK1.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:18838687,
ECO:0000269|PubMed:26122121}.
MOD_RES 637 637 Phosphoserine; by CAMK1 and PKA.
{ECO:0000269|PubMed:17553808,
ECO:0000269|PubMed:18695047,
ECO:0000269|PubMed:18838687,
ECO:0000269|PubMed:23283981,
ECO:0000269|PubMed:26122121}.
MOD_RES 644 644 S-nitrosocysteine.
{ECO:0000269|PubMed:19342591}.
CARBOHYD 585 585 O-linked (GlcNAc) threonine.
{ECO:0000250}.
CARBOHYD 586 586 O-linked (GlcNAc) threonine.
{ECO:0000250}.
CROSSLNK 532 532 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:19638400}.
CROSSLNK 535 535 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:19638400}.
CROSSLNK 558 558 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:19638400}.
CROSSLNK 568 568 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:19638400}.
CROSSLNK 594 594 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:19638400}.
CROSSLNK 597 597 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate.
CROSSLNK 606 606 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:19638400}.
CROSSLNK 608 608 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:19638400}.
VAR_SEQ 1 43 MEALIPVINKLQDVFNTVGADIIQLPQIVVVGTQSSGKSSV
LE -> MFHKKINGKQQEKKMTLLHGKTQDTFLKGWKQKNG
VNFFTPKI (in isoform 7).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054544.
VAR_SEQ 44 246 Missing (in isoform 7).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054545.
VAR_SEQ 83 83 N -> NDPATWKNSRHLSK (in isoform 6 and
isoform 8). {ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.6}.
/FTId=VSP_039097.
VAR_SEQ 533 569 Missing (in isoform 3).
{ECO:0000303|PubMed:10749171,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:9731200}.
/FTId=VSP_013685.
VAR_SEQ 533 558 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_013686.
VAR_SEQ 544 569 Missing (in isoform 5).
{ECO:0000303|PubMed:10749171}.
/FTId=VSP_013687.
VAR_SEQ 559 569 Missing (in isoform 4 and isoform 8).
{ECO:0000303|PubMed:10749171,
ECO:0000303|Ref.6}.
/FTId=VSP_013688.
VARIANT 71 71 S -> T (in dbSNP:rs1064610).
{ECO:0000269|PubMed:10749171,
ECO:0000269|PubMed:9570752,
ECO:0000269|PubMed:9731200}.
/FTId=VAR_022446.
VARIANT 362 362 G -> D (in EMPF1; unknown pathological
significance; presence of concentric
cristae and/or increased dense granules
in some mitochondria; dbSNP:rs879255685).
{ECO:0000269|PubMed:26604000}.
/FTId=VAR_076316.
VARIANT 362 362 G -> S (in EMPF1; the mutation acts in a
dominant-negative manner; defects
observed in mitochondrial fission;
significant decrease in mitochondrial
respiratory chain complex IV activity).
{ECO:0000269|PubMed:26992161}.
/FTId=VAR_076317.
VARIANT 395 395 A -> D (in EMPF1; the mutation acts in a
dominant-negative manner; defects
observed in both mitochondrial and
peroxisomal fission; reduced
oligomerization, decreased mitochondrial
recruitment; dbSNP:rs121908531).
{ECO:0000269|PubMed:17460227,
ECO:0000269|PubMed:27145208}.
/FTId=VAR_063704.
VARIANT 403 403 R -> C (in EMPF1; the mutation acts in a
dominant-negative manner; reduced
oligomerization; decreased mitochondrial
recruitment; defects observed in
mitochondrial fission;
dbSNP:rs863223953).
{ECO:0000269|PubMed:27145208}.
/FTId=VAR_076318.
VARIANT 426 426 E -> D (in dbSNP:rs2389105).
/FTId=VAR_030489.
MUTAGEN 34 34 Q->A: Abolishes GTP hydrolysis.
{ECO:0000269|PubMed:23977156}.
MUTAGEN 38 38 K->A: Loss of GTPase activity. Impairs
mitochondrial division and induces
changes in peroxisome morphology. No
effect on oligomerization. Increase in
sumoylation by SUMO3.
{ECO:0000269|PubMed:11514614,
ECO:0000269|PubMed:12499366,
ECO:0000269|PubMed:15208300,
ECO:0000269|PubMed:19638400,
ECO:0000269|PubMed:23977156,
ECO:0000269|PubMed:9570752}.
MUTAGEN 38 38 K->E: Overexpression delays protein
secretion. {ECO:0000269|PubMed:11514614,
ECO:0000269|PubMed:12499366,
ECO:0000269|PubMed:15208300,
ECO:0000269|PubMed:19638400,
ECO:0000269|PubMed:23977156,
ECO:0000269|PubMed:9570752}.
MUTAGEN 39 39 S->A: Abolishes GTP hydrolysis.
{ECO:0000269|PubMed:12618434,
ECO:0000269|PubMed:23977156,
ECO:0000269|PubMed:9422767}.
MUTAGEN 39 39 S->I: Decreased localization to the
perinuclear region.
{ECO:0000269|PubMed:12618434,
ECO:0000269|PubMed:23977156,
ECO:0000269|PubMed:9422767}.
MUTAGEN 39 39 S->N: Reduces peroxisomal abundance.
{ECO:0000269|PubMed:12618434,
ECO:0000269|PubMed:23977156,
ECO:0000269|PubMed:9422767}.
MUTAGEN 41 41 V->F: Temperature-sensitive. Impairs
mitochondrial division.
{ECO:0000269|PubMed:11514614}.
MUTAGEN 59 59 T->A: Abolishes GTP hydrolysis. Impairs
mitochondrial division. Reduces
peroxisomal abundance.
{ECO:0000269|PubMed:11514614,
ECO:0000269|PubMed:12618434,
ECO:0000269|PubMed:23977156}.
MUTAGEN 146 146 D->A: Abolishes GTP hydrolysis.
{ECO:0000269|PubMed:23977156}.
MUTAGEN 149 149 G->A: Abolishes GTP hydrolysis.
{ECO:0000269|PubMed:23977156}.
MUTAGEN 216 216 K->A: Abolishes GTP hydrolysis.
{ECO:0000269|PubMed:23977156}.
MUTAGEN 218 218 D->A: Abolishes GTP hydrolysis.
{ECO:0000269|PubMed:23977156}.
MUTAGEN 281 281 G->D: Temperature-sensitive. Impairs
mitochondrial division.
{ECO:0000269|PubMed:11514614}.
MUTAGEN 300 300 C->A: No effect on S-nitrosylation.
{ECO:0000269|PubMed:19342591}.
MUTAGEN 345 345 C->A: No effect on S-nitrosylation.
{ECO:0000269|PubMed:19342591}.
MUTAGEN 361 361 C->A: No effect on S-nitrosylation.
{ECO:0000269|PubMed:19342591}.
MUTAGEN 367 367 C->A: No effect on S-nitrosylation.
{ECO:0000269|PubMed:19342591}.
MUTAGEN 401 404 GPRP->AAAA: Impairs formation of higher
order oligomers, but not
homodimerization.
{ECO:0000269|PubMed:23584531}.
MUTAGEN 431 431 C->A: No effect on S-nitrosylation.
{ECO:0000269|PubMed:19342591}.
MUTAGEN 446 446 C->A: No effect on S-nitrosylation.
{ECO:0000269|PubMed:19342591}.
MUTAGEN 470 470 C->A: No effect on S-nitrosylation.
{ECO:0000269|PubMed:19342591}.
MUTAGEN 490 490 E->A: Does not impair homodimerization
and formation of higher order oligomers.
{ECO:0000269|PubMed:23584531}.
MUTAGEN 490 490 E->R: Impairs homodimerization and
formation of higher order oligomers.
{ECO:0000269|PubMed:23584531}.
MUTAGEN 505 505 C->A: No effect on S-nitrosylation.
{ECO:0000269|PubMed:19342591}.
MUTAGEN 532 532 K->R: Some loss of sumoylation in B
domain. Complete loss of sumoylation in B
domain; when associated with R-535; R-558
and R-568. {ECO:0000269|PubMed:19638400}.
MUTAGEN 535 535 K->R: Some loss of sumoylation in B
domain. Complete loss of sumoylation in B
domain; when associated with R-532; R-558
and R-568. {ECO:0000269|PubMed:19638400}.
MUTAGEN 558 558 K->R: Some loss of sumoylation in B
domain. Complete loss of sumoylation in B
domain; when associated with R-532; R-535
and R-568. {ECO:0000269|PubMed:19638400}.
MUTAGEN 568 568 K->R: Some loss of sumoylation in B
domain. Complete loss of sumoylation in B
domain; when associated with R-532; R-535
and R-558. {ECO:0000269|PubMed:19638400}.
MUTAGEN 594 594 K->R: Some loss of sumoylation in the GED
domain; Complete loss of sumoylation in
the GED domain; when associated with R-
597; R-606 and R-608.
{ECO:0000269|PubMed:19638400}.
MUTAGEN 597 597 K->R: Some loss of sumoylation in the GED
domain; Complete loss of sumoylation in
the GED domain; when associated with R-
594; R-606 and R-608.
{ECO:0000269|PubMed:19638400}.
MUTAGEN 606 606 K->R: Some loss of sumoylation in the GED
domain; Complete loss of sumoylation in
the GED domain; when associated with R-
594; R-597 and R-608.
{ECO:0000269|PubMed:19638400}.
MUTAGEN 608 608 K->R: Some loss of sumoylation in the GED
domain; Complete loss of sumoylation in
the GED domain; when associated with R-
594; R-597 and R-606.
{ECO:0000269|PubMed:19638400}.
MUTAGEN 616 616 S->A: Little effect on mitochondrial
morphology. Translocated to mitochondria.
{ECO:0000269|PubMed:18838687}.
MUTAGEN 637 637 S->A: Abolishes phosphorylation. Reduces
interaction with MIEF1 and MIEF2.
Promotes mitochondrial fission and cell
vulnerability to apoptotic insults.
Mostly mitochondrial. Disrupts, in vitro,
binding to FIS1.
{ECO:0000269|PubMed:17553808,
ECO:0000269|PubMed:18695047,
ECO:0000269|PubMed:18838687,
ECO:0000269|PubMed:23283981}.
MUTAGEN 637 637 S->D: Impairs intramolecular, but not
intermolecular interactions. Slight
reduction in GTPase activity. Does not
reduce interaction with MIEF1 and MIEF2.
Inhibits mitochondrial fission. Retained
in cytoplasm.
{ECO:0000269|PubMed:17553808,
ECO:0000269|PubMed:18695047,
ECO:0000269|PubMed:18838687,
ECO:0000269|PubMed:23283981}.
MUTAGEN 644 644 C->A: Abolishes S-nitrosylation. Reduced
dimerization and no enhancement of GTPase
activity. {ECO:0000269|PubMed:19342591}.
MUTAGEN 668 668 K->A: Abolishes homodimerization and
formation of higher order oligomers.
{ECO:0000269|PubMed:23584531}.
MUTAGEN 679 679 K->A: Diminishes intermolecular
interaction between GTP-middle domain and
GED domain but no effect on
oligomerization. Marked reduction in
GTPase activity, in vitro. Decreased
mitochondrial division.
{ECO:0000269|PubMed:15208300}.
CONFLICT 208 208 R -> C (in Ref. 2; AAC35283 and 4;
AAD39541). {ECO:0000305}.
HELIX 5 18 {ECO:0000244|PDB:3W6P}.
TURN 21 23 {ECO:0000244|PDB:4H1U}.
STRAND 27 31 {ECO:0000244|PDB:3W6P}.
HELIX 34 36 {ECO:0000244|PDB:4BEJ}.
HELIX 38 44 {ECO:0000244|PDB:3W6P}.
STRAND 55 57 {ECO:0000244|PDB:3W6P}.
STRAND 63 69 {ECO:0000244|PDB:3W6P}.
STRAND 86 88 {ECO:0000244|PDB:4H1U}.
STRAND 90 93 {ECO:0000244|PDB:3W6P}.
HELIX 94 96 {ECO:0000244|PDB:3W6P}.
HELIX 104 119 {ECO:0000244|PDB:3W6P}.
STRAND 121 123 {ECO:0000244|PDB:3W6P}.
STRAND 130 136 {ECO:0000244|PDB:3W6P}.
STRAND 141 146 {ECO:0000244|PDB:3W6P}.
HELIX 155 157 {ECO:0000244|PDB:4H1U}.
HELIX 162 174 {ECO:0000244|PDB:3W6P}.
STRAND 179 186 {ECO:0000244|PDB:3W6P}.
HELIX 191 193 {ECO:0000244|PDB:3W6P}.
HELIX 195 203 {ECO:0000244|PDB:3W6P}.
STRAND 205 207 {ECO:0000244|PDB:4H1U}.
STRAND 210 215 {ECO:0000244|PDB:3W6P}.
HELIX 217 219 {ECO:0000244|PDB:3W6P}.
STRAND 222 225 {ECO:0000244|PDB:4BEJ}.
HELIX 227 230 {ECO:0000244|PDB:3W6P}.
STRAND 233 235 {ECO:0000244|PDB:3W6P}.
STRAND 237 239 {ECO:0000244|PDB:4H1V}.
STRAND 241 243 {ECO:0000244|PDB:3W6P}.
HELIX 249 253 {ECO:0000244|PDB:3W6P}.
HELIX 258 272 {ECO:0000244|PDB:3W6P}.
TURN 274 276 {ECO:0000244|PDB:3W6P}.
HELIX 277 279 {ECO:0000244|PDB:3W6P}.
HELIX 282 317 {ECO:0000244|PDB:3W6P}.
HELIX 336 353 {ECO:0000244|PDB:3W6P}.
HELIX 363 371 {ECO:0000244|PDB:4BEJ}.
HELIX 373 380 {ECO:0000244|PDB:4BEJ}.
HELIX 389 399 {ECO:0000244|PDB:4BEJ}.
HELIX 409 420 {ECO:0000244|PDB:4BEJ}.
HELIX 421 424 {ECO:0000244|PDB:4BEJ}.
HELIX 425 440 {ECO:0000244|PDB:4BEJ}.
TURN 441 443 {ECO:0000244|PDB:4BEJ}.
HELIX 444 446 {ECO:0000244|PDB:4BEJ}.
HELIX 458 493 {ECO:0000244|PDB:4BEJ}.
HELIX 501 504 {ECO:0000244|PDB:4BEJ}.
HELIX 650 653 {ECO:0000244|PDB:3W6N}.
TURN 655 657 {ECO:0000244|PDB:3W6N}.
HELIX 658 660 {ECO:0000244|PDB:3W6N}.
HELIX 663 692 {ECO:0000244|PDB:3W6N}.
HELIX 695 699 {ECO:0000244|PDB:4H1U}.
HELIX 712 732 {ECO:0000244|PDB:3W6N}.
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


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PC-Drp Dynamin related protein 1, WB control 100-150ul
LF-MA10088 anti-Dynamin 2 (6C9), Mouse monoclonal to Dynamin 2, Isotype IgG1, Host Mouse 100 ug
LF-PA41410 anti-Dynamin 1, Rabbit polyclonal to Dynamin 1, Isotype IgG, Host Rabbit 100 ul
P-Drp Dynamin related protein 1, Antigen blocking peptide 100ul
AO1089a Dynamin-2 Antibody Mouse Monoclonal Antibody to Dynamin-2 Applications WB, IHC, E 0.1ml
251634-22-7 Dynamin inhibitory peptide, myristoylated Dynamin inhibitory pept 1g
AO1062a Dynamin-1 Antibody Mouse Monoclonal Antibody to Dynamin-1 Applications WB, IHC, E 0.1ml


 

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