DYN2_HUMAN
ID DYN2_HUMAN Reviewed; 870 AA.
AC P50570; A8K1B6; E7EV30; E9PEQ4; K7ESI9; Q5I0Y0; Q7Z5S3; Q9UPH4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 223.
DE RecName: Full=Dynamin-2;
DE EC=3.6.5.5;
GN Name=DNM2; Synonyms=DYN2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX PubMed=7590285; DOI=10.1016/0378-1119(95)00275-b;
RA Diatloff-Zito C., Gordon A.J.E., Duchaud E., Merlin G.;
RT "Isolation of an ubiquitously expressed cDNA encoding human dynamin II, a
RT member of the large GTP-binding protein family.";
RL Gene 163:301-306(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5).
RC TISSUE=Astrocyte, and Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Ovary, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH SHANK PROTEINS.
RX PubMed=11583995; DOI=10.1074/jbc.m104927200;
RA Okamoto P.M., Gamby C., Wells D., Fallon J., Vallee R.B.;
RT "Dynamin isoform-specific interaction with the shank/ProSAP scaffolding
RT proteins of the postsynaptic density and actin cytoskeleton.";
RL J. Biol. Chem. 276:48458-48465(2001).
RN [6]
RP FUNCTION IN CYTOKINESIS, AND SUBCELLULAR LOCATION.
RX PubMed=12498685; DOI=10.1016/s0960-9822(02)01390-8;
RA Thompson H.M., Skop A.R., Euteneuer U., Meyer B.J., McNiven M.A.;
RT "The large GTPase dynamin associates with the spindle midzone and is
RT required for cytokinesis.";
RL Curr. Biol. 12:2111-2117(2002).
RN [7]
RP INTERACTION WITH SH3BP4.
RX PubMed=16325581; DOI=10.1016/j.cell.2005.10.021;
RA Tosoni D., Puri C., Confalonieri S., Salcini A.E., De Camilli P.,
RA Tacchetti C., Di Fiore P.P.;
RT "TTP specifically regulates the internalization of the transferrin
RT receptor.";
RL Cell 123:875-888(2005).
RN [8]
RP INTERACTION WITH NOSTRIN.
RX PubMed=16234328; DOI=10.1242/jcs.02620;
RA Icking A., Matt S., Opitz N., Wiesenthal A., Mueller-Esterl W.,
RA Schilling K.;
RT "NOSTRIN functions as a homotrimeric adaptor protein facilitating
RT internalization of eNOS.";
RL J. Cell Sci. 118:5059-5069(2005).
RN [9]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SNX9.
RX PubMed=15703209; DOI=10.1091/mbc.e04-11-1016;
RA Soulet F., Yarar D., Leonard M., Schmid S.L.;
RT "SNX9 regulates dynamin assembly and is required for efficient clathrin-
RT mediated endocytosis.";
RL Mol. Biol. Cell 16:2058-2067(2005).
RN [10]
RP INTERACTION WITH MYO1E.
RX PubMed=17257598; DOI=10.1016/j.febslet.2007.01.021;
RA Krendel M., Osterweil E.K., Mooseker M.S.;
RT "Myosin 1E interacts with synaptojanin-1 and dynamin and is involved in
RT endocytosis.";
RL FEBS Lett. 581:644-650(2007).
RN [11]
RP INTERACTION WITH BIN1.
RX PubMed=17676042; DOI=10.1038/ng2086;
RA Nicot A.-S., Toussaint A., Tosch V., Kretz C., Wallgren-Pettersson C.,
RA Iwarsson E., Kingston H., Garnier J.-M., Biancalana V., Oldfors A.,
RA Mandel J.-L., Laporte J.;
RT "Mutations in amphiphysin 2 (BIN1) disrupt interaction with dynamin 2 and
RT cause autosomal recessive centronuclear myopathy.";
RL Nat. Genet. 39:1134-1139(2007).
RN [12]
RP INTERACTION WITH SNX33.
RX PubMed=18353773; DOI=10.1074/jbc.m801531200;
RA Schobel S., Neumann S., Hertweck M., Dislich B., Kuhn P.H., Kremmer E.,
RA Seed B., Baumeister R., Haass C., Lichtenthaler S.F.;
RT "A novel sorting nexin modulates endocytic trafficking and alpha-secretase
RT cleavage of the amyloid precursor protein.";
RL J. Biol. Chem. 283:14257-14268(2008).
RN [13]
RP INTERACTION WITH PSTPIP1.
RX PubMed=18480402; DOI=10.1091/mbc.e08-02-0225;
RA Cooper K.M., Bennin D.A., Huttenlocher A.;
RT "The PCH family member proline-serine-threonine phosphatase-interacting
RT protein 1 targets to the leukocyte uropod and regulates directed cell
RT migration.";
RL Mol. Biol. Cell 19:3180-3191(2008).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-598, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP INTERACTION WITH CTNND2.
RX PubMed=22022388; DOI=10.1371/journal.pone.0025379;
RA Koutras C., Levesque G.;
RT "Identification of novel NPRAP/delta-catenin-interacting proteins and the
RT direct association of NPRAP with dynamin 2.";
RL PLoS ONE 6:E25379-E25379(2011).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-755, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [22]
RP INTERACTION WITH SNX18.
RX PubMed=29437695; DOI=10.15252/embr.201744837;
RA Soereng K., Munson M.J., Lamb C.A., Bjoerndal G.T., Pankiv S.,
RA Carlsson S.R., Tooze S.A., Simonsen A.;
RT "SNX18 regulates ATG9A trafficking from recycling endosomes by recruiting
RT Dynamin-2.";
RL EMBO Rep. 19:0-0(2018).
RN [23]
RP FUNCTION.
RX PubMed=33713620; DOI=10.1016/j.cell.2021.02.053;
RA Yeung M.L., Teng J.L.L., Jia L., Zhang C., Huang C., Cai J.P., Zhou R.,
RA Chan K.H., Zhao H., Zhu L., Siu K.L., Fung S.Y., Yung S., Chan T.M.,
RA To K.K., Chan J.F., Cai Z., Lau S.K.P., Chen Z., Jin D.Y., Woo P.C.Y.,
RA Yuen K.Y.;
RT "Soluble ACE2-mediated cell entry of SARS-CoV-2 via interaction with
RT proteins related to the renin-angiotensin system.";
RL Cell 0:0-0(2021).
RN [24]
RP STRUCTURE BY NMR OF 514-625.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the PH domain of dynamin-2 from human.";
RL Submitted (APR-2008) to the PDB data bank.
RN [25]
RP VARIANTS CMTDIB 555-ASP--GLU-557 DEL; LYS-562 DEL AND GLU-562, AND
RP CHARACTERIZATION OF VARIANT CMTDIB 555-ASP--GLU-557 DEL.
RX PubMed=15731758; DOI=10.1038/ng1514;
RA Zuechner S., Noureddine M., Kennerson M., Verhoeven K., Claeys K.,
RA De Jonghe P., Merory J., Oliveira S.A., Speer M.C., Stenger J.E.,
RA Walizada G., Zhu D., Pericak-Vance M.A., Nicholson G., Timmerman V.,
RA Vance J.M.;
RT "Mutations in the pleckstrin homology domain of dynamin 2 cause dominant
RT intermediate Charcot-Marie-Tooth disease.";
RL Nat. Genet. 37:289-294(2005).
RN [26]
RP VARIANTS CNM1 LYS-368; TRP-369; GLN-369 AND TRP-465, AND CHARACTERIZATION
RP OF VARIANTS CNM1 TRP-369 AND TRP-465.
RX PubMed=16227997; DOI=10.1038/ng1657;
RA Bitoun M., Maugenre S., Jeannet P.-Y., Lacene E., Ferrer X., Laforet P.,
RA Martin J.-J., Laporte J., Lochmueller H., Beggs A.H., Fardeau M.,
RA Eymard B., Romero N.B., Guicheney P.;
RT "Mutations in dynamin 2 cause dominant centronuclear myopathy.";
RL Nat. Genet. 37:1207-1209(2005).
RN [27]
RP VARIANTS CNM1 THR-618; LEU-619; TRP-619 AND VAL-625 DEL.
RX PubMed=17932957; DOI=10.1002/ana.21235;
RA Bitoun M., Bevilacqua J.A., Prudhon B., Maugenre S., Taratuto A.L.,
RA Monges S., Lubieniecki F., Cances C., Uro-Coste E., Mayer M., Fardeau M.,
RA Romero N.B., Guicheney P.;
RT "Dynamin 2 mutations cause sporadic centronuclear myopathy with neonatal
RT onset.";
RL Ann. Neurol. 62:666-670(2007).
RN [28]
RP VARIANTS CMT2M CYS-537 AND HIS-570.
RX PubMed=17636067; DOI=10.1212/01.wnl.0000265820.51075.61;
RA Fabrizi G.M., Ferrarini M., Cavallaro T., Cabrini I., Cerini R.,
RA Bertolasi L., Rizzuto N.;
RT "Two novel mutations in dynamin-2 cause axonal Charcot-Marie-Tooth
RT disease.";
RL Neurology 69:291-295(2007).
RN [29]
RP VARIANT CNM1 GLN-368.
RX PubMed=17825552; DOI=10.1016/j.nmd.2007.06.467;
RA Echaniz-Laguna A., Nicot A.S., Carre S., Franques J., Tranchant C.,
RA Dondaine N., Biancalana V., Mandel J.L., Laporte J.;
RT "Subtle central and peripheral nervous system abnormalities in a family
RT with centronuclear myopathy and a novel dynamin 2 gene mutation.";
RL Neuromuscul. Disord. 17:955-959(2007).
RN [30]
RP VARIANT CMT2M ARG-358.
RX PubMed=18560793; DOI=10.1007/s00415-008-0808-8;
RA Gallardo E., Claeys K.G., Nelis E., Garcia A., Canga A., Combarros O.,
RA Timmerman V., De Jonghe P., Berciano J.;
RT "Magnetic resonance imaging findings of leg musculature in Charcot-Marie-
RT Tooth disease type 2 due to dynamin 2 mutation.";
RL J. Neurol. 255:986-992(2008).
RN [31]
RP VARIANT CNM1 LYS-650, CHARACTERIZATION OF VARIANTS CNM1 TRP-465; VAL-625
RP DEL AND LYS-650, CHARACTERIZATION OF VARIANT CMTDIB GLU-562, AND
RP PATHOPHYSIOLOGICAL PATHWAY IN THE AUTOSOMAL FORMS OF CNM AND DNM2-CMT
RP NEUROPATHY.
RX PubMed=19623537; DOI=10.1002/humu.21086;
RA Bitoun M., Durieux A.-C., Prudhon B., Bevilacqua J.A., Herledan A.,
RA Sakanyan V., Urtizberea A., Cartier L., Romero N.B., Guicheney P.;
RT "Dynamin 2 mutations associated with human diseases impair clathrin-
RT mediated receptor endocytosis.";
RL Hum. Mutat. 30:1419-1427(2009).
RN [32]
RP VARIANT CNM1 LYS-560.
RX PubMed=19122038; DOI=10.1212/01.wnl.0000338624.25852.12;
RA Bitoun M., Bevilacqua J.A., Eymard B., Prudhon B., Fardeau M.,
RA Guicheney P., Romero N.B.;
RT "A new centronuclear myopathy phenotype due to a novel dynamin 2
RT mutation.";
RL Neurology 72:93-95(2009).
RN [33]
RP VARIANT CNM1 PRO-621.
RX PubMed=19932620; DOI=10.1016/j.nmd.2009.10.005;
RA Jungbluth H., Cullup T., Lillis S., Zhou H., Abbs S., Sewry C., Muntoni F.;
RT "Centronuclear myopathy with cataracts due to a novel dynamin 2 (DNM2)
RT mutation.";
RL Neuromuscul. Disord. 20:49-52(2010).
RN [34]
RP VARIANT CNM1 ASP-618.
RX PubMed=19932619; DOI=10.1016/j.nmd.2009.10.006;
RA Melberg A., Kretz C., Kalimo H., Wallgren-Pettersson C., Toussaint A.,
RA Bohm J., Stalberg E., Laporte J.;
RT "Adult course in dynamin 2 dominant centronuclear myopathy with neonatal
RT onset.";
RL Neuromuscul. Disord. 20:53-56(2010).
RN [35]
RP VARIANTS CNM1 LYS-368; TRP-465; HIS-522; THR-618; LEU-619 AND HIS-627.
RX PubMed=20227276; DOI=10.1016/j.nmd.2010.02.016;
RA Susman R.D., Quijano-Roy S., Yang N., Webster R., Clarke N.F., Dowling J.,
RA Kennerson M., Nicholson G., Biancalana V., Ilkovski B., Flanigan K.M.,
RA Arbuckle S., Malladi C., Robinson P., Vucic S., Mayer M., Romero N.B.,
RA Urtizberea J.A., Garcia-Bragado F., Guicheney P., Bitoun M., Carlier R.Y.,
RA North K.N.;
RT "Expanding the clinical, pathological and MRI phenotype of DNM2-related
RT centronuclear myopathy.";
RL Neuromuscul. Disord. 20:229-237(2010).
RN [36]
RP VARIANTS CNM1 CYS-522; GLY-523 AND ARG-627.
RX PubMed=22396310; DOI=10.1002/humu.22067;
RA Bohm J., Biancalana V., Dechene E.T., Bitoun M., Pierson C.R., Schaefer E.,
RA Karasoy H., Dempsey M.A., Klein F., Dondaine N., Kretz C., Haumesser N.,
RA Poirson C., Toussaint A., Greenleaf R.S., Barger M.A., Mahoney L.J.,
RA Kang P.B., Zanoteli E., Vissing J., Witting N., Echaniz-Laguna A.,
RA Wallgren-Pettersson C., Dowling J., Merlini L., Oldfors A.,
RA Bomme Ousager L., Melki J., Krause A., Jern C., Oliveira A.S., Petit F.,
RA Jacquette A., Chaussenot A., Mowat D., Leheup B., Cristofano M.,
RA Poza Aldea J.J., Michel F., Furby A., Llona J.E., Van Coster R.,
RA Bertini E., Urtizberea J.A., Drouin-Garraud V., Beroud C., Prudhon B.,
RA Bedford M., Mathews K., Erby L.A., Smith S.A., Roggenbuck J., Crowe C.A.,
RA Brennan Spitale A., Johal S.C., Amato A.A., Demmer L.A., Jonas J.,
RA Darras B.T., Bird T.D., Laurino M., Welt S.I., Trotter C., Guicheney P.,
RA Das S., Mandel J.L., Beggs A.H., Laporte J.;
RT "Mutation spectrum in the large GTPase dynamin 2, and genotype-phenotype
RT correlation in autosomal dominant centronuclear myopathy.";
RL Hum. Mutat. 33:949-959(2012).
RN [37]
RP VARIANT LCCS5 VAL-379.
RX PubMed=23092955; DOI=10.1038/ejhg.2012.226;
RA Koutsopoulos O.S., Kretz C., Weller C.M., Roux A., Mojzisova H., Boehm J.,
RA Koch C., Toussaint A., Heckel E., Stemkens D., Ter Horst S.A., Thibault C.,
RA Koch M., Mehdi S.Q., Bijlsma E.K., Mandel J.L., Vermot J., Laporte J.;
RT "Dynamin 2 homozygous mutation in humans with a lethal congenital
RT syndrome.";
RL Eur. J. Hum. Genet. 21:637-642(2013).
CC -!- FUNCTION: Microtubule-associated force-producing protein involved in
CC producing microtubule bundles and able to bind and hydrolyze GTP. Plays
CC a role in the regulation of neuron morphology, axon growth and
CC formation of neuronal growth cones (By similarity). Plays an important
CC role in vesicular trafficking processes, in particular endocytosis
CC (PubMed:33713620). Involved in cytokinesis (PubMed:12498685). Regulates
CC maturation of apoptotic cell corpse-containing phagosomes by recruiting
CC PIK3C3 to the phagosome membrane (By similarity).
CC {ECO:0000250|UniProtKB:P39052, ECO:0000250|UniProtKB:P39054,
CC ECO:0000269|PubMed:12498685, ECO:0000269|PubMed:33713620}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.5;
CC -!- SUBUNIT: Interacts with MYOF (By similarity). Interacts with CTTN and
CC ACTN1 (By similarity). Interacts with SHANK1, SHANK2, SH3BP4 and
CC NOSTRIN. Interacts with SNX9 (PubMed:15703209). Interacts with SNX18
CC (PubMed:29437695). Interacts with SNX33 (via SH3 domain)
CC (PubMed:18353773). Interacts with MYO1E (via SH3 domain)
CC (PubMed:17257598). Interacts with PSTPIP1 (PubMed:18480402). Interacts
CC with CTNND2 (PubMed:22022388). May interact with PIK3C3 (By
CC similarity). May be a component of a complex composed of RAB5A (in GDP-
CC bound form), DYN2 and PIK3C3 (By similarity). Interacts with BIN1
CC (PubMed:17676042). {ECO:0000250|UniProtKB:P39052,
CC ECO:0000250|UniProtKB:P39054, ECO:0000269|PubMed:11583995,
CC ECO:0000269|PubMed:15703209, ECO:0000269|PubMed:16234328,
CC ECO:0000269|PubMed:16325581, ECO:0000269|PubMed:17257598,
CC ECO:0000269|PubMed:17676042, ECO:0000269|PubMed:18353773,
CC ECO:0000269|PubMed:18480402, ECO:0000269|PubMed:22022388,
CC ECO:0000269|PubMed:29437695}.
CC -!- INTERACTION:
CC P50570; Q8N157: AHI1; NbExp=2; IntAct=EBI-346547, EBI-1049056;
CC P50570; O95817: BAG3; NbExp=3; IntAct=EBI-346547, EBI-747185;
CC P50570; Q14247: CTTN; NbExp=5; IntAct=EBI-346547, EBI-351886;
CC P50570; Q8NFF5-2: FLAD1; NbExp=3; IntAct=EBI-346547, EBI-11526128;
CC P50570; P62993: GRB2; NbExp=8; IntAct=EBI-346547, EBI-401755;
CC P50570; Q15811: ITSN1; NbExp=2; IntAct=EBI-346547, EBI-602041;
CC P50570; Q12965: MYO1E; NbExp=2; IntAct=EBI-346547, EBI-4279548;
CC P50570; P22392: NME2; NbExp=2; IntAct=EBI-346547, EBI-713693;
CC P50570; Q9UNF0: PACSIN2; NbExp=4; IntAct=EBI-346547, EBI-742503;
CC P50570; P54646: PRKAA2; NbExp=3; IntAct=EBI-346547, EBI-1383852;
CC P50570; P47897: QARS1; NbExp=3; IntAct=EBI-346547, EBI-347462;
CC P50570; O76064: RNF8; NbExp=3; IntAct=EBI-346547, EBI-373337;
CC P50570; O00560: SDCBP; NbExp=3; IntAct=EBI-346547, EBI-727004;
CC P50570; Q15436: SEC23A; NbExp=3; IntAct=EBI-346547, EBI-81088;
CC P50570; Q9P0V3: SH3BP4; NbExp=3; IntAct=EBI-346547, EBI-1049513;
CC P50570; Q99962: SH3GL2; NbExp=2; IntAct=EBI-346547, EBI-77938;
CC P50570; Q96B97: SH3KBP1; NbExp=5; IntAct=EBI-346547, EBI-346595;
CC P50570; Q9Y5X1: SNX9; NbExp=4; IntAct=EBI-346547, EBI-77848;
CC P50570; Q9BUZ4: TRAF4; NbExp=3; IntAct=EBI-346547, EBI-3650647;
CC P50570; P57075-2: UBASH3A; NbExp=3; IntAct=EBI-346547, EBI-7353612;
CC P50570; Q9QPN3: nef; Xeno; NbExp=4; IntAct=EBI-346547, EBI-7355146;
CC P50570-2; Q9H7C9: AAMDC; NbExp=3; IntAct=EBI-10968534, EBI-10308705;
CC P50570-2; Q6PCB6: ABHD17C; NbExp=3; IntAct=EBI-10968534, EBI-22011868;
CC P50570-2; Q9NP61: ARFGAP3; NbExp=3; IntAct=EBI-10968534, EBI-2875816;
CC P50570-2; Q86TN1: ARNT2; NbExp=3; IntAct=EBI-10968534, EBI-25844820;
CC P50570-2; Q9NWX5-2: ASB6; NbExp=3; IntAct=EBI-10968534, EBI-25838672;
CC P50570-2; Q96FT7-4: ASIC4; NbExp=3; IntAct=EBI-10968534, EBI-9089489;
CC P50570-2; Q8WXF7: ATL1; NbExp=3; IntAct=EBI-10968534, EBI-2410266;
CC P50570-2; Q9UII2: ATP5IF1; NbExp=3; IntAct=EBI-10968534, EBI-718459;
CC P50570-2; P54252: ATXN3; NbExp=3; IntAct=EBI-10968534, EBI-946046;
CC P50570-2; Q9UQB8-6: BAIAP2; NbExp=3; IntAct=EBI-10968534, EBI-9092016;
CC P50570-2; Q9UMX3: BOK; NbExp=3; IntAct=EBI-10968534, EBI-7105206;
CC P50570-2; Q8WUW1: BRK1; NbExp=3; IntAct=EBI-10968534, EBI-2837444;
CC P50570-2; Q5JTY5: CBWD3; NbExp=3; IntAct=EBI-10968534, EBI-723434;
CC P50570-2; P83916: CBX1; NbExp=3; IntAct=EBI-10968534, EBI-78129;
CC P50570-2; Q53EZ4: CEP55; NbExp=3; IntAct=EBI-10968534, EBI-747776;
CC P50570-2; Q96FZ7: CHMP6; NbExp=3; IntAct=EBI-10968534, EBI-1049648;
CC P50570-2; Q9NSE2: CISH; NbExp=3; IntAct=EBI-10968534, EBI-617866;
CC P50570-2; Q92478: CLEC2B; NbExp=3; IntAct=EBI-10968534, EBI-13350535;
CC P50570-2; Q16740: CLPP; NbExp=3; IntAct=EBI-10968534, EBI-1056029;
CC P50570-2; P04141: CSF2; NbExp=3; IntAct=EBI-10968534, EBI-1809826;
CC P50570-2; Q9NR90-2: DAZ3; NbExp=3; IntAct=EBI-10968534, EBI-25830216;
CC P50570-2; Q9H816: DCLRE1B; NbExp=3; IntAct=EBI-10968534, EBI-3508943;
CC P50570-2; Q9UHI6: DDX20; NbExp=3; IntAct=EBI-10968534, EBI-347658;
CC P50570-2; Q14154: DELE1; NbExp=3; IntAct=EBI-10968534, EBI-2805660;
CC P50570-2; Q9H147: DNTTIP1; NbExp=3; IntAct=EBI-10968534, EBI-2795449;
CC P50570-2; Q9UI08-2: EVL; NbExp=3; IntAct=EBI-10968534, EBI-6448852;
CC P50570-2; Q99504: EYA3; NbExp=3; IntAct=EBI-10968534, EBI-9089567;
CC P50570-2; Q6SJ93: FAM111B; NbExp=3; IntAct=EBI-10968534, EBI-6309082;
CC P50570-2; Q9UKA2: FBXL4; NbExp=3; IntAct=EBI-10968534, EBI-2869903;
CC P50570-2; Q6P3S6: FBXO42; NbExp=3; IntAct=EBI-10968534, EBI-2506081;
CC P50570-2; Q9UHY8: FEZ2; NbExp=3; IntAct=EBI-10968534, EBI-396453;
CC P50570-2; Q9Y261-2: FOXA2; NbExp=3; IntAct=EBI-10968534, EBI-25830360;
CC P50570-2; Q6PIV2: FOXR1; NbExp=3; IntAct=EBI-10968534, EBI-10253815;
CC P50570-2; P02792: FTL; NbExp=3; IntAct=EBI-10968534, EBI-713279;
CC P50570-2; P06241-3: FYN; NbExp=3; IntAct=EBI-10968534, EBI-10691738;
CC P50570-2; Q9ULV1: FZD4; NbExp=3; IntAct=EBI-10968534, EBI-2466380;
CC P50570-2; Q9H4A5: GOLPH3L; NbExp=3; IntAct=EBI-10968534, EBI-4403434;
CC P50570-2; Q13588: GRAP; NbExp=3; IntAct=EBI-10968534, EBI-2847510;
CC P50570-2; P0C0S5: H2AZ1; NbExp=3; IntAct=EBI-10968534, EBI-1199859;
CC P50570-2; P68431: H3C12; NbExp=3; IntAct=EBI-10968534, EBI-79722;
CC P50570-2; P52790: HK3; NbExp=3; IntAct=EBI-10968534, EBI-2965780;
CC P50570-2; Q8WVV9-3: HNRNPLL; NbExp=3; IntAct=EBI-10968534, EBI-25845242;
CC P50570-2; P09017: HOXC4; NbExp=3; IntAct=EBI-10968534, EBI-3923226;
CC P50570-2; P42858: HTT; NbExp=6; IntAct=EBI-10968534, EBI-466029;
CC P50570-2; Q6DN90-2: IQSEC1; NbExp=3; IntAct=EBI-10968534, EBI-21911304;
CC P50570-2; Q8NA54: IQUB; NbExp=3; IntAct=EBI-10968534, EBI-10220600;
CC P50570-2; Q92993: KAT5; NbExp=3; IntAct=EBI-10968534, EBI-399080;
CC P50570-2; Q92993-2: KAT5; NbExp=3; IntAct=EBI-10968534, EBI-20795332;
CC P50570-2; A1A512: KIAA0355; NbExp=3; IntAct=EBI-10968534, EBI-25844799;
CC P50570-2; Q3SY46: KRTAP13-3; NbExp=3; IntAct=EBI-10968534, EBI-10241252;
CC P50570-2; Q8IUB9: KRTAP19-1; NbExp=3; IntAct=EBI-10968534, EBI-12811111;
CC P50570-2; Q3LI72: KRTAP19-5; NbExp=3; IntAct=EBI-10968534, EBI-1048945;
CC P50570-2; Q3SYF9: KRTAP19-7; NbExp=3; IntAct=EBI-10968534, EBI-10241353;
CC P50570-2; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-10968534, EBI-10261141;
CC P50570-2; Q6DKI2: LGALS9C; NbExp=3; IntAct=EBI-10968534, EBI-9088829;
CC P50570-2; A2RU56: LOC401296; NbExp=3; IntAct=EBI-10968534, EBI-9088215;
CC P50570-2; Q4G0S1: LOC730441; NbExp=3; IntAct=EBI-10968534, EBI-10241801;
CC P50570-2; P07948: LYN; NbExp=3; IntAct=EBI-10968534, EBI-79452;
CC P50570-2; Q9UI95: MAD2L2; NbExp=3; IntAct=EBI-10968534, EBI-77889;
CC P50570-2; Q9UDY8-2: MALT1; NbExp=3; IntAct=EBI-10968534, EBI-12056869;
CC P50570-2; Q99683: MAP3K5; NbExp=3; IntAct=EBI-10968534, EBI-476263;
CC P50570-2; Q15759: MAPK11; NbExp=3; IntAct=EBI-10968534, EBI-298304;
CC P50570-2; Q8TDB4: MGARP; NbExp=3; IntAct=EBI-10968534, EBI-4397720;
CC P50570-2; P41218: MNDA; NbExp=3; IntAct=EBI-10968534, EBI-2829677;
CC P50570-2; Q9Y605: MRFAP1; NbExp=3; IntAct=EBI-10968534, EBI-995714;
CC P50570-2; O43196-2: MSH5; NbExp=3; IntAct=EBI-10968534, EBI-25844576;
CC P50570-2; Q99457: NAP1L3; NbExp=3; IntAct=EBI-10968534, EBI-8645631;
CC P50570-2; O76041: NEBL; NbExp=3; IntAct=EBI-10968534, EBI-2880203;
CC P50570-2; Q15466: NR0B2; NbExp=3; IntAct=EBI-10968534, EBI-3910729;
CC P50570-2; Q9NPJ8-3: NXT2; NbExp=3; IntAct=EBI-10968534, EBI-10698339;
CC P50570-2; Q16625: OCLN; NbExp=3; IntAct=EBI-10968534, EBI-2903088;
CC P50570-2; Q96CV9-2: OPTN; NbExp=3; IntAct=EBI-10968534, EBI-9091423;
CC P50570-2; Q96FW1: OTUB1; NbExp=3; IntAct=EBI-10968534, EBI-1058491;
CC P50570-2; O15460-2: P4HA2; NbExp=3; IntAct=EBI-10968534, EBI-10182841;
CC P50570-2; Q99497: PARK7; NbExp=3; IntAct=EBI-10968534, EBI-1164361;
CC P50570-2; Q13113: PDZK1IP1; NbExp=3; IntAct=EBI-10968534, EBI-716063;
CC P50570-2; O14813: PHOX2A; NbExp=3; IntAct=EBI-10968534, EBI-25844430;
CC P50570-2; P27986-2: PIK3R1; NbExp=3; IntAct=EBI-10968534, EBI-9090282;
CC P50570-2; P12273: PIP; NbExp=3; IntAct=EBI-10968534, EBI-1049746;
CC P50570-2; Q96J94: PIWIL1; NbExp=3; IntAct=EBI-10968534, EBI-527417;
CC P50570-2; O75626-3: PRDM1; NbExp=3; IntAct=EBI-10968534, EBI-25829882;
CC P50570-2; Q15286: RAB35; NbExp=3; IntAct=EBI-10968534, EBI-722275;
CC P50570-2; P57729: RAB38; NbExp=3; IntAct=EBI-10968534, EBI-6552718;
CC P50570-2; Q96QF0-7: RAB3IP; NbExp=3; IntAct=EBI-10968534, EBI-11984839;
CC P50570-2; Q9NS23-4: RASSF1; NbExp=3; IntAct=EBI-10968534, EBI-438710;
CC P50570-2; Q9GZR2: REXO4; NbExp=3; IntAct=EBI-10968534, EBI-2856313;
CC P50570-2; Q96D59: RNF183; NbExp=3; IntAct=EBI-10968534, EBI-743938;
CC P50570-2; Q9BY12-3: SCAPER; NbExp=3; IntAct=EBI-10968534, EBI-25837959;
CC P50570-2; Q2NKQ1-4: SGSM1; NbExp=3; IntAct=EBI-10968534, EBI-10182463;
CC P50570-2; Q9NQ40: SLC52A3; NbExp=3; IntAct=EBI-10968534, EBI-25845274;
CC P50570-2; Q12824: SMARCB1; NbExp=3; IntAct=EBI-10968534, EBI-358419;
CC P50570-2; Q12824-2: SMARCB1; NbExp=3; IntAct=EBI-10968534, EBI-358436;
CC P50570-2; Q16637-3: SMN2; NbExp=3; IntAct=EBI-10968534, EBI-395447;
CC P50570-2; O60749: SNX2; NbExp=3; IntAct=EBI-10968534, EBI-1046690;
CC P50570-2; Q8WV41: SNX33; NbExp=3; IntAct=EBI-10968534, EBI-2481535;
CC P50570-2; Q05C28: SPACA3; NbExp=3; IntAct=EBI-10968534, EBI-25845337;
CC P50570-2; Q7Z6I5: SPATA12; NbExp=3; IntAct=EBI-10968534, EBI-10696971;
CC P50570-2; Q7Z698: SPRED2; NbExp=3; IntAct=EBI-10968534, EBI-7082156;
CC P50570-2; O75558: STX11; NbExp=3; IntAct=EBI-10968534, EBI-714135;
CC P50570-2; Q8N4C7: STX19; NbExp=3; IntAct=EBI-10968534, EBI-8484990;
CC P50570-2; P37802: TAGLN2; NbExp=3; IntAct=EBI-10968534, EBI-1056740;
CC P50570-2; O95551: TDP2; NbExp=3; IntAct=EBI-10968534, EBI-2819865;
CC P50570-2; P28347-2: TEAD1; NbExp=3; IntAct=EBI-10968534, EBI-12151837;
CC P50570-2; Q10587: TEF; NbExp=3; IntAct=EBI-10968534, EBI-2796967;
CC P50570-2; Q03403: TFF2; NbExp=3; IntAct=EBI-10968534, EBI-4314702;
CC P50570-2; P21980-2: TGM2; NbExp=3; IntAct=EBI-10968534, EBI-25842075;
CC P50570-2; Q53EQ6-2: TIGD5; NbExp=3; IntAct=EBI-10968534, EBI-10242213;
CC P50570-2; Q12888: TP53BP1; NbExp=3; IntAct=EBI-10968534, EBI-396540;
CC P50570-2; Q9BUZ4: TRAF4; NbExp=3; IntAct=EBI-10968534, EBI-3650647;
CC P50570-2; Q9NX07-2: TRNAU1AP; NbExp=3; IntAct=EBI-10968534, EBI-21894090;
CC P50570-2; Q5W5X9-3: TTC23; NbExp=3; IntAct=EBI-10968534, EBI-9090990;
CC P50570-2; P10599: TXN; NbExp=3; IntAct=EBI-10968534, EBI-594644;
CC P50570-2; P58304: VSX2; NbExp=3; IntAct=EBI-10968534, EBI-6427899;
CC P50570-2; O00308: WWP2; NbExp=3; IntAct=EBI-10968534, EBI-743923;
CC P50570-2; Q8NAP3: ZBTB38; NbExp=3; IntAct=EBI-10968534, EBI-5235984;
CC P50570-2; Q8IUH5: ZDHHC17; NbExp=3; IntAct=EBI-10968534, EBI-524753;
CC P50570-2; Q05CR2: ZNF248; NbExp=3; IntAct=EBI-10968534, EBI-25835471;
CC P50570-2; Q8N895: ZNF366; NbExp=3; IntAct=EBI-10968534, EBI-2813661;
CC P50570-2; Q14966-2: ZNF638; NbExp=3; IntAct=EBI-10968534, EBI-25845021;
CC P50570-2; Q5TEC3: ZNF697; NbExp=3; IntAct=EBI-10968534, EBI-25845217;
CC P50570-2; B7Z3E8; NbExp=3; IntAct=EBI-10968534, EBI-25831617;
CC P50570-2; Q99KR7: Ppif; Xeno; NbExp=3; IntAct=EBI-10968534, EBI-6455001;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Cell junction
CC {ECO:0000250|UniProtKB:P39052}. Membrane, clathrin-coated pit
CC {ECO:0000250|UniProtKB:P39052}. Postsynaptic density. Synapse. Midbody.
CC Cell projection, phagocytic cup {ECO:0000250|UniProtKB:P39054}.
CC Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:P39054};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:P39054}.
CC Note=Colocalizes with CTTN at the basis of filopodia in hippocampus
CC neuron growth zones (By similarity). Microtubule-associated. Also found
CC in the postsynaptic density of neuronal cells. Co-localizes with PIK3C3
CC and RAB5A to the nascent phagosome (By similarity).
CC {ECO:0000250|UniProtKB:P39052, ECO:0000250|UniProtKB:P39054}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=P50570-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P50570-2; Sequence=VSP_001325;
CC Name=3;
CC IsoId=P50570-3; Sequence=VSP_044280, VSP_001325;
CC Name=4;
CC IsoId=P50570-4; Sequence=VSP_044280;
CC Name=5;
CC IsoId=P50570-5; Sequence=VSP_047534;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC -!- PTM: Phosphorylation at Ser-764 by CDK1 is greatly increased upon
CC mitotic entry. It regulates cytokinesis downstream of calcineurin, and
CC does not affect clathrin-mediated endocytosis. Dephosphorylated by
CC calcineurin/PP2 (By similarity). Phosphorylated on tyrosine residues
CC after activation of SRC (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P39052}.
CC -!- DISEASE: Myopathy, centronuclear, 1 (CNM1) [MIM:160150]: A congenital
CC muscle disorder characterized by progressive muscular weakness and
CC wasting involving mainly limb girdle, trunk, and neck muscles. It may
CC also affect distal muscles. Weakness may be present during childhood or
CC adolescence or may not become evident until the third decade of life.
CC Ptosis is a frequent clinical feature. The most prominent
CC histopathologic features include high frequency of centrally located
CC nuclei in muscle fibers not secondary to regeneration, radial
CC arrangement of sarcoplasmic strands around the central nuclei, and
CC predominance and hypotrophy of type 1 fibers.
CC {ECO:0000269|PubMed:16227997, ECO:0000269|PubMed:17825552,
CC ECO:0000269|PubMed:17932957, ECO:0000269|PubMed:19122038,
CC ECO:0000269|PubMed:19623537, ECO:0000269|PubMed:19932619,
CC ECO:0000269|PubMed:19932620, ECO:0000269|PubMed:20227276,
CC ECO:0000269|PubMed:22396310}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Lethal congenital contracture syndrome 5 (LCCS5) [MIM:615368]:
CC A form of lethal congenital contracture syndrome, an autosomal
CC recessive disorder characterized by degeneration of anterior horn
CC neurons, extreme skeletal muscle atrophy and congenital non-progressive
CC joint contractures. The contractures can involve the upper or lower
CC limbs and/or the vertebral column, leading to various degrees of
CC flexion or extension limitations evident at birth.
CC {ECO:0000269|PubMed:23092955}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Charcot-Marie-Tooth disease, dominant, intermediate type, B
CC (CMTDIB) [MIM:606482]: A form of Charcot-Marie-Tooth disease, a
CC disorder of the peripheral nervous system, characterized by progressive
CC weakness and atrophy, initially of the peroneal muscles and later of
CC the distal muscles of the arms. The dominant intermediate type B is
CC characterized by clinical and pathologic features intermediate between
CC demyelinating and axonal peripheral neuropathies, and motor median
CC nerve conduction velocities ranging from 25 to 45 m/sec.
CC {ECO:0000269|PubMed:15731758, ECO:0000269|PubMed:19623537}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Charcot-Marie-Tooth disease 2M (CMT2M) [MIM:606482]: An axonal
CC form of Charcot-Marie-Tooth disease, a disorder of the peripheral
CC nervous system, characterized by progressive weakness and atrophy,
CC initially of the peroneal muscles and later of the distal muscles of
CC the arms. Charcot-Marie-Tooth disease is classified in two main groups
CC on the basis of electrophysiologic properties and histopathology:
CC primary peripheral demyelinating neuropathies (designated CMT1 when
CC they are dominantly inherited) and primary peripheral axonal
CC neuropathies (CMT2). Neuropathies of the CMT2 group are characterized
CC by signs of axonal degeneration in the absence of obvious myelin
CC alterations, normal or slightly reduced nerve conduction velocities,
CC and progressive distal muscle weakness and atrophy.
CC {ECO:0000269|PubMed:17636067, ECO:0000269|PubMed:18560793}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: Overexpression of CNM- and CMT-related DNM2 mutants in
CC COS7 cells, whatever the mutated domain, led to a reduction in
CC clathrin-mediated receptor endocytosis associated with MAPK ERK-1 and
CC ERK-2 impairment. The membrane trafficking impairment process may
CC represent a common pathophysiological pathway in the autosomal forms of
CC CNM DNM2-CMT neuropathy.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. Dynamin/Fzo/YdjA family. {ECO:0000255|PROSITE-
CC ProRule:PRU01055}.
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DR EMBL; L36983; AAA88025.1; -; mRNA.
DR EMBL; AK289831; BAF82520.1; -; mRNA.
DR EMBL; AK312260; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC007229; AAD23604.1; -; Genomic_DNA.
DR EMBL; AC011475; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC011552; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC011554; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC112707; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC039596; AAH39596.1; -; mRNA.
DR EMBL; BC054501; AAH54501.1; -; mRNA.
DR CCDS; CCDS32907.1; -. [P50570-2]
DR CCDS; CCDS32908.1; -. [P50570-3]
DR CCDS; CCDS45968.1; -. [P50570-1]
DR CCDS; CCDS45969.1; -. [P50570-4]
DR CCDS; CCDS59351.1; -. [P50570-5]
DR PIR; JC4305; JC4305.
DR RefSeq; NP_001005360.1; NM_001005360.2. [P50570-1]
DR RefSeq; NP_001005361.1; NM_001005361.2. [P50570-4]
DR RefSeq; NP_001005362.1; NM_001005362.2. [P50570-3]
DR RefSeq; NP_001177645.1; NM_001190716.1. [P50570-5]
DR RefSeq; NP_004936.2; NM_004945.3. [P50570-2]
DR PDB; 2YS1; NMR; -; A=520-625.
DR PDBsum; 2YS1; -.
DR AlphaFoldDB; P50570; -.
DR BMRB; P50570; -.
DR SMR; P50570; -.
DR BioGRID; 108122; 237.
DR CORUM; P50570; -.
DR DIP; DIP-31244N; -.
DR ELM; P50570; -.
DR IntAct; P50570; 245.
DR MINT; P50570; -.
DR STRING; 9606.ENSP00000373905; -.
DR BindingDB; P50570; -.
DR ChEMBL; CHEMBL5812; -.
DR MoonDB; P50570; Curated.
DR TCDB; 1.R.1.1.1; the membrane contact site (mcs) family.
DR TCDB; 8.A.34.1.4; the endophilin (endophilin) family.
DR GlyGen; P50570; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P50570; -.
DR MetOSite; P50570; -.
DR PhosphoSitePlus; P50570; -.
DR SwissPalm; P50570; -.
DR BioMuta; DNM2; -.
DR DMDM; 47117856; -.
DR EPD; P50570; -.
DR jPOST; P50570; -.
DR MassIVE; P50570; -.
DR MaxQB; P50570; -.
DR PaxDb; P50570; -.
DR PeptideAtlas; P50570; -.
DR PRIDE; P50570; -.
DR ProteomicsDB; 1845; -.
DR ProteomicsDB; 19939; -.
DR ProteomicsDB; 56250; -. [P50570-1]
DR ProteomicsDB; 56251; -. [P50570-2]
DR Antibodypedia; 25505; 252 antibodies from 34 providers.
DR DNASU; 1785; -.
DR Ensembl; ENST00000355667.11; ENSP00000347890.6; ENSG00000079805.19. [P50570-1]
DR Ensembl; ENST00000359692.10; ENSP00000352721.6; ENSG00000079805.19. [P50570-2]
DR Ensembl; ENST00000389253.9; ENSP00000373905.4; ENSG00000079805.19. [P50570-4]
DR Ensembl; ENST00000408974.8; ENSP00000386192.3; ENSG00000079805.19. [P50570-3]
DR Ensembl; ENST00000585892.5; ENSP00000468734.1; ENSG00000079805.19. [P50570-5]
DR GeneID; 1785; -.
DR KEGG; hsa:1785; -.
DR MANE-Select; ENST00000389253.9; ENSP00000373905.4; NM_001005361.3; NP_001005361.1. [P50570-4]
DR UCSC; uc002mps.3; human. [P50570-1]
DR CTD; 1785; -.
DR DisGeNET; 1785; -.
DR GeneCards; DNM2; -.
DR HGNC; HGNC:2974; DNM2.
DR HPA; ENSG00000079805; Low tissue specificity.
DR MalaCards; DNM2; -.
DR MIM; 160150; phenotype.
DR MIM; 602378; gene.
DR MIM; 606482; phenotype.
DR MIM; 615368; phenotype.
DR neXtProt; NX_P50570; -.
DR OpenTargets; ENSG00000079805; -.
DR Orphanet; 169189; Autosomal dominant centronuclear myopathy.
DR Orphanet; 228179; Autosomal dominant Charcot-Marie-Tooth disease type 2M.
DR Orphanet; 100044; Autosomal dominant intermediate Charcot-Marie-Tooth disease type B.
DR Orphanet; 363409; Fetal akinesia-cerebral and retinal hemorrhage syndrome.
DR PharmGKB; PA27442; -.
DR VEuPathDB; HostDB:ENSG00000079805; -.
DR eggNOG; KOG0446; Eukaryota.
DR GeneTree; ENSGT00940000155764; -.
DR HOGENOM; CLU_008964_1_1_1; -.
DR InParanoid; P50570; -.
DR OMA; REYKAYQ; -.
DR OrthoDB; 264244at2759; -.
DR PhylomeDB; P50570; -.
DR TreeFam; TF300362; -.
DR BRENDA; 3.6.5.5; 2681.
DR PathwayCommons; P50570; -.
DR Reactome; R-HSA-166016; Toll Like Receptor 4 (TLR4) Cascade.
DR Reactome; R-HSA-177504; Retrograde neurotrophin signalling.
DR Reactome; R-HSA-190873; Gap junction degradation.
DR Reactome; R-HSA-196025; Formation of annular gap junctions.
DR Reactome; R-HSA-203641; NOSTRIN mediated eNOS trafficking.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-HSA-437239; Recycling pathway of L1.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-HSA-9031628; NGF-stimulated transcription.
DR SignaLink; P50570; -.
DR SIGNOR; P50570; -.
DR BioGRID-ORCS; 1785; 721 hits in 1093 CRISPR screens.
DR ChiTaRS; DNM2; human.
DR EvolutionaryTrace; P50570; -.
DR GeneWiki; DNM2; -.
DR GenomeRNAi; 1785; -.
DR Pharos; P50570; Tchem.
DR PRO; PR:P50570; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P50570; protein.
DR Bgee; ENSG00000079805; Expressed in metanephros cortex and 152 other tissues.
DR ExpressionAtlas; P50570; baseline and differential.
DR Genevisible; P50570; HS.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0045334; C:clathrin-coated endocytic vesicle; IEA:Ensembl.
DR GO; GO:0005905; C:clathrin-coated pit; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005768; C:endosome; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0030426; C:growth cone; IEA:Ensembl.
DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0001891; C:phagocytic cup; IEA:UniProtKB-SubCell.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0099092; C:postsynaptic density, intracellular component; IEA:Ensembl.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:UniProtKB.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0032587; C:ruffle membrane; IEA:Ensembl.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; IEA:Ensembl.
DR GO; GO:0031749; F:D2 dopamine receptor binding; IEA:Ensembl.
DR GO; GO:0019899; F:enzyme binding; NAS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; NAS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0050998; F:nitric-oxide synthase binding; IEA:Ensembl.
DR GO; GO:0036312; F:phosphatidylinositol 3-kinase regulatory subunit binding; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0017124; F:SH3 domain binding; IDA:UniProtKB.
DR GO; GO:0050699; F:WW domain binding; IEA:Ensembl.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
DR GO; GO:0071245; P:cellular response to carbon monoxide; IEA:Ensembl.
DR GO; GO:1903351; P:cellular response to dopamine; IEA:Ensembl.
DR GO; GO:0071732; P:cellular response to nitric oxide; IEA:Ensembl.
DR GO; GO:0071481; P:cellular response to X-ray; IEA:Ensembl.
DR GO; GO:0006897; P:endocytosis; IDA:UniProtKB.
DR GO; GO:0002031; P:G protein-coupled receptor internalization; IEA:Ensembl.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; NAS:UniProtKB.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; IEA:Ensembl.
DR GO; GO:0044351; P:macropinocytosis; IEA:Ensembl.
DR GO; GO:0061024; P:membrane organization; TAS:Reactome.
DR GO; GO:1903526; P:negative regulation of membrane tubulation; IDA:UniProtKB.
DR GO; GO:1902856; P:negative regulation of non-motile cilium assembly; IEA:Ensembl.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
DR GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
DR GO; GO:0043065; P:positive regulation of apoptotic process; NAS:UniProtKB.
DR GO; GO:2000370; P:positive regulation of clathrin-dependent endocytosis; IEA:Ensembl.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; IEA:Ensembl.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IEA:Ensembl.
DR GO; GO:1903408; P:positive regulation of P-type sodium:potassium-exchanging transporter activity; IEA:Ensembl.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IEA:Ensembl.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; NAS:UniProtKB.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; TAS:Reactome.
DR GO; GO:0031623; P:receptor internalization; IMP:BHF-UCL.
DR GO; GO:0006898; P:receptor-mediated endocytosis; ISS:UniProtKB.
DR GO; GO:0030516; P:regulation of axon extension; ISS:UniProtKB.
DR GO; GO:1903358; P:regulation of Golgi organization; IEA:Ensembl.
DR GO; GO:0035020; P:regulation of Rac protein signal transduction; IEA:Ensembl.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
DR GO; GO:0042220; P:response to cocaine; IEA:Ensembl.
DR GO; GO:0009416; P:response to light stimulus; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IBA:GO_Central.
DR GO; GO:0048489; P:synaptic vesicle transport; NAS:UniProtKB.
DR GO; GO:0033572; P:transferrin transport; IMP:BHF-UCL.
DR CDD; cd08771; DLP_1; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027188; DNM2.
DR InterPro; IPR022812; Dynamin.
DR InterPro; IPR001401; Dynamin_GTPase.
DR InterPro; IPR019762; Dynamin_GTPase_CS.
DR InterPro; IPR045063; Dynamin_N.
DR InterPro; IPR000375; Dynamin_stalk.
DR InterPro; IPR030381; G_DYNAMIN_dom.
DR InterPro; IPR003130; GED.
DR InterPro; IPR020850; GED_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR11566; PTHR11566; 1.
DR PANTHER; PTHR11566:SF23; PTHR11566:SF23; 1.
DR Pfam; PF01031; Dynamin_M; 1.
DR Pfam; PF00350; Dynamin_N; 1.
DR Pfam; PF02212; GED; 1.
DR Pfam; PF00169; PH; 1.
DR PRINTS; PR00195; DYNAMIN.
DR SMART; SM00053; DYNc; 1.
DR SMART; SM00302; GED; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00410; G_DYNAMIN_1; 1.
DR PROSITE; PS51718; G_DYNAMIN_2; 1.
DR PROSITE; PS51388; GED; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell junction;
KW Cell projection; Charcot-Marie-Tooth disease; Coated pit; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; Disease variant; Endocytosis;
KW GTP-binding; Hydrolase; Membrane; Microtubule; Motor protein;
KW Neurodegeneration; Neuropathy; Nucleotide-binding; Phagocytosis;
KW Phosphoprotein; Reference proteome; Synapse.
FT CHAIN 1..870
FT /note="Dynamin-2"
FT /id="PRO_0000206570"
FT DOMAIN 28..294
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 519..625
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 653..744
FT /note="GED"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
FT REGION 38..45
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 64..66
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 136..139
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 205..208
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 235..238
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 741..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..770
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..796
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..859
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 38..46
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O00429"
FT BINDING 205..211
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O00429"
FT BINDING 236..239
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O00429"
FT MOD_RES 231
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P39052"
FT MOD_RES 299
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P39054"
FT MOD_RES 597
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P39052"
FT MOD_RES 598
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 755
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 764
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:P39052"
FT VAR_SEQ 407..444
FT /note="LAFEAIVKKQVVKLKEPCLKCVDLVIQELINTVRQCTS -> MAFEAIVKKQ
FT IVKLKEPSLKCVDLVVSELATVIKKCAE (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044280"
FT VAR_SEQ 516..519
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:7590285"
FT /id="VSP_001325"
FT VAR_SEQ 848
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047534"
FT VARIANT 263
FT /note="P -> L (in dbSNP:rs3745674)"
FT /id="VAR_031961"
FT VARIANT 358
FT /note="G -> R (in CMT2M; dbSNP:rs267606772)"
FT /evidence="ECO:0000269|PubMed:18560793"
FT /id="VAR_068425"
FT VARIANT 368
FT /note="E -> K (in CNM1; dbSNP:rs121909092)"
FT /evidence="ECO:0000269|PubMed:16227997,
FT ECO:0000269|PubMed:20227276"
FT /id="VAR_031962"
FT VARIANT 368
FT /note="E -> Q (in CNM1)"
FT /evidence="ECO:0000269|PubMed:17825552"
FT /id="VAR_068365"
FT VARIANT 369
FT /note="R -> Q (in CNM1; dbSNP:rs121909089)"
FT /evidence="ECO:0000269|PubMed:16227997"
FT /id="VAR_031963"
FT VARIANT 369
FT /note="R -> W (in CNM1; reduced association with the
FT centrosome; dbSNP:rs121909090)"
FT /evidence="ECO:0000269|PubMed:16227997"
FT /id="VAR_031964"
FT VARIANT 379
FT /note="F -> V (in LCCS5; hypomorphic mutation impacting on
FT endocytosis; dbSNP:rs397514735)"
FT /evidence="ECO:0000269|PubMed:23092955"
FT /id="VAR_070163"
FT VARIANT 465
FT /note="R -> W (in CNM1; reduced association with the
FT centrosome; COS7 cells show a reduced uptake of transferrin
FT and low-density lipoprotein complex; dbSNP:rs121909091)"
FT /evidence="ECO:0000269|PubMed:16227997,
FT ECO:0000269|PubMed:19623537, ECO:0000269|PubMed:20227276"
FT /id="VAR_031965"
FT VARIANT 522
FT /note="R -> C (in CNM1)"
FT /evidence="ECO:0000269|PubMed:22396310"
FT /id="VAR_068366"
FT VARIANT 522
FT /note="R -> H (in CNM1; dbSNP:rs587783595)"
FT /evidence="ECO:0000269|PubMed:20227276"
FT /id="VAR_068367"
FT VARIANT 523
FT /note="R -> G (in CNM1; dbSNP:rs587783596)"
FT /evidence="ECO:0000269|PubMed:22396310"
FT /id="VAR_068368"
FT VARIANT 537
FT /note="G -> C (in CMT2M; dbSNP:rs121909093)"
FT /evidence="ECO:0000269|PubMed:17636067"
FT /id="VAR_062574"
FT VARIANT 555..557
FT /note="Missing (in CMTDIB; may affect binding to vesicles
FT and membranes in favor of binding to microtubules; may
FT affect receptor-mediated endocytosis)"
FT /evidence="ECO:0000269|PubMed:15731758"
FT /id="VAR_031966"
FT VARIANT 560
FT /note="E -> K (in CNM1; dbSNP:rs879254086)"
FT /evidence="ECO:0000269|PubMed:19122038"
FT /id="VAR_068369"
FT VARIANT 562
FT /note="K -> E (in CMTDIB; with neutropenia; COS7 cells show
FT a reduced uptake of transferrin and low-density lipoprotein
FT complex; dbSNP:rs121909088)"
FT /evidence="ECO:0000269|PubMed:15731758,
FT ECO:0000269|PubMed:19623537"
FT /id="VAR_031967"
FT VARIANT 562
FT /note="Missing (in CMTDIB; dbSNP:rs1599620408)"
FT /evidence="ECO:0000269|PubMed:15731758"
FT /id="VAR_070164"
FT VARIANT 570
FT /note="L -> H (in CMT2M; dbSNP:rs121909094)"
FT /evidence="ECO:0000269|PubMed:17636067"
FT /id="VAR_062575"
FT VARIANT 618
FT /note="A -> D (in CNM1; dbSNP:rs1555715869)"
FT /evidence="ECO:0000269|PubMed:19932619"
FT /id="VAR_068370"
FT VARIANT 618
FT /note="A -> T (in CNM1; severe; dbSNP:rs773598203)"
FT /evidence="ECO:0000269|PubMed:17932957,
FT ECO:0000269|PubMed:20227276"
FT /id="VAR_039041"
FT VARIANT 619
FT /note="S -> L (in CNM1; severe; dbSNP:rs121909095)"
FT /evidence="ECO:0000269|PubMed:17932957,
FT ECO:0000269|PubMed:20227276"
FT /id="VAR_039042"
FT VARIANT 619
FT /note="S -> W (in CNM1; severe; dbSNP:rs121909095)"
FT /evidence="ECO:0000269|PubMed:17932957"
FT /id="VAR_039043"
FT VARIANT 621
FT /note="L -> P (in CNM1; centronuclear myopathy with
FT cataracts; dbSNP:rs587783597)"
FT /evidence="ECO:0000269|PubMed:19932620"
FT /id="VAR_068371"
FT VARIANT 625
FT /note="Missing (in CNM1; severe; COS7 cells show a reduced
FT uptake of transferrin and low-density lipoprotein complex)"
FT /evidence="ECO:0000269|PubMed:17932957,
FT ECO:0000269|PubMed:19623537"
FT /id="VAR_039044"
FT VARIANT 627
FT /note="P -> H (in CNM1)"
FT /evidence="ECO:0000269|PubMed:20227276"
FT /id="VAR_068372"
FT VARIANT 627
FT /note="P -> R (in CNM1; dbSNP:rs587783598)"
FT /evidence="ECO:0000269|PubMed:22396310"
FT /id="VAR_068373"
FT VARIANT 650
FT /note="E -> K (in CNM1; COS7 cells show a reduced uptake of
FT transferrin and low-density lipoprotein complex)"
FT /evidence="ECO:0000269|PubMed:19623537"
FT /id="VAR_062576"
FT CONFLICT 155..156
FT /note="QI -> RV (in Ref. 1; AAA88025)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="L -> P (in Ref. 2; AK312260)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="N -> I (in Ref. 1; AAA88025)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="R -> P (in Ref. 1; AAA88025)"
FT /evidence="ECO:0000305"
FT CONFLICT 475
FT /note="I -> T (in Ref. 2; AK312260)"
FT /evidence="ECO:0000305"
FT STRAND 522..530
FT /evidence="ECO:0007829|PDB:2YS1"
FT STRAND 533..535
FT /evidence="ECO:0007829|PDB:2YS1"
FT STRAND 540..545
FT /evidence="ECO:0007829|PDB:2YS1"
FT STRAND 550..555
FT /evidence="ECO:0007829|PDB:2YS1"
FT STRAND 560..565
FT /evidence="ECO:0007829|PDB:2YS1"
FT STRAND 567..573
FT /evidence="ECO:0007829|PDB:2YS1"
FT STRAND 585..590
FT /evidence="ECO:0007829|PDB:2YS1"
FT STRAND 596..599
FT /evidence="ECO:0007829|PDB:2YS1"
FT STRAND 601..606
FT /evidence="ECO:0007829|PDB:2YS1"
FT HELIX 610..623
FT /evidence="ECO:0007829|PDB:2YS1"
SQ SEQUENCE 870 AA; 98064 MW; 2F4567B75980935D CRC64;
MGNRGMEELI PLVNKLQDAF SSIGQSCHLD LPQIAVVGGQ SAGKSSVLEN FVGRDFLPRG
SGIVTRRPLI LQLIFSKTEH AEFLHCKSKK FTDFDEVRQE IEAETDRVTG TNKGISPVPI
NLRVYSPHVL NLTLIDLPGI TKVPVGDQPP DIEYQIKDMI LQFISRESSL ILAVTPANMD
LANSDALKLA KEVDPQGLRT IGVITKLDLM DEGTDARDVL ENKLLPLRRG YIGVVNRSQK
DIEGKKDIRA ALAAERKFFL SHPAYRHMAD RMGTPHLQKT LNQQLTNHIR ESLPALRSKL
QSQLLSLEKE VEEYKNFRPD DPTRKTKALL QMVQQFGVDF EKRIEGSGDQ VDTLELSGGA
RINRIFHERF PFELVKMEFD EKDLRREISY AIKNIHGVRT GLFTPDLAFE AIVKKQVVKL
KEPCLKCVDL VIQELINTVR QCTSKLSSYP RLREETERIV TTYIREREGR TKDQILLLID
IEQSYINTNH EDFIGFANAQ QRSTQLNKKR AIPNQGEILV IRRGWLTINN ISLMKGGSKE
YWFVLTAESL SWYKDEEEKE KKYMLPLDNL KIRDVEKGFM SNKHVFAIFN TEQRNVYKDL
RQIELACDSQ EDVDSWKASF LRAGVYPEKD QAENEDGAQE NTFSMDPQLE RQVETIRNLV
DSYVAIINKS IRDLMPKTIM HLMINNTKAF IHHELLAYLY SSADQSSLME ESADQAQRRD
DMLRMYHALK EALNIIGDIS TSTVSTPVPP PVDDTWLQSA SSHSPTPQRR PVSSIHPPGR
PPAVRGPTPG PPLIPVPVGA AASFSAPPIP SRPGPQSVFA NSDLFPAPPQ IPSRPVRIPP
GIPPGVPSRR PPAAPSRPTI IRPAEPSLLD
