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Dynamin-2 (EC 3.6.5.5)

 DYN2_HUMAN              Reviewed;         870 AA.
P50570; A8K1B6; E7EV30; E9PEQ4; K7ESI9; Q5I0Y0; Q7Z5S3; Q9UPH4;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
10-MAY-2004, sequence version 2.
30-AUG-2017, entry version 186.
RecName: Full=Dynamin-2;
EC=3.6.5.5;
Name=DNM2; Synonyms=DYN2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
PubMed=7590285; DOI=10.1016/0378-1119(95)00275-B;
Diatloff-Zito C., Gordon A.J.E., Duchaud E., Merlin G.;
"Isolation of an ubiquitously expressed cDNA encoding human dynamin
II, a member of the large GTP-binding protein family.";
Gene 163:301-306(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5).
TISSUE=Astrocyte, 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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Ovary, and Uterus;
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).
[5]
INTERACTION WITH SHANK PROTEINS.
PubMed=11583995; DOI=10.1074/jbc.M104927200;
Okamoto P.M., Gamby C., Wells D., Fallon J., Vallee R.B.;
"Dynamin isoform-specific interaction with the shank/ProSAP
scaffolding proteins of the postsynaptic density and actin
cytoskeleton.";
J. Biol. Chem. 276:48458-48465(2001).
[6]
FUNCTION IN CYTOKINESIS, AND SUBCELLULAR LOCATION.
PubMed=12498685; DOI=10.1016/S0960-9822(02)01390-8;
Thompson H.M., Skop A.R., Euteneuer U., Meyer B.J., McNiven M.A.;
"The large GTPase dynamin associates with the spindle midzone and is
required for cytokinesis.";
Curr. Biol. 12:2111-2117(2002).
[7]
INTERACTION WITH SH3BP4.
PubMed=16325581; DOI=10.1016/j.cell.2005.10.021;
Tosoni D., Puri C., Confalonieri S., Salcini A.E., De Camilli P.,
Tacchetti C., Di Fiore P.P.;
"TTP specifically regulates the internalization of the transferrin
receptor.";
Cell 123:875-888(2005).
[8]
INTERACTION WITH NOSTRIN.
PubMed=16234328; DOI=10.1242/jcs.02620;
Icking A., Matt S., Opitz N., Wiesenthal A., Mueller-Esterl W.,
Schilling K.;
"NOSTRIN functions as a homotrimeric adaptor protein facilitating
internalization of eNOS.";
J. Cell Sci. 118:5059-5069(2005).
[9]
SUBCELLULAR LOCATION, AND INTERACTION WITH SNX9.
PubMed=15703209; DOI=10.1091/mbc.E04-11-1016;
Soulet F., Yarar D., Leonard M., Schmid S.L.;
"SNX9 regulates dynamin assembly and is required for efficient
clathrin-mediated endocytosis.";
Mol. Biol. Cell 16:2058-2067(2005).
[10]
INTERACTION WITH MYO1E.
PubMed=17257598; DOI=10.1016/j.febslet.2007.01.021;
Krendel M., Osterweil E.K., Mooseker M.S.;
"Myosin 1E interacts with synaptojanin-1 and dynamin and is involved
in endocytosis.";
FEBS Lett. 581:644-650(2007).
[11]
INTERACTION WITH SNX33.
PubMed=18353773; DOI=10.1074/jbc.M801531200;
Schobel S., Neumann S., Hertweck M., Dislich B., Kuhn P.H.,
Kremmer E., Seed B., Baumeister R., Haass C., Lichtenthaler S.F.;
"A novel sorting nexin modulates endocytic trafficking and alpha-
secretase cleavage of the amyloid precursor protein.";
J. Biol. Chem. 283:14257-14268(2008).
[12]
INTERACTION WITH PSTPIP1.
PubMed=18480402; DOI=10.1091/mbc.E08-02-0225;
Cooper K.M., Bennin D.A., Huttenlocher A.;
"The PCH family member proline-serine-threonine phosphatase-
interacting protein 1 targets to the leukocyte uropod and regulates
directed cell migration.";
Mol. Biol. Cell 19:3180-3191(2008).
[13]
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).
[14]
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).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-598, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[16]
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).
[17]
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).
[18]
INTERACTION WITH CTNND2.
PubMed=22022388; DOI=10.1371/journal.pone.0025379;
Koutras C., Levesque G.;
"Identification of novel NPRAP/delta-catenin-interacting proteins and
the direct association of NPRAP with dynamin 2.";
PLoS ONE 6:E25379-E25379(2011).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-755, 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).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[21]
STRUCTURE BY NMR OF 514-625.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the PH domain of dynamin-2 from human.";
Submitted (APR-2008) to the PDB data bank.
[22]
VARIANTS CMTDIB 555-ASP--GLU-557 DEL; LYS-562 DEL AND GLU-562, AND
CHARACTERIZATION OF VARIANT CMTDIB 555-ASP--GLU-557 DEL.
PubMed=15731758; DOI=10.1038/ng1514;
Zuechner S., Noureddine M., Kennerson M., Verhoeven K., Claeys K.,
De Jonghe P., Merory J., Oliveira S.A., Speer M.C., Stenger J.E.,
Walizada G., Zhu D., Pericak-Vance M.A., Nicholson G., Timmerman V.,
Vance J.M.;
"Mutations in the pleckstrin homology domain of dynamin 2 cause
dominant intermediate Charcot-Marie-Tooth disease.";
Nat. Genet. 37:289-294(2005).
[23]
VARIANTS CNM1 LYS-368; TRP-369; GLN-369 AND TRP-465, AND
CHARACTERIZATION OF VARIANTS CNM1 TRP-369 AND TRP-465.
PubMed=16227997; DOI=10.1038/ng1657;
Bitoun M., Maugenre S., Jeannet P.-Y., Lacene E., Ferrer X.,
Laforet P., Martin J.-J., Laporte J., Lochmueller H., Beggs A.H.,
Fardeau M., Eymard B., Romero N.B., Guicheney P.;
"Mutations in dynamin 2 cause dominant centronuclear myopathy.";
Nat. Genet. 37:1207-1209(2005).
[24]
VARIANTS CNM1 THR-618; LEU-619; TRP-619 AND VAL-625 DEL.
PubMed=17932957; DOI=10.1002/ana.21235;
Bitoun M., Bevilacqua J.A., Prudhon B., Maugenre S., Taratuto A.L.,
Monges S., Lubieniecki F., Cances C., Uro-Coste E., Mayer M.,
Fardeau M., Romero N.B., Guicheney P.;
"Dynamin 2 mutations cause sporadic centronuclear myopathy with
neonatal onset.";
Ann. Neurol. 62:666-670(2007).
[25]
VARIANTS CMT2M CYS-537 AND HIS-570.
PubMed=17636067; DOI=10.1212/01.wnl.0000265820.51075.61;
Fabrizi G.M., Ferrarini M., Cavallaro T., Cabrini I., Cerini R.,
Bertolasi L., Rizzuto N.;
"Two novel mutations in dynamin-2 cause axonal Charcot-Marie-Tooth
disease.";
Neurology 69:291-295(2007).
[26]
VARIANT CNM1 GLN-368.
PubMed=17825552; DOI=10.1016/j.nmd.2007.06.467;
Echaniz-Laguna A., Nicot A.S., Carre S., Franques J., Tranchant C.,
Dondaine N., Biancalana V., Mandel J.L., Laporte J.;
"Subtle central and peripheral nervous system abnormalities in a
family with centronuclear myopathy and a novel dynamin 2 gene
mutation.";
Neuromuscul. Disord. 17:955-959(2007).
[27]
VARIANT CMT2M ARG-358.
PubMed=18560793; DOI=10.1007/s00415-008-0808-8;
Gallardo E., Claeys K.G., Nelis E., Garcia A., Canga A., Combarros O.,
Timmerman V., De Jonghe P., Berciano J.;
"Magnetic resonance imaging findings of leg musculature in Charcot-
Marie-Tooth disease type 2 due to dynamin 2 mutation.";
J. Neurol. 255:986-992(2008).
[28]
VARIANT CNM1 LYS-650, CHARACTERIZATION OF VARIANTS CNM1 TRP-465;
VAL-625 DEL AND LYS-650, CHARACTERIZATION OF VARIANT CMTDIB GLU-562,
AND PATHOPHYSIOLOGICAL PATHWAY IN THE AUTOSOMAL FORMS OF CNM AND
DNM2-CMT NEUROPATHY.
PubMed=19623537; DOI=10.1002/humu.21086;
Bitoun M., Durieux A.-C., Prudhon B., Bevilacqua J.A., Herledan A.,
Sakanyan V., Urtizberea A., Cartier L., Romero N.B., Guicheney P.;
"Dynamin 2 mutations associated with human diseases impair clathrin-
mediated receptor endocytosis.";
Hum. Mutat. 30:1419-1427(2009).
[29]
VARIANT CNM1 LYS-560.
PubMed=19122038; DOI=10.1212/01.wnl.0000338624.25852.12;
Bitoun M., Bevilacqua J.A., Eymard B., Prudhon B., Fardeau M.,
Guicheney P., Romero N.B.;
"A new centronuclear myopathy phenotype due to a novel dynamin 2
mutation.";
Neurology 72:93-95(2009).
[30]
VARIANT CNM1 PRO-621.
PubMed=19932620; DOI=10.1016/j.nmd.2009.10.005;
Jungbluth H., Cullup T., Lillis S., Zhou H., Abbs S., Sewry C.,
Muntoni F.;
"Centronuclear myopathy with cataracts due to a novel dynamin 2 (DNM2)
mutation.";
Neuromuscul. Disord. 20:49-52(2010).
[31]
VARIANT CNM1 ASP-618.
PubMed=19932619; DOI=10.1016/j.nmd.2009.10.006;
Melberg A., Kretz C., Kalimo H., Wallgren-Pettersson C., Toussaint A.,
Bohm J., Stalberg E., Laporte J.;
"Adult course in dynamin 2 dominant centronuclear myopathy with
neonatal onset.";
Neuromuscul. Disord. 20:53-56(2010).
[32]
VARIANTS CNM1 LYS-368; TRP-465; HIS-522; THR-618; LEU-619 AND HIS-627.
PubMed=20227276; DOI=10.1016/j.nmd.2010.02.016;
Susman R.D., Quijano-Roy S., Yang N., Webster R., Clarke N.F.,
Dowling J., Kennerson M., Nicholson G., Biancalana V., Ilkovski B.,
Flanigan K.M., Arbuckle S., Malladi C., Robinson P., Vucic S.,
Mayer M., Romero N.B., Urtizberea J.A., Garcia-Bragado F.,
Guicheney P., Bitoun M., Carlier R.Y., North K.N.;
"Expanding the clinical, pathological and MRI phenotype of DNM2-
related centronuclear myopathy.";
Neuromuscul. Disord. 20:229-237(2010).
[33]
VARIANTS CNM1 CYS-522; GLY-523 AND ARG-627.
PubMed=22396310; DOI=10.1002/humu.22067;
Bohm J., Biancalana V., Dechene E.T., Bitoun M., Pierson C.R.,
Schaefer E., Karasoy H., Dempsey M.A., Klein F., Dondaine N.,
Kretz C., Haumesser N., Poirson C., Toussaint A., Greenleaf R.S.,
Barger M.A., Mahoney L.J., Kang P.B., Zanoteli E., Vissing J.,
Witting N., Echaniz-Laguna A., Wallgren-Pettersson C., Dowling J.,
Merlini L., Oldfors A., Bomme Ousager L., Melki J., Krause A.,
Jern C., Oliveira A.S., Petit F., Jacquette A., Chaussenot A.,
Mowat D., Leheup B., Cristofano M., Poza Aldea J.J., Michel F.,
Furby A., Llona J.E., Van Coster R., Bertini E., Urtizberea J.A.,
Drouin-Garraud V., Beroud C., Prudhon B., Bedford M., Mathews K.,
Erby L.A., Smith S.A., Roggenbuck J., Crowe C.A., Brennan Spitale A.,
Johal S.C., Amato A.A., Demmer L.A., Jonas J., Darras B.T., Bird T.D.,
Laurino M., Welt S.I., Trotter C., Guicheney P., Das S., Mandel J.L.,
Beggs A.H., Laporte J.;
"Mutation spectrum in the large GTPase dynamin 2, and genotype-
phenotype correlation in autosomal dominant centronuclear myopathy.";
Hum. Mutat. 33:949-959(2012).
[34]
VARIANT LCCS5 VAL-379.
PubMed=23092955; DOI=10.1038/ejhg.2012.226;
Koutsopoulos O.S., Kretz C., Weller C.M., Roux A., Mojzisova H.,
Boehm J., Koch C., Toussaint A., Heckel E., Stemkens D.,
Ter Horst S.A., Thibault C., Koch M., Mehdi S.Q., Bijlsma E.K.,
Mandel J.L., Vermot J., Laporte J.;
"Dynamin 2 homozygous mutation in humans with a lethal congenital
syndrome.";
Eur. J. Hum. Genet. 21:637-642(2013).
-!- FUNCTION: Microtubule-associated force-producing protein involved
in producing microtubule bundles and able to bind and hydrolyze
GTP. Plays a role in the regulation of neuron morphology, axon
growth and formation of neuronal growth cones (By similarity).
Plays an important role in vesicular trafficking processes, in
particular endocytosis. Involved in cytokinesis (PubMed:12498685).
Regulates maturation of apoptotic cell corpse-containing
phagosomes by recruiting PIK3C3 to the phagosome membrane (By
similarity). {ECO:0000250|UniProtKB:P39052,
ECO:0000250|UniProtKB:P39054, ECO:0000269|PubMed:12498685}.
-!- CATALYTIC ACTIVITY: GTP + H(2)O = GDP + phosphate.
-!- SUBUNIT: Interacts with MYOF (By similarity). Interacts with CTTN
and ACTN1 (By similarity). Interacts with SHANK1, SHANK2, SH3BP4
and NOSTRIN. Interacts with SNX9. Interacts with SNX33 (via SH3
domain). Interacts with MYO1E (via SH3 domain). Interacts with
PSTPIP1. Interacts with CTNND2 (PubMed:22022388). May interact
with PIK3C3 (By similarity). May be a component of a complex
composed of RAB5A (in GDP-bound form), DYN2 and PIK3C3 (By
similarity). {ECO:0000250|UniProtKB:P39052,
ECO:0000250|UniProtKB:P39054, ECO:0000269|PubMed:11583995,
ECO:0000269|PubMed:15703209, ECO:0000269|PubMed:16234328,
ECO:0000269|PubMed:16325581, ECO:0000269|PubMed:17257598,
ECO:0000269|PubMed:18353773, ECO:0000269|PubMed:18480402,
ECO:0000269|PubMed:22022388}.
-!- INTERACTION:
Q8N157:AHI1; NbExp=2; IntAct=EBI-346547, EBI-1049056;
Q14247:CTTN; NbExp=5; IntAct=EBI-346547, EBI-351886;
P62993:GRB2; NbExp=6; IntAct=EBI-346547, EBI-401755;
Q15811:ITSN1; NbExp=2; IntAct=EBI-346547, EBI-602041;
Q12965:MYO1E; NbExp=2; IntAct=EBI-346547, EBI-4279548;
Q9UNF0:PACSIN2; NbExp=4; IntAct=EBI-346547, EBI-742503;
P54646:PRKAA2; NbExp=4; IntAct=EBI-346547, EBI-1383852;
Q15436:SEC23A; NbExp=4; IntAct=EBI-346547, EBI-81088;
Q9P0V3:SH3BP4; NbExp=3; IntAct=EBI-346547, EBI-1049513;
Q99962:SH3GL2; NbExp=2; IntAct=EBI-346547, EBI-77938;
Q96B97:SH3KBP1; NbExp=5; IntAct=EBI-346547, EBI-346595;
Q9Y5X1:SNX9; NbExp=4; IntAct=EBI-346547, EBI-77848;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Cell
junction {ECO:0000250|UniProtKB:P39052}. Membrane, clathrin-coated
pit {ECO:0000250|UniProtKB:P39052}. Cell junction, synapse,
postsynaptic cell membrane, postsynaptic density. Cell junction,
synapse. Midbody. Cell projection, phagocytic cup
{ECO:0000250|UniProtKB:P39054}. Cytoplasmic vesicle, phagosome
membrane {ECO:0000250|UniProtKB:P39054}; Peripheral membrane
protein {ECO:0000250|UniProtKB:P39054}. Note=Colocalizes with CTTN
at the basis of filopodia in hippocampus neuron growth zones (By
similarity). Microtubule-associated. Also found in the
postsynaptic density of neuronal cells. Co-localizes with PIK3C3
and RAB5A to the nascent phagosome (By similarity).
{ECO:0000250|UniProtKB:P39052, ECO:0000250|UniProtKB:P39054}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=P50570-1; Sequence=Displayed;
Name=2;
IsoId=P50570-2; Sequence=VSP_001325;
Name=3;
IsoId=P50570-3; Sequence=VSP_044280, VSP_001325;
Name=4;
IsoId=P50570-4; Sequence=VSP_044280;
Note=Gene prediction based on EST data.;
Name=5;
IsoId=P50570-5; Sequence=VSP_047534;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
-!- PTM: Phosphorylation at Ser-764 by CDK1 is greatly increased upon
mitotic entry. It regulates cytokinesis downstream of calcineurin,
and does not affect clathrin-mediated endocytosis.
Dephosphorylated by calcineurin/PP2 (By similarity).
Phosphorylated on tyrosine residues after activation of SRC (By
similarity). {ECO:0000250, ECO:0000250|UniProtKB:P39052}.
-!- DISEASE: Myopathy, centronuclear, 1 (CNM1) [MIM:160150]: A
congenital muscle disorder characterized by progressive muscular
weakness and wasting involving mainly limb girdle, trunk, and neck
muscles. It may also affect distal muscles. Weakness may be
present during childhood or adolescence or may not become evident
until the third decade of life. Ptosis is a frequent clinical
feature. The most prominent histopathologic features include high
frequency of centrally located nuclei in muscle fibers not
secondary to regeneration, radial arrangement of sarcoplasmic
strands around the central nuclei, and predominance and hypotrophy
of type 1 fibers. {ECO:0000269|PubMed:16227997,
ECO:0000269|PubMed:17825552, ECO:0000269|PubMed:17932957,
ECO:0000269|PubMed:19122038, ECO:0000269|PubMed:19623537,
ECO:0000269|PubMed:19932619, ECO:0000269|PubMed:19932620,
ECO:0000269|PubMed:20227276, ECO:0000269|PubMed:22396310}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Lethal congenital contracture syndrome 5 (LCCS5)
[MIM:615368]: A form of lethal congenital contracture syndrome, an
autosomal recessive disorder characterized by degeneration of
anterior horn neurons, extreme skeletal muscle atrophy and
congenital non-progressive joint contractures. The contractures
can involve the upper or lower limbs and/or the vertebral column,
leading to various degrees of flexion or extension limitations
evident at birth. {ECO:0000269|PubMed:23092955}. Note=The disease
is caused by mutations affecting the gene represented in this
entry.
-!- DISEASE: Charcot-Marie-Tooth disease, dominant, intermediate type,
B (CMTDIB) [MIM:606482]: A form of Charcot-Marie-Tooth disease, a
disorder of the peripheral nervous system, characterized by
progressive weakness and atrophy, initially of the peroneal
muscles and later of the distal muscles of the arms. The dominant
intermediate type B is characterized by clinical and pathologic
features intermediate between demyelinating and axonal peripheral
neuropathies, and motor median nerve conduction velocities ranging
from 25 to 45 m/sec. {ECO:0000269|PubMed:15731758,
ECO:0000269|PubMed:19623537}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Charcot-Marie-Tooth disease 2M (CMT2M) [MIM:606482]: An
axonal form of Charcot-Marie-Tooth disease, a disorder of the
peripheral nervous system, characterized by progressive weakness
and atrophy, initially of the peroneal muscles and later of the
distal muscles of the arms. Charcot-Marie-Tooth disease is
classified in two main groups on the basis of electrophysiologic
properties and histopathology: primary peripheral demyelinating
neuropathies (designated CMT1 when they are dominantly inherited)
and primary peripheral axonal neuropathies (CMT2). Neuropathies of
the CMT2 group are characterized by signs of axonal degeneration
in the absence of obvious myelin alterations, normal or slightly
reduced nerve conduction velocities, and progressive distal muscle
weakness and atrophy. Nerve conduction velocities are normal or
slightly reduced. {ECO:0000269|PubMed:17636067,
ECO:0000269|PubMed:18560793}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: Overexpression of CNM- and CMT-related DNM2 mutants
in COS7 cells, whatever the mutated domain, led to a reduction in
clathrin-mediated receptor endocytosis associated with MAPK ERK-1
and ERK-2 impairment. The membrane trafficking impairment process
may represent a common pathophysiological pathway in the autosomal
forms of CNM DNM2-CMT neuropathy.
-!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
superfamily. Dynamin/Fzo/YdjA family. {ECO:0000305}.
-!- WEB RESOURCE: Name=The UMD-DNM2-isoform 1 mutations database;
URL="http://www.umd.be/DNM2/";
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; L36983; AAA88025.1; -; mRNA.
EMBL; AK289831; BAF82520.1; -; mRNA.
EMBL; AK312260; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AC007229; AAD23604.1; -; Genomic_DNA.
EMBL; AC011475; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC011552; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC011554; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC112707; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC039596; AAH39596.1; -; mRNA.
EMBL; BC054501; AAH54501.1; -; mRNA.
CCDS; CCDS32907.1; -. [P50570-2]
CCDS; CCDS32908.1; -. [P50570-3]
CCDS; CCDS45968.1; -. [P50570-1]
CCDS; CCDS45969.1; -. [P50570-4]
CCDS; CCDS59351.1; -. [P50570-5]
PIR; JC4305; JC4305.
RefSeq; NP_001005360.1; NM_001005360.2. [P50570-1]
RefSeq; NP_001005361.1; NM_001005361.2. [P50570-4]
RefSeq; NP_001005362.1; NM_001005362.2. [P50570-3]
RefSeq; NP_001177645.1; NM_001190716.1. [P50570-5]
RefSeq; NP_004936.2; NM_004945.3. [P50570-2]
UniGene; Hs.211463; -.
PDB; 2YS1; NMR; -; A=520-625.
PDBsum; 2YS1; -.
ProteinModelPortal; P50570; -.
SMR; P50570; -.
BioGrid; 108122; 122.
DIP; DIP-31244N; -.
ELM; P50570; -.
IntAct; P50570; 98.
MINT; MINT-5004324; -.
STRING; 9606.ENSP00000347890; -.
BindingDB; P50570; -.
ChEMBL; CHEMBL5812; -.
iPTMnet; P50570; -.
PhosphoSitePlus; P50570; -.
SwissPalm; P50570; -.
BioMuta; DNM2; -.
DMDM; 47117856; -.
EPD; P50570; -.
MaxQB; P50570; -.
PaxDb; P50570; -.
PeptideAtlas; P50570; -.
PRIDE; P50570; -.
Ensembl; ENST00000355667; ENSP00000347890; ENSG00000079805. [P50570-1]
Ensembl; ENST00000359692; ENSP00000352721; ENSG00000079805. [P50570-2]
Ensembl; ENST00000389253; ENSP00000373905; ENSG00000079805. [P50570-4]
Ensembl; ENST00000408974; ENSP00000386192; ENSG00000079805. [P50570-3]
Ensembl; ENST00000585892; ENSP00000468734; ENSG00000079805. [P50570-5]
GeneID; 1785; -.
KEGG; hsa:1785; -.
UCSC; uc002mps.3; human. [P50570-1]
CTD; 1785; -.
DisGeNET; 1785; -.
GeneCards; DNM2; -.
GeneReviews; DNM2; -.
HGNC; HGNC:2974; DNM2.
HPA; HPA054246; -.
MalaCards; DNM2; -.
MIM; 160150; phenotype.
MIM; 602378; gene.
MIM; 606482; phenotype.
MIM; 615368; phenotype.
neXtProt; NX_P50570; -.
OpenTargets; ENSG00000079805; -.
Orphanet; 169189; Autosomal dominant centronuclear myopathy.
Orphanet; 228179; Autosomal dominant Charcot-Marie-Tooth disease type 2M.
Orphanet; 100044; Autosomal dominant intermediate Charcot-Marie-Tooth disease type B.
Orphanet; 363409; Fetal akinesia-cerebral and retinal hemorrhage syndrome.
PharmGKB; PA27442; -.
eggNOG; KOG0446; Eukaryota.
eggNOG; COG0699; LUCA.
GeneTree; ENSGT00760000119213; -.
HOGENOM; HOG000161069; -.
HOVERGEN; HBG107833; -.
InParanoid; P50570; -.
KO; K01528; -.
OMA; VESWKAS; -.
OrthoDB; EOG091G0EIQ; -.
PhylomeDB; P50570; -.
TreeFam; TF300362; -.
BRENDA; 3.6.5.5; 2681.
Reactome; R-HSA-166016; Toll Like Receptor 4 (TLR4) Cascade.
Reactome; R-HSA-177504; Retrograde neurotrophin signalling.
Reactome; R-HSA-190873; Gap junction degradation.
Reactome; R-HSA-196025; Formation of annular gap junctions.
Reactome; R-HSA-203641; NOSTRIN mediated eNOS trafficking.
Reactome; R-HSA-2132295; MHC class II antigen presentation.
Reactome; R-HSA-432720; Lysosome Vesicle Biogenesis.
Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
Reactome; R-HSA-437239; Recycling pathway of L1.
Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
SignaLink; P50570; -.
SIGNOR; P50570; -.
ChiTaRS; DNM2; human.
EvolutionaryTrace; P50570; -.
GeneWiki; DNM2; -.
GenomeRNAi; 1785; -.
PRO; PR:P50570; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000079805; -.
CleanEx; HS_DNM2; -.
ExpressionAtlas; P50570; baseline and differential.
Genevisible; P50570; HS.
GO; GO:0005813; C:centrosome; IEA:Ensembl.
GO; GO:0045334; C:clathrin-coated endocytic vesicle; IEA:Ensembl.
GO; GO:0005905; C:clathrin-coated pit; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
GO; GO:0005768; C:endosome; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0030426; C:growth cone; IEA:Ensembl.
GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
GO; GO:0005874; C:microtubule; IDA:UniProtKB.
GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
GO; GO:0031966; C:mitochondrial membrane; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0001891; C:phagocytic cup; IEA:UniProtKB-SubCell.
GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0001917; C:photoreceptor inner segment; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
GO; GO:0045211; C:postsynaptic membrane; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IEA:Ensembl.
GO; GO:0032587; C:ruffle membrane; IEA:Ensembl.
GO; GO:0005802; C:trans-Golgi network; IEA:Ensembl.
GO; GO:0031749; F:D2 dopamine receptor binding; IEA:Ensembl.
GO; GO:0019899; F:enzyme binding; NAS:UniProtKB.
GO; GO:0005525; F:GTP binding; NAS:UniProtKB.
GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
GO; GO:0050998; F:nitric-oxide synthase binding; IEA:Ensembl.
GO; GO:0036312; F:phosphatidylinositol 3-kinase regulatory subunit binding; IEA:Ensembl.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0017124; F:SH3 domain binding; IDA:UniProtKB.
GO; GO:0050699; F:WW domain binding; IEA:Ensembl.
GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
GO; GO:0035904; P:aorta development; IEA:Ensembl.
GO; GO:0071245; P:cellular response to carbon monoxide; IEA:Ensembl.
GO; GO:1903351; P:cellular response to dopamine; IEA:Ensembl.
GO; GO:0071732; P:cellular response to nitric oxide; IEA:Ensembl.
GO; GO:0071481; P:cellular response to X-ray; IEA:Ensembl.
GO; GO:0060976; P:coronary vasculature development; IEA:Ensembl.
GO; GO:0003374; P:dynamin family protein polymerization involved in mitochondrial fission; IBA:GO_Central.
GO; GO:0006897; P:endocytosis; NAS:UniProtKB.
GO; GO:0002031; P:G-protein coupled receptor internalization; IEA:Ensembl.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; NAS:UniProtKB.
GO; GO:0006893; P:Golgi to plasma membrane transport; IEA:Ensembl.
GO; GO:0044351; P:macropinocytosis; IEA:Ensembl.
GO; GO:0061025; P:membrane fusion; IBA:GO_Central.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0000266; P:mitochondrial fission; IBA:GO_Central.
GO; GO:1903526; P:negative regulation of membrane tubulation; IDA:UniProtKB.
GO; GO:1902856; P:negative regulation of non-motile cilium assembly; IEA:Ensembl.
GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
GO; GO:0043065; P:positive regulation of apoptotic process; NAS:UniProtKB.
GO; GO:0010592; P:positive regulation of lamellipodium assembly; IEA:Ensembl.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IEA:Ensembl.
GO; GO:0050766; P:positive regulation of phagocytosis; IEA:Ensembl.
GO; GO:1903408; P:positive regulation of sodium:potassium-exchanging ATPase activity; IEA:Ensembl.
GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IEA:Ensembl.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; NAS:UniProtKB.
GO; GO:0031623; P:receptor internalization; IMP:BHF-UCL.
GO; GO:0006898; P:receptor-mediated endocytosis; ISS:UniProtKB.
GO; GO:0030516; P:regulation of axon extension; ISS:UniProtKB.
GO; GO:1903358; P:regulation of Golgi organization; IEA:Ensembl.
GO; GO:0050999; P:regulation of nitric-oxide synthase activity; TAS:Reactome.
GO; GO:0035020; P:regulation of Rac protein signal transduction; IEA:Ensembl.
GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
GO; GO:0042220; P:response to cocaine; IEA:Ensembl.
GO; GO:0009416; P:response to light stimulus; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
GO; GO:0048489; P:synaptic vesicle transport; NAS:UniProtKB.
GO; GO:0033572; P:transferrin transport; IMP:BHF-UCL.
GO; GO:0003281; P:ventricular septum development; IEA:Ensembl.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR027188; DNM2.
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.
InterPro; IPR011993; PH_dom-like.
InterPro; IPR001849; PH_domain.
PANTHER; PTHR11566; PTHR11566; 1.
PANTHER; PTHR11566:SF94; PTHR11566:SF94; 1.
Pfam; PF01031; Dynamin_M; 1.
Pfam; PF00350; Dynamin_N; 1.
Pfam; PF02212; GED; 1.
Pfam; PF00169; PH; 1.
PRINTS; PR00195; DYNAMIN.
SMART; SM00053; DYNc; 1.
SMART; SM00302; GED; 1.
SMART; SM00233; PH; 1.
SUPFAM; SSF50729; SSF50729; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS00410; G_DYNAMIN_1; 1.
PROSITE; PS51718; G_DYNAMIN_2; 1.
PROSITE; PS51388; GED; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cell junction;
Cell membrane; Cell projection; Charcot-Marie-Tooth disease;
Coated pit; Complete proteome; Cytoplasm; Cytoplasmic vesicle;
Cytoskeleton; Disease mutation; Endocytosis; GTP-binding; Hydrolase;
Membrane; Microtubule; Motor protein; Neurodegeneration; Neuropathy;
Nucleotide-binding; Phagocytosis; Phosphoprotein; Polymorphism;
Postsynaptic cell membrane; Reference proteome; Synapse.
CHAIN 1 870 Dynamin-2.
/FTId=PRO_0000206570.
DOMAIN 28 294 Dynamin-type G.
DOMAIN 519 625 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 653 744 GED. {ECO:0000255|PROSITE-
ProRule:PRU00720}.
NP_BIND 38 46 GTP. {ECO:0000250|UniProtKB:O00429}.
NP_BIND 205 211 GTP. {ECO:0000250|UniProtKB:O00429}.
NP_BIND 236 239 GTP. {ECO:0000250|UniProtKB:O00429}.
COMPBIAS 747 866 Pro-rich.
MOD_RES 299 299 N6-acetyllysine.
{ECO:0000250|UniProtKB:P39054}.
MOD_RES 598 598 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 755 755 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 764 764 Phosphoserine; by CDK1.
{ECO:0000250|UniProtKB:P39052}.
VAR_SEQ 407 444 LAFEAIVKKQVVKLKEPCLKCVDLVIQELINTVRQCTS ->
MAFEAIVKKQIVKLKEPSLKCVDLVVSELATVIKKCAE
(in isoform 3 and isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044280.
VAR_SEQ 516 519 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:7590285}.
/FTId=VSP_001325.
VAR_SEQ 848 848 Missing (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_047534.
VARIANT 263 263 P -> L (in dbSNP:rs3745674).
/FTId=VAR_031961.
VARIANT 358 358 G -> R (in CMT2M; dbSNP:rs267606772).
{ECO:0000269|PubMed:18560793}.
/FTId=VAR_068425.
VARIANT 368 368 E -> K (in CNM1; dbSNP:rs121909092).
{ECO:0000269|PubMed:16227997,
ECO:0000269|PubMed:20227276}.
/FTId=VAR_031962.
VARIANT 368 368 E -> Q (in CNM1).
{ECO:0000269|PubMed:17825552}.
/FTId=VAR_068365.
VARIANT 369 369 R -> Q (in CNM1; dbSNP:rs121909089).
{ECO:0000269|PubMed:16227997}.
/FTId=VAR_031963.
VARIANT 369 369 R -> W (in CNM1; reduced association with
the centrosome; dbSNP:rs121909090).
{ECO:0000269|PubMed:16227997}.
/FTId=VAR_031964.
VARIANT 379 379 F -> V (in LCCS5; hypomorphic mutation
impacting on endocytosis;
dbSNP:rs397514735).
{ECO:0000269|PubMed:23092955}.
/FTId=VAR_070163.
VARIANT 465 465 R -> W (in CNM1; reduced association with
the centrosome; COS7 cells show a reduced
uptake of transferrin and low-density
lipoprotein complex; dbSNP:rs121909091).
{ECO:0000269|PubMed:16227997,
ECO:0000269|PubMed:19623537,
ECO:0000269|PubMed:20227276}.
/FTId=VAR_031965.
VARIANT 522 522 R -> C (in CNM1).
{ECO:0000269|PubMed:22396310}.
/FTId=VAR_068366.
VARIANT 522 522 R -> H (in CNM1; dbSNP:rs587783595).
{ECO:0000269|PubMed:20227276}.
/FTId=VAR_068367.
VARIANT 523 523 R -> G (in CNM1; dbSNP:rs587783596).
{ECO:0000269|PubMed:22396310}.
/FTId=VAR_068368.
VARIANT 537 537 G -> C (in CMT2M; dbSNP:rs121909093).
{ECO:0000269|PubMed:17636067}.
/FTId=VAR_062574.
VARIANT 555 557 Missing (in CMTDIB; may affect binding to
vesicles and membranes in favor of
binding to microtubules; may affect
receptor-mediated endocytosis).
{ECO:0000269|PubMed:15731758}.
/FTId=VAR_031966.
VARIANT 560 560 E -> K (in CNM1; dbSNP:rs879254086).
{ECO:0000269|PubMed:19122038}.
/FTId=VAR_068369.
VARIANT 562 562 K -> E (in CMTDIB; with neutropenia; COS7
cells show a reduced uptake of
transferrin and low-density lipoprotein
complex; dbSNP:rs121909088).
{ECO:0000269|PubMed:15731758,
ECO:0000269|PubMed:19623537}.
/FTId=VAR_031967.
VARIANT 562 562 Missing (in CMTDIB).
{ECO:0000269|PubMed:15731758}.
/FTId=VAR_070164.
VARIANT 570 570 L -> H (in CMT2M; dbSNP:rs121909094).
{ECO:0000269|PubMed:17636067}.
/FTId=VAR_062575.
VARIANT 618 618 A -> D (in CNM1).
{ECO:0000269|PubMed:19932619}.
/FTId=VAR_068370.
VARIANT 618 618 A -> T (in CNM1; severe).
{ECO:0000269|PubMed:17932957,
ECO:0000269|PubMed:20227276}.
/FTId=VAR_039041.
VARIANT 619 619 S -> L (in CNM1; severe;
dbSNP:rs121909095).
{ECO:0000269|PubMed:17932957,
ECO:0000269|PubMed:20227276}.
/FTId=VAR_039042.
VARIANT 619 619 S -> W (in CNM1; severe;
dbSNP:rs121909095).
{ECO:0000269|PubMed:17932957}.
/FTId=VAR_039043.
VARIANT 621 621 L -> P (in CNM1; centronuclear myopathy
with cataracts; dbSNP:rs587783597).
{ECO:0000269|PubMed:19932620}.
/FTId=VAR_068371.
VARIANT 625 625 Missing (in CNM1; severe; COS7 cells show
a reduced uptake of transferrin and low-
density lipoprotein complex).
{ECO:0000269|PubMed:17932957,
ECO:0000269|PubMed:19623537}.
/FTId=VAR_039044.
VARIANT 627 627 P -> H (in CNM1).
{ECO:0000269|PubMed:20227276}.
/FTId=VAR_068372.
VARIANT 627 627 P -> R (in CNM1; dbSNP:rs587783598).
{ECO:0000269|PubMed:22396310}.
/FTId=VAR_068373.
VARIANT 650 650 E -> K (in CNM1; COS7 cells show a
reduced uptake of transferrin and low-
density lipoprotein complex).
{ECO:0000269|PubMed:19623537}.
/FTId=VAR_062576.
CONFLICT 155 156 QI -> RV (in Ref. 1; AAA88025).
{ECO:0000305}.
CONFLICT 207 207 L -> P (in Ref. 2; AK312260).
{ECO:0000305}.
CONFLICT 316 316 N -> I (in Ref. 1; AAA88025).
{ECO:0000305}.
CONFLICT 324 324 R -> P (in Ref. 1; AAA88025).
{ECO:0000305}.
CONFLICT 475 475 I -> T (in Ref. 2; AK312260).
{ECO:0000305}.
STRAND 522 530 {ECO:0000244|PDB:2YS1}.
STRAND 533 535 {ECO:0000244|PDB:2YS1}.
STRAND 540 545 {ECO:0000244|PDB:2YS1}.
STRAND 550 555 {ECO:0000244|PDB:2YS1}.
STRAND 560 565 {ECO:0000244|PDB:2YS1}.
STRAND 567 573 {ECO:0000244|PDB:2YS1}.
STRAND 585 590 {ECO:0000244|PDB:2YS1}.
STRAND 596 599 {ECO:0000244|PDB:2YS1}.
STRAND 601 606 {ECO:0000244|PDB:2YS1}.
HELIX 610 623 {ECO:0000244|PDB:2YS1}.
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


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