DYN2_MOUSE
ID DYN2_MOUSE Reviewed; 870 AA.
AC P39054; Q9DBE1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 26-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Dynamin-2;
DE EC=3.6.5.5;
DE AltName: Full=Dynamin UDNM;
GN Name=Dnm2; Synonyms=Dyn2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=NIH Swiss;
RX PubMed=9143510; DOI=10.1006/geno.1997.4634;
RA Klocke R., Augustin A., Ronsiek M., Stief A., van der Putten H.,
RA Jockusch H.;
RT "Dynamin genes Dnm1 and Dnm2 are located on proximal mouse chromosomes 2
RT and 9, respectively.";
RL Genomics 41:290-292(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP PROTEIN SEQUENCE OF 45-54; 91-107; 114-142; 207-217; 230-237; 300-309;
RP 370-376 AND 678-688, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
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 [5]
RP INTERACTION WITH MYOF.
RX PubMed=17702744; DOI=10.1074/jbc.m704798200;
RA Bernatchez P.N., Acevedo L., Fernandez-Hernando C., Murata T., Chalouni C.,
RA Kim J., Erdjument-Bromage H., Shah V., Gratton J.-P., McNally E.M.,
RA Tempst P., Sessa W.C.;
RT "Myoferlin regulates vascular endothelial growth factor receptor-2
RT stability and function.";
RL J. Biol. Chem. 282:30745-30753(2007).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18923138; DOI=10.1091/mbc.e08-08-0890;
RA Liu Y.W., Surka M.C., Schroeter T., Lukiyanchuk V., Schmid S.L.;
RT "Isoform and splice-variant specific functions of dynamin-2 revealed by
RT analysis of conditional knock-out cells.";
RL Mol. Biol. Cell 19:5347-5359(2008).
RN [7]
RP FUNCTION, INTERACTION WITH PIK3C3, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP LYS-44.
RX PubMed=18425118; DOI=10.1038/ncb1718;
RA Kinchen J.M., Doukoumetzidis K., Almendinger J., Stergiou L.,
RA Tosello-Trampont A., Sifri C.D., Hengartner M.O., Ravichandran K.S.;
RT "A pathway for phagosome maturation during engulfment of apoptotic cells.";
RL Nat. Cell Biol. 10:556-566(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=23092955; DOI=10.1038/ejhg.2012.226;
RA Koutsopoulos O.S., Kretz C., Weller C.M., Roux A., Mojzisova H., Boehm J.,
RA Koch C., Toussaint A., Heckel E., Stemkens D., Ter Horst S.A., Thibault C.,
RA Koch M., Mehdi S.Q., Bijlsma E.K., Mandel J.L., Vermot J., Laporte J.;
RT "Dynamin 2 homozygous mutation in humans with a lethal congenital
RT syndrome.";
RL Eur. J. Hum. Genet. 21:637-642(2013).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-299, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(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 Involved in cytokinesis (PubMed:18923138). Regulates maturation of
CC apoptotic cell corpse-containing phagosomes by recruiting PIK3C3 to the
CC phagosome membrane (PubMed:18425118). {ECO:0000250|UniProtKB:P39052,
CC ECO:0000269|PubMed:18425118, ECO:0000269|PubMed:18923138}.
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 (PubMed:17702744). Interacts with CTTN and
CC ACTN1 (By similarity). Interacts with SHANK1, SHANK2 and NOSTRIN.
CC Interacts with SH3BP4 (PubMed:17702744, PubMed:16325581). Interacts
CC with SNX9. Interacts with SNX18. Interacts with SNX33 (via SH3 domain).
CC Interacts with MYO1E (via SH3 domain). Interacts with PSTPIP1.
CC Interacts with CTNND2 (By similarity). May interact with PIK3C3
CC (PubMed:18425118). May be a component of a complex composed of RAB5A
CC (in GDP-bound form), DYN2 and PIK3C3 (PubMed:18425118). Interacts with
CC BIN1 (By similarity). {ECO:0000250|UniProtKB:P39052,
CC ECO:0000250|UniProtKB:P50570, ECO:0000269|PubMed:16325581,
CC ECO:0000269|PubMed:17702744, ECO:0000305|PubMed:18425118}.
CC -!- INTERACTION:
CC P39054; Q7TQF7: Amph; NbExp=5; IntAct=EBI-642337, EBI-775139;
CC P39054; Q60598: Cttn; NbExp=2; IntAct=EBI-642337, EBI-397955;
CC P39054; Q01406: CTTN1; Xeno; NbExp=2; IntAct=EBI-642337, EBI-2530463;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P50570}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P50570}. Cell junction
CC {ECO:0000250|UniProtKB:P39052}. Membrane, clathrin-coated pit
CC {ECO:0000250|UniProtKB:P39052}. Postsynaptic density
CC {ECO:0000250|UniProtKB:P50570}. Synapse {ECO:0000250|UniProtKB:P50570}.
CC Midbody {ECO:0000250|UniProtKB:P50570}. Cell projection, phagocytic cup
CC {ECO:0000269|PubMed:18425118}. Cytoplasmic vesicle, phagosome membrane
CC {ECO:0000269|PubMed:18425118}; Peripheral membrane protein
CC {ECO:0000269|PubMed:18425118}. Note=Colocalizes with CTTN at the basis
CC of filopodia in hippocampus neuron growth zones. Microtubule-
CC associated. Also found in the postsynaptic density of neuronal cells
CC (By similarity). Co-localizes with PIK3C3 and RAB5A to the nascent
CC phagosome (PubMed:18425118). {ECO:0000250|UniProtKB:P39052,
CC ECO:0000250|UniProtKB:P50570, ECO:0000269|PubMed:18425118}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P39054-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P39054-2; Sequence=VSP_001326;
CC -!- TISSUE SPECIFICITY: Expressed in most tissues during embryonic
CC development, including the peripheral nervous system although no
CC expression is evident in skeletal muscle or heart.
CC {ECO:0000269|PubMed:23092955}.
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 -!- DISRUPTION PHENOTYPE: Exhibits growth and cytokinesis defects.
CC {ECO:0000269|PubMed:18923138}.
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; L31398; AAA40523.1; -; mRNA.
DR EMBL; AK005012; BAB23745.1; -; mRNA.
DR CCDS; CCDS57657.1; -. [P39054-1]
DR CCDS; CCDS57659.1; -. [P39054-2]
DR RefSeq; NP_001240822.1; NM_001253893.1. [P39054-1]
DR RefSeq; NP_001240823.1; NM_001253894.1.
DR RefSeq; NP_031897.2; NM_007871.2. [P39054-2]
DR AlphaFoldDB; P39054; -.
DR BMRB; P39054; -.
DR SMR; P39054; -.
DR BioGRID; 199258; 34.
DR IntAct; P39054; 20.
DR MINT; P39054; -.
DR STRING; 10090.ENSMUSP00000133564; -.
DR iPTMnet; P39054; -.
DR PhosphoSitePlus; P39054; -.
DR REPRODUCTION-2DPAGE; IPI00131445; -.
DR EPD; P39054; -.
DR jPOST; P39054; -.
DR MaxQB; P39054; -.
DR PaxDb; P39054; -.
DR PeptideAtlas; P39054; -.
DR PRIDE; P39054; -.
DR ProteomicsDB; 277426; -. [P39054-1]
DR ProteomicsDB; 277427; -. [P39054-2]
DR Antibodypedia; 25505; 252 antibodies from 34 providers.
DR DNASU; 13430; -.
DR Ensembl; ENSMUST00000091087; ENSMUSP00000088616; ENSMUSG00000033335. [P39054-2]
DR Ensembl; ENSMUST00000172482; ENSMUSP00000133564; ENSMUSG00000033335. [P39054-1]
DR GeneID; 13430; -.
DR KEGG; mmu:13430; -.
DR UCSC; uc009olk.2; mouse. [P39054-2]
DR UCSC; uc029wxt.1; mouse. [P39054-1]
DR CTD; 1785; -.
DR MGI; MGI:109547; Dnm2.
DR VEuPathDB; HostDB:ENSMUSG00000033335; -.
DR eggNOG; KOG0446; Eukaryota.
DR GeneTree; ENSGT00940000155764; -.
DR HOGENOM; CLU_008964_5_0_1; -.
DR InParanoid; P39054; -.
DR OrthoDB; 264244at2759; -.
DR PhylomeDB; P39054; -.
DR TreeFam; TF300362; -.
DR BRENDA; 3.6.5.5; 3474.
DR Reactome; R-MMU-166016; Toll Like Receptor 4 (TLR4) Cascade.
DR Reactome; R-MMU-190873; Gap junction degradation.
DR Reactome; R-MMU-196025; Formation of annular gap junctions.
DR Reactome; R-MMU-203641; NOSTRIN mediated eNOS trafficking.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-MMU-437239; Recycling pathway of L1.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 13430; 30 hits in 74 CRISPR screens.
DR ChiTaRS; Dnm2; mouse.
DR PRO; PR:P39054; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P39054; protein.
DR Bgee; ENSMUSG00000033335; Expressed in granulocyte and 243 other tissues.
DR ExpressionAtlas; P39054; baseline and differential.
DR Genevisible; P39054; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0030054; C:cell junction; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0045334; C:clathrin-coated endocytic vesicle; ISO:MGI.
DR GO; GO:0005905; C:clathrin-coated pit; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; ISO:MGI.
DR GO; GO:0030426; C:growth cone; ISO:MGI.
DR GO; GO:0030027; C:lamellipodium; ISO:MGI.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0001891; C:phagocytic cup; ISO:MGI.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001917; C:photoreceptor inner segment; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0099092; C:postsynaptic density, intracellular component; ISO:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0032587; C:ruffle membrane; ISO:MGI.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
DR GO; GO:0031749; F:D2 dopamine receptor binding; ISO:MGI.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0050998; F:nitric-oxide synthase binding; ISO:MGI.
DR GO; GO:0036312; F:phosphatidylinositol 3-kinase regulatory subunit binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
DR GO; GO:0050699; F:WW domain binding; ISO:MGI.
DR GO; GO:0035904; P:aorta development; IMP:MGI.
DR GO; GO:1903351; P:cellular response to dopamine; ISO:MGI.
DR GO; GO:0060976; P:coronary vasculature development; IMP:MGI.
DR GO; GO:0006897; P:endocytosis; ISO:MGI.
DR GO; GO:0002031; P:G protein-coupled receptor internalization; ISO:MGI.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; ISO:MGI.
DR GO; GO:0044351; P:macropinocytosis; ISO:MGI.
DR GO; GO:1903526; P:negative regulation of membrane tubulation; ISO:MGI.
DR GO; GO:1902856; P:negative regulation of non-motile cilium assembly; ISO:MGI.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISO:MGI.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
DR GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
DR GO; GO:2000370; P:positive regulation of clathrin-dependent endocytosis; ISO:MGI.
DR GO; GO:0045807; P:positive regulation of endocytosis; ISO:MGI.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; ISO:MGI.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISO:MGI.
DR GO; GO:1903408; P:positive regulation of P-type sodium:potassium-exchanging transporter activity; ISO:MGI.
DR GO; GO:0050766; P:positive regulation of phagocytosis; ISO:MGI.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISO:MGI.
DR GO; GO:0031623; P:receptor internalization; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0035020; P:regulation of Rac protein signal transduction; ISO:MGI.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IDA:SynGO.
DR GO; GO:0033572; P:transferrin transport; ISO:MGI.
DR GO; GO:0003281; P:ventricular septum development; IMP:MGI.
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 Acetylation; Alternative splicing; Cell junction; Cell projection;
KW Coated pit; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW Direct protein sequencing; Endocytosis; GTP-binding; Hydrolase; Membrane;
KW Microtubule; Motor protein; Nucleotide-binding; Phagocytosis;
KW Phosphoprotein; Reference proteome; Synapse.
FT CHAIN 1..870
FT /note="Dynamin-2"
FT /id="PRO_0000206571"
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 741..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..851
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:0007744|PubMed:23806337"
FT MOD_RES 597
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P39052"
FT MOD_RES 598
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P50570"
FT MOD_RES 755
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P50570"
FT MOD_RES 764
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:P39052"
FT VAR_SEQ 516..519
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9143510"
FT /id="VSP_001326"
FT MUTAGEN 44
FT /note="K->A: Apoptotic cell corpse-containing phagosomes
FT fail to mature into acidic phagosomes. Loss of PIK3C3 and
FT RAB5A recruitment to phagosomes."
FT /evidence="ECO:0000269|PubMed:18425118"
FT CONFLICT 297..298
FT /note="RS -> HG (in Ref. 1; AAA40523)"
FT /evidence="ECO:0000305"
FT CONFLICT 848..870
FT /note="SRRAPAAPSRPTIIRPAEPSLLD -> RRPPPLAPARPFF (in Ref. 2;
FT BAB23745)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 870 AA; 98145 MW; E80864AF94B8F778 CRC64;
MGNRGMEELI PLVNKLQDAF SSIGQSCHLD LPQIAVVGGQ SAGKSSVLEN FVGRDFLPRG
SGIVTRRPLI LQLIFSKTEY AEFLHCKSKK FTDFDEVRQE IEAETDRVTG TNKGISPVPI
NLRVYSPHVL NLTLIDLPGI TKVPVGDQPP DIEYQIKDMI LQFISRESSL ILAVTPANMD
LANSDALKLA KEVDPQGLRT IGVITKLDLM DEGTDARDVL ENKLLPLRRG YIGVVNRSQK
DIEGKKDIRA ALAAERKFFL SHPAYRHMAD RMGTPHLQKT LNQQLTNHIR ESLPTLRSKL
QSQLLSLEKE VEEYKNFRPD DPTRKTKALL QMVQQFGVDF EKRIEGSGDQ VDTLELSGGA
RINRIFHERF PFELVKMEFD EKDLRREISY AIKNIHGVRT GLFTPDLAFE AIVKKQVVKL
KEPCLKCVDL VIQELISTVR 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 ESAEQAQRRD
DMLRMYHALK EALNIIGDIS TSTVSTPVPP PVDDTWLQNT SGHSPTPQRR PVSSVHPPGR
PPAVRGPTPG PPLIPMPVGA TSSFSAPPIP SRPGPQSVFA NNDPFSAPPQ IPSRPARIPP
GIPPGVPSRR APAAPSRPTI IRPAEPSLLD
