DYN1_MOUSE
ID DYN1_MOUSE Reviewed; 867 AA.
AC P39053; A2AN50; A2AN51; A2AN54; A2AN55; Q3UNM1; Q5DTN7; Q61358; Q61359;
AC Q61360; Q6PDM5; Q8JZZ4; Q9CSY7; Q9QXX1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Dynamin-1;
DE EC=3.6.5.5;
GN Name=Dnm1; Synonyms=Dnm, Kiaa4093;
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] (ISOFORMS 3; 4; 5 AND 6).
RC STRAIN=NIH Swiss; TISSUE=Brain;
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 6).
RC STRAIN=C57BL/6J; TISSUE=Colon, and Embryo;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Retina;
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32.
RX PubMed=11042120; DOI=10.1042/bj3510661;
RA Yoo J., Lee S.S., Jeong M.J., Lee K.I., Kwon B.M., Kim S.H., Park Y.M.,
RA Han M.Y.;
RT "Characterization of the mouse dynamin I gene promoter and identification
RT of sequences that direct expression in neuronal cells.";
RL Biochem. J. 351:661-668(2000).
RN [7]
RP PROTEIN SEQUENCE OF 5-54; 67-87; 91-107; 114-188; 207-217; 230-237;
RP 247-266; 280-290; 300-309; 328-361; 370-376; 400-414; 511-535; 563-571;
RP 584-594; 664-675 AND 684-694.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [8]
RP INTERACTION WITH PACSIN1; PACSIN2 AND PACSIN3, AND SUBCELLULAR LOCATION.
RX PubMed=11082044; DOI=10.1242/jcs.113.24.4511;
RA Modregger J., Ritter B., Witter B., Paulsson M., Plomann M.;
RT "All three PACSIN isoforms bind to endocytic proteins and inhibit
RT endocytosis.";
RL J. Cell Sci. 113:4511-4521(2000).
RN [9]
RP INTERACTION WITH CAV1, AND PHOSPHORYLATION.
RX PubMed=11956154; DOI=10.1210/endo.143.5.8814;
RA Kim Y.N., Bertics P.J.;
RT "The endocytosis-linked protein dynamin associates with caveolin-1 and is
RT tyrosine phosphorylated in response to the activation of a noninternalizing
RT epidermal growth factor receptor mutant.";
RL Endocrinology 143:1726-1731(2002).
RN [10]
RP INTERACTION WITH SH3GLB1.
RX PubMed=12456676; DOI=10.1074/jbc.m208568200;
RA Modregger J., Schmidt A.A., Ritter B., Huttner W.B., Plomann M.;
RT "Characterization of endophilin B1b, a brain-specific membrane-associated
RT lysophosphatidic acid acyl transferase with properties distinct from
RT endophilin A1.";
RL J. Biol. Chem. 278:4160-4167(2003).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [12]
RP NITRATION [LARGE SCALE ANALYSIS] AT TYR-125, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16800626; DOI=10.1021/bi060474w;
RA Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H., Lacan G.,
RA Melega W.P., Camp D.G. II, Smith R.D., Smith D.J., Squier T.C.,
RA Bigelow D.J.;
RT "Endogenously nitrated proteins in mouse brain: links to neurodegenerative
RT disease.";
RL Biochemistry 45:8009-8022(2006).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-80; TYR-125 AND TYR-354, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-847 (ISOFORM 6), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306 AND SER-512,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-851 AND SER-857 (ISOFORM 4),
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, 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 [16]
RP INTERACTION WITH UNC119.
RX PubMed=19781630; DOI=10.1016/j.cellsig.2009.09.022;
RA Karim Z., Vepachedu R., Gorska M., Alam R.;
RT "UNC119 inhibits dynamin and dynamin-dependent endocytic processes.";
RL Cell. Signal. 22:128-137(2010).
RN [17]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-796, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Microtubule-associated force-producing protein involved in
CC producing microtubule bundles and able to bind and hydrolyze GTP. Most
CC probably involved in vesicular trafficking processes. Involved in
CC receptor-mediated endocytosis (By similarity). {ECO:0000250}.
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: Binds SH3GL1, SH3GL2 and SH3GL3 (By similarity). Interacts
CC with SNX9 (By similarity). Interacts with PHOCN. Interacts with MYO1E
CC (via SH3 domain). Interacts with SNX33 (via SH3 domain) (By
CC similarity). Interacts with CAV1 and SH3GLB1. Interacts with PACSIN1,
CC PACSIN2 and PACSIN3. Interacts with UNC119; leading to a decrease of
CC DNM1 GTPase activity. Interacts with DIAPH1 (By similarity). Interacts
CC with AMPH, BIN1 AND SYNJ1 (By similarity).
CC {ECO:0000250|UniProtKB:P21575, ECO:0000250|UniProtKB:Q05193,
CC ECO:0000269|PubMed:11082044, ECO:0000269|PubMed:11956154,
CC ECO:0000269|PubMed:12456676, ECO:0000269|PubMed:19781630}.
CC -!- INTERACTION:
CC P39053; Q7TQF7: Amph; NbExp=3; IntAct=EBI-397785, EBI-775139;
CC P39053; Q9JJV2-1: Pfn2; NbExp=2; IntAct=EBI-397785, EBI-990256;
CC P39053; Q5S007: LRRK2; Xeno; NbExp=3; IntAct=EBI-397785, EBI-5323863;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11082044}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11082044}.
CC Note=Microtubule-associated.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=P39053-1; Sequence=Displayed;
CC Name=3; Synonyms=BraDnm8;
CC IsoId=P39053-3; Sequence=VSP_007643, VSP_007645;
CC Name=4; Synonyms=BraDnm2;
CC IsoId=P39053-4; Sequence=VSP_007647;
CC Name=5; Synonyms=BreDnm15;
CC IsoId=P39053-5; Sequence=VSP_007645;
CC Name=6;
CC IsoId=P39053-6; Sequence=VSP_007644, VSP_024845;
CC -!- PTM: Phosphorylated in response to EGF stimulation in cells expressing
CC truncated EGFR. {ECO:0000269|PubMed:11956154}.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. Dynamin/Fzo/YdjA family. {ECO:0000255|PROSITE-
CC ProRule:PRU01055}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD90284.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- SEQUENCE CAUTION: [Isoform 6]:
CC Sequence=AAA37324.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L29457; AAA37319.1; -; mRNA.
DR EMBL; L31395; AAA37318.1; -; mRNA.
DR EMBL; L31396; AAA37323.1; -; mRNA.
DR EMBL; L31397; AAA37324.1; ALT_FRAME; mRNA.
DR EMBL; AK011651; BAB27759.1; -; mRNA.
DR EMBL; AK144142; BAE25726.1; -; mRNA.
DR EMBL; AK220483; BAD90284.1; ALT_INIT; mRNA.
DR EMBL; AL808027; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC034679; AAH34679.1; -; mRNA.
DR EMBL; BC058623; AAH58623.1; -; mRNA.
DR EMBL; AF170568; AAF24220.1; -; Genomic_DNA.
DR CCDS; CCDS38102.1; -. [P39053-6]
DR CCDS; CCDS79772.1; -. [P39053-3]
DR RefSeq; NP_001288666.1; NM_001301737.1. [P39053-3]
DR RefSeq; NP_034195.2; NM_010065.3. [P39053-6]
DR RefSeq; XP_006497718.2; XM_006497655.2. [P39053-4]
DR RefSeq; XP_006497721.2; XM_006497658.3. [P39053-3]
DR RefSeq; XP_006497722.2; XM_006497659.3. [P39053-3]
DR RefSeq; XP_006497723.2; XM_006497660.2. [P39053-3]
DR RefSeq; XP_006497724.2; XM_006497661.2. [P39053-5]
DR RefSeq; XP_017170817.1; XM_017315328.1. [P39053-5]
DR AlphaFoldDB; P39053; -.
DR BMRB; P39053; -.
DR SMR; P39053; -.
DR BioGRID; 199257; 57.
DR CORUM; P39053; -.
DR IntAct; P39053; 36.
DR MINT; P39053; -.
DR STRING; 10090.ENSMUSP00000088618; -.
DR ChEMBL; CHEMBL4523222; -.
DR iPTMnet; P39053; -.
DR PhosphoSitePlus; P39053; -.
DR SwissPalm; P39053; -.
DR EPD; P39053; -.
DR jPOST; P39053; -.
DR MaxQB; P39053; -.
DR PaxDb; P39053; -.
DR PeptideAtlas; P39053; -.
DR PRIDE; P39053; -.
DR ProteomicsDB; 277649; -. [P39053-1]
DR ProteomicsDB; 277650; -. [P39053-3]
DR ProteomicsDB; 277651; -. [P39053-4]
DR ProteomicsDB; 277652; -. [P39053-5]
DR ProteomicsDB; 277653; -. [P39053-6]
DR Antibodypedia; 3472; 688 antibodies from 46 providers.
DR DNASU; 13429; -.
DR Ensembl; ENSMUST00000078352; ENSMUSP00000077461; ENSMUSG00000026825. [P39053-3]
DR Ensembl; ENSMUST00000091089; ENSMUSP00000088618; ENSMUSG00000026825. [P39053-6]
DR Ensembl; ENSMUST00000113350; ENSMUSP00000108977; ENSMUSG00000026825. [P39053-5]
DR Ensembl; ENSMUST00000113352; ENSMUSP00000108979; ENSMUSG00000026825. [P39053-5]
DR Ensembl; ENSMUST00000113365; ENSMUSP00000108992; ENSMUSG00000026825. [P39053-4]
DR Ensembl; ENSMUST00000139624; ENSMUSP00000122679; ENSMUSG00000026825. [P39053-1]
DR Ensembl; ENSMUST00000202578; ENSMUSP00000143955; ENSMUSG00000026825. [P39053-3]
DR GeneID; 13429; -.
DR KEGG; mmu:13429; -.
DR UCSC; uc008jfc.2; mouse. [P39053-6]
DR UCSC; uc008jfd.3; mouse. [P39053-3]
DR UCSC; uc029twn.1; mouse. [P39053-5]
DR CTD; 1759; -.
DR MGI; MGI:107384; Dnm1.
DR VEuPathDB; HostDB:ENSMUSG00000026825; -.
DR eggNOG; KOG0446; Eukaryota.
DR GeneTree; ENSGT00940000155214; -.
DR InParanoid; P39053; -.
DR OMA; MQMVQTF; -.
DR OrthoDB; 264244at2759; -.
DR PhylomeDB; P39053; -.
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-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-437239; Recycling pathway of L1.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 13429; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Dnm1; mouse.
DR PRO; PR:P39053; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P39053; protein.
DR Bgee; ENSMUSG00000026825; Expressed in CA3 field of hippocampus and 224 other tissues.
DR ExpressionAtlas; P39053; baseline and differential.
DR Genevisible; P39053; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IMP:SynGO.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0030117; C:membrane coat; IDA:MGI.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0001917; C:photoreceptor inner segment; IDA:MGI.
DR GO; GO:0098684; C:photoreceptor ribbon synapse; IDA:SynGO.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0098835; C:presynaptic endocytic zone membrane; IDA:SynGO.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR GO; GO:0043196; C:varicosity; 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; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI: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:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
DR GO; GO:0006897; P:endocytosis; ISO:MGI.
DR GO; GO:0007032; P:endosome organization; ISO:MGI.
DR GO; GO:0002031; P:G protein-coupled receptor internalization; ISO:MGI.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IMP:SynGO.
DR GO; GO:1900244; P:positive regulation of synaptic vesicle endocytosis; ISO:MGI.
DR GO; GO:1903423; P:positive regulation of synaptic vesicle recycling; ISO:MGI.
DR GO; GO:0031623; P:receptor internalization; ISO:MGI.
DR GO; GO:0006898; P:receptor-mediated endocytosis; ISO:MGI.
DR GO; GO:1900242; P:regulation of synaptic vesicle endocytosis; ISO:MGI.
DR GO; GO:0016185; P:synaptic vesicle budding from presynaptic endocytic zone membrane; IGI:SynGO.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IDA:SynGO.
DR GO; GO:1901998; P:toxin transport; IMP:MGI.
DR CDD; cd08771; DLP_1; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027741; DNM1.
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:SF32; PTHR11566:SF32; 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 Alternative splicing; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Endocytosis; GTP-binding; Hydrolase; Methylation; Microtubule;
KW Motor protein; Nitration; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..867
FT /note="Dynamin-1"
FT /id="PRO_0000206564"
FT DOMAIN 28..294
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 515..625
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 659..750
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 767..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..781
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..840
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 38..45
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 136..140
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 205..208
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 80
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 125
FT /note="3'-nitrotyrosine; alternate"
FT /evidence="ECO:0007744|PubMed:16800626"
FT MOD_RES 125
FT /note="Phosphotyrosine; alternate"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21575"
FT MOD_RES 354
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 512
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 774
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21575"
FT MOD_RES 778
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21575"
FT MOD_RES 796
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 822
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21575"
FT VAR_SEQ 407..444
FT /note="MAFETIVKKQVKKIREPCLKCVDMVISELISTVRQCTK -> LAFEATVKKQ
FT VQKLKEPSIKCVDMVVSELTSTIRKCSE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9143510, ECO:0000303|Ref.3"
FT /id="VSP_007643"
FT VAR_SEQ 516..519
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:9143510"
FT /id="VSP_007644"
FT VAR_SEQ 845..867
FT /note="SLGAWRLNSPQGKHENRAGKARL -> RITISDP (in isoform 3 and
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9143510, ECO:0000303|Ref.3"
FT /id="VSP_007645"
FT VAR_SEQ 846..867
FT /note="LGAWRLNSPQGKHENRAGKARL -> RSGQASPSRPESPRPPFDL (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:9143510"
FT /id="VSP_007647"
FT VAR_SEQ 846..867
FT /note="LGAWRLNSPQGKHENRAGKARL -> RKGPASPTRPAAPRPTEAPLLDL
FT (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024845"
FT CONFLICT 135
FT /note="V -> A (in Ref. 1; AAA37318)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="P -> R (in Ref. 1; AAA37318)"
FT /evidence="ECO:0000305"
FT CONFLICT 531
FT /note="I -> S (in Ref. 1; AAA37318)"
FT /evidence="ECO:0000305"
FT CONFLICT 573
FT /note="R -> H (in Ref. 2; BAE25726)"
FT /evidence="ECO:0000305"
FT CONFLICT 600
FT /note="Y -> N (in Ref. 1; AAA37318)"
FT /evidence="ECO:0000305"
FT CONFLICT 703
FT /note="A -> V (in Ref. 5; AAH58623)"
FT /evidence="ECO:0000305"
FT CONFLICT 722
FT /note="A -> R (in Ref. 1; AAA37319/AAA37323/AAA37324)"
FT /evidence="ECO:0000305"
FT MOD_RES P39053-4:851
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES P39053-4:857
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES P39053-6:847
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
SQ SEQUENCE 867 AA; 97803 MW; F48EC3DF5F39A08B CRC64;
MGNRGMEDLI PLVNRLQDAF SAIGQNADLD LPQIAVVGGQ SAGKSSVLEN FVGRDFLPRG
SGIVTRRPLV LQLVNSTTEY AEFLHCKGKK FTDFEEVRLE IEAETDRVTG TNKGISPVPI
NLRVYSPHVL NLTLVDLPGM TKVPVGDQPP DIEFQIRDML MQFVTKENCL ILAVSPANSD
LANSDALKIA KEVDPQGQRT IGVITKLDLM DEGTDARDVL ENKLLPLRRG YIGVVNRSQK
DIDGKKDITA ALAAERKFFL SHPSYRHLAD RMGTPYLQKV LNQQLTNHIR DTLPGLRNKL
QSQLLSIEKE VDEYKNFRPD DPARKTKALL QMVQQFAVDF EKRIEGSGDQ IDTYELSGGA
RINRIFHERF PFELVKMEFD EKELRREISY AIKNIHGIRT GLFTPDMAFE TIVKKQVKKI
REPCLKCVDM VISELISTVR QCTKKLQQYP RLREEMERIV TTHIREREGR TKEQVMLLID
IELAYMNTNH EDFIGFANAQ QRSNQMNKKK TSGNQDEILV IRKGWLTINN IGIMKGGSKE
YWFVLTAENL SWYKDDEEKE KKYMLSVDNL KLRDVEKGFM SSKHIFALFN TEQRNVYKDY
RQLELACETQ EEVDSWKASF LRAGVYPERV GDKEKASETE ENGSDSFMHS MDPQLERQVE
TIRNLVDSYM AIVNKTVRDL MPKTIMHLMI NNTKEFIFSE LLANLYSCGD QNTLMEESAE
QAQRRDEMLR MYHALKEALS IIGDINTTTV STPMPPPVDD SWLQVQSVPA GRRSPTSSPT
PQRRAPAVPP ARPGSRGPAP GPPPAGSALG GAPPVPSRPG ASPDPFGPPP QVPSRPNRAP
PGVPSLGAWR LNSPQGKHEN RAGKARL
