DYN1_HUMAN
ID DYN1_HUMAN Reviewed; 864 AA.
AC Q05193; A6NLM6; Q5SYX0; Q5SYX2; Q6P3T6; Q86VD2;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, 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;
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] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF
RP 387-466 (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF 726-856 (ISOFORM 3),
RP MUTAGENESIS OF LYS-44, AND VARIANT ASN-744.
RX PubMed=8101525; DOI=10.1083/jcb.122.3.553;
RA van der Bliek A.M., Redelmeier T.E., Tisdale E.J., Meyerowitz E.M.,
RA Schmid S.L.;
RT "Mutations in human dynamin block an intermediate stage in coated vesicle
RT formation.";
RL J. Cell Biol. 122:553-563(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain, and PNS;
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 [4]
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [6]
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 [7]
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [9]
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 [10]
RP INTERACTION WITH DIAPH1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=23325789; DOI=10.1091/mbc.e12-08-0597;
RA Li D., Dammer E.B., Lucki N.C., Sewer M.B.;
RT "cAMP-stimulated phosphorylation of diaphanous 1 regulates protein
RT stability and interaction with binding partners in adrenocortical cells.";
RL Mol. Biol. Cell 24:848-857(2013).
RN [11]
RP INVOLVEMENT IN DEE31, AND VARIANTS DEE31 PRO-177; ASN-206; TRP-237 AND
RP ALA-359.
RX PubMed=25262651; DOI=10.1016/j.ajhg.2014.08.013;
RG EuroEPINOMICS-RES Consortium;
RA Appenzeller S., Balling R., Barisic N., Baulac S., Caglayan H., Craiu D.,
RA De Jonghe P., Depienne C., Dimova P., Djemie T., Gormley P., Guerrini R.,
RA Helbig I., Hjalgrim H., Hoffman-Zacharska D., Jahn J., Klein K.M.,
RA Koeleman B., Komarek V., Krause R., Kuhlenbaumer G., Leguern E.,
RA Lehesjoki A.E., Lemke J.R., Lerche H., Linnankivi T., Marini C., May P.,
RA Moller R.S., Muhle H., Pal D., Palotie A., Pendziwiat M., Robbiano A.,
RA Roelens F., Rosenow F., Selmer K., Serratosa J.M., Sisodiya S.,
RA Stephani U., Sterbova K., Striano P., Suls A., Talvik T., von Spiczak S.,
RA Weber Y., Weckhuysen S., Zara F., Abou-Khalil B., Alldredge B.K.,
RA Andermann E., Andermann F., Amron D., Bautista J.F., Berkovic S.F.,
RA Bluvstein J., Boro A., Cascino G., Consalvo D., Crumrine P., Devinsky O.,
RA Dlugos D., Epstein M.P., Fiol M., Fountain N.B., French J., Friedman D.,
RA Geller E.B., Glauser T., Glynn S., Haas K., Haut S.R., Hayward J.,
RA Helmers S.L., Joshi S., Kanner A., Kirsch H.E., Knowlton R.C.,
RA Kossoff E.H., Kuperman R., Kuzniecky R., Lowenstein D.H., McGuire S.M.,
RA Motika P.V., Novotny E.J., Ottman R., Paolicchi J.M., Parent J., Park K.,
RA Poduri A., Sadleir L., Scheffer I.E., Shellhaas R.A., Sherr E., Shih J.J.,
RA Singh R., Sirven J., Smith M.C., Sullivan J., Thio L.L., Venkat A.,
RA Vining E.P., Von Allmen G.K., Weisenberg J.L., Widdess-Walsh P.,
RA Winawer M.R., Allen A.S., Berkovic S.F., Cossette P., Delanty N.,
RA Dlugos D., Eichler E.E., Epstein M.P., Glauser T., Goldstein D.B., Han Y.,
RA Heinzen E.L., Johnson M.R., Kuzniecky R., Lowenstein D.H., Marson A.G.,
RA Mefford H.C., Nieh S.E., O'Brien T.J., Ottman R., Petrou S., Petrovski S.,
RA Poduri A., Ruzzo E.K., Scheffer I.E., Sherr E.;
RT "De novo mutations in synaptic transmission genes including DNM1 cause
RT epileptic encephalopathies.";
RL Am. J. Hum. Genet. 95:360-370(2014).
RN [12]
RP INVOLVEMENT IN DEE31.
RX PubMed=25533962; DOI=10.1038/nature14135;
RG Deciphering Developmental Disorders Study;
RT "Large-scale discovery of novel genetic causes of developmental
RT disorders.";
RL Nature 519:223-228(2015).
RN [13]
RP STRUCTURE BY NMR OF 511-630.
RX PubMed=7850421; DOI=10.1016/s0960-9822(00)00197-4;
RA Downing A.K., Driscoll P.C., Gout I., Salim K., Zvelebil M.J.,
RA Waterfield M.D.;
RT "Three-dimensional solution structure of the pleckstrin homology domain
RT from dynamin.";
RL Curr. Biol. 4:884-891(1994).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 509-633.
RX PubMed=7954789; DOI=10.1016/0092-8674(94)90190-2;
RA Ferguson K.M., Lemmon M.A., Schlessinger J., Sigler P.B.;
RT "Crystal structure at 2.2-A resolution of the pleckstrin homology domain
RT from human dynamin.";
RL Cell 79:199-209(1994).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 509-630.
RX PubMed=7634088; DOI=10.1038/nsb1194-782;
RA Timm D., Salim K., Gout I., Guruprasad L., Waterfield M., Blundell T.;
RT "Crystal structure of the pleckstrin homology domain from dynamin.";
RL Nat. Struct. Biol. 1:782-788(1994).
RN [16]
RP VARIANT DEE31 TRP-237.
RX PubMed=27476654; DOI=10.1016/j.ajhg.2016.06.003;
RG Epi4K Consortium;
RT "De novo mutations in SLC1A2 and CACNA1A are important causes of epileptic
RT encephalopathies.";
RL Am. J. Hum. Genet. 99:287-298(2016).
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.
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 CAV1 and SH3GLB1. Binds SH3GL1, SH3GL2 and
CC SH3GL3 (By similarity). Interacts with PHOCN. Interacts with PACSIN1,
CC PACSIN2 and PACSIN3 (By similarity). Interacts with SNX9. Interacts
CC with MYO1E (via SH3 domain). Interacts with SNX33 (via SH3 domain).
CC Interacts with UNC119; leading to a decrease of DNM1 GTPase activity
CC (By similarity). Interacts with DIAPH1 (PubMed:23325789). Interacts
CC with AMPH, BIN1 AND SYNJ1 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P21575, ECO:0000269|PubMed:23325789}.
CC -!- INTERACTION:
CC Q05193; Q05193: DNM1; NbExp=13; IntAct=EBI-713135, EBI-713135;
CC Q05193; Q96RU3: FNBP1; NbExp=5; IntAct=EBI-713135, EBI-1111248;
CC Q05193; P62993: GRB2; NbExp=5; IntAct=EBI-713135, EBI-401755;
CC Q05193; P42858: HTT; NbExp=3; IntAct=EBI-713135, EBI-466029;
CC Q05193; Q5S007: LRRK2; NbExp=4; IntAct=EBI-713135, EBI-5323863;
CC Q05193; P16333: NCK1; NbExp=2; IntAct=EBI-713135, EBI-389883;
CC Q05193; P29474: NOS3; NbExp=2; IntAct=EBI-713135, EBI-1391623;
CC Q05193; Q8IVI9: NOSTRIN; NbExp=3; IntAct=EBI-713135, EBI-1391643;
CC Q05193; Q8WV41: SNX33; NbExp=2; IntAct=EBI-713135, EBI-2481535;
CC Q05193; Q9Y5X1: SNX9; NbExp=2; IntAct=EBI-713135, EBI-77848;
CC Q05193; Q96JI7: SPG11; NbExp=2; IntAct=EBI-713135, EBI-2822128;
CC Q05193-5; P68135: ACTA1; Xeno; NbExp=5; IntAct=EBI-8446026, EBI-367540;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15703209}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15703209}.
CC Note=Microtubule-associated.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q05193-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q05193-2; Sequence=VSP_031518;
CC Name=3;
CC IsoId=Q05193-3; Sequence=VSP_031519;
CC Name=4;
CC IsoId=Q05193-5; Sequence=VSP_031518, VSP_031519;
CC -!- DISEASE: Developmental and epileptic encephalopathy 31 (DEE31)
CC [MIM:616346]: A form of epileptic encephalopathy, a heterogeneous group
CC of severe early-onset epilepsies characterized by refractory seizures,
CC neurodevelopmental impairment, and poor prognosis. Development is
CC normal prior to seizure onset, after which cognitive and motor delays
CC become apparent. {ECO:0000269|PubMed:25262651,
CC ECO:0000269|PubMed:25533962, ECO:0000269|PubMed:27476654}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
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=AAA02805.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; L07807; AAA02803.1; -; mRNA.
DR EMBL; L07808; AAA02804.1; -; mRNA.
DR EMBL; L07809; AAA02805.1; ALT_SEQ; mRNA.
DR EMBL; L07810; AAA02806.1; -; mRNA.
DR EMBL; AL590708; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC050279; AAH50279.2; -; mRNA.
DR EMBL; BC063850; AAH63850.1; -; mRNA.
DR CCDS; CCDS43882.1; -. [Q05193-3]
DR CCDS; CCDS6895.1; -. [Q05193-1]
DR CCDS; CCDS75911.1; -. [Q05193-5]
DR CCDS; CCDS75912.1; -. [Q05193-2]
DR PIR; A40671; A40671.
DR RefSeq; NP_001005336.1; NM_001005336.2. [Q05193-3]
DR RefSeq; NP_001275666.1; NM_001288737.1. [Q05193-5]
DR RefSeq; NP_001275667.1; NM_001288738.1. [Q05193-5]
DR RefSeq; NP_001275668.1; NM_001288739.1. [Q05193-2]
DR RefSeq; NP_004399.2; NM_004408.3. [Q05193-1]
DR RefSeq; XP_005251825.1; XM_005251768.2.
DR RefSeq; XP_005251826.1; XM_005251769.2.
DR RefSeq; XP_016869860.1; XM_017014371.1.
DR PDB; 1DYN; X-ray; 2.20 A; A/B=510-633.
DR PDB; 2DYN; X-ray; 2.30 A; A/B=509-630.
DR PDB; 2X2E; X-ray; 2.00 A; A/D=6-320, A/D=726-750.
DR PDB; 2X2F; X-ray; 2.00 A; A/D=6-320, A/D=726-750.
DR PDB; 3SNH; X-ray; 3.70 A; A=6-746.
DR PDB; 3ZYC; X-ray; 2.20 A; A/D=6-320, A/D=726-750.
DR PDB; 3ZYS; EM; 12.20 A; A/D=6-320, A/D=726-750, C/F=518-630.
DR PDB; 4UUD; EM; 12.50 A; A/B/C/D/E/F/G/H/I/J/K/L=1-864.
DR PDB; 4UUK; EM; 12.50 A; A/B/C/D/E/F/G/H/I/J/K/L=1-864.
DR PDB; 5D3Q; X-ray; 1.70 A; A/B=5-320, A/B=726-746.
DR PDB; 6DLU; EM; 3.75 A; B/P=1-748.
DR PDB; 6DLV; EM; 10.10 A; b/c/f/g=1-748.
DR PDB; 6S9A; X-ray; 2.00 A; A/B=6-746.
DR PDB; 7AX3; EM; 3.74 A; A/A2/B/B2/C/C2/D/D2/E/E2/F/F2/G/G2/H/H2/I/I2/J/J2/K/L/M/N/O/P/Q/R/S/T=1-864.
DR PDBsum; 1DYN; -.
DR PDBsum; 2DYN; -.
DR PDBsum; 2X2E; -.
DR PDBsum; 2X2F; -.
DR PDBsum; 3SNH; -.
DR PDBsum; 3ZYC; -.
DR PDBsum; 3ZYS; -.
DR PDBsum; 4UUD; -.
DR PDBsum; 4UUK; -.
DR PDBsum; 5D3Q; -.
DR PDBsum; 6DLU; -.
DR PDBsum; 6DLV; -.
DR PDBsum; 6S9A; -.
DR PDBsum; 7AX3; -.
DR AlphaFoldDB; Q05193; -.
DR BMRB; Q05193; -.
DR SMR; Q05193; -.
DR BioGRID; 108099; 119.
DR CORUM; Q05193; -.
DR DIP; DIP-36242N; -.
DR IntAct; Q05193; 49.
DR MINT; Q05193; -.
DR STRING; 9606.ENSP00000362014; -.
DR BindingDB; Q05193; -.
DR ChEMBL; CHEMBL4958; -.
DR DrugCentral; Q05193; -.
DR iPTMnet; Q05193; -.
DR PhosphoSitePlus; Q05193; -.
DR BioMuta; DNM1; -.
DR DMDM; 172046078; -.
DR EPD; Q05193; -.
DR jPOST; Q05193; -.
DR MassIVE; Q05193; -.
DR MaxQB; Q05193; -.
DR PaxDb; Q05193; -.
DR PeptideAtlas; Q05193; -.
DR PRIDE; Q05193; -.
DR ProteomicsDB; 58309; -. [Q05193-1]
DR ProteomicsDB; 58310; -. [Q05193-2]
DR ProteomicsDB; 58311; -. [Q05193-3]
DR ProteomicsDB; 58313; -. [Q05193-5]
DR Antibodypedia; 3472; 688 antibodies from 46 providers.
DR DNASU; 1759; -.
DR Ensembl; ENST00000341179.11; ENSP00000345680.7; ENSG00000106976.21. [Q05193-3]
DR Ensembl; ENST00000372923.8; ENSP00000362014.4; ENSG00000106976.21. [Q05193-1]
DR Ensembl; ENST00000393594.7; ENSP00000377219.3; ENSG00000106976.21. [Q05193-5]
DR Ensembl; ENST00000475805.5; ENSP00000419225.1; ENSG00000106976.21. [Q05193-5]
DR Ensembl; ENST00000486160.3; ENSP00000420045.1; ENSG00000106976.21. [Q05193-2]
DR Ensembl; ENST00000627543.2; ENSP00000487310.1; ENSG00000106976.21. [Q05193-3]
DR GeneID; 1759; -.
DR KEGG; hsa:1759; -.
DR MANE-Select; ENST00000372923.8; ENSP00000362014.4; NM_004408.4; NP_004399.2.
DR UCSC; uc064wcg.1; human. [Q05193-1]
DR CTD; 1759; -.
DR DisGeNET; 1759; -.
DR GeneCards; DNM1; -.
DR HGNC; HGNC:2972; DNM1.
DR HPA; ENSG00000106976; Tissue enriched (brain).
DR MalaCards; DNM1; -.
DR MIM; 602377; gene.
DR MIM; 616346; phenotype.
DR neXtProt; NX_Q05193; -.
DR OpenTargets; ENSG00000106976; -.
DR Orphanet; 2382; Lennox-Gastaut syndrome.
DR Orphanet; 442835; Non-specific early-onset epileptic encephalopathy.
DR PharmGKB; PA27440; -.
DR VEuPathDB; HostDB:ENSG00000106976; -.
DR eggNOG; KOG0446; Eukaryota.
DR GeneTree; ENSGT00940000155214; -.
DR InParanoid; Q05193; -.
DR OMA; MQMVQTF; -.
DR OrthoDB; 264244at2759; -.
DR PhylomeDB; Q05193; -.
DR TreeFam; TF300362; -.
DR BRENDA; 3.6.5.5; 2681.
DR PathwayCommons; Q05193; -.
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-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-3928665; EPH-ephrin mediated repulsion of cells.
DR Reactome; R-HSA-437239; Recycling pathway of L1.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR SignaLink; Q05193; -.
DR SIGNOR; Q05193; -.
DR BioGRID-ORCS; 1759; 69 hits in 1083 CRISPR screens.
DR ChiTaRS; DNM1; human.
DR EvolutionaryTrace; Q05193; -.
DR GeneWiki; DNM1; -.
DR GenomeRNAi; 1759; -.
DR Pharos; Q05193; Tbio.
DR PRO; PR:Q05193; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q05193; protein.
DR Bgee; ENSG00000106976; Expressed in right hemisphere of cerebellum and 173 other tissues.
DR ExpressionAtlas; Q05193; baseline and differential.
DR Genevisible; Q05193; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0030117; C:membrane coat; IEA:Ensembl.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0001917; C:photoreceptor inner segment; IEA:Ensembl.
DR GO; GO:0098684; C:photoreceptor ribbon synapse; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098835; C:presynaptic endocytic zone membrane; IEA:Ensembl.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
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:IntAct.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IMP:BHF-UCL.
DR GO; GO:0007032; P:endosome organization; IMP:BHF-UCL.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:Ensembl.
DR GO; GO:0031623; P:receptor internalization; IBA:GO_Central.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IMP:UniProtKB.
DR GO; GO:0016185; P:synaptic vesicle budding from presynaptic endocytic zone membrane; IEA:Ensembl.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IBA:GO_Central.
DR GO; GO:1901998; P:toxin transport; IEA:Ensembl.
DR CDD; cd08771; DLP_1; 1.
DR DisProt; DP02976; -.
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 3D-structure; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Disease variant; Endocytosis; Epilepsy; GTP-binding; Hydrolase;
KW Methylation; Microtubule; Motor protein; Nitration; Nucleotide-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..864
FT /note="Dynamin-1"
FT /id="PRO_0000206563"
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 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..864
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:0000250|UniProtKB:P39053"
FT MOD_RES 125
FT /note="3'-nitrotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P39053"
FT MOD_RES 125
FT /note="Phosphotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P39053"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39053"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21575"
FT MOD_RES 354
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P39053"
FT MOD_RES 512
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39053"
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:0000250|UniProtKB:P39053"
FT MOD_RES 822
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21575"
FT MOD_RES 851
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21575"
FT MOD_RES 857
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21575"
FT VAR_SEQ 407..444
FT /note="MAFETIVKKQVKKIREPCLKCVDMVISELISTVRQCTK -> LAFEATVKKQ
FT VQKLKEPSIKCVDMVVSELTATIRKCSE (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:8101525"
FT /id="VSP_031518"
FT VAR_SEQ 845..864
FT /note="SRSGQASPSRPESPRPPFDL -> RITISDP (in isoform 3 and
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8101525"
FT /id="VSP_031519"
FT VARIANT 177
FT /note="A -> P (in DEE31; dbSNP:rs587777860)"
FT /evidence="ECO:0000269|PubMed:25262651"
FT /id="VAR_073710"
FT VARIANT 206
FT /note="K -> N (in DEE31; dbSNP:rs587777861)"
FT /evidence="ECO:0000269|PubMed:25262651"
FT /id="VAR_073711"
FT VARIANT 237
FT /note="R -> W (in DEE31; dbSNP:rs760270633)"
FT /evidence="ECO:0000269|PubMed:25262651,
FT ECO:0000269|PubMed:27476654"
FT /id="VAR_073712"
FT VARIANT 359
FT /note="G -> A (in DEE31; dbSNP:rs587777862)"
FT /evidence="ECO:0000269|PubMed:25262651"
FT /id="VAR_073713"
FT VARIANT 744
FT /note="D -> N (in dbSNP:rs1042007)"
FT /evidence="ECO:0000269|PubMed:8101525"
FT /id="VAR_048904"
FT MUTAGEN 44
FT /note="K->A: Inhibits receptor-mediated endocytosis."
FT /evidence="ECO:0000269|PubMed:8101525"
FT CONFLICT 188
FT /note="K -> E (in Ref. 3; AAH50279)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="N -> D (in Ref. 3; AAH50279)"
FT /evidence="ECO:0000305"
FT CONFLICT 809
FT /note="L -> M (in Ref. 3; AAH50279)"
FT /evidence="ECO:0000305"
FT HELIX 9..21
FT /evidence="ECO:0007829|PDB:5D3Q"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:5D3Q"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:5D3Q"
FT STRAND 32..39
FT /evidence="ECO:0007829|PDB:5D3Q"
FT HELIX 44..52
FT /evidence="ECO:0007829|PDB:5D3Q"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:5D3Q"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:5D3Q"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:5D3Q"
FT TURN 85..88
FT /evidence="ECO:0007829|PDB:6S9A"
FT HELIX 94..109
FT /evidence="ECO:0007829|PDB:5D3Q"
FT TURN 110..113
FT /evidence="ECO:0007829|PDB:5D3Q"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:5D3Q"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:5D3Q"
FT HELIX 152..164
FT /evidence="ECO:0007829|PDB:5D3Q"
FT STRAND 169..176
FT /evidence="ECO:0007829|PDB:5D3Q"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:5D3Q"
FT HELIX 185..193
FT /evidence="ECO:0007829|PDB:5D3Q"
FT STRAND 198..205
FT /evidence="ECO:0007829|PDB:5D3Q"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:5D3Q"
FT HELIX 217..220
FT /evidence="ECO:0007829|PDB:5D3Q"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:5D3Q"
FT HELIX 239..243
FT /evidence="ECO:0007829|PDB:5D3Q"
FT HELIX 248..261
FT /evidence="ECO:0007829|PDB:5D3Q"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:5D3Q"
FT HELIX 266..271
FT /evidence="ECO:0007829|PDB:5D3Q"
FT HELIX 274..311
FT /evidence="ECO:0007829|PDB:5D3Q"
FT HELIX 312..316
FT /evidence="ECO:0007829|PDB:3ZYC"
FT STRAND 520..529
FT /evidence="ECO:0007829|PDB:1DYN"
FT HELIX 533..535
FT /evidence="ECO:0007829|PDB:1DYN"
FT STRAND 537..555
FT /evidence="ECO:0007829|PDB:1DYN"
FT STRAND 561..566
FT /evidence="ECO:0007829|PDB:1DYN"
FT STRAND 570..574
FT /evidence="ECO:0007829|PDB:1DYN"
FT STRAND 579..582
FT /evidence="ECO:0007829|PDB:1DYN"
FT STRAND 584..590
FT /evidence="ECO:0007829|PDB:1DYN"
FT STRAND 601..609
FT /evidence="ECO:0007829|PDB:1DYN"
FT HELIX 610..622
FT /evidence="ECO:0007829|PDB:1DYN"
SQ SEQUENCE 864 AA; 97408 MW; 7FCD8CB572FFEAEF CRC64;
MGNRGMEDLI PLVNRLQDAF SAIGQNADLD LPQIAVVGGQ SAGKSSVLEN FVGRDFLPRG
SGIVTRRPLV LQLVNATTEY AEFLHCKGKK FTDFEEVRLE IEAETDRVTG TNKGISPVPI
NLRVYSPHVL NLTLVDLPGM TKVPVGDQPP DIEFQIRDML MQFVTKENCL ILAVSPANSD
LANSDALKVA KEVDPQGQRT IGVITKLDLM DEGTDARDVL ENKLLPLRRG YIGVVNRSQK
DIDGKKDITA ALAAERKFFL SHPSYRHLAD RMGTPYLQKV LNQQLTNHIR DTLPGLRNKL
QSQLLSIEKE VEEYKNFRPD 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
PGVPSRSGQA SPSRPESPRP PFDL
