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Dynamin-1 (EC 3.6.5.5)

 DYN1_HUMAN              Reviewed;         864 AA.
Q05193; A6NLM6; Q5SYX0; Q5SYX2; Q6P3T6; Q86VD2;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
18-MAR-2008, sequence version 2.
05-DEC-2018, entry version 187.
RecName: Full=Dynamin-1;
EC=3.6.5.5;
Name=DNM1; Synonyms=DNM;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF
387-466 (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF 726-856 (ISOFORM
3), MUTAGENESIS OF LYS-44, AND VARIANT ASN-744.
PubMed=8101525; DOI=10.1083/jcb.122.3.553;
van der Bliek A.M., Redelmeier T.E., Tisdale E.J., Meyerowitz E.M.,
Schmid S.L.;
"Mutations in human dynamin block an intermediate stage in coated
vesicle formation.";
J. Cell Biol. 122:553-563(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Brain, and PNS;
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).
[4]
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).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[6]
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).
[7]
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).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[9]
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).
[10]
INTERACTION WITH DIAPH1, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=23325789; DOI=10.1091/mbc.E12-08-0597;
Li D., Dammer E.B., Lucki N.C., Sewer M.B.;
"cAMP-stimulated phosphorylation of diaphanous 1 regulates protein
stability and interaction with binding partners in adrenocortical
cells.";
Mol. Biol. Cell 24:848-857(2013).
[11]
INVOLVEMENT IN EIEE31, AND VARIANTS EIEE31 PRO-177; ASN-206; TRP-237
AND ALA-359.
PubMed=25262651; DOI=10.1016/j.ajhg.2014.08.013;
EuroEPINOMICS-RES Consortium;
Appenzeller S., Balling R., Barisic N., Baulac S., Caglayan H.,
Craiu D., De Jonghe P., Depienne C., Dimova P., Djemie T., Gormley P.,
Guerrini R., Helbig I., Hjalgrim H., Hoffman-Zacharska D., Jahn J.,
Klein K.M., Koeleman B., Komarek V., Krause R., Kuhlenbaumer G.,
Leguern E., Lehesjoki A.E., Lemke J.R., Lerche H., Linnankivi T.,
Marini C., May P., Moller R.S., Muhle H., Pal D., Palotie A.,
Pendziwiat M., Robbiano A., Roelens F., Rosenow F., Selmer K.,
Serratosa J.M., Sisodiya S., Stephani U., Sterbova K., Striano P.,
Suls A., Talvik T., von Spiczak S., Weber Y., Weckhuysen S., Zara F.,
Abou-Khalil B., Alldredge B.K., Andermann E., Andermann F., Amron D.,
Bautista J.F., Berkovic S.F., Bluvstein J., Boro A., Cascino G.,
Consalvo D., Crumrine P., Devinsky O., Dlugos D., Epstein M.P.,
Fiol M., Fountain N.B., French J., Friedman D., Geller E.B.,
Glauser T., Glynn S., Haas K., Haut S.R., Hayward J., Helmers S.L.,
Joshi S., Kanner A., Kirsch H.E., Knowlton R.C., Kossoff E.H.,
Kuperman R., Kuzniecky R., Lowenstein D.H., McGuire S.M., Motika P.V.,
Novotny E.J., Ottman R., Paolicchi J.M., Parent J., Park K.,
Poduri A., Sadleir L., Scheffer I.E., Shellhaas R.A., Sherr E.,
Shih J.J., Singh R., Sirven J., Smith M.C., Sullivan J., Thio L.L.,
Venkat A., Vining E.P., Von Allmen G.K., Weisenberg J.L.,
Widdess-Walsh P., Winawer M.R., Allen A.S., Berkovic S.F.,
Cossette P., Delanty N., Dlugos D., Eichler E.E., Epstein M.P.,
Glauser T., Goldstein D.B., Han Y., Heinzen E.L., Johnson M.R.,
Kuzniecky R., Lowenstein D.H., Marson A.G., Mefford H.C., Nieh S.E.,
O'Brien T.J., Ottman R., Petrou S., Petrovski S., Poduri A.,
Ruzzo E.K., Scheffer I.E., Sherr E.;
"De novo mutations in synaptic transmission genes including DNM1 cause
epileptic encephalopathies.";
Am. J. Hum. Genet. 95:360-370(2014).
[12]
INVOLVEMENT IN EIEE31.
PubMed=25533962; DOI=10.1038/nature14135;
Deciphering Developmental Disorders Study;
"Large-scale discovery of novel genetic causes of developmental
disorders.";
Nature 519:223-228(2015).
[13]
STRUCTURE BY NMR OF 511-630.
PubMed=7850421; DOI=10.1016/S0960-9822(00)00197-4;
Downing A.K., Driscoll P.C., Gout I., Salim K., Zvelebil M.J.,
Waterfield M.D.;
"Three-dimensional solution structure of the pleckstrin homology
domain from dynamin.";
Curr. Biol. 4:884-891(1994).
[14]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 509-633.
PubMed=7954789; DOI=10.1016/0092-8674(94)90190-2;
Ferguson K.M., Lemmon M.A., Schlessinger J., Sigler P.B.;
"Crystal structure at 2.2-A resolution of the pleckstrin homology
domain from human dynamin.";
Cell 79:199-209(1994).
[15]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 509-630.
PubMed=7634088; DOI=10.1038/nsb1194-782;
Timm D., Salim K., Gout I., Guruprasad L., Waterfield M., Blundell T.;
"Crystal structure of the pleckstrin homology domain from dynamin.";
Nat. Struct. Biol. 1:782-788(1994).
[16]
VARIANT EIEE31 TRP-237.
PubMed=27476654; DOI=10.1016/j.ajhg.2016.06.003;
Epi4K Consortium;
"De novo mutations in SLC1A2 and CACNA1A are important causes of
epileptic encephalopathies.";
Am. J. Hum. Genet. 99:287-298(2016).
-!- FUNCTION: Microtubule-associated force-producing protein involved
in producing microtubule bundles and able to bind and hydrolyze
GTP. Most probably involved in vesicular trafficking processes.
Involved in receptor-mediated endocytosis.
-!- CATALYTIC ACTIVITY:
Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.5;
-!- SUBUNIT: Interacts with CAV1 and SH3GLB1. Binds SH3GL1, SH3GL2 and
SH3GL3 (By similarity). Interacts with PHOCN. Interacts with
PACSIN1, PACSIN2 and PACSIN3 (By similarity). Interacts with SNX9.
Interacts with MYO1E (via SH3 domain). Interacts with SNX33 (via
SH3 domain). Interacts with UNC119; leading to a decrease of DNM1
GTPase activity (By similarity). Interacts with DIAPH1
(PubMed:23325789). Interacts with AMPH, BIN1 AND SYNJ1 (By
similarity). {ECO:0000250, ECO:0000250|UniProtKB:P21575,
ECO:0000269|PubMed:23325789}.
-!- INTERACTION:
Self; NbExp=13; IntAct=EBI-713135, EBI-713135;
P68135:ACTA1 (xeno); NbExp=5; IntAct=EBI-8446026, EBI-367540;
Q96RU3:FNBP1; NbExp=5; IntAct=EBI-713135, EBI-1111248;
P62993:GRB2; NbExp=3; IntAct=EBI-713135, EBI-401755;
P42858:HTT; NbExp=3; IntAct=EBI-713135, EBI-466029;
Q5S007:LRRK2; NbExp=4; IntAct=EBI-713135, EBI-5323863;
P16333:NCK1; NbExp=2; IntAct=EBI-713135, EBI-389883;
P29474:NOS3; NbExp=2; IntAct=EBI-713135, EBI-1391623;
Q8IVI9:NOSTRIN; NbExp=3; IntAct=EBI-713135, EBI-1391643;
Q8WV41:SNX33; NbExp=2; IntAct=EBI-713135, EBI-2481535;
Q9Y5X1:SNX9; NbExp=2; IntAct=EBI-713135, EBI-77848;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15703209}.
Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15703209}.
Note=Microtubule-associated.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q05193-1; Sequence=Displayed;
Name=2;
IsoId=Q05193-2; Sequence=VSP_031518;
Name=3;
IsoId=Q05193-3; Sequence=VSP_031519;
Name=4;
IsoId=Q05193-5; Sequence=VSP_031518, VSP_031519;
-!- DISEASE: Epileptic encephalopathy, early infantile, 31 (EIEE31)
[MIM:616346]: A form of epileptic encephalopathy, a heterogeneous
group of severe childhood onset epilepsies characterized by
refractory seizures, neurodevelopmental impairment, and poor
prognosis. Development is normal prior to seizure onset, after
which cognitive and motor delays become apparent.
{ECO:0000269|PubMed:25262651, ECO:0000269|PubMed:25533962,
ECO:0000269|PubMed:27476654}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
superfamily. Dynamin/Fzo/YdjA family. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
-!- SEQUENCE CAUTION:
Sequence=AAA02805.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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EMBL; L07807; AAA02803.1; -; mRNA.
EMBL; L07808; AAA02804.1; -; mRNA.
EMBL; L07809; AAA02805.1; ALT_SEQ; mRNA.
EMBL; L07810; AAA02806.1; -; mRNA.
EMBL; AL590708; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC050279; AAH50279.2; -; mRNA.
EMBL; BC063850; AAH63850.1; -; mRNA.
CCDS; CCDS43882.1; -. [Q05193-3]
CCDS; CCDS6895.1; -. [Q05193-1]
CCDS; CCDS75911.1; -. [Q05193-5]
CCDS; CCDS75912.1; -. [Q05193-2]
PIR; A40671; A40671.
RefSeq; NP_001005336.1; NM_001005336.2. [Q05193-3]
RefSeq; NP_001275666.1; NM_001288737.1. [Q05193-5]
RefSeq; NP_001275667.1; NM_001288738.1. [Q05193-5]
RefSeq; NP_001275668.1; NM_001288739.1. [Q05193-2]
RefSeq; NP_004399.2; NM_004408.3. [Q05193-1]
RefSeq; XP_005251825.1; XM_005251768.2. [Q05193-5]
RefSeq; XP_005251826.1; XM_005251769.2. [Q05193-3]
RefSeq; XP_016869860.1; XM_017014371.1. [Q05193-3]
UniGene; Hs.522413; -.
PDB; 1DYN; X-ray; 2.20 A; A/B=510-633.
PDB; 2DYN; X-ray; 2.30 A; A/B=509-630.
PDB; 2X2E; X-ray; 2.00 A; A/D=6-320, A/D=726-750.
PDB; 2X2F; X-ray; 2.00 A; A/D=6-320, A/D=726-750.
PDB; 3SNH; X-ray; 3.70 A; A=6-746.
PDB; 3ZYC; X-ray; 2.20 A; A/D=6-320, A/D=726-750.
PDB; 3ZYS; EM; 12.20 A; A/D=6-320, A/D=726-750, C/F=518-630.
PDB; 4UUD; EM; 12.50 A; A/B/C/D/E/F/G/H/I/J/K/L=1-864.
PDB; 4UUK; EM; 12.50 A; A/B/C/D/E/F/G/H/I/J/K/L=1-864.
PDB; 5D3Q; X-ray; 1.70 A; A/B=5-320, A/B=726-746.
PDB; 6DLU; EM; 3.75 A; B/P=1-748.
PDB; 6DLV; EM; 10.10 A; b/c/f/g=1-748.
PDBsum; 1DYN; -.
PDBsum; 2DYN; -.
PDBsum; 2X2E; -.
PDBsum; 2X2F; -.
PDBsum; 3SNH; -.
PDBsum; 3ZYC; -.
PDBsum; 3ZYS; -.
PDBsum; 4UUD; -.
PDBsum; 4UUK; -.
PDBsum; 5D3Q; -.
PDBsum; 6DLU; -.
PDBsum; 6DLV; -.
ProteinModelPortal; Q05193; -.
SMR; Q05193; -.
BioGrid; 108099; 67.
CORUM; Q05193; -.
DIP; DIP-36242N; -.
IntAct; Q05193; 33.
MINT; Q05193; -.
STRING; 9606.ENSP00000362014; -.
BindingDB; Q05193; -.
ChEMBL; CHEMBL4958; -.
iPTMnet; Q05193; -.
PhosphoSitePlus; Q05193; -.
DMDM; 172046078; -.
EPD; Q05193; -.
MaxQB; Q05193; -.
PaxDb; Q05193; -.
PeptideAtlas; Q05193; -.
PRIDE; Q05193; -.
ProteomicsDB; 58309; -.
ProteomicsDB; 58310; -. [Q05193-2]
ProteomicsDB; 58311; -. [Q05193-3]
ProteomicsDB; 58313; -. [Q05193-5]
Ensembl; ENST00000341179; ENSP00000345680; ENSG00000106976. [Q05193-3]
Ensembl; ENST00000372923; ENSP00000362014; ENSG00000106976. [Q05193-1]
Ensembl; ENST00000393594; ENSP00000377219; ENSG00000106976. [Q05193-5]
Ensembl; ENST00000475805; ENSP00000419225; ENSG00000106976. [Q05193-5]
Ensembl; ENST00000486160; ENSP00000420045; ENSG00000106976. [Q05193-2]
Ensembl; ENST00000627543; ENSP00000487310; ENSG00000106976. [Q05193-3]
GeneID; 1759; -.
KEGG; hsa:1759; -.
UCSC; uc064wcg.1; human. [Q05193-1]
CTD; 1759; -.
DisGeNET; 1759; -.
EuPathDB; HostDB:ENSG00000106976.19; -.
GeneCards; DNM1; -.
H-InvDB; HIX0026786; -.
H-InvDB; HIX0211497; -.
HGNC; HGNC:2972; DNM1.
HPA; CAB005920; -.
HPA; HPA049910; -.
HPA; HPA061801; -.
MalaCards; DNM1; -.
MIM; 602377; gene.
MIM; 616346; phenotype.
neXtProt; NX_Q05193; -.
OpenTargets; ENSG00000106976; -.
Orphanet; 2382; Lennox-Gastaut syndrome.
Orphanet; 442835; Undetermined early-onset epileptic encephalopathy.
PharmGKB; PA27440; -.
eggNOG; KOG0446; Eukaryota.
eggNOG; COG0699; LUCA.
GeneTree; ENSGT00940000155214; -.
HOGENOM; HOG000161069; -.
HOVERGEN; HBG107833; -.
InParanoid; Q05193; -.
KO; K01528; -.
OrthoDB; EOG091G0EIQ; -.
PhylomeDB; Q05193; -.
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-2132295; MHC class II antigen presentation.
Reactome; R-HSA-3928665; EPH-ephrin mediated repulsion of cells.
Reactome; R-HSA-437239; Recycling pathway of L1.
Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
SIGNOR; Q05193; -.
EvolutionaryTrace; Q05193; -.
GeneWiki; DNM1; -.
GenomeRNAi; 1759; -.
PRO; PR:Q05193; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000106976; Expressed in 205 organ(s), highest expression level in frontal cortex.
CleanEx; HS_DNM1; -.
ExpressionAtlas; Q05193; baseline and differential.
Genevisible; Q05193; HS.
GO; GO:0030424; C:axon; IBA:GO_Central.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
GO; GO:0044327; C:dendritic spine head; IBA:GO_Central.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
GO; GO:0016020; C:membrane; IBA:GO_Central.
GO; GO:0030117; C:membrane coat; IEA:Ensembl.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0001917; C:photoreceptor inner segment; IEA:Ensembl.
GO; GO:0098684; C:photoreceptor ribbon synapse; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
GO; GO:0098844; C:postsynaptic endocytic zone membrane; IBA:GO_Central.
GO; GO:0045211; C:postsynaptic membrane; IBA:GO_Central.
GO; GO:0098835; C:presynaptic endocytic zone membrane; IEA:Ensembl.
GO; GO:0045202; C:synapse; IBA:GO_Central.
GO; GO:0008021; C:synaptic vesicle; IEA:Ensembl.
GO; GO:0043196; C:varicosity; IEA:Ensembl.
GO; GO:0031749; F:D2 dopamine receptor binding; IEA:Ensembl.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
GO; GO:0050998; F:nitric-oxide synthase binding; IEA:Ensembl.
GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
GO; GO:0019901; F:protein kinase binding; ISS:ParkinsonsUK-UCL.
GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0017124; F:SH3 domain binding; IEA:Ensembl.
GO; GO:0072583; P:clathrin-dependent endocytosis; IEA:InterPro.
GO; GO:0006897; P:endocytosis; IMP:BHF-UCL.
GO; GO:0007032; P:endosome organization; IMP:BHF-UCL.
GO; GO:0048013; P:ephrin receptor signaling pathway; TAS:Reactome.
GO; GO:0002031; P:G protein-coupled receptor internalization; IEA:Ensembl.
GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:Ensembl.
GO; GO:1900244; P:positive regulation of synaptic vesicle endocytosis; IEA:Ensembl.
GO; GO:0098884; P:postsynaptic neurotransmitter receptor internalization; IBA:GO_Central.
GO; GO:0031623; P:receptor internalization; IBA:GO_Central.
GO; GO:0006898; P:receptor-mediated endocytosis; IMP:UniProtKB.
GO; GO:0050803; P:regulation of synapse structure or activity; IBA:GO_Central.
GO; GO:1904645; P:response to amyloid-beta; IEA:Ensembl.
GO; GO:0016185; P:synaptic vesicle budding from presynaptic endocytic zone membrane; IBA:GO_Central.
GO; GO:1901998; P:toxin transport; IEA:Ensembl.
CDD; cd08771; DLP_1; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR027741; DNM1.
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-like_dom_sf.
InterPro; IPR001849; PH_domain.
PANTHER; PTHR11566; PTHR11566; 1.
PANTHER; PTHR11566:SF32; PTHR11566:SF32; 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; 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; Alternative splicing; Complete proteome; Cytoplasm;
Cytoskeleton; Disease mutation; Endocytosis; Epilepsy; GTP-binding;
Hydrolase; Methylation; Microtubule; Motor protein; Nitration;
Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome.
CHAIN 1 864 Dynamin-1.
/FTId=PRO_0000206563.
DOMAIN 28 294 Dynamin-type G. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
DOMAIN 519 625 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 659 750 GED. {ECO:0000255|PROSITE-
ProRule:PRU00720}.
NP_BIND 38 45 GTP. {ECO:0000250}.
NP_BIND 136 140 GTP. {ECO:0000250}.
NP_BIND 205 208 GTP. {ECO:0000250}.
REGION 38 45 G1 motif. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
REGION 64 66 G2 motif. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
REGION 136 139 G3 motif. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
REGION 205 208 G4 motif. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
REGION 235 238 G5 motif. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
MOD_RES 80 80 Phosphotyrosine.
{ECO:0000250|UniProtKB:P39053}.
MOD_RES 125 125 Nitrated tyrosine; alternate.
{ECO:0000250|UniProtKB:P39053}.
MOD_RES 125 125 Phosphotyrosine; alternate.
{ECO:0000250|UniProtKB:P39053}.
MOD_RES 306 306 Phosphoserine.
{ECO:0000250|UniProtKB:P39053}.
MOD_RES 347 347 Phosphoserine.
{ECO:0000250|UniProtKB:P21575}.
MOD_RES 354 354 Phosphotyrosine.
{ECO:0000250|UniProtKB:P39053}.
MOD_RES 512 512 Phosphoserine.
{ECO:0000250|UniProtKB:P39053}.
MOD_RES 774 774 Phosphoserine.
{ECO:0000250|UniProtKB:P21575}.
MOD_RES 778 778 Phosphoserine.
{ECO:0000250|UniProtKB:P21575}.
MOD_RES 796 796 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P39053}.
MOD_RES 822 822 Phosphoserine.
{ECO:0000250|UniProtKB:P21575}.
MOD_RES 851 851 Phosphoserine.
{ECO:0000250|UniProtKB:P21575}.
MOD_RES 857 857 Phosphoserine.
{ECO:0000250|UniProtKB:P21575}.
VAR_SEQ 407 444 MAFETIVKKQVKKIREPCLKCVDMVISELISTVRQCTK ->
LAFEATVKKQVQKLKEPSIKCVDMVVSELTATIRKCSE
(in isoform 2 and isoform 4).
{ECO:0000303|PubMed:8101525}.
/FTId=VSP_031518.
VAR_SEQ 845 864 SRSGQASPSRPESPRPPFDL -> RITISDP (in
isoform 3 and isoform 4).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8101525}.
/FTId=VSP_031519.
VARIANT 177 177 A -> P (in EIEE31; dbSNP:rs587777860).
{ECO:0000269|PubMed:25262651}.
/FTId=VAR_073710.
VARIANT 206 206 K -> N (in EIEE31; dbSNP:rs587777861).
{ECO:0000269|PubMed:25262651}.
/FTId=VAR_073711.
VARIANT 237 237 R -> W (in EIEE31; dbSNP:rs760270633).
{ECO:0000269|PubMed:25262651,
ECO:0000269|PubMed:27476654}.
/FTId=VAR_073712.
VARIANT 359 359 G -> A (in EIEE31; dbSNP:rs587777862).
{ECO:0000269|PubMed:25262651}.
/FTId=VAR_073713.
VARIANT 744 744 D -> N (in dbSNP:rs1042007).
{ECO:0000269|PubMed:8101525}.
/FTId=VAR_048904.
MUTAGEN 44 44 K->A: Inhibits receptor-mediated
endocytosis.
{ECO:0000269|PubMed:8101525}.
CONFLICT 188 188 K -> E (in Ref. 3; AAH50279).
{ECO:0000305}.
CONFLICT 287 287 N -> D (in Ref. 3; AAH50279).
{ECO:0000305}.
CONFLICT 809 809 L -> M (in Ref. 3; AAH50279).
{ECO:0000305}.
HELIX 9 21 {ECO:0000244|PDB:5D3Q}.
TURN 22 24 {ECO:0000244|PDB:5D3Q}.
HELIX 27 29 {ECO:0000244|PDB:5D3Q}.
STRAND 32 39 {ECO:0000244|PDB:5D3Q}.
HELIX 44 52 {ECO:0000244|PDB:5D3Q}.
STRAND 60 62 {ECO:0000244|PDB:5D3Q}.
STRAND 69 75 {ECO:0000244|PDB:5D3Q}.
STRAND 80 83 {ECO:0000244|PDB:5D3Q}.
HELIX 84 86 {ECO:0000244|PDB:2X2F}.
HELIX 94 109 {ECO:0000244|PDB:5D3Q}.
TURN 110 113 {ECO:0000244|PDB:5D3Q}.
STRAND 120 126 {ECO:0000244|PDB:5D3Q}.
STRAND 131 136 {ECO:0000244|PDB:5D3Q}.
HELIX 152 164 {ECO:0000244|PDB:5D3Q}.
STRAND 169 176 {ECO:0000244|PDB:5D3Q}.
HELIX 181 183 {ECO:0000244|PDB:5D3Q}.
HELIX 185 193 {ECO:0000244|PDB:5D3Q}.
STRAND 198 205 {ECO:0000244|PDB:5D3Q}.
HELIX 207 209 {ECO:0000244|PDB:5D3Q}.
HELIX 217 220 {ECO:0000244|PDB:5D3Q}.
STRAND 231 233 {ECO:0000244|PDB:5D3Q}.
HELIX 239 243 {ECO:0000244|PDB:5D3Q}.
HELIX 248 261 {ECO:0000244|PDB:5D3Q}.
TURN 263 265 {ECO:0000244|PDB:5D3Q}.
HELIX 266 271 {ECO:0000244|PDB:5D3Q}.
HELIX 274 311 {ECO:0000244|PDB:5D3Q}.
HELIX 312 316 {ECO:0000244|PDB:3ZYC}.
STRAND 520 529 {ECO:0000244|PDB:1DYN}.
HELIX 533 535 {ECO:0000244|PDB:1DYN}.
STRAND 537 555 {ECO:0000244|PDB:1DYN}.
STRAND 561 566 {ECO:0000244|PDB:1DYN}.
STRAND 570 574 {ECO:0000244|PDB:1DYN}.
STRAND 579 582 {ECO:0000244|PDB:1DYN}.
STRAND 584 590 {ECO:0000244|PDB:1DYN}.
STRAND 601 609 {ECO:0000244|PDB:1DYN}.
HELIX 610 622 {ECO:0000244|PDB:1DYN}.
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


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