DNM1
entrez
1759
canonical
uniprot
Q05193
canonical
ensembl
ENSG00000106976
resolver
ensp
ENSP00000345680
resolver
ensp
ENSP00000362014
resolver
ensp
ENSP00000377219
resolver
ensp
ENSP00000419225
resolver
ensp
ENSP00000420045
resolver
ensp
ENSP00000516205
resolver
enst
ENST00000706053
resolver
genesymbol
DNM1
resolver
genesymbol_syn
DNM
resolver
hgnc
HGNC:2972
resolver
uniprot
A0A994J7J4
resolver
uniprot
A6NLM6
resolver
uniprot
B4DK06
resolver
uniprot
B7ZAC0
resolver
uniprot
Q5SYX0
resolver
uniprot
Q5SYX2
resolver
uniprot
Q6P3T6
resolver
uniprot
Q86VD2
resolver
uniprot_entry
A0A994J7J4_HUMAN
resolver
uniprot_entry
B4DK06_HUMAN
resolver
uniprot_entry
B7ZAC0_HUMAN
resolver
uniprot_entry
DYN1_HUMAN
resolver
uniprot_sec
A6NLM6
resolver
uniprot_sec
Q5SYX0
resolver
uniprot_sec
Q5SYX2
resolver
uniprot_sec
Q6P3T6
resolver
uniprot_sec
Q86VD2
resolver
activity_regulation
ACTIVITY REGULATION: GTPase activity is activated by 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate (PubMed:8910402). GTPase activity is inhibited by the heterodimer G protein formed by GNB1 and GNG2 with an IC(50)=400 nM when DNM1 concentration is 5 nM (PubMed:8910402). {ECO:0000269|PubMed:8910402}.
uniprot
proteins
amino_acid_sequence
MGNRGMEDLIPLVNRLQDAFSAIGQNADLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNATTEYAEFLHCKGKKFTDFEEVRLEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQPPDIEFQIRDMLMQFVTKENCLILAVSPANSDLANSDALKVAKEVDPQGQRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQKDIDGKKDITAALAAERKFFLSHPSYRHLADRMGTPYLQKVLNQQLTNHIRDTLPGLRNKLQSQLLSIEKEVEEYKNFRPDDPARKTKALLQMVQQFAVDFEKRIEGSGDQIDTYELSGGARINRIFHERFPFELVKMEFDEKELRREISYAIKNIHGIRTGLFTPDMAFETIVKKQVKKIREPCLKCVDMVISELISTVRQCTKKLQQYPRLREEMERIVTTHIREREGRTKEQVMLLIDIELAYMNTNHEDFIGFANAQQRSNQMNKKKTSGNQDEILVIRKGWLTINNIGIMKGGSKEYWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKGFMSSKHIFALFNTEQRNVYKDYRQLELACETQEEVDSWKASFLRAGVYPERVGDKEKASETEENGSDSFMHSMDPQLERQVETIRNLVDSYMAIVNKTVRDLMPKTIMHLMINNTKEFIFSELLANLYSCGDQNTLMEESAEQAQRRDEMLRMYHALKEALSIIGDINTTTVSTPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQVPSRPNRAPPGVPSRSGQASPSRPESPRPPFDL
uniprot
proteins
disease_involvement
DISEASE: Developmental and epileptic encephalopathy 31A (DEE31A) [MIM:616346]: An autosomal dominant epileptic encephalopathy, a heterogeneous group of severe early-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 variants affecting the gene represented in this entry.; DISEASE: Developmental and epileptic encephalopathy 31B (DEE31B) [MIM:620352]: A form of epileptic encephalopathy, a heterogeneous group of severe early-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. DEE31B is an autosomal recessive form with onset in the first months of life. {ECO:0000269|PubMed:34172529, ECO:0000269|PubMed:36553519}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.6.5.5
uniprot
proteins
function
FUNCTION: Catalyzes the hydrolysis of GTP and utilizes this energy to mediate vesicle scission and participates in many forms of endocytosis, such as clathrin-mediated endocytosis or synaptic vesicle endocytosis as well as rapid endocytosis (RE) (PubMed:15703209, PubMed:20428113, PubMed:29668686, PubMed:8101525, PubMed:8910402, PubMed:9362482). Associates to the membrane, through lipid binding, and self-assembles into rings and stacks of interconnected rings through oligomerization to form a helical polymer around the vesicle membrane leading to constriction of invaginated coated pits around their necks (PubMed:30069048, PubMed:7877694, PubMed:9922133). Self-assembly of the helical polymer induces membrane tubules narrowing until the polymer reaches a length sufficient to trigger GTP hydrolysis (PubMed:19084269). Depending on the curvature imposed on the tubules, membrane detachment from the helical polymer upon GTP hydrolysis can cause spontaneous hemifission followed by complete fission (PubMed:19084269). May play a role in regulating early stages of clathrin-mediated endocytosis in non-neuronal cells through its activation by dephosphorylation via the signaling downstream of EGFR (PubMed:29668686). Controls vesicle size at a step before fission, during formation of membrane pits, at hippocampal synapses (By similarity). Controls plastic adaptation of the synaptic vesicle recycling machinery to high levels of activity (By similarity). Mediates rapid endocytosis (RE), a Ca(2+)-dependent and clathrin- and K(+)-independent process in chromaffin cells (By similarity). Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP (By similarity). Through its interaction with DNAJC6, acts during the early steps of clathrin-coated vesicle (CCV) formation (PubMed:12791276). {ECO:0000250|UniProtKB:P39053, ECO:0000250|UniProtKB:Q08DF4, ECO:0000269|PubMed:12791276, ECO:0000269|PubMed:15703209, ECO:0000269|PubMed:19084269, ECO:0000269|PubMed:20428113, ECO:0000269|PubMed:29668686, ECO:0000269|PubMed:30069048, ECO:0000269|PubMed:7877694, ECO:0000269|PubMed:8101525, ECO:0000269|PubMed:8910402, ECO:0000269|PubMed:9362482, ECO:0000269|PubMed:9922133}.
uniprot
proteins
mass_dalton
97408
uniprot
proteins
mutagenesis
MUTAGEN 40; /note="Q->E: Impairs assembly-stimulated GTPase activity. Does not affect basal GTPase activity. Does not affect membrane binding. Does not affect self-assembly. Completely inhibits receptor internalization."; /evidence="ECO:0000269|PubMed:20428113"; MUTAGEN 41; /note="S->A: Impairs assembly-stimulated GTPase activity. Does not affect basal GTPase activity. Does not affect membrane binding. Does not affect self-assembly."; /evidence="ECO:0000269|PubMed:20428113"; MUTAGEN 44; /note="K->A: Inhibits receptor-mediated endocytosis. Significantly decreases endocytosis. Impairs receptor-mediated endocytosis. Impairs receptor-mediated endocytosis; when associated with 591-K--T-602. Does not affect self-assembly into rings and stacks."; /evidence="ECO:0000269|PubMed:30069048, ECO:0000269|PubMed:7877694, ECO:0000269|PubMed:7954789, ECO:0000269|PubMed:8101525"; MUTAGEN 180; /note="D->A: Inhibits assembly-stimulated GTPase activity. Significantly increases basal GTPase activity Does not affect membrane binding. Does not affect self-assembly."; /evidence="ECO:0000269|PubMed:20428113"; MUTAGEN 290; /note="R->A: Does not significantly affect receptor-mediated endocytosis; when associated with A-291 and A-292."; /evidence="ECO:0000269|PubMed:30069048"; MUTAGEN 291; /note="D->A: Does not significantly affect receptor-mediated endocytosis; when associated with A-290 and A-292."; /evidence="ECO:0000269|PubMed:30069048"; MUTAGEN 292; /note="T->A: Does not significantly affect receptor-mediated endocytosis; when associated with A-290 and A-291."; /evidence="ECO:0000269|PubMed:30069048"; MUTAGEN 292; /note="T->A: Substantially reduces receptor-mediated endocytosis; whena ssociated with A-293 and A-294."; /evidence="ECO:0000269|PubMed:30069048"; MUTAGEN 293; /note="L->A: Substantially reduces receptor-mediated endocytosis; whena ssociated with A-292 and A-294."; /evidence="ECO:0000269|PubMed:30069048"; MUTAGEN 294; /note="P->A: Does not significantly affect receptor-mediated endocytosis. Substantially reduces receptor-mediated endocytosis; whena ssociated with A-292 and A-293."; /evidence="ECO:0000269|PubMed:30069048"; MUTAGEN 330; /note="L->R: Significantly decreases receptor-mediated endocytosis; when associated with R-334 and R-702."; /evidence="ECO:0000269|PubMed:30069048"; MUTAGEN 334; /note="Q->R: Significantly decreases receptor-mediated endocytosis; when associated with R-330 and R-702."; /evidence="ECO:0000269|PubMed:30069048"; MUTAGEN 406; /note="D->R: Significantly decreases receptor-mediated endocytosis; when associated with R-407 and W-488."; /evidence="ECO:0000269|PubMed:30069048"; MUTAGEN 407; /note="M->R: Significantly decreases receptor-mediated endocytosis; when associated with R-406 and W-488."; /evidence="ECO:0000269|PubMed:30069048"; MUTAGEN 488; /note="T->W: Significantly decreases receptor-mediated endocytosis; when associated with R-406 and W-407."; /evidence="ECO:0000269|PubMed:30069048"; MUTAGEN 591..602; /note="TEQRNVYKDYRQ->KDQRNT: Abolishes 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate binding. Impairs receptor-mediated endocytosis. Impairs receptor-mediated endocytosis; when associated with A-44."; /evidence="ECO:0000269|PubMed:7954789"; MUTAGEN 702; /note="L->R: Significantly decreases endocytosis; when associated with R-330 and R-334."; /evidence="ECO:0000269|PubMed:30069048"; MUTAGEN 774; /note="S->A: Increases clathrin-mediated endocytosis (CME); when associated with A-778. Increases interaction with SNX9; when associated with A-778."; /evidence="ECO:0000269|PubMed:29668686"; MUTAGEN 778; /note="S->A: Increases clathrin-mediated endocytosis (CME); when associated with A-774. Increases interaction with SNX9; when associated with A-774."; /evidence="ECO:0000269|PubMed:29668686
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-774 by GSK3B/GSK3-beta leads to inactivation of receptor-mediated endocytosis in non-neuronal cells (PubMed:29668686). Dephosphorylation at Ser-774, through the EGFR downstream signaling, leads to activation and regulates early stages of clathrin-mediated endocytosis (CME) (PubMed:29668686). Phosphorylated by CDK5 leading to synaptic vesicle endocytosis (SVE) activation (By similarity). {ECO:0000250|UniProtKB:P21575, ECO:0000269|PubMed:29668686}.
uniprot
proteins
protein_family
Dynamin/Fzo/YdjA family
uniprot
proteins
protein_family
TRAFAC class dynamin-like GTPase superfamily
uniprot
proteins
pubmed
10074457
uniprot
proteins
pubmed
12198492
uniprot
proteins
pubmed
12791276
uniprot
proteins
pubmed
15164053
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15703209
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17257598
uniprot
proteins
pubmed
18088087
uniprot
proteins
pubmed
18353773
uniprot
proteins
pubmed
19084269
uniprot
proteins
pubmed
20428113
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23325789
uniprot
proteins
pubmed
25262651
uniprot
proteins
pubmed
25533962
uniprot
proteins
pubmed
26612256
uniprot
proteins
pubmed
27476654
uniprot
proteins
pubmed
29668686
uniprot
proteins
pubmed
30069048
uniprot
proteins
pubmed
34172529
uniprot
proteins
pubmed
36553519
uniprot
proteins
pubmed
7634088
uniprot
proteins
pubmed
7850421
uniprot
proteins
pubmed
7877694
uniprot
proteins
pubmed
7954789
uniprot
proteins
pubmed
8101525
uniprot
proteins
pubmed
8910402
uniprot
proteins
pubmed
9362482
uniprot
proteins
pubmed
9765310
uniprot
proteins
pubmed
9922133
uniprot
proteins
sequence_length
864
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15703209}. Membrane, clathrin-coated pit {ECO:0000269|PubMed:15703209, ECO:0000269|PubMed:8101525}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:P21575, ECO:0000250|UniProtKB:P39053}. Presynapse {ECO:0000250|UniProtKB:P21575}. Cytoplasmic vesicle, secretory vesicle, chromaffin granule {ECO:0000250|UniProtKB:Q08DF4}. Note=Associated to the membrane in a helical polymer shape in a GTP bound state (PubMed:30069048). Transiently recruited to endocytic clathrin-coated pits (CCPs) at a late stage of clathrin-coated vesicle (CCV) formation (PubMed:15703209). {ECO:0000269|PubMed:15703209, ECO:0000269|PubMed:30069048}.
uniprot
proteins