Dnm1
entrez
140694
canonical
uniprot
P21575
canonical
ensembl
ENSRNOG00000033835
resolver
ensp
ENSRNOP00000060845
resolver
ensp
ENSRNOP00000091634
resolver
ensp
ENSRNOP00000092707
resolver
ensp
ENSRNOP00000095659
resolver
enst
ENSRNOT00000110861
resolver
enst
ENSRNOT00000118464
resolver
genesymbol
Dnm1
resolver
genesymbol_syn
Dnm
resolver
uniprot
A0A8I6AHJ0
resolver
uniprot
A0A8I6ALW7
resolver
uniprot_entry
A0A8I6AHJ0_RAT
resolver
uniprot_entry
A0A8I6ALW7_RAT
resolver
uniprot_entry
DYN1_RAT
resolver
amino_acid_sequence
MGNRGMEDLIPLVNRLQDAFSAIGQNADLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNSTTEYAEFLHCKGKKFTDFEEVRLEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQPPDIEFQIRDMLMQFVTKENCLILAVSPANSDLANSDALKIAKEVDPQGQRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQKDIDGKKDITAALAAERKFFLSHPSYRHLADRMGTPYLQKVLNQQLTNHIRDTLPGLRNKLQSQLLSIEKEVDEYKNFRPDDPARKTKALLQMVQQFAVDFEKRIEGSGDQIDTYELSGGARINRIFHERFPFELVKMEFDEKELRREISYAIKNIHGIRTGLFTPDLAFEATVKKQVQKLKEPSIKCVDMVVSELTSTIRKCSEKLQQYPRLREEMERIVTTHIREREGRTKEQVMLLIDIELAYMNTNHEDFIGFANAQQRSNQMNKKKTSGNQDEILVIRKGWLTINNIGIMKGGSKEYWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKGFMSSKHIFALFNTEQRNVYKDYRQLELACETQEEVDSWKASFLRAGVYPERVGDKEKASETEENGSDSFMHSMDPQLERQVETIRNLVDSYMAIVNKTVRDLMPKTIMHLMINNTKEFIFSELLANLYSCGDQNTLMEESAEQAQRRDEMLRMYHALKEALSIIGDINTTTVSTPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQVPSRPNRAPPGVPSRSGQASPSRPESPRPPFDL
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). 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. Self-assembly of the helical polymer induces membrane tubules narrowing until the polymer reaches a length sufficient to trigger GTP hydrolysis. 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. 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 (By similarity). Controls vesicle size at a step before fission, during formation of membrane pits, at hippocampal synapses. 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. 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 (By similarity). {ECO:0000250|UniProtKB:P39053, ECO:0000250|UniProtKB:Q05193, ECO:0000250|UniProtKB:Q08DF4}.
uniprot
proteins
mass_dalton
97295
uniprot
proteins
mutagenesis
MUTAGEN 59; /note="R->A: Decreases of 32% the basal GTPase activity. Decreases of 44% the assembly-stimulated GTPase activity."; /evidence="ECO:0000269|PubMed:16141317"; MUTAGEN 59; /note="R->K: Decreases of 67% the basal GTPase activity. Decreases of 80% the assembly-stimulated GTPase activity."; /evidence="ECO:0000269|PubMed:16141317"; MUTAGEN 774; /note="S->A: Does not affect phosphorylation by CDK5. Significantly reduces phosphorylation by CDK5; when associated with A-778 and A-780."; /evidence="ECO:0000269|PubMed:17376771"; MUTAGEN 778; /note="S->A: Does not affect phosphorylation by CDK5. Significantly reduces phosphorylation by CDK5; when associated with A-774 and A-780."; /evidence="ECO:0000269|PubMed:17376771"; MUTAGEN 780; /note="T->A: Does not affect phosphorylation by CDK5. Significantly reduces phosphorylation by CDK5; when associated with A-774 and A-778."; /evidence="ECO:0000269|PubMed:17376771
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. Dephosphorylation at Ser-774, through the EGFR downstream signaling, leads to activation and regulates early stages of clathrin-mediated endocytosis (CME) (By similarity). Phosphorylated by CDK5 leading to synaptic vesicle endocytosis (SVE) activation (PubMed:12855954). {ECO:0000250|UniProtKB:Q05193, ECO:0000269|PubMed:12855954}.
uniprot
proteins
protein_family
Dynamin/Fzo/YdjA family
uniprot
proteins
protein_family
TRAFAC class dynamin-like GTPase superfamily
uniprot
proteins
pubmed
11872741
uniprot
proteins
pubmed
12855954
uniprot
proteins
pubmed
12896979
uniprot
proteins
pubmed
15252117
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141317
uniprot
proteins
pubmed
17257598
uniprot
proteins
pubmed
17376771
uniprot
proteins
pubmed
2144893
uniprot
proteins
pubmed
21927001
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
25964652
uniprot
proteins
pubmed
9238017
uniprot
proteins
pubmed
9341169
uniprot
proteins
pubmed
9725914
uniprot
proteins
sequence_length
864
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:9725914}. Note=Strongly associated with clathrin-coated vesicles at the plasma membrane. {ECO:0000269|PubMed:9725914}.; SUBCELLULAR LOCATION: [Isoform 6]: Golgi apparatus {ECO:0000269|PubMed:9725914}. Note=Diffuse cytoplasmic distribution. {ECO:0000269|PubMed:9725914}.; SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q05193}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:Q05193}. Cytoplasmic vesicle {ECO:0000305|PubMed:17257598}. Presynapse {ECO:0000269|PubMed:9238017}. 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. Transiently recruited to endocytic clathrin-coated pits (CCPs) at a late stage of clathrin-coated vesicle (CCV) formation. {ECO:0000250|UniProtKB:Q05193}.
uniprot
proteins