Dnm2
entrez
13430
canonical
uniprot
P39054
canonical
ensembl
ENSMUSG00000033335
resolver
ensp
ENSMUSP00000072199
resolver
ensp
ENSMUSP00000088616
resolver
ensp
ENSMUSP00000128961
resolver
ensp
ENSMUSP00000133564
resolver
ensp
ENSMUSP00000134243
resolver
ensp
ENSMUSP00000134696
resolver
ensp
ENSMUSP00000310389
resolver
ensp
ENSMUSP00000310390
resolver
ensp
ENSMUSP00000310393
resolver
ensp
ENSMUSP00000310394
resolver
ensp
ENSMUSP00000310395
resolver
ensp
ENSMUSP00000310396
resolver
ensp
ENSMUSP00000310397
resolver
ensp
ENSMUSP00000310417
resolver
ensp
ENSMUSP00000310418
resolver
ensp
ENSMUSP00000310424
resolver
ensp
ENSMUSP00000310427
resolver
ensp
ENSMUSP00000310437
resolver
ensp
ENSMUSP00000310451
resolver
ensp
ENSMUSP00000310471
resolver
enst
ENSMUST00000072362
resolver
enst
ENSMUST00000165766
resolver
enst
ENSMUST00000173397
resolver
genesymbol
Dnm2
resolver
genesymbol_syn
Dyn2
resolver
uniprot
F7B287
resolver
uniprot
G3UYW0
resolver
uniprot
G3X9G4
resolver
uniprot
Q3T9X3
resolver
uniprot
Q3TCR7
resolver
uniprot
Q9DBE1
resolver
uniprot_entry
DYN2_MOUSE
resolver
uniprot_entry
F7B287_MOUSE
resolver
uniprot_entry
G3UYW0_MOUSE
resolver
uniprot_entry
G3X9G4_MOUSE
resolver
uniprot_entry
Q3T9X3_MOUSE
resolver
uniprot_entry
Q3TCR7_MOUSE
resolver
uniprot_sec
Q9DBE1
resolver
amino_acid_sequence
MGNRGMEELIPLVNKLQDAFSSIGQSCHLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIFSKTEYAEFLHCKSKKFTDFDEVRQEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIKDMILQFISRESSLILAVTPANMDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQKDIEGKKDIRAALAAERKFFLSHPAYRHMADRMGTPHLQKTLNQQLTNHIRESLPTLRSKLQSQLLSLEKEVEEYKNFRPDDPTRKTKALLQMVQQFGVDFEKRIEGSGDQVDTLELSGGARINRIFHERFPFELVKMEFDEKDLRREISYAIKNIHGVRTGLFTPDLAFEAIVKKQVVKLKEPCLKCVDLVIQELISTVRQCTSKLSSYPRLREETERIVTTYIREREGRTKDQILLLIDIEQSYINTNHEDFIGFANAQQRSTQLNKKRAIPNQGEILVIRRGWLTINNISLMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSNKHVFAIFNTEQRNVYKDLRQIELACDSQEDVDSWKASFLRAGVYPEKDQAENEDGAQENTFSMDPQLERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESAEQAQRRDDMLRMYHALKEALNIIGDISTSTVSTPVPPPVDDTWLQNTSGHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPMPVGATSSFSAPPIPSRPGPQSVFANNDPFSAPPQIPSRPARIPPGIPPGVPSRRAPAAPSRPTIIRPAEPSLLD
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 at plasma membrane during endocytosis and filament remodeling at many actin structures during organization of the actin cytoskeleton (By similarity). Plays an important role in vesicular trafficking processes, namely clathrin-mediated endocytosis (CME), exocytic and clathrin-coated vesicle from the trans-Golgi network, and PDGF stimulated macropinocytosis (PubMed:18923138). During vesicular trafficking process, associates to the membrane, through lipid binding, and self-assembles into ring-like structure through oligomerization to form a helical polymer around the vesicle membrane and leading to vesicle scission (By similarity). Plays a role in organization of the actin cytoskeleton by mediating arrangement of stress fibers and actin bundles in podocytes (By similarity). During organization of the actin cytoskeleton, self-assembles into ring-like structure that directly bundles actin filaments to form typical membrane tubules decorated with dynamin spiral polymers (PubMed:33113375). Self-assembly increases GTPase activity and the GTP hydrolysis causes the rapid depolymerization of dynamin spiral polymers, and results in dispersion of actin bundles (By similarity). Remodels, through its interaction with CTTN, bundled actin filaments in a GTPase-dependent manner and plays a role in orchestrating the global actomyosin cytoskeleton (By similarity). The interaction with CTTN stabilizes the interaction of DNM2 and actin filaments and stimulates the intrinsic GTPase activity that results in actin filament-barbed ends and increases the sensitivity of filaments in bundles to the actin depolymerizing factor, CFL1 (By similarity). Plays a role in the autophagy process, by participating in the formation of ATG9A vesicles destined for the autophagosomes through its interaction with SNX18, by mediating recycling endosome scission leading to autophagosome release through MAP1LC3B interaction (By similarity). Also regulates maturation of apoptotic cell corpse-containing phagosomes by recruiting PIK3C3 to the phagosome membrane (PubMed:18425118). Also plays a role in cytokinesis (PubMed:18923138). May participate in centrosome cohesion through its interaction with TUBG1 (By similarity). Plays a role in the regulation of neuron morphology, axon growth and formation of neuronal growth cones (By similarity). Involved in membrane tubulation (By similarity). {ECO:0000250|UniProtKB:P39052, ECO:0000250|UniProtKB:P50570, ECO:0000269|PubMed:18425118, ECO:0000269|PubMed:18923138, ECO:0000269|PubMed:33113375}.
uniprot
proteins
mass_dalton
98145
uniprot
proteins
mutagenesis
MUTAGEN 44; /note="K->A: Apoptotic cell corpse-containing phagosomes fail to mature into acidic phagosomes. Loss of PIK3C3 and RAB5A recruitment to phagosomes."; /evidence="ECO:0000269|PubMed:18425118
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-848 by GSK3-alpha relieves the inhibition of BIN1 and promotes endocytosis. Phosphorylation at Ser-764 by CDK1 is greatly increased upon mitotic entry (By similarity). It regulates cytokinesis downstream of calcineurin, and does not affect clathrin-mediated endocytosis (By similarity). Dephosphorylated by calcineurin/PP2 during cytokinesis in a Ca(2+)- and calmodulin-dependent manner (By similarity). Phosphorylated on tyrosine residues by EGFR (PubMed:16325581). Phosphorylated on tyrosine residues after activation of SRC (By similarity). {ECO:0000250|UniProtKB:P39052, ECO:0000250|UniProtKB:P50570, ECO:0000269|PubMed:16325581}.
uniprot
proteins
protein_family
Dynamin/Fzo/YdjA family
uniprot
proteins
protein_family
TRAFAC class dynamin-like GTPase superfamily
uniprot
proteins
pubmed
15694365
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16325581
uniprot
proteins
pubmed
17702744
uniprot
proteins
pubmed
18425118
uniprot
proteins
pubmed
18923138
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23092955
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
33113375
uniprot
proteins
pubmed
9143510
uniprot
proteins
sequence_length
870
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P50570}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:P50570}. Cell projection, uropodium {ECO:0000250|UniProtKB:P50570}. Endosome {ECO:0000250|UniProtKB:P50570}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P50570}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:P50570}. Recycling endosome {ECO:0000250|UniProtKB:P50570}. Cell projection, phagocytic cup {ECO:0000269|PubMed:18425118}. Cytoplasmic vesicle, phagosome membrane {ECO:0000269|PubMed:18425118}; Peripheral membrane protein {ECO:0000269|PubMed:18425118}. Cell projection, podosome {ECO:0000269|PubMed:33113375}. Cytoplasm {ECO:0000250|UniProtKB:P39052}. Cell junction {ECO:0000250|UniProtKB:P39052}. Postsynaptic density {ECO:0000250|UniProtKB:P39052}. Synapse, synaptosome {ECO:0000250|UniProtKB:P39052}. Midbody {ECO:0000250|UniProtKB:P39052}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:P39052}. Note=Localized in recycling endosomes fragment to release nascent autophagosomes (By similarity). Co-localizes with PIK3C3 and RAB5A to the nascent phagosome (PubMed:18425118). Localized at focal ahesion site upon induction of focal adhesions and stress-fiber formation, when interacts with SDC4 (PubMed:15694365). Exists as a dynamic component of the centrosome. Associates with clathrin-coated vesicles at both the plasma membrane and the trans-Golgi network (TGN) (By similarity). {ECO:0000250|UniProtKB:P39052, ECO:0000250|UniProtKB:P50570, ECO:0000269|PubMed:15694365, ECO:0000269|PubMed:18425118}.
uniprot
proteins