Dnm2
entrez
25751
canonical
uniprot
P39052
canonical
ensembl
ENSRNOG00000007649
resolver
ensp
ENSRNOP00000010948
resolver
ensp
ENSRNOP00000059940
resolver
ensp
ENSRNOP00000060296
resolver
ensp
ENSRNOP00000086498
resolver
ensp
ENSRNOP00000089994
resolver
enst
ENSRNOT00000065028
resolver
enst
ENSRNOT00000094915
resolver
enst
ENSRNOT00000115745
resolver
genesymbol
Dnm2
resolver
genesymbol_syn
Dyn2
resolver
uniprot
A0A0A0MY49
resolver
uniprot
A0A8I6A1C6
resolver
uniprot
A0A8I6ADL1
resolver
uniprot_entry
A0A0A0MY49_RAT
resolver
uniprot_entry
A0A8I6A1C6_RAT
resolver
uniprot_entry
A0A8I6ADL1_RAT
resolver
uniprot_entry
DYN2_RAT
resolver
amino_acid_sequence
MGNRGMEELIPLVNKLQDAFSSIGQSCHLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIFSKTEYAEFLHCKSKKFTDFDEVRQEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIKDMILQFISRESSLILAVTPANMDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQKDIEGRKDIRAALAAERKFFLSHPAYRHMADRMGTPHLQKTLNQQLTNHIRESLPTLRSKLQSQLLSLEKEVEEYKNFRPDDPTRKTKALLQMVQQFGVDFEKRIEGSGDQVDTLELSGGARINRIFHERFPFELVKMEFDEKDLRREISYAIKNIHGVRTGLFTPDLAFEAIVKKQVVKLKEPCLKCVDLVIQELISTVRQCTSKLSSYPRLREETERIVTTYIREREGRTKDQILLLIDIEQSYINTNHEDFIGFANAQQRSTQLNKKRAIPNQGEILVIRRGWLTINNISLMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSNKHVFAIFNTEQRNVYKDLRQIELACDSQEDVDSWKASFLRAGVYPEKDQAENEDGAQENTFSMDPQLERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESAEQAQRRDDMLRMYHALKEALNIIGDISTSTVSTPVPPPVDDTWLQNTSSHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPMPVGATSSFSAPPIPSRPGPQNVFANNDPFSAPPQIPSRPARIPPGIPPGVPSRRAPAAPSRPTIIRPAEPSLLD
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 (PubMed:19605363, PubMed:19995918, PubMed:35620056). 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:19995918, PubMed:21195118, PubMed:9438853). 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 (PubMed:35620056). Plays a role in organization of the actin cytoskeleton by mediating arrangement of stress fibers and actin bundles in podocytes (PubMed:35620056). 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:35620056). Self-assembly increases GTPase activity and the GTP hydrolysis causes the rapid depolymerization of dynamin spiral polymers, and results in dispersion of actin bundles (PubMed:35620056). Remodels, through its interaction with CTTN, bundled actin filaments in a GTPase-dependent manner and plays a role in orchestrating the global actomyosin cytoskeleton (PubMed:19605363). 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 (PubMed:19605363). 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 and by regulating maturation of apoptotic cell corpse-containing phagosomes by recruiting PIK3C3 to the phagosome membrane (By similarity). Also plays a role in cytokinesis (PubMed:21195118). May participate in centrosome cohesion through its interaction with TUBG1 (PubMed:15048127). Plays a role in the regulation of neuron morphology, axon growth and formation of neuronal growth cones (PubMed:21210813). Involved in membrane tubulation (By similarity). {ECO:0000250|UniProtKB:P39054, ECO:0000250|UniProtKB:P50570, ECO:0000269|PubMed:15048127, ECO:0000269|PubMed:19605363, ECO:0000269|PubMed:19995918, ECO:0000269|PubMed:21195118, ECO:0000269|PubMed:21210813, ECO:0000269|PubMed:35620056, ECO:0000269|PubMed:9438853}.
uniprot
proteins
mass_dalton
98230
uniprot
proteins
mutagenesis
MUTAGEN 231; /note="Y->F: Strongly reduced phosphorylation. Decreases receptor-mediated endocytosis."; /evidence="ECO:0000269|PubMed:19995918"; MUTAGEN 399; /note="R->A: Does not Affect stimulation of GTPase activity by CTTN."; /evidence="ECO:0000269|PubMed:19605363"; MUTAGEN 555..557; /note="Missing: Does not affect organization of the actin cytoskeleton."; /evidence="ECO:0000269|PubMed:35620056"; MUTAGEN 562; /note="K->E: Decreases about 50% the stress fiber density. Significantly decreases GTPase activity. Impairs membrane bound-stimulated GTPase activity. Decreases membrane tubulation decorated with spiral polymers. Retains self-assembly into rings. Does not affect bundle actin filaments. Reduces the association between membranes during actin bundles."; /evidence="ECO:0000269|PubMed:35620056"; MUTAGEN 597; /note="Y->F: Strongly reduced phosphorylation. Decreases receptor-mediated endocytosis."; /evidence="ECO:0000269|PubMed:19995918"; MUTAGEN 764; /note="S->A: Reduces proline-rich domain phosphorylation by 80%."; /evidence="ECO:0000269|PubMed:21195118"; MUTAGEN 764; /note="S->E: Abolishes midbody localization and shows increased multinucleation."; /evidence="ECO:0000269|PubMed:21195118
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-848 by GSK3-alpha relieves the inhibition of BIN1 and promotes endocytosis (By similarity). Phosphorylation at Ser-764 by CDK1 is greatly increased upon mitotic entry (PubMed:21195118). It regulates cytokinesis downstream of calcineurin, and does not affect clathrin-mediated endocytosis (PubMed:21195118). Dephosphorylated by calcineurin/PP2 during cytokinesis in a Ca(2+)- and calmodulin-dependent manner (By similarity). Phosphorylated on tyrosine residues by EGFR (By similarity). Phosphorylated on tyrosine residues after activation of SRC (PubMed:19995918). {ECO:0000250|UniProtKB:P39054, ECO:0000250|UniProtKB:P50570, ECO:0000269|PubMed:19995918, ECO:0000269|PubMed:21195118}.
uniprot
proteins
protein_family
Dynamin/Fzo/YdjA family
uniprot
proteins
protein_family
TRAFAC class dynamin-like GTPase superfamily
uniprot
proteins
pubmed
11583995
uniprot
proteins
pubmed
15048127
uniprot
proteins
pubmed
16234328
uniprot
proteins
pubmed
16325581
uniprot
proteins
pubmed
17257598
uniprot
proteins
pubmed
19605363
uniprot
proteins
pubmed
19995918
uniprot
proteins
pubmed
21195118
uniprot
proteins
pubmed
21210813
uniprot
proteins
pubmed
35620056
uniprot
proteins
pubmed
8290576
uniprot
proteins
pubmed
8308025
uniprot
proteins
pubmed
9438853
uniprot
proteins
pubmed
9725914
uniprot
proteins
sequence_length
870
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:21210813}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:9438853}. Cell projection, uropodium {ECO:0000250|UniProtKB:P50570}. Endosome {ECO:0000250|UniProtKB:P50570}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:15048127}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:P50570}. Recycling endosome {ECO:0000250|UniProtKB:P50570}. Cell projection, phagocytic cup {ECO:0000250|UniProtKB:P39054}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:P39054}; Peripheral membrane protein {ECO:0000250|UniProtKB:P39054}. Cell projection, podosome {ECO:0000250|UniProtKB:P39054}. Cytoplasm {ECO:0000269|PubMed:21210813}. Cell junction {ECO:0000269|PubMed:21210813}. Postsynaptic density {ECO:0000269|PubMed:11583995}. Synapse, synaptosome {ECO:0000269|PubMed:11583995}. Midbody {ECO:0000269|PubMed:21195118, ECO:0000269|PubMed:9725914}. Membrane, clathrin-coated pit {ECO:0000269|PubMed:19995918}. Note=Localized in recycling endosomes fragment to release nascent autophagosomes (By similarity). Co-localizes with PIK3C3 and RAB5A to the nascent phagosome. Localized at focal ahesion site upon induction of focal adhesions and stress-fiber formation, when interacts with SDC4 (By similarity). Exists as a dynamic component of the centrosome (PubMed:15048127). Associates with clathrin-coated vesicles at both the plasma membrane and the trans-Golgi network (TGN) (PubMed:9438853). {ECO:0000250|UniProtKB:P39054, ECO:0000250|UniProtKB:P50570, ECO:0000269|PubMed:15048127, ECO:0000269|PubMed:9438853}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:9725914}. Membrane, clathrin-coated pit {ECO:0000269|PubMed:9725914}. Note=Sequestered to clathrin-coated pits and vesicles at the plasma membrane and the Golgi apparatus. {ECO:0000269|PubMed:9725914}.; SUBCELLULAR LOCATION: [Isoform 4]: Cell membrane {ECO:0000269|PubMed:9725914}. Note=Localized to numerous punctate spots on the plasma membrane. {ECO:0000269|PubMed:9725914}.
uniprot
proteins