DNM2
entrez
1785
canonical
uniprot
P50570
canonical
ensembl
ENSG00000079805
resolver
ensp
ENSP00000347890
resolver
ensp
ENSP00000352721
resolver
ensp
ENSP00000373905
resolver
ensp
ENSP00000386192
resolver
ensp
ENSP00000468734
resolver
genesymbol
DNM2
resolver
genesymbol_syn
DYN2
resolver
hgnc
HGNC:2974
resolver
uniprot
A8K1B6
resolver
uniprot
E7EV30
resolver
uniprot
E9PEQ4
resolver
uniprot
K7ESI9
resolver
uniprot
Q5I0Y0
resolver
uniprot
Q7Z5S3
resolver
uniprot
Q8N1K8
resolver
uniprot
Q9UPH4
resolver
uniprot_entry
DYN2_HUMAN
resolver
uniprot_entry
Q8N1K8_HUMAN
resolver
uniprot_sec
A8K1B6
resolver
uniprot_sec
E7EV30
resolver
uniprot_sec
E9PEQ4
resolver
uniprot_sec
K7ESI9
resolver
uniprot_sec
Q5I0Y0
resolver
uniprot_sec
Q7Z5S3
resolver
uniprot_sec
Q9UPH4
resolver
amino_acid_sequence
MGNRGMEELIPLVNKLQDAFSSIGQSCHLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIFSKTEHAEFLHCKSKKFTDFDEVRQEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIKDMILQFISRESSLILAVTPANMDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQKDIEGKKDIRAALAAERKFFLSHPAYRHMADRMGTPHLQKTLNQQLTNHIRESLPALRSKLQSQLLSLEKEVEEYKNFRPDDPTRKTKALLQMVQQFGVDFEKRIEGSGDQVDTLELSGGARINRIFHERFPFELVKMEFDEKDLRREISYAIKNIHGVRTGLFTPDLAFEAIVKKQVVKLKEPCLKCVDLVIQELINTVRQCTSKLSSYPRLREETERIVTTYIREREGRTKDQILLLIDIEQSYINTNHEDFIGFANAQQRSTQLNKKRAIPNQGEILVIRRGWLTINNISLMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSNKHVFAIFNTEQRNVYKDLRQIELACDSQEDVDSWKASFLRAGVYPEKDQAENEDGAQENTFSMDPQLERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESADQAQRRDDMLRMYHALKEALNIIGDISTSTVSTPVPPPVDDTWLQSASSHSPTPQRRPVSSIHPPGRPPAVRGPTPGPPLIPVPVGAAASFSAPPIPSRPGPQSVFANSDLFPAPPQIPSRPVRIPPGIPPGVPSRRPPAAPSRPTIIRPAEPSLLD
uniprot
proteins
disease_involvement
DISEASE: Myopathy, centronuclear, 1 (CNM1) [MIM:160150]: A congenital muscle disorder characterized by progressive muscular weakness and wasting involving mainly limb girdle, trunk, and neck muscles. It may also affect distal muscles. Weakness may be present during childhood or adolescence or may not become evident until the third decade of life. Ptosis is a frequent clinical feature. The most prominent histopathologic features include high frequency of centrally located nuclei in muscle fibers not secondary to regeneration, radial arrangement of sarcoplasmic strands around the central nuclei, and predominance and hypotrophy of type 1 fibers. {ECO:0000269|PubMed:16227997, ECO:0000269|PubMed:17825552, ECO:0000269|PubMed:17932957, ECO:0000269|PubMed:19122038, ECO:0000269|PubMed:19623537, ECO:0000269|PubMed:19932619, ECO:0000269|PubMed:19932620, ECO:0000269|PubMed:20227276, ECO:0000269|PubMed:22396310, ECO:0000269|PubMed:24135484, ECO:0000269|PubMed:32315611, ECO:0000269|PubMed:34744632, ECO:0000269|PubMed:36445308}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Lethal congenital contracture syndrome 5 (LCCS5) [MIM:615368]: A form of lethal congenital contracture syndrome, an autosomal recessive disorder characterized by degeneration of anterior horn neurons, extreme skeletal muscle atrophy and congenital non-progressive joint contractures. The contractures can involve the upper or lower limbs and/or the vertebral column, leading to various degrees of flexion or extension limitations evident at birth. {ECO:0000269|PubMed:23092955}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Charcot-Marie-Tooth disease, dominant intermediate B (CMTDIB) [MIM:606482]: A form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. The dominant intermediate type B is characterized by clinical and pathologic features intermediate between demyelinating and axonal peripheral neuropathies, and motor median nerve conduction velocities ranging from 25 to 45 m/sec. {ECO:0000269|PubMed:15731758, ECO:0000269|PubMed:19623537}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Charcot-Marie-Tooth disease, axonal, type 2M (CMT2M) [MIM:606482]: An axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. {ECO:0000269|PubMed:17636067, ECO:0000269|PubMed:18560793}. 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 at plasma membrane during endocytosis and filament remodeling at many actin structures during organization of the actin cytoskeleton (PubMed:15731758, PubMed:19605363, PubMed:19623537, PubMed:33713620, PubMed:34744632). 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:15731758, PubMed:19623537, PubMed:33713620). 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:17636067, PubMed:34744632, PubMed:36445308). 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 (By similarity). 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 (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 (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 (PubMed:29437695), by mediating recycling endosome scission leading to autophagosome release through MAP1LC3B interaction (PubMed:29437695, PubMed:32315611). Also regulates maturation of apoptotic cell corpse-containing phagosomes by recruiting PIK3C3 to the phagosome membrane (By similarity). Also plays a role in cytokinesis (By similarity). 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 (PubMed:24135484). {ECO:0000250|UniProtKB:P39052, ECO:0000250|UniProtKB:P39054, ECO:0000269|PubMed:15731758, ECO:0000269|PubMed:17636067, ECO:0000269|PubMed:19605363, ECO:0000269|PubMed:19623537, ECO:0000269|PubMed:24135484, ECO:0000269|PubMed:29437695, ECO:0000269|PubMed:32315611, ECO:0000269|PubMed:33713620, ECO:0000269|PubMed:34744632, ECO:0000269|PubMed:36445308}.
uniprot
proteins
mass_dalton
98064
uniprot
proteins
mutagenesis
MUTAGEN 44; /note="K->A: Inhibits receptor-mediated endocytosis. Inhibits EGF-induced MAPK3 and MAPK1 activation."; /evidence="ECO:0000269|PubMed:19623537"; MUTAGEN 231; /note="Y->F: Greatly reduces tyrosine phosphorylation; when associated with F-597."; /evidence="ECO:0000269|PubMed:34744632"; MUTAGEN 525; /note="W->L: Abolishes interaction with MAP1LC3B. Does not affect interaction with ITSN1. Affects nascent autophagosome membranes. Does not affect the trafficking of ATG9A and ATG16L1. Does not affect SNX18 interaction. Decreases autophagosome maturation."; /evidence="ECO:0000269|PubMed:32315611"; MUTAGEN 597; /note="Y->F: Greatly reduces tyrosine phosphorylation; when associated with F-231."; /evidence="ECO:0000269|PubMed:34744632"; MUTAGEN 848; /note="S->A: Decreases receptor internalization."; /evidence="ECO:0000269|PubMed:36445308"; MUTAGEN 848; /note="S->E: Decreases binding affinity to BIN1. Increases GTPase mediated-membrane fission activity by BIN1. Decreases cell surface expression of SLC2A4."; /evidence="ECO:0000269|PubMed:36445308
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-848 by GSK3-alpha relieves the inhibition of BIN1 and promotes endocytosis (PubMed:36445308). Phosphorylation at Ser-764 by CDK1 is greatly increased upon mitotic entry (PubMed:20496096). 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 (PubMed:20496096). Phosphorylated on tyrosine residues by EGFR and after activation of SRC (By similarity). {ECO:0000250|UniProtKB:P39052, ECO:0000250|UniProtKB:P39054, ECO:0000269|PubMed:20496096, ECO:0000269|PubMed:36445308}.
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
14702039
uniprot
proteins
pubmed
15048127
uniprot
proteins
pubmed
15057824
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15703209
uniprot
proteins
pubmed
15731758
uniprot
proteins
pubmed
16227997
uniprot
proteins
pubmed
16325581
uniprot
proteins
pubmed
17257598
uniprot
proteins
pubmed
17636067
uniprot
proteins
pubmed
17676042
uniprot
proteins
pubmed
17825552
uniprot
proteins
pubmed
17932957
uniprot
proteins
pubmed
18353773
uniprot
proteins
pubmed
18480402
uniprot
proteins
pubmed
18560793
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19122038
uniprot
proteins
pubmed
19605363
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19623537
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19932619
uniprot
proteins
pubmed
19932620
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20227276
uniprot
proteins
pubmed
20496096
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22022388
uniprot
proteins
pubmed
22396310
uniprot
proteins
pubmed
23092955
uniprot
proteins
pubmed
24135484
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
29437695
uniprot
proteins
pubmed
32315611
uniprot
proteins
pubmed
33713620
uniprot
proteins
pubmed
34744632
uniprot
proteins
pubmed
36445308
uniprot
proteins
pubmed
7590285
uniprot
proteins
sequence_length
870
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15731758}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:15731758}. Cell projection, uropodium {ECO:0000269|PubMed:18480402}. Endosome {ECO:0000269|PubMed:15731758}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:16227997}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:15048127}. Recycling endosome {ECO:0000269|PubMed:32315611}. 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: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 (PubMed:32315611). 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. 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:P39054, ECO:0000269|PubMed:32315611}.
uniprot
proteins