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Details on Person UniProt:P50570 DNM2

Class:Id	ReferenceGeneProduct:404254
_chainChangeLog	chain:1-870 added on Sat February 7 2015
_displayName	UniProt:P50570 DNM2
_timestamp	2025-05-21 21:29:45
chain	chain:1-870
checksum	2F4567B75980935D
comment	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).CATALYTIC ACTIVITY GTP + H2O = GDP + phosphate + H(+)SUBUNIT Oligomerizes into a helical polymer that self-assembles around the vesicle membrane, when associated to the menbrane through lipid binding (PubMed:34744632, PubMed:36445308). Interacts with SHANK1 and SHANK2 (PubMed:11583995). Interacts with SNX9 (PubMed:15703209). Interacts (via C-terminal proline-rich domain (PRD)) with SNX18 (via SH3 domain); this interaction regulates ATG9A and ATG16L1 trafficking from recycling endosomes to sites of autophagosome formation (PubMed:29437695, PubMed:32315611). Interacts with SNX33 (via SH3 domain) (PubMed:18353773). Interacts with MYO1E (via SH3 domain) (PubMed:17257598). Interacts with PSTPIP1 (via SH3 domain) (PubMed:18480402). Interacts with CTNND2 (PubMed:22022388). Interacts (via C-terminal proline-rich domain (PRD)) with BIN1 (via SH3 domain); this interaction allows the recruitment of DNM2 to the membrane tubules and inhibits self-assembly-stimulated GTPase activity on the membrane (PubMed:17676042, PubMed:36445308). Interacts with GABARAP, GABARAPL1 and GABARAPL2 (PubMed:32315611). Interacts with MAP1LC3B (the lipidate and non-lipidated LC3 form); this interaction mediates recycling endosome scission leading to autophagosome release (PubMed:32315611). Interacts with ITSN1 (PubMed:32315611). Interacts (via C-terminal proline-rich domain (PRD)) with SH3BP4 (via SH3 domain); this interaction controls the GTPase activity and is prevented by EGFR-induced tyrosine phosphorylation of either DNM2 or SH3BP4 (PubMed:16325581). May interact with PIK3C3. May be a component of a complex composed of RAB5A (in GDP-bound form), DYN2 and PIK3C3. Interacts with SDC4; this interaction is markedly enhanced at focal ahesion site upon induction of focal adhesions and stress-fiber formation (By similarity). Interacts with ACTN1. Interacts with CTTN; this interaction stimulates the intrinsic GTPase activity of DNM2 and stabilizes the association of DNM2 and actin filaments; in addition this interaction is stimulated by ligand binding to the receptor, leading to the recruitment of the DNM2-CTTN complex to the sequestered receptor-ligand complex to its internalization. Interacts with NOSTRIN (via SH3 domain); this interaction allows the recruitment of NOS3 to dynamin-positive structures. Interacts with TUBG1; this interaction may participate in centrosome cohesion (By similarity).INTERACTION 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).ALTERNATIVE PRODUCTS Widely expressed (PubMed:7590285). Expressed in skeletal muscle and the peripheral nerve (PubMed:19623537).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).DISEASE The disease is caused by variants affecting the gene represented in this entry.DISEASE The disease is caused by variants affecting the gene represented in this entry.DISEASE The disease is caused by variants affecting the gene represented in this entry.DISEASE The disease is caused by variants affecting the gene represented in this entry.MISCELLANEOUS Overexpression of CNM- and CMT-related DNM2 mutants in COS7 cells, whatever the mutated domain, led to a reduction in clathrin-mediated receptor endocytosis associated with MAPK ERK-1 and ERK-2 impairment. The membrane trafficking impairment process may represent a common pathophysiological pathway in the autosomal forms of CNM DNM2-CMT neuropathy.SIMILARITY Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family.
created	[InstanceEdit:400710] Schmidt, EE, 2009-03-25 05:33:35
description	recommendedName: fullName evidence="42"Dynamin-2 ecNumber evidence="36"3.6.5.5 alternativeName: fullName evidence="41"Dynamin 2 alternativeName: fullName evidence="43"Dynamin II
geneName	DNM2 DYN2
identifier	P50570
isSequenceChanged	FALSE
keyword	3D-structure Acetylation Alternative splicing Cell junction Cell projection Charcot-Marie-Tooth disease Coated pit Cytoplasm Cytoplasmic vesicle Cytoskeleton Disease variant Endocytosis Endosome GTP-binding Hydrolase Membrane Microtubule Motor protein Neurodegeneration Neuropathy Nucleotide-binding Phagocytosis Phosphoprotein Proteomics identification Reference proteome Synapse Synaptosome
modified	[InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9862192] Weiser, Joel, 2024-02-26 [InstanceEdit:9917590] Weiser, Joel, 2024-08-09 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9939033] Weiser, Joel, 2025-02-21 [InstanceEdit:9948485] Weiser, Joel, 2025-05-21
name	DNM2
referenceDatabase	[ReferenceDatabase:2] UniProt
referenceGene	[ReferenceDNASequence:8962232] ENSEMBL:ENSG00000079805 DNM2 [Homo sapiens]
secondaryIdentifier	DYN2_HUMAN A8K1B6 E7EV30 E9PEQ4 K7ESI9 Q5I0Y0 Q7Z5S3 Q9UPH4
sequenceLength	870
species	[Species:48887] Homo sapiens
(isoformParent)	[ReferenceIsoform:54034] UniProt:P50570-1 DNM2 [Homo sapiens] [ReferenceIsoform:146638] UniProt:P50570-2 DNM2 [Homo sapiens] [ReferenceIsoform:8975973] UniProt:P50570-3 DNM2 [Homo sapiens] [ReferenceIsoform:8975974] UniProt:P50570-4 DNM2 [Homo sapiens] [ReferenceIsoform:8975975] UniProt:P50570-5 DNM2 [Homo sapiens]
(referenceEntity)	[EntityWithAccessionedSequence:2029000] DNM2 [endocytic vesicle membrane] [Homo sapiens] [EntityWithAccessionedSequence:2029041] DNM2 [phagocytic vesicle membrane] [Homo sapiens] [EntityWithAccessionedSequence:2213180] DNM2 [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:2980840] DNM2 [lysosomal membrane] [Homo sapiens] [EntityWithAccessionedSequence:2980842] DNM2 [Golgi membrane] [Homo sapiens] [EntityWithAccessionedSequence:2984201] DNM2 [plasma membrane] [Homo sapiens]
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No pathways have been reviewed or authored by UniProt:P50570 DNM2 (404254)