{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P50570","secondaryAccessions":["A8K1B6","E7EV30","E9PEQ4","K7ESI9","Q5I0Y0","Q7Z5S3","Q9UPH4"],"uniProtkbId":"DYN2_HUMAN","entryAudit":{"firstPublicDate":"1996-10-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2004-05-10","entryVersion":242,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"29437695"}],"value":"Dynamin-2"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34744632"}],"value":"3.6.5.5"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"17676042"}],"value":"Dynamin 2"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"7590285"}],"value":"Dynamin II"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:2974"}],"value":"DNM2"},"synonyms":[{"value":"DYN2"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P39052"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P39054"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15731758"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17636067"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19605363"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19623537"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24135484"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29437695"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32315611"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33713620"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34744632"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36445308"}],"value":"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)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"GTP + H2O = GDP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19669"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:37565"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58189"}],"ecNumber":"3.6.5.5","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34744632"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:19670"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34744632"}]}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P39052"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P39054"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11583995"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15703209"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16325581"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17257598"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17676042"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18353773"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18480402"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22022388"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29437695"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32315611"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34744632"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36445308"}],"value":"Oligomerizes into a helical polymer that self-assembles around the vesicle membrane, when associated to the membrane 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)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P50570","intActId":"EBI-346547"},"interactantTwo":{"uniProtKBAccession":"Q8N157","geneName":"AHI1","intActId":"EBI-1049056"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P50570","intActId":"EBI-346547"},"interactantTwo":{"uniProtKBAccession":"O95817","geneName":"BAG3","intActId":"EBI-747185"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P50570","intActId":"EBI-346547"},"interactantTwo":{"uniProtKBAccession":"Q14247","geneName":"CTTN","intActId":"EBI-351886"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P50570","intActId":"EBI-346547"},"interactantTwo":{"uniProtKBAccession":"Q05193","geneName":"DNM1","intActId":"EBI-713135"},"numberOfExperiments":6,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P50570","intActId":"EBI-346547"},"interactantTwo":{"uniProtKBAccession":"Q8NFF5-2","geneName":"FLAD1","intActId":"EBI-11526128"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P50570","intActId":"EBI-346547"},"interactantTwo":{"uniProtKBAccession":"P62993","geneName":"GRB2","intActId":"EBI-401755"},"numberOfExperiments":10,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P50570","intActId":"EBI-346547"},"interactantTwo":{"uniProtKBAccession":"Q15811","geneName":"ITSN1","intActId":"EBI-602041"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P50570","intActId":"EBI-346547"},"interactantTwo":{"uniProtKBAccession":"Q12965","geneName":"MYO1E","intActId":"EBI-4279548"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P50570","intActId":"EBI-346547"},"interactantTwo":{"uniProtKBAccession":"P22392","geneName":"NME2","intActId":"EBI-713693"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P50570","intActId":"EBI-346547"},"interactantTwo":{"uniProtKBAccession":"Q9UNF0","geneName":"PACSIN2","intActId":"EBI-742503"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P50570","intActId":"EBI-346547"},"interactantTwo":{"uniProtKBAccession":"P54646","geneName":"PRKAA2","intActId":"EBI-1383852"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P50570","intActId":"EBI-346547"},"interactantTwo":{"uniProtKBAccession":"P47897","geneName":"QARS1","intActId":"EBI-347462"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P50570","intActId":"EBI-346547"},"interactantTwo":{"uniProtKBAccession":"O76064","geneName":"RNF8","intActId":"EBI-373337"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P50570","intActId":"EBI-346547"},"interactantTwo":{"uniProtKBAccession":"O00560","geneName":"SDCBP","intActId":"EBI-727004"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P50570","intActId":"EBI-346547"},"interactantTwo":{"uniProtKBAccession":"Q15436","geneName":"SEC23A","intActId":"EBI-81088"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P50570","intActId":"EBI-346547"},"interactantTwo":{"uniProtKBAccession":"Q9P0V3","geneName":"SH3BP4","intActId":"EBI-1049513"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P50570","intActId":"EBI-346547"},"interactantTwo":{"uniProtKBAccession":"Q99962","geneName":"SH3GL2","intActId":"EBI-77938"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P50570","intActId":"EBI-346547"},"interactantTwo":{"uniProtKBAccession":"Q96B97","geneName":"SH3KBP1","intActId":"EBI-346595"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P50570","intActId":"EBI-346547"},"interactantTwo":{"uniProtKBAccession":"Q8WV41","geneName":"SNX33","intActId":"EBI-2481535"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P50570","intActId":"EBI-346547"},"interactantTwo":{"uniProtKBAccession":"Q9Y5X1","geneName":"SNX9","intActId":"EBI-77848"},"numberOfExperiments":8,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P50570","intActId":"EBI-346547"},"interactantTwo":{"uniProtKBAccession":"Q9BUZ4","geneName":"TRAF4","intActId":"EBI-3650647"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P50570","intActId":"EBI-346547"},"interactantTwo":{"uniProtKBAccession":"P57075-2","geneName":"UBASH3A","intActId":"EBI-7353612"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P50570","intActId":"EBI-346547"},"interactantTwo":{"uniProtKBAccession":"Q9QPN3","geneName":"nef","intActId":"EBI-7355146"},"numberOfExperiments":4,"orga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Phosphorylated on tyrosine residues by EGFR and after activation of SRC (By similarity)"}],"commentType":"PTM"},{"commentType":"DISEASE","disease":{"diseaseId":"Myopathy, centronuclear, 1","diseaseAccession":"DI-00252","acronym":"CNM1","description":"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. 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