P39054 · DYN2_MOUSE
- ProteinDynamin-2
- GeneDnm2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids870 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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).
Catalytic activity
- GTP + H2O = GDP + H+ + phosphateThis reaction proceeds in the forward direction.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 41 | GDP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 43 | GDP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 44 | GDP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 45 | GDP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 46 | GDP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 59 | GDP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 60 | GDP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 206 | GDP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 208 | GDP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 211 | GDP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 236 | GDP (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 237 | GDP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 239 | GDP (UniProtKB | ChEBI) | ||||
Sequence: Q |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDynamin-2
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP39054
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cytoplasmic vesicle, phagosome membrane ; Peripheral membrane protein
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).
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).
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Exhibits growth and cytokinesis defects.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 44 | Apoptotic cell corpse-containing phagosomes fail to mature into acidic phagosomes. Loss of PIK3C3 and RAB5A recruitment to phagosomes. | ||||
Sequence: K → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 37 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000206571 | 1-870 | Dynamin-2 | |||
Sequence: MGNRGMEELIPLVNKLQDAFSSIGQSCHLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIFSKTEYAEFLHCKSKKFTDFDEVRQEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIKDMILQFISRESSLILAVTPANMDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQKDIEGKKDIRAALAAERKFFLSHPAYRHMADRMGTPHLQKTLNQQLTNHIRESLPTLRSKLQSQLLSLEKEVEEYKNFRPDDPTRKTKALLQMVQQFGVDFEKRIEGSGDQVDTLELSGGARINRIFHERFPFELVKMEFDEKDLRREISYAIKNIHGVRTGLFTPDLAFEAIVKKQVVKLKEPCLKCVDLVIQELISTVRQCTSKLSSYPRLREETERIVTTYIREREGRTKDQILLLIDIEQSYINTNHEDFIGFANAQQRSTQLNKKRAIPNQGEILVIRRGWLTINNISLMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSNKHVFAIFNTEQRNVYKDLRQIELACDSQEDVDSWKASFLRAGVYPEKDQAENEDGAQENTFSMDPQLERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESAEQAQRRDDMLRMYHALKEALNIIGDISTSTVSTPVPPPVDDTWLQNTSGHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPMPVGATSSFSAPPIPSRPGPQSVFANNDPFSAPPQIPSRPARIPPGIPPGVPSRRAPAAPSRPTIIRPAEPSLLD | ||||||
Modified residue | 231 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 299 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 597 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 598 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 755 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 764 | Phosphoserine; by CDK1 | ||||
Sequence: S |
Post-translational modification
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 Ca2+- and calmodulin-dependent manner (By similarity).
Phosphorylated on tyrosine residues by EGFR (PubMed:16325581).
Phosphorylated on tyrosine residues after activation of SRC (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 Ca2+- and calmodulin-dependent manner (By similarity).
Phosphorylated on tyrosine residues by EGFR (PubMed:16325581).
Phosphorylated on tyrosine residues after activation of SRC (By similarity).
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Tissue specificity
Expressed in most tissues during embryonic development, including the peripheral nervous system although no expression is evident in skeletal muscle or heart.
Gene expression databases
Interaction
Subunit
Oligomerizes into a helical polymer that self-assembles around the vesicle membrane, when associated to the menbrane through lipid binding. Interacts with SHANK1 and SHANK2. Interacts with SNX9. 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. Interacts with SNX33 (via SH3 domain). Interacts with MYO1E (via SH3 domain). Interacts with PSTPIP1 (via SH3 domain). Interacts with CTNND2. 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. Interacts with GABARAP, GABARAPL1 and GABARAPL2. Interacts with MAP1LC3B (the lipidate and non-lipidated LC3 form); this interaction mediates recycling endosome scission leading to autophagosome release. Interacts with ITSN1 (By similarity).
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).
Interacts with MYOF (PubMed:17702744).
May interact with PIK3C3 (Probable). May be a component of a complex composed of RAB5A (in GDP-bound form), DYN2 and PIK3C3 (PubMed:18425118).
Interacts with SDC4; this interaction is markedly enhanced at focal ahesion site upon induction of focal adhesions and stress-fiber formation (PubMed:15694365).
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).
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).
Interacts with MYOF (PubMed:17702744).
May interact with PIK3C3 (Probable). May be a component of a complex composed of RAB5A (in GDP-bound form), DYN2 and PIK3C3 (PubMed:18425118).
Interacts with SDC4; this interaction is markedly enhanced at focal ahesion site upon induction of focal adhesions and stress-fiber formation (PubMed:15694365).
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).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P39054 | Amph Q7TQF7 | 5 | EBI-642337, EBI-775139 | |
BINARY | P39054 | Cttn Q60598 | 2 | EBI-642337, EBI-397955 | |
XENO | P39054 | CTTN1 Q01406 | 2 | EBI-642337, EBI-2530463 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 28-294 | Dynamin-type G | ||||
Sequence: HLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIFSKTEYAEFLHCKSKKFTDFDEVRQEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIKDMILQFISRESSLILAVTPANMDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQKDIEGKKDIRAALAAERKFFLSHPAYRHMADRMGTPHLQKTLNQQLTNHIRESLP | ||||||
Region | 38-45 | G1 motif | ||||
Sequence: GGQSAGKS | ||||||
Region | 64-66 | G2 motif | ||||
Sequence: VTR | ||||||
Region | 136-139 | G3 motif | ||||
Sequence: DLPG | ||||||
Region | 205-208 | G4 motif | ||||
Sequence: TKLD | ||||||
Region | 235-238 | G5 motif | ||||
Sequence: VNRS | ||||||
Domain | 519-625 | PH | ||||
Sequence: LVIRRGWLTINNISLMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSNKHVFAIFNTEQRNVYKDLRQIELACDSQEDVDSWKASFLRAGV | ||||||
Domain | 653-744 | GED | ||||
Sequence: VETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESAEQAQRRDDMLRMYHALKEALNIIGDISTSTV | ||||||
Compositional bias | 741-770 | Polar residues | ||||
Sequence: TSTVSTPVPPPVDDTWLQNTSGHSPTPQRR | ||||||
Region | 741-870 | Disordered | ||||
Sequence: TSTVSTPVPPPVDDTWLQNTSGHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPMPVGATSSFSAPPIPSRPGPQSVFANNDPFSAPPQIPSRPARIPPGIPPGVPSRRAPAAPSRPTIIRPAEPSLLD | ||||||
Compositional bias | 771-796 | Pro residues | ||||
Sequence: PVSSVHPPGRPPAVRGPTPGPPLIPM | ||||||
Compositional bias | 828-851 | Pro residues | ||||
Sequence: PPQIPSRPARIPPGIPPGVPSRRA |
Sequence similarities
Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family.
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
P39054-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length870
- Mass (Da)98,145
- Last updated2002-07-26 v2
- ChecksumE80864AF94B8F778
P39054-2
- Name2
- Differences from canonical
- 516-519: Missing
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Features
Showing features for sequence conflict, alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 297-298 | in Ref. 1; AAA40523 | ||||
Sequence: RS → HG | ||||||
Alternative sequence | VSP_001326 | 516-519 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 741-770 | Polar residues | ||||
Sequence: TSTVSTPVPPPVDDTWLQNTSGHSPTPQRR | ||||||
Compositional bias | 771-796 | Pro residues | ||||
Sequence: PVSSVHPPGRPPAVRGPTPGPPLIPM | ||||||
Compositional bias | 828-851 | Pro residues | ||||
Sequence: PPQIPSRPARIPPGIPPGVPSRRA | ||||||
Sequence conflict | 848-870 | in Ref. 2; BAB23745 | ||||
Sequence: SRRAPAAPSRPTIIRPAEPSLLD → RRPPPLAPARPFF |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L31398 EMBL· GenBank· DDBJ | AAA40523.1 EMBL· GenBank· DDBJ | mRNA | ||
AK005012 EMBL· GenBank· DDBJ | BAB23745.1 EMBL· GenBank· DDBJ | mRNA |