P39053 · DYN1_MOUSE
- ProteinDynamin-1
- GeneDnm1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids867 (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 and participates in many forms of endocytosis, such as clathrin-mediated endocytosis or synaptic vesicle endocytosis as well as rapid endocytosis (RE). Associates to the membrane, through lipid binding, and self-assembles into rings and stacks of interconnected rings through oligomerization to form a helical polymer around the vesicle membrane leading to constriction of invaginated coated pits around their necks. Self-assembly of the helical polymer induces membrane tubules narrowing until the polymer reaches a length sufficient to trigger GTP hydrolysis. Depending on the curvature imposed on the tubules, membrane detachment from the helical polymer upon GTP hydrolysis can cause spontaneous hemifission followed by complete fission. May play a role in regulating early stages of clathrin-mediated endocytosis in non-neuronal cells through its activation by dephosphorylation via the signaling downstream of EGFR (By similarity).
Controls vesicle size at a step before fission, during formation of membrane pits, at hippocampal synapses (PubMed:35220002).
Controls plastic adaptation of the synaptic vesicle recycling machinery to high levels of activity (PubMed:35220002).
Mediates rapid endocytosis (RE), a Ca2+-dependent and clathrin- and K+-independent process in chromaffin cells. Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP (By similarity).
Through its interaction with DNAJC6, acts during the early steps of clathrin-coated vesicle (CCV) formation (By similarity).
Controls vesicle size at a step before fission, during formation of membrane pits, at hippocampal synapses (PubMed:35220002).
Controls plastic adaptation of the synaptic vesicle recycling machinery to high levels of activity (PubMed:35220002).
Mediates rapid endocytosis (RE), a Ca2+-dependent and clathrin- and K+-independent process in chromaffin cells. Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP (By similarity).
Through its interaction with DNAJC6, acts during the early steps of clathrin-coated vesicle (CCV) formation (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-1
- 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 accessionP39053
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Associated to the membrane in a helical polymer shape in a GTP bound state. Transiently recruited to endocytic clathrin-coated pits (CCPs) at a late stage of clathrin-coated vesicle (CCV) formation.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Homozygous knockout mice pups liking Dnm1 are in the expected Mendelian ratio (PubMed:17463283).
At birth, pups mice breath, move, and suckle (PubMed:17463283).
However, a reduction in the ingestion of milk is apparent in pups within several hours after birth, and poor motor coordination becomes obvious over the following days (PubMed:17463283).
Pups fail to thrive and die within 2 weeks (PubMed:17463283).
At birth, pups mice breath, move, and suckle (PubMed:17463283).
However, a reduction in the ingestion of milk is apparent in pups within several hours after birth, and poor motor coordination becomes obvious over the following days (PubMed:17463283).
Pups fail to thrive and die within 2 weeks (PubMed:17463283).
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 31 variants from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000206564 | 1-867 | Dynamin-1 | |||
Sequence: MGNRGMEDLIPLVNRLQDAFSAIGQNADLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNSTTEYAEFLHCKGKKFTDFEEVRLEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQPPDIEFQIRDMLMQFVTKENCLILAVSPANSDLANSDALKIAKEVDPQGQRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQKDIDGKKDITAALAAERKFFLSHPSYRHLADRMGTPYLQKVLNQQLTNHIRDTLPGLRNKLQSQLLSIEKEVDEYKNFRPDDPARKTKALLQMVQQFAVDFEKRIEGSGDQIDTYELSGGARINRIFHERFPFELVKMEFDEKELRREISYAIKNIHGIRTGLFTPDMAFETIVKKQVKKIREPCLKCVDMVISELISTVRQCTKKLQQYPRLREEMERIVTTHIREREGRTKEQVMLLIDIELAYMNTNHEDFIGFANAQQRSNQMNKKKTSGNQDEILVIRKGWLTINNIGIMKGGSKEYWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKGFMSSKHIFALFNTEQRNVYKDYRQLELACETQEEVDSWKASFLRAGVYPERVGDKEKASETEENGSDSFMHSMDPQLERQVETIRNLVDSYMAIVNKTVRDLMPKTIMHLMINNTKEFIFSELLANLYSCGDQNTLMEESAEQAQRRDEMLRMYHALKEALSIIGDINTTTVSTPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQVPSRPNRAPPGVPSLGAWRLNSPQGKHENRAGKARL | ||||||
Modified residue | 80 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 125 | 3'-nitrotyrosine; alternate | ||||
Sequence: Y | ||||||
Modified residue | 125 | Phosphotyrosine; alternate | ||||
Sequence: Y | ||||||
Modified residue | 306 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 347 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 354 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 512 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 774 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 778 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 796 | Omega-N-methylarginine | ||||
Sequence: R | ||||||
Modified residue | 822 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 847 | In isoform P39053-6; Phosphoserine | ||||
Sequence: G | ||||||
Modified residue | 851 | In isoform P39053-4; Phosphoserine | ||||
Sequence: L | ||||||
Modified residue | 857 | In isoform P39053-4; Phosphoserine | ||||
Sequence: K |
Post-translational modification
Phosphorylation at Ser-774 by GSK3B/GSK3-beta leads to inactivation of receptor-mediated endocytosis in non-neuronal cells. Dephosphorylation at Ser-774, through the EGFR downstream signaling, leads to activation and regulates early stages of clathrin-mediated endocytosis (CME) (By similarity).
Phosphorylated on Tyr in response to EGF stimulation in cells expressing truncated EGFR (PubMed:11956154).
Phosphorylated by CDK5 leading to synaptic vesicle endocytosis (SVE) activation (By similarity).
Phosphorylated on Tyr in response to EGF stimulation in cells expressing truncated EGFR (PubMed:11956154).
Phosphorylated by CDK5 leading to synaptic vesicle endocytosis (SVE) activation (By similarity).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Homodimer; homodimerization is mediated by the dynamin-type G domain which promotes assembly-stimulated GTPase activity. Homo-tetramer formed from two dimers in the absence of lipid. Oligomerizes into a helical polymer that self-assembles around the vesicle membrane, when associated to the menbrane through lipid binding. Interacts (via C-terminal proline-rich domain (PRD)) with SNX9 (via SH3 domain); this interaction allows regulation of DNM1 self-assembly during late stages of endocytic vesicle formation and supports DNM1's early functions in accelerating clathrin-coated pits (CCPs) maturation in non neuronals cell. Interacts (via C-terminal proline-rich domain (PRD)) with MYO1E (via SH3 domain); this interaction regulates receptor-mediated endocytosis. Interacts with SNX33 (via SH3 domain); this interaction decreases DNM1-dependent endocytosis. Interacts with DIAPH1. Interacts with GRB2 (via SH3 domain); this interaction mediates disassembly of DNM1 polymers, therefore modulates self-assembly (By similarity).
Forms a complex with BIN1 (via SH3 domain) and SH3GL2 (via SH3 domain). Forms a complex with SH3GL2 (via SH3 domain) and AMPH (via SH3 domain). Forms a complex with SH3GL2 (via SH3 domain) and SYNJ1. Interacts (via C-terminal proline-rich domain (PRD)) with SYT1; this interaction facilitates vesicle fission during clathrin-mediated endocytosis (CME). Interacts (via C-terminal proline-rich domain (PRD)) with PLCG1 (via SH3 domain); this interaction stimulates the release of GDP from DNM1 and enhances DNM1-dependent endocytosis. Interacts with SNPH; this interaction inhibits the binding of DNM1 to AMPH and DNM1-receptor-mediated endocytosis (By similarity).
Interacts with CAV1 (PubMed:11956154).
Interacts with SH3GLB1 (via SH3 domain) (PubMed:12456676).
Interacts with PACSIN1 (via SH3 domain), PACSIN2 (via SH3 domain) and PACSIN3 (via SH3 domain) (PubMed:11082044).
Interacts with UNC119; this interaction decreases DNM1's GTPase activity and affects DNM1's interaction with AMPH (PubMed:19781630).
Interacts with AMPH (PubMed:11956154).
Interacts (GTP-bound form) with DNAJC6; this interaction allows clathrin-coated vesicle (CCV) formation at the plasma membrane (By similarity).
Forms a complex with BIN1 (via SH3 domain) and SH3GL2 (via SH3 domain). Forms a complex with SH3GL2 (via SH3 domain) and AMPH (via SH3 domain). Forms a complex with SH3GL2 (via SH3 domain) and SYNJ1. Interacts (via C-terminal proline-rich domain (PRD)) with SYT1; this interaction facilitates vesicle fission during clathrin-mediated endocytosis (CME). Interacts (via C-terminal proline-rich domain (PRD)) with PLCG1 (via SH3 domain); this interaction stimulates the release of GDP from DNM1 and enhances DNM1-dependent endocytosis. Interacts with SNPH; this interaction inhibits the binding of DNM1 to AMPH and DNM1-receptor-mediated endocytosis (By similarity).
Interacts with CAV1 (PubMed:11956154).
Interacts with SH3GLB1 (via SH3 domain) (PubMed:12456676).
Interacts with PACSIN1 (via SH3 domain), PACSIN2 (via SH3 domain) and PACSIN3 (via SH3 domain) (PubMed:11082044).
Interacts with UNC119; this interaction decreases DNM1's GTPase activity and affects DNM1's interaction with AMPH (PubMed:19781630).
Interacts with AMPH (PubMed:11956154).
Interacts (GTP-bound form) with DNAJC6; this interaction allows clathrin-coated vesicle (CCV) formation at the plasma membrane (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P39053 | Amph Q7TQF7 | 3 | EBI-397785, EBI-775139 | |
XENO | P39053 | LRRK2 Q5S007 | 3 | EBI-397785, EBI-5323863 | |
BINARY | P39053 | Pfn2 Q9JJV2-1 | 2 | EBI-397785, EBI-990256 |
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: DLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNSTTEYAEFLHCKGKKFTDFEEVRLEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQPPDIEFQIRDMLMQFVTKENCLILAVSPANSDLANSDALKIAKEVDPQGQRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQKDIDGKKDITAALAAERKFFLSHPSYRHLADRMGTPYLQKVLNQQLTNHIRDTLP | ||||||
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 | 515-625 | PH | ||||
Sequence: QDEILVIRKGWLTINNIGIMKGGSKEYWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKGFMSSKHIFALFNTEQRNVYKDYRQLELACETQEEVDSWKASFLRAGV | ||||||
Domain | 659-750 | GED | ||||
Sequence: VETIRNLVDSYMAIVNKTVRDLMPKTIMHLMINNTKEFIFSELLANLYSCGDQNTLMEESAEQAQRRDEMLRMYHALKEALSIIGDINTTTV | ||||||
Compositional bias | 767-781 | Polar residues | ||||
Sequence: SVPAGRRSPTSSPTP | ||||||
Region | 767-867 | Disordered | ||||
Sequence: SVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQVPSRPNRAPPGVPSLGAWRLNSPQGKHENRAGKARL | ||||||
Compositional bias | 782-840 | Pro residues | ||||
Sequence: QRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQVPSRPNRAP |
Domain
The dynamin-type G mediates homodimerization and plays a role in self-assembly.
The C-terminal proline-rich domain (PRD) mediates interaction with SH3-binding partners (By similarity).
Is required for DNM1 self-assembly (By similarity).
Is required for DNM1 self-assembly (By similarity).
The PH domain binds phosphoinositides such as 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate, 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate and 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate, and mediates receptor-mediated endocytosis.
Sequence similarities
Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 5 isoforms produced by Alternative splicing.
P39053-1
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
- Length867
- Mass (Da)97,803
- Last updated2003-06-20 v2
- ChecksumF48EC3DF5F39A08B
P39053-3
- Name3
- SynonymsBraDnm8
P39053-4
- Name4
- SynonymsBraDnm2
- Differences from canonical
- 846-867: LGAWRLNSPQGKHENRAGKARL → RSGQASPSRPESPRPPFDL
P39053-5
- Name5
- SynonymsBreDnm15
- Differences from canonical
- 845-867: SLGAWRLNSPQGKHENRAGKARL → RITISDP
P39053-6
- Name6
Computationally mapped potential isoform sequences
There are 7 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0J9YUE9 | A0A0J9YUE9_MOUSE | Dnm1 | 835 | ||
A0A0J9YUN4 | A0A0J9YUN4_MOUSE | Dnm1 | 864 | ||
A0A0J9YUS0 | A0A0J9YUS0_MOUSE | Dnm1 | 110 | ||
F6TH70 | F6TH70_MOUSE | Dnm1 | 149 | ||
D6RH60 | D6RH60_MOUSE | Dnm1 | 59 | ||
F6RRH9 | F6RRH9_MOUSE | Dnm1 | 159 | ||
F6W8Z8 | F6W8Z8_MOUSE | Dnm1 | 283 |
Sequence caution
Features
Showing features for sequence conflict, alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 135 | in Ref. 1; AAA37318 | ||||
Sequence: V → A | ||||||
Alternative sequence | VSP_007643 | 407-444 | in isoform 3 | |||
Sequence: MAFETIVKKQVKKIREPCLKCVDMVISELISTVRQCTK → LAFEATVKKQVQKLKEPSIKCVDMVVSELTSTIRKCSE | ||||||
Sequence conflict | 450 | in Ref. 1; AAA37318 | ||||
Sequence: P → R | ||||||
Alternative sequence | VSP_007644 | 516-519 | in isoform 6 | |||
Sequence: Missing | ||||||
Sequence conflict | 531 | in Ref. 1; AAA37318 | ||||
Sequence: I → S | ||||||
Sequence conflict | 573 | in Ref. 2; BAE25726 | ||||
Sequence: R → H | ||||||
Sequence conflict | 600 | in Ref. 1; AAA37318 | ||||
Sequence: Y → N | ||||||
Sequence conflict | 703 | in Ref. 5; AAH58623 | ||||
Sequence: A → V | ||||||
Sequence conflict | 722 | in Ref. 1; AAA37319/AAA37323/AAA37324 | ||||
Sequence: A → R | ||||||
Compositional bias | 767-781 | Polar residues | ||||
Sequence: SVPAGRRSPTSSPTP | ||||||
Compositional bias | 782-840 | Pro residues | ||||
Sequence: QRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQVPSRPNRAP | ||||||
Alternative sequence | VSP_007645 | 845-867 | in isoform 3 and isoform 5 | |||
Sequence: SLGAWRLNSPQGKHENRAGKARL → RITISDP | ||||||
Alternative sequence | VSP_007647 | 846-867 | in isoform 4 | |||
Sequence: LGAWRLNSPQGKHENRAGKARL → RSGQASPSRPESPRPPFDL | ||||||
Alternative sequence | VSP_024845 | 846-867 | in isoform 6 | |||
Sequence: LGAWRLNSPQGKHENRAGKARL → RKGPASPTRPAAPRPTEAPLLDL |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L29457 EMBL· GenBank· DDBJ | AAA37319.1 EMBL· GenBank· DDBJ | mRNA | ||
L31395 EMBL· GenBank· DDBJ | AAA37318.1 EMBL· GenBank· DDBJ | mRNA | ||
L31396 EMBL· GenBank· DDBJ | AAA37323.1 EMBL· GenBank· DDBJ | mRNA | ||
L31397 EMBL· GenBank· DDBJ | AAA37324.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AK011651 EMBL· GenBank· DDBJ | BAB27759.1 EMBL· GenBank· DDBJ | mRNA | ||
AK144142 EMBL· GenBank· DDBJ | BAE25726.1 EMBL· GenBank· DDBJ | mRNA | ||
AK220483 EMBL· GenBank· DDBJ | BAD90284.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AL808027 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC034679 EMBL· GenBank· DDBJ | AAH34679.1 EMBL· GenBank· DDBJ | mRNA | ||
BC058623 EMBL· GenBank· DDBJ | AAH58623.1 EMBL· GenBank· DDBJ | mRNA | ||
AF170568 EMBL· GenBank· DDBJ | AAF24220.1 EMBL· GenBank· DDBJ | Genomic DNA |