P39053 · DYN1_MOUSE

  • Protein
    Dynamin-1
  • Gene
    Dnm1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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).

Catalytic activity

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site41GDP (UniProtKB | ChEBI)
Binding site43GDP (UniProtKB | ChEBI)
Binding site44GDP (UniProtKB | ChEBI)
Binding site45GDP (UniProtKB | ChEBI)
Binding site46GDP (UniProtKB | ChEBI)
Binding site59GDP (UniProtKB | ChEBI)
Binding site60GDP (UniProtKB | ChEBI)
Binding site206GDP (UniProtKB | ChEBI)
Binding site208GDP (UniProtKB | ChEBI)
Binding site211GDP (UniProtKB | ChEBI)
Binding site236GDP (UniProtKB | ChEBI)
Binding site237GDP (UniProtKB | ChEBI)
Binding site239GDP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentchromaffin granule
Cellular Componentclathrin-coated pit
Cellular Componentclathrin-coated vesicle
Cellular Componentcytoplasm
Cellular Componentendocytic vesicle
Cellular Componentglutamatergic synapse
Cellular ComponentGolgi apparatus
Cellular Componentmembrane coat
Cellular Componentmicrotubule
Cellular Componentmyelin sheath
Cellular Componentphotoreceptor inner segment
Cellular Componentphotoreceptor ribbon synapse
Cellular Componentplasma membrane
Cellular Componentpresynapse
Cellular Componentpresynaptic endocytic zone membrane
Cellular Componentprotein-containing complex
Cellular Componentsynapse
Cellular Componentsynaptic vesicle
Cellular Componentvaricosity
Molecular FunctionD2 dopamine receptor binding
Molecular FunctionGDP binding
Molecular FunctionGTP binding
Molecular FunctionGTPase activity
Molecular Functionidentical protein binding
Molecular Functionmicrotubule binding
Molecular Functionnitric-oxide synthase binding
Molecular Functionphosphatidylinositol-3,4,5-trisphosphate binding
Molecular Functionphosphatidylinositol-4,5-bisphosphate binding
Molecular Functionprotein homodimerization activity
Molecular Functionprotein kinase binding
Molecular Functionprotein serine/threonine kinase binding
Molecular Functionprotein-containing complex binding
Molecular FunctionSH3 domain binding
Biological Processclathrin coat assembly involved in endocytosis
Biological Processendosome organization
Biological ProcessG protein-coupled receptor internalization
Biological Processmodulation of chemical synaptic transmission
Biological Processpositive regulation of synaptic vesicle endocytosis
Biological Processpositive regulation of synaptic vesicle recycling
Biological Processprotein homotetramerization
Biological Processreceptor internalization
Biological Processreceptor-mediated endocytosis
Biological Processregulation of synaptic vesicle endocytosis
Biological Processregulation of vesicle size
Biological Processsynaptic vesicle budding from presynaptic endocytic zone membrane
Biological Processsynaptic vesicle endocytosis
Biological Processvesicle scission

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Dynamin-1
  • EC number
  • Alternative names
    • Dynamin
    • Dynamin I

Gene names

    • Name
      Dnm1
    • Synonyms
      Dnm, Kiaa4093

Organism names

  • Taxonomic identifier
  • Strains
    • NIH Swiss
    • C57BL/6J
    • OF1
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    P39053
  • Secondary accessions
    • A2AN50
    • A2AN51
    • A2AN54
    • A2AN55
    • Q3UNM1

Proteomes

Organism-specific databases

Subcellular Location

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).

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.

Go to variant viewer

Chemistry

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00002065641-867Dynamin-1
Modified residue80Phosphotyrosine
Modified residue1253'-nitrotyrosine; alternate
Modified residue125Phosphotyrosine; alternate
Modified residue306Phosphoserine
Modified residue347Phosphoserine
Modified residue354Phosphotyrosine
Modified residue512Phosphoserine
Modified residue774Phosphoserine
Modified residue778Phosphoserine
Modified residue796Omega-N-methylarginine
Modified residue822Phosphoserine
Modified residue847In isoform P39053-6; Phosphoserine
Modified residue851In isoform P39053-4; Phosphoserine
Modified residue857In isoform P39053-4; Phosphoserine

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).

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed exclusively in the brain.

Gene expression databases

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).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P39053Amph Q7TQF73EBI-397785, EBI-775139
XENO P39053LRRK2 Q5S0073EBI-397785, EBI-5323863
BINARY P39053Pfn2 Q9JJV2-12EBI-397785, EBI-990256

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain28-294Dynamin-type G
Region38-45G1 motif
Region64-66G2 motif
Region136-139G3 motif
Region205-208G4 motif
Region235-238G5 motif
Domain515-625PH
Domain659-750GED
Compositional bias767-781Polar residues
Region767-867Disordered
Compositional bias782-840Pro residues

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).
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

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (5)
  • Sequence status
    Complete

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.

  • Length
    867
  • Mass (Da)
    97,803
  • Last updated
    2003-06-20 v2
  • Checksum
    F48EC3DF5F39A08B
MGNRGMEDLIPLVNRLQDAFSAIGQNADLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNSTTEYAEFLHCKGKKFTDFEEVRLEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQPPDIEFQIRDMLMQFVTKENCLILAVSPANSDLANSDALKIAKEVDPQGQRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQKDIDGKKDITAALAAERKFFLSHPSYRHLADRMGTPYLQKVLNQQLTNHIRDTLPGLRNKLQSQLLSIEKEVDEYKNFRPDDPARKTKALLQMVQQFAVDFEKRIEGSGDQIDTYELSGGARINRIFHERFPFELVKMEFDEKELRREISYAIKNIHGIRTGLFTPDMAFETIVKKQVKKIREPCLKCVDMVISELISTVRQCTKKLQQYPRLREEMERIVTTHIREREGRTKEQVMLLIDIELAYMNTNHEDFIGFANAQQRSNQMNKKKTSGNQDEILVIRKGWLTINNIGIMKGGSKEYWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKGFMSSKHIFALFNTEQRNVYKDYRQLELACETQEEVDSWKASFLRAGVYPERVGDKEKASETEENGSDSFMHSMDPQLERQVETIRNLVDSYMAIVNKTVRDLMPKTIMHLMINNTKEFIFSELLANLYSCGDQNTLMEESAEQAQRRDEMLRMYHALKEALSIIGDINTTTVSTPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQVPSRPNRAPPGVPSLGAWRLNSPQGKHENRAGKARL

P39053-3

  • Name
    3
  • Synonyms
    BraDnm8
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 407-444: MAFETIVKKQVKKIREPCLKCVDMVISELISTVRQCTK → LAFEATVKKQVQKLKEPSIKCVDMVVSELTSTIRKCSE
    • 845-867: SLGAWRLNSPQGKHENRAGKARL → RITISDP

P39053-4

  • Name
    4
  • Synonyms
    BraDnm2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 846-867: LGAWRLNSPQGKHENRAGKARL → RSGQASPSRPESPRPPFDL

P39053-5

  • Name
    5
  • Synonyms
    BreDnm15
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 845-867: SLGAWRLNSPQGKHENRAGKARL → RITISDP

P39053-6

  • Name
    6
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 516-519: Missing
    • 846-867: LGAWRLNSPQGKHENRAGKARL → RKGPASPTRPAAPRPTEAPLLDL

Computationally mapped potential isoform sequences

There are 7 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A0J9YUE9A0A0J9YUE9_MOUSEDnm1835
A0A0J9YUN4A0A0J9YUN4_MOUSEDnm1864
A0A0J9YUS0A0A0J9YUS0_MOUSEDnm1110
F6TH70F6TH70_MOUSEDnm1149
D6RH60D6RH60_MOUSEDnm159
F6RRH9F6RRH9_MOUSEDnm1159
F6W8Z8F6W8Z8_MOUSEDnm1283

Sequence caution

The sequence BAD90284.1 differs from that shown. Reason: Erroneous initiation Extended N-terminus.
The sequence AAA37324.1 differs from that shown. Reason: Frameshift

Features

Showing features for sequence conflict, alternative sequence, compositional bias.

TypeIDPosition(s)Description
Sequence conflict135in Ref. 1; AAA37318
Alternative sequenceVSP_007643407-444in isoform 3
Sequence conflict450in Ref. 1; AAA37318
Alternative sequenceVSP_007644516-519in isoform 6
Sequence conflict531in Ref. 1; AAA37318
Sequence conflict573in Ref. 2; BAE25726
Sequence conflict600in Ref. 1; AAA37318
Sequence conflict703in Ref. 5; AAH58623
Sequence conflict722in Ref. 1; AAA37319/AAA37323/AAA37324
Compositional bias767-781Polar residues
Compositional bias782-840Pro residues
Alternative sequenceVSP_007645845-867in isoform 3 and isoform 5
Alternative sequenceVSP_007647846-867in isoform 4
Alternative sequenceVSP_024845846-867in isoform 6

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

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