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0DNM1L_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameDNM1L
DescriptionDynamin-1-like protein (ec 3.6.5.5) (dynamin-like protein) (dnm1p/vps1p-like protein) (dvlp) (dynamin family member proline-rich carboxyl-terminal domain less) (dymple) (dynamin-related protein 1) (dynamin-like protein 4) (dynamin-like protein iv) (hdyniv).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005783 endoplasmic reticulum (TAS)
0005801 Golgi cis-face (TAS)
0003924 GTPase activity (TAS)
0007154 cell communication (TAS)
0007275 development (TAS)
0007006 mitochondrial membrane organization and bio... (TAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Dynamin is a microtubule-associated force-producing protein of 100 Kdwhich is involved in the production of microtubule bundles. At the N terminus ofdynamin is a GTPase domain (see ).nd at the C-terminus is a PH domain (see ).Between these two domains lies a central region of unknown function.
  IPR000375:Dynamin central region
Membrane transport between compartments in eukaryotic cells requires proteins that allow the budding and scission of nascent cargo vesicles from one compartment and their targeting and fusion with another. Dynamins are large GTPases that belong to a protein superfamily that.n eukaryotic cells.ncludes classical dynamins.ynamin-like proteins.PA1.x proteins.itofusins and guanylate-binding proteins/atlastins and are involved in the scission of a wide range of vesicles and organelles. They play a role in many processes including budding of transport vesicles.ivision of organelles.ytokinesis and pathogen resistance. The minimal distinguishing architectural features that are common to all dynamins and are distinct from other GTPases are the structure of the large GTPase domain (300 amino acids) and the presence of two additional domains; the middle domain and the GTPase effector domain (GED).hich are involved in oligomerization and regulation of the GTPase activity. The GTPase domain contains the GTP-binding motifs that are needed for guanine-nucleotide binding and hydrolysis. The conservation of these motifs is absolute except for the the final motif in guanylate-binding proteins. The GTPase catalytic activity can be stimulated by oligomerisation of the protein.hich is mediated by interactions between the GTPase domain.he middle domain and the GED.
  IPR001401:Dynamin
Dynamin GTPase effector domain found in proteins related to dynamin. Dynamin is a GTP-hydrolysing protein that is an essential participant in clathrin-mediated endocytosis by cells. It self-assembles into collars in vivo at the necks of invaginated coated pits; the self-assembly of dynamin being coordinated by the GTPase domain. Mutation studies indicate that dynamin functions as a molecular regulator of receptor-mediated endocytosis .
  IPR003130:Dynamin GTPase effector
IPR000375:Dynamin_M 
Evalue:-158.455932617187 
Location:226-517IPR001401:Dynamin_N 
Evalue:-90.3767471313477 
Location:28-217IPR003130:GED 
Evalue:-46.9586067199707 
Location:639-730
SequencesProtein: DNM1L_HUMAN (736 aa)
mRNA: NM_012062
Local Annotation
Synapse Ontology
Postsynaptic compartment is represented by a patch of plasma membrane containing a packed array of neurotransmitter receptors and by an underlying dense matrix, the postsynaptic density (PSD).
sdb:0005 Postsynaptic compartment  (Evidence:keywords)
endocytosis may be initiated or blocked by all kinds of signal.
sdb:0257 regulation of endocytosis  (Evidence:keywords)
the cycle of the clathrin coat
sdb:0258 The cycle of the clathrin coat  (Evidence:keywords)
?
sdb:0328 transmitters release and endocytosis  (Evidence:keywords)
KO assignmentK01528
  Level 3 annotation:
    dynamin GTPase
  Level 2 annotation:
    Other enzymes
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 59 residues, 32723490-32723666Exon2: 51 residues, 32745615-32745763Exon3: 17 residues, 32751567-32751614Exon4: 26 residues, 32752353-32752425Exon5: 31 residues, 32755129-32755216Exon6: 56 residues, 32757409-32757572Exon7: 42 residues, 32762843-32762964Exon8: 46 residues, 32764864-32764996Exon9: 71 residues, 32766627-32766834Exon10: 42 residues, 32775214-32775335Exon11: 54 residues, 32775556-32775712Exon12: 32 residues, 32776054-32776144Exon13: 33 residues, 32777915-32778008Exon14: 21 residues, 32781305-32781362Exon15: 28 residues, 32782065-32782143Exon16: 13 residues, 32782464-32782497Exon17: 61 residues, 32784264-32784441Exon18: 38 residues, 32784609-32784719Exon19: 55 residues, 32786789-32786949Exon20: 357 residues, 32787554-32788620Exon21: 2 residues, -Jump to DNM1L_HUMAN  
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