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Entry version 158 (22 Apr 2020)
Sequence version 1 (01 Jan 1998)
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Protein

Dynamin-1-like protein

Gene

Dnm1l

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Functions in mitochondrial and peroxisomal division. Mediates membrane fission through oligomerization into membrane-associated tubular structures that wrap around the scission site to constrict and sever the mitochondrial membrane through a GTP hydrolysis-dependent mechanism. The specific recruitment at scission sites is mediated by membrane receptors like MFF, MIEF1 and MIEF2 for mitochondrial membranes. While the recruitment by the membrane receptors is GTP-dependent, the following hydrolysis of GTP induces the dissociation from the receptors and allows DNM1L filaments to curl into closed rings that are probably sufficient to sever a double membrane. Through its function in mitochondrial division, ensures the survival of at least some types of postmitotic neurons, including Purkinje cells, by suppressing oxidative damage. Required for normal brain development, including that of cerebellum. Facilitates developmentally regulated apoptosis during neural tube formation. Required for a normal rate of cytochrome c release and caspase activation during apoptosis; this requirement may depend upon the cell type and the physiological apoptotic cues. Plays an important role in mitochondrial fission during mitosis. Required for formation of endocytic vesicles. Proposed to regulate synaptic vesicle membrane dynamics through association with BCL2L1 isoform Bcl-X(L) which stimulates its GTPase activity in synaptic vesicles; the function may require its recruitment by MFF to clathrin-containing vesicles. Required for programmed necrosis execution. Rhythmic control of its activity following phosphorylation at Ser-656 is essential for the circadian control of mitochondrial ATP production (By similarity).By similarity6 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi32 – 40GTPBy similarity9
Nucleotide bindingi228 – 234GTPBy similarity7
Nucleotide bindingi259 – 262GTPBy similarity4

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase
Biological processBiological rhythms, Endocytosis, Necrosis
LigandGTP-binding, Lipid-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-75153 Apoptotic execution phase

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Dynamin-1-like protein (EC:3.6.5.5)
Alternative name(s):
Dynamin-like protein
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Dnm1l
Synonyms:Dlp1, Drp1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 11

Organism-specific databases

Rat genome database

More...
RGDi
620416 Dnm1l

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell junction, Coated pit, Cytoplasm, Cytoplasmic vesicle, Golgi apparatus, Membrane, Mitochondrion, Mitochondrion outer membrane, Peroxisome, Synapse

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi38K → A: Defective in GTP hydrolysis. Tubulates spherical liposomes. Impairs mitochondrial division. Decreases the BCL2L1-mediated induction of synapse number and size of synaptic vesicle clusters. 2 Publications1
Mutagenesisi71S → A: No effect on mitotic phosphorylation. 1 Publication1
Mutagenesisi139S → A: No effect on mitotic phosphorylation. 1 Publication1
Mutagenesisi149S → A: No effect on mitotic phosphorylation. 1 Publication1
Mutagenesisi231D → N: Defective in GTP-binding. 1 Publication1
Mutagenesisi635S → A: Abolishes mitotic phosphorylation. Reduced mitotic mitochondrial fragmentation. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002065681 – 755Dynamin-1-like proteinAdd BLAST755

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1N-acetylmethionineBy similarity1
Modified residuei542PhosphoserineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki545Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Cross-linki548Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei561PhosphoserineBy similarity1
Cross-linki571Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Cross-linki581Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi604O-linked (GlcNAc) threonine1 Publication1
Glycosylationi605O-linked (GlcNAc) threonine1 Publication1
Cross-linki613Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei616N6-acetyllysine; alternateBy similarity1
Cross-linki616Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki625Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei626PhosphoserineBy similarity1
Cross-linki627Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei635Phosphoserine; by CDK1Combined sources1 Publication1
Modified residuei656Phosphoserine; by CAMK1 and PKA1 Publication1
Modified residuei663S-nitrosocysteineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylation/dephosphorylation events on two sites near the GED domain regulate mitochondrial fission. Phosphorylation on Ser-656 inhibits mitochondrial fission probably through preventing intramolecular interaction. Dephosphorylated on this site by PPP3CA which promotes mitochondrial fission. Phosphorylation on Ser-635 also promotes mitochondrial fission (By similarity). Phosphorylated in a circadian manner at Ser-656 (By similarity).By similarity
Sumoylated on various lysine residues within the B domain, probably by MUL1. Sumoylation positively regulates mitochondrial fission. Desumoylated by SENP5 during G2/M transition of mitosis. Appears to be linked to its catalytic activity (By similarity).By similarity
S-nitrosylation increases DNM1L dimerization, mitochondrial fission and causes neuronal damage.By similarity
Ubiquitinated by MARCHF5.By similarity
O-GlcNAcylation augments the level of the GTP-bound active form of DRP1 and induces translocation from the cytoplasm to mitochondria in cardiomyocytes. It also decreases phosphorylation at Ser-656.1 Publication

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Phosphoprotein, S-nitrosylation, Ubl conjugation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
O35303

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
O35303

PeptideAtlas

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PeptideAtlasi
O35303

PRoteomics IDEntifications database

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PRIDEi
O35303

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
O35303

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
O35303

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
O35303

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in all tissues tested (at protein level). Longer isoforms are preferentially expressed in brain.2 Publications

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By bezafibrate.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSRNOG00000001813 Expressed in brain and 9 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
O35303 RN

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotetramer; dimerizes through the N-terminal GTP-middle region of one molecule binding to the GED domain of another DNM1L molecule. Oligomerizes in a GTP-dependent manner to form membrane-associated tubules with a spiral pattern.

Interacts with GSK3B and MARCHF5 (PubMed:10679301).

Interacts (via the GTPase and B domains) with UBE2I; the interaction promotes sumoylation of DNM1L, mainly in its B domain.

Interacts with PPP3CA; the interaction dephosphorylates DNM1L and regulates its transition to mitochondria.

Interacts with BCL2L1 isoform BCL-X(L) and CLTA; DNM1L and BCL2L1 isoform BCL-X(L) may form a complex in synaptic vesicles that also contains clathrin and MFF (PubMed:23792689, PubMed:18250306).

Interacts with MFF; the interaction is inhinited by C11orf65/MFI (By similarity).

Interacts with FIS1 (PubMed:12861026).

Interacts with MIEF2 and MIEF1; GTP-dependent this regulates GTP hydrolysis and DNM1L oligomerization.

Interacts with PGAM5; this interaction leads to dephosphorylation at Ser-656 and activation of GTPase activity and eventually to mitochondria fragmentation.

By similarity4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
250292, 4 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
O35303

Database of interacting proteins

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DIPi
DIP-29699N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
O35303

Protein interaction database and analysis system

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IntActi
O35303, 7 interactors

Molecular INTeraction database

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MINTi
O35303

STRING: functional protein association networks

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STRINGi
10116.ENSRNOP00000002478

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
O35303

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini22 – 315Dynamin-type GPROSITE-ProRule annotationAdd BLAST294
Domaini663 – 754GEDPROSITE-ProRule annotationAdd BLAST92

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni32 – 39G1 motifPROSITE-ProRule annotation8
Regioni58 – 60G2 motifPROSITE-ProRule annotation3
Regioni159 – 162G3 motifPROSITE-ProRule annotation4
Regioni228 – 231G4 motifPROSITE-ProRule annotation4
Regioni258 – 261G5 motifPROSITE-ProRule annotation4
Regioni357 – 502Middle domainBy similarityAdd BLAST146
Regioni461 – 704Interaction with GSK3BBy similarityAdd BLAST244
Regioni515 – 582B domainBy similarityAdd BLAST68
Regioni673 – 687Important for homodimerizationBy similarityAdd BLAST15

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The GED domain folds back to interact, in cis, with the GTP-binding domain and middle domain, and interacts, in trans, with the GED domains of other DNM1L molecules, and is thus critical for activating GTPase activity and for DNM1L dimerization.By similarity

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family.PROSITE-ProRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0446 Eukaryota
COG0699 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000155504

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_008964_5_0_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O35303

KEGG Orthology (KO)

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KOi
K17065

Identification of Orthologs from Complete Genome Data

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OMAi
LTRANHI

Database of Orthologous Groups

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OrthoDBi
264244at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
O35303

TreeFam database of animal gene trees

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TreeFami
TF352031

Family and domain databases

Conserved Domains Database

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CDDi
cd08771 DLP_1, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.30.29.30, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR030556 DNM1L
IPR000375 Dynamin_central
IPR001401 Dynamin_GTPase
IPR019762 Dynamin_GTPase_CS
IPR022812 Dynamin_SF
IPR030381 G_DYNAMIN_dom
IPR003130 GED
IPR020850 GED_dom
IPR027417 P-loop_NTPase
IPR011993 PH-like_dom_sf

The PANTHER Classification System

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PANTHERi
PTHR11566 PTHR11566, 1 hit
PTHR11566:SF39 PTHR11566:SF39, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF01031 Dynamin_M, 1 hit
PF00350 Dynamin_N, 1 hit
PF02212 GED, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00195 DYNAMIN

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00053 DYNc, 1 hit
SM00302 GED, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF52540 SSF52540, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00410 G_DYNAMIN_1, 1 hit
PS51718 G_DYNAMIN_2, 1 hit
PS51388 GED, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (6)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 6 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: O35303-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MEALIPVINK LQDVFNTVGA DIIQLPQIVV VGTQSSGKSS VLESLVGRDL
60 70 80 90 100
LPRGTGVVTR RPLILQLVHV SPEDKRKTTG EENDPATWKN SRHLSKGVEA
110 120 130 140 150
EEWGKFLHTK NKLYTDFDEI RQEIENETER ISGNNKGVSP EPIHLKVFSP
160 170 180 190 200
NVVNLTLVDL PGMTKVPVGD QPKDIELQIR ELILRFISNP NSIILAVTAA
210 220 230 240 250
NTDMATSEAL KISREVDPDG RRTLAVITKL DLMDAGTDAM DVLMGRVIPV
260 270 280 290 300
KLGIIGVVNR SQLDINNKKS VTDSIRDEYA FLQKKYPSLA NRNGTKYLAR
310 320 330 340 350
TLNRLLMHHI RDCLPELKTR INVLAAQYQS LLNSYGEPVD DKSATLLQLI
360 370 380 390 400
TKFATEYCNT IEGTAKYIET SELCGGARIC YIFHETFGRT LESVDPLGGL
410 420 430 440 450
NTIDILTAIR NATGPRPALF VPEVSFELLV KRQIKRLEEP SLRCVELVHE
460 470 480 490 500
EMQRIIQHCS NYSTQELLRF PKLHDAIVEV VTCLLRKRLP VTNEMVHNLV
510 520 530 540 550
AIELAYINTK HPDFADACGL MNNNIEEQRR NRLARELPSA VSRDKSSKVP
560 570 580 590 600
SALAPASQEP SPAASAEADG KLIQDNRRET KNVASAGGGI GDGGRIGDGG
610 620 630 640 650
QEPTTGNWRG MLKTSKAEEL LAEEKSKPIP IMPASPQKGH AVNLLDVPVP
660 670 680 690 700
VARKLSAREQ RDCEVIERLI KSYFLIVRKN IQDSVPKAVM HFLVNHVKDT
710 720 730 740 750
LQSELVGQLY KSSLLDDLLT ESEDMAQRRK EAADMLKALQ GASQIIAEIR

ETHLW
Length:755
Mass (Da):83,908
Last modified:January 1, 1998 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i0568353907794C43
GO
Isoform 2 (identifier: O35303-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     84-96: Missing.
     546-571: Missing.

Show »
Length:716
Mass (Da):79,951
Checksum:iE7A629A401FA7004
GO
Isoform 3 (identifier: O35303-3) [UniParc]FASTAAdd to basket
Also known as: DLP1-37

The sequence of this isoform differs from the canonical sequence as follows:
     84-84: D → GKFQSWN
     546-596: SSKVPSALAPASQEPSPAASAEADGKLIQDNRRETKNVASAGGGIGDGGRI → VASGGGGV

Show »
Length:718
Mass (Da):80,253
Checksum:iBC6D99B05A12B398
GO
Isoform 4 (identifier: O35303-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     84-97: DPATWKNSRHLSKG → GKFQSWR

Show »
Length:748
Mass (Da):83,220
Checksum:iFFF210166CD3398E
GO
Isoform 5 (identifier: O35303-5) [UniParc]FASTAAdd to basket
Also known as: DLP1-11

The sequence of this isoform differs from the canonical sequence as follows:
     572-582: Missing.

Show »
Length:744
Mass (Da):82,540
Checksum:i5C1E562180C58035
GO
Isoform 6 (identifier: O35303-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     546-582: Missing.

Show »
Length:718
Mass (Da):80,104
Checksum:i459857BD43835FE5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti517A → V in AAB71237 (PubMed:9472031).Curated1
Sequence conflicti600G → V in AAD31278 (PubMed:10679301).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_01369684 – 97DPATW…HLSKG → GKFQSWR in isoform 4. 1 PublicationAdd BLAST14
Alternative sequenceiVSP_01369784 – 96Missing in isoform 2. 2 PublicationsAdd BLAST13
Alternative sequenceiVSP_01369884D → GKFQSWN in isoform 3. 2 Publications1
Alternative sequenceiVSP_013699546 – 596SSKVP…DGGRI → VASGGGGV in isoform 3. 2 PublicationsAdd BLAST51
Alternative sequenceiVSP_013700546 – 582Missing in isoform 6. 1 PublicationAdd BLAST37
Alternative sequenceiVSP_013701546 – 571Missing in isoform 2. 2 PublicationsAdd BLAST26
Alternative sequenceiVSP_013702572 – 582Missing in isoform 5. 2 PublicationsAdd BLAST11

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF019043 mRNA Translation: AAB72197.1
AF020207 mRNA Translation: AAB71232.1
AF020208 mRNA Translation: AAB71233.1
AF020209 mRNA Translation: AAB71234.1
AF020210 mRNA Translation: AAB71235.1
AF020211 mRNA Translation: AAB71236.1
AF020212 mRNA Translation: AAB71237.1
AF020213 mRNA Translation: AAB71238.1
AF107048 mRNA Translation: AAD22412.1
AF132727 mRNA Translation: AAD31278.1
BC085843 mRNA Translation: AAH85843.1

NCBI Reference Sequences

More...
RefSeqi
NP_446107.2, NM_053655.3 [O35303-2]
XP_006248785.1, XM_006248723.3 [O35303-6]
XP_008767063.1, XM_008768841.2 [O35303-1]
XP_008767064.1, XM_008768842.2 [O35303-4]
XP_008767065.1, XM_008768843.2 [O35303-5]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000002477; ENSRNOP00000002477; ENSRNOG00000001813 [O35303-2]
ENSRNOT00000002478; ENSRNOP00000002478; ENSRNOG00000001813 [O35303-1]
ENSRNOT00000002482; ENSRNOP00000002482; ENSRNOG00000001813 [O35303-6]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
114114

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:114114

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF019043 mRNA Translation: AAB72197.1
AF020207 mRNA Translation: AAB71232.1
AF020208 mRNA Translation: AAB71233.1
AF020209 mRNA Translation: AAB71234.1
AF020210 mRNA Translation: AAB71235.1
AF020211 mRNA Translation: AAB71236.1
AF020212 mRNA Translation: AAB71237.1
AF020213 mRNA Translation: AAB71238.1
AF107048 mRNA Translation: AAD22412.1
AF132727 mRNA Translation: AAD31278.1
BC085843 mRNA Translation: AAH85843.1
RefSeqiNP_446107.2, NM_053655.3 [O35303-2]
XP_006248785.1, XM_006248723.3 [O35303-6]
XP_008767063.1, XM_008768841.2 [O35303-1]
XP_008767064.1, XM_008768842.2 [O35303-4]
XP_008767065.1, XM_008768843.2 [O35303-5]

3D structure databases

SMRiO35303
ModBaseiSearch...

Protein-protein interaction databases

BioGridi250292, 4 interactors
CORUMiO35303
DIPiDIP-29699N
ELMiO35303
IntActiO35303, 7 interactors
MINTiO35303
STRINGi10116.ENSRNOP00000002478

PTM databases

iPTMnetiO35303
PhosphoSitePlusiO35303
SwissPalmiO35303

Proteomic databases

jPOSTiO35303
PaxDbiO35303
PeptideAtlasiO35303
PRIDEiO35303

Genome annotation databases

EnsembliENSRNOT00000002477; ENSRNOP00000002477; ENSRNOG00000001813 [O35303-2]
ENSRNOT00000002478; ENSRNOP00000002478; ENSRNOG00000001813 [O35303-1]
ENSRNOT00000002482; ENSRNOP00000002482; ENSRNOG00000001813 [O35303-6]
GeneIDi114114
KEGGirno:114114

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
10059
RGDi620416 Dnm1l

Phylogenomic databases

eggNOGiKOG0446 Eukaryota
COG0699 LUCA
GeneTreeiENSGT00940000155504
HOGENOMiCLU_008964_5_0_1
InParanoidiO35303
KOiK17065
OMAiLTRANHI
OrthoDBi264244at2759
PhylomeDBiO35303
TreeFamiTF352031

Enzyme and pathway databases

ReactomeiR-RNO-75153 Apoptotic execution phase

Miscellaneous databases

Protein Ontology

More...
PROi
PR:O35303

Gene expression databases

BgeeiENSRNOG00000001813 Expressed in brain and 9 other tissues
GenevisibleiO35303 RN

Family and domain databases

CDDicd08771 DLP_1, 1 hit
Gene3Di2.30.29.30, 1 hit
InterProiView protein in InterPro
IPR030556 DNM1L
IPR000375 Dynamin_central
IPR001401 Dynamin_GTPase
IPR019762 Dynamin_GTPase_CS
IPR022812 Dynamin_SF
IPR030381 G_DYNAMIN_dom
IPR003130 GED
IPR020850 GED_dom
IPR027417 P-loop_NTPase
IPR011993 PH-like_dom_sf
PANTHERiPTHR11566 PTHR11566, 1 hit
PTHR11566:SF39 PTHR11566:SF39, 1 hit
PfamiView protein in Pfam
PF01031 Dynamin_M, 1 hit
PF00350 Dynamin_N, 1 hit
PF02212 GED, 1 hit
PRINTSiPR00195 DYNAMIN
SMARTiView protein in SMART
SM00053 DYNc, 1 hit
SM00302 GED, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS00410 G_DYNAMIN_1, 1 hit
PS51718 G_DYNAMIN_2, 1 hit
PS51388 GED, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiDNM1L_RAT
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O35303
Secondary accession number(s): O35318
, O35319, O35320, O35321, O35322, O35323, Q5U2W1, Q792T7, Q9R234, Q9R277
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: January 1, 1998
Last modified: April 22, 2020
This is version 158 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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