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Entry version 156 (05 Jun 2019)
Sequence version 2 (10 May 2005)
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Protein

Dynamin-1-like protein

Gene

Dnm1l

Organism
Mus musculus (Mouse)
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-643 is essential for the circadian control of mitochondrial ATP production (PubMed:29478834).By similarity6 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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_section">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 bindingi221 – 227GTPBy similarity7
Nucleotide bindingi252 – 255GTPBy 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-MMU-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_and_taxonomy_section">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 family member proline-rich carboxyl-terminal domain less
Short name:
Dymple
Dynamin-related protein 1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:Drp1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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 16

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1921256 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

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Mutant mice show severe developmental abnormalities and die between 10.5 and 12.5 dpc. Compared to wild-type littermates, mutant embryos at 9.5-11.5 dpc have a significantly smaller body size, pulsing, but less developed cardiac structures, a poorly developed liver and a thinner neural tube cell layer. They lack trophoblastic giant cell layer in the placenta. Primary cultures of mutant neuronal cells have severe defects in synapse formation and high sensitivity to Ca2+-dependent apoptosis. Within cerebellar neurons, Purkinje cells are particularly sensitive to Dnm1l ablation. Conditional knockout in postmitotic Purkinje cells leads to 40% neuronal degeneration after 3 months and 90% after 6 months.3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi59T → A: Abolishes GTP hydrolysis. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2331072

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002065671 – 742Dynamin-1-like proteinAdd BLAST742

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 residuei535PhosphoserineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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-linki538Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Cross-linki541Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Cross-linki564Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Cross-linki574Glycyl 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_processing_section">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>Glycosylationi591O-linked (GlcNAc) threonineBy similarity1
Glycosylationi592O-linked (GlcNAc) threonineBy similarity1
Cross-linki600Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei603N6-acetyllysine; alternateCombined sources1
Cross-linki603Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki612Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei613PhosphoserineBy similarity1
Cross-linki614Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei622PhosphoserineCombined sources1
Modified residuei643Phosphoserine; by CAMK1 and PKABy similarity1
Modified residuei650S-nitrosocysteineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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-643 inhibits mitochondrial fission probably through preventing intramolecular interaction. Dephosphorylated on this site by PPP3CA which promotes mitochondrial fission. Phosphorylation on Ser-622 also promotes mitochondrial fission (By similarity). Phosphorylated in a circadian manner at Ser-643 (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
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-643 (By similarity).By similarity

Keywords - PTMi

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

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q8K1M6

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q8K1M6

PeptideAtlas

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PeptideAtlasi
Q8K1M6

PRoteomics IDEntifications database

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PRIDEi
Q8K1M6

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q8K1M6

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

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PhosphoSitePlusi
Q8K1M6

SwissPalm database of S-palmitoylation events

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SwissPalmi
Q8K1M6

<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 the cerebellum and in several regions of the cerebrum and diencephalon. Strongly expressed in the cerebellar Purkinje cells and in the pontile giant neurons.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000022789 Expressed in 291 organ(s), highest expression level in brainstem

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q8K1M6 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q8K1M6 MM

<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_section">'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_section">'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 MARCH5. 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. Interacts with FIS1. Interacts with MIEF2 and MIEF1; GTP-dependent this regulates GTP hydrolysis and DNM1L oligomerization (PubMed:24508339). Interacts with PGAM5; this interaction leads to dephosphorylation at Ser-656 and activation of GTPase activity and eventually to mitochondria fragmentation.By similarity1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<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)

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BioGridi
216417, 10 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q8K1M6

Database of interacting proteins

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DIPi
DIP-54818N

Protein interaction database and analysis system

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IntActi
Q8K1M6, 28 interactors

Molecular INTeraction database

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MINTi
Q8K1M6

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000111415

<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
Q8K1M6

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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_and_domains_section">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 – 308Dynamin-type GPROSITE-ProRule annotationAdd BLAST287
Domaini650 – 741GEDPROSITE-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
Regioni152 – 155G3 motifPROSITE-ProRule annotation4
Regioni221 – 224G4 motifPROSITE-ProRule annotation4
Regioni251 – 254G5 motifPROSITE-ProRule annotation4
Regioni350 – 495Middle domainBy similarityAdd BLAST146
Regioni454 – 691Interaction with GSK3BBy similarityAdd BLAST238
Regioni508 – 575B domainBy similarityAdd BLAST68
Regioni548 – 742C-terminal dimerization domainBy similarityAdd BLAST195
Regioni660 – 674Important 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

Ensembl GeneTree

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GeneTreei
ENSGT00940000155504

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000161068

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q8K1M6

KEGG Orthology (KO)

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KOi
K17065

Database of Orthologous Groups

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OrthoDBi
264244at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q8K1M6

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_length">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 (5+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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 5 <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.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 5 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q8K1M6-1) [UniParc]FASTAAdd to basket

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.

« Hide
        10         20         30         40         50
MEALIPVINK LQDVFNTVGA DIIQLPQIVV VGTQSSGKSS VLESLVGRDL
60 70 80 90 100
LPRGTGVVTR RPLILQLVHV SPEDKRKTTG EENGKFQSWR VEAEEWGKFL
110 120 130 140 150
HTKNKLYTDF DEIRQEIENE TERISGNNKG VSPEPIHLKV FSPNVVNLTL
160 170 180 190 200
VDLPGMTKVP VGDQPKDIEL QIRELILRFI SNPNSIILAV TAANTDMATS
210 220 230 240 250
EALKISREVD PDGRRTLAVI TKLDLMDAGT DAMDVLMGRV IPVKLGIIGV
260 270 280 290 300
VNRSQLDINN KKSVTDSIRD EYAFLQKKYP SLANRNGTKY LARTLNRLLM
310 320 330 340 350
HHIRDCLPEL KTRINVLAAQ YQSLLNSYGE PVDDKSATLL QLITKFATEY
360 370 380 390 400
CNTIEGTAKY IETSELCGGA RICYIFHETF GRTLESVDPL GGLNTIDILT
410 420 430 440 450
AIRNATGPRP ALFVPEVSFE LLVKRQIKRL EEPSLRCVEL VHEEMQRIIQ
460 470 480 490 500
HCSNYSTQEL LRFPKLHDAI VEVVTCLLRK RLPVTNEMVH NLVAIELAYI
510 520 530 540 550
NTKHPDFADA CGLMNNNIEE QRRNRLAREL PSAGSRDKSS KVPSALAPAS
560 570 580 590 600
QEPPPAASAE ADGKLIQDNR RETKNVPSAG GGIGDGGQEP TTGNWRGMLK
610 620 630 640 650
TSKAEELLAE EKSKPIPIMP ASPQKGHAVN LLDVPVPVAR KLSAREQRDC
660 670 680 690 700
EVIERLIKSY FLIVRKNIQD SVPKAVMHFL VNHVKDTLQS ELVGQLYKSS
710 720 730 740
LLDDLLTESE DMAQRRKEAA DMLKALQGAS QIIAEIRETH LW
Note: No experimental confirmation available.
Length:742
Mass (Da):82,658
Last modified:May 10, 2005 - v2
<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:i5A8679B61A444847
GO
Isoform 2 (identifier: Q8K1M6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     539-564: Missing.

Show »
Length:716
Mass (Da):80,212
Checksum:i3C922A7A135B9A37
GO
Isoform 3 (identifier: Q8K1M6-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     85-90: Missing.
     539-575: Missing.

Show »
Length:699
Mass (Da):78,011
Checksum:i68ED85D93914B4DC
GO
Isoform 4 (identifier: Q8K1M6-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-104: Missing.
     105-105: K → M
     539-564: Missing.

Show »
Length:612
Mass (Da):68,701
Checksum:iC5D0BCE4B4622502
GO
Isoform 5 (identifier: Q8K1M6-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     85-90: Missing.
     214-227: RRTLAVITKLDLMD → KGRCLYLMDVDLQW
     228-742: Missing.

Show »
Length:221
Mass (Da):24,488
Checksum:i29C66A3A04924F55
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E9PUD2E9PUD2_MOUSE
Dynamin-1-like protein
Dnm1l
712Annotation score:

Annotation score:2 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>
A0A2U3TZ67A0A2U3TZ67_MOUSE
Dynamin-1-like protein
Dnm1l
587Annotation score:

Annotation score:1 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 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 conflicti165P → L in BAC06576 (PubMed:14592431).Curated1
Sequence conflicti320Q → R in BAC06576 (PubMed:14592431).Curated1
Sequence conflicti519E → A in BAC34640 (PubMed:16141072).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_0136891 – 104Missing in isoform 4. 1 PublicationAdd BLAST104
Alternative sequenceiVSP_01369085 – 90Missing in isoform 3 and isoform 5. 2 Publications6
Alternative sequenceiVSP_013691105K → M in isoform 4. 1 Publication1
Alternative sequenceiVSP_013692214 – 227RRTLA…LDLMD → KGRCLYLMDVDLQW in isoform 5. CuratedAdd BLAST14
Alternative sequenceiVSP_013693228 – 742Missing in isoform 5. CuratedAdd BLAST515
Alternative sequenceiVSP_013694539 – 575Missing in isoform 3. 2 PublicationsAdd BLAST37
Alternative sequenceiVSP_013695539 – 564Missing in isoform 2 and isoform 4. 2 PublicationsAdd BLAST26

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AB079133 mRNA Translation: BAC06576.1
AK051443 mRNA Translation: BAC34640.1
AK080871 mRNA Translation: BAC38054.1
BC027538 mRNA Translation: AAH27538.1
BC040777 mRNA Translation: AAH40777.1
BC079635 mRNA Translation: AAH79635.1
CF914619 mRNA No translation available.

The Consensus CDS (CCDS) project

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CCDSi
CCDS27984.1 [Q8K1M6-3]
CCDS70689.1 [Q8K1M6-2]

NCBI Reference Sequences

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RefSeqi
NP_001021118.1, NM_001025947.2 [Q8K1M6-3]
NP_001263269.1, NM_001276340.1 [Q8K1M6-2]
NP_001263270.1, NM_001276341.1 [Q8K1M6-4]
NP_690029.2, NM_152816.3
XP_006522694.1, XM_006522631.3 [Q8K1M6-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000023477; ENSMUSP00000023477; ENSMUSG00000022789 [Q8K1M6-3]
ENSMUST00000230022; ENSMUSP00000155429; ENSMUSG00000022789 [Q8K1M6-4]
ENSMUST00000230038; ENSMUSP00000155605; ENSMUSG00000022789 [Q8K1M6-5]
ENSMUST00000230980; ENSMUSP00000155155; ENSMUSG00000022789 [Q8K1M6-2]

Database of genes from NCBI RefSeq genomes

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GeneIDi
74006

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:74006

UCSC genome browser

More...
UCSCi
uc007yij.2 mouse [Q8K1M6-1]
uc007yik.2 mouse [Q8K1M6-4]
uc007yim.2 mouse [Q8K1M6-3]
uc007yin.2 mouse [Q8K1M6-2]
uc007yio.2 mouse [Q8K1M6-5]

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
AB079133 mRNA Translation: BAC06576.1
AK051443 mRNA Translation: BAC34640.1
AK080871 mRNA Translation: BAC38054.1
BC027538 mRNA Translation: AAH27538.1
BC040777 mRNA Translation: AAH40777.1
BC079635 mRNA Translation: AAH79635.1
CF914619 mRNA No translation available.
CCDSiCCDS27984.1 [Q8K1M6-3]
CCDS70689.1 [Q8K1M6-2]
RefSeqiNP_001021118.1, NM_001025947.2 [Q8K1M6-3]
NP_001263269.1, NM_001276340.1 [Q8K1M6-2]
NP_001263270.1, NM_001276341.1 [Q8K1M6-4]
NP_690029.2, NM_152816.3
XP_006522694.1, XM_006522631.3 [Q8K1M6-1]

3D structure databases

SMRiQ8K1M6
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi216417, 10 interactors
CORUMiQ8K1M6
DIPiDIP-54818N
IntActiQ8K1M6, 28 interactors
MINTiQ8K1M6
STRINGi10090.ENSMUSP00000111415

Chemistry databases

ChEMBLiCHEMBL2331072

PTM databases

iPTMnetiQ8K1M6
PhosphoSitePlusiQ8K1M6
SwissPalmiQ8K1M6

Proteomic databases

EPDiQ8K1M6
jPOSTiQ8K1M6
PeptideAtlasiQ8K1M6
PRIDEiQ8K1M6

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023477; ENSMUSP00000023477; ENSMUSG00000022789 [Q8K1M6-3]
ENSMUST00000230022; ENSMUSP00000155429; ENSMUSG00000022789 [Q8K1M6-4]
ENSMUST00000230038; ENSMUSP00000155605; ENSMUSG00000022789 [Q8K1M6-5]
ENSMUST00000230980; ENSMUSP00000155155; ENSMUSG00000022789 [Q8K1M6-2]
GeneIDi74006
KEGGimmu:74006
UCSCiuc007yij.2 mouse [Q8K1M6-1]
uc007yik.2 mouse [Q8K1M6-4]
uc007yim.2 mouse [Q8K1M6-3]
uc007yin.2 mouse [Q8K1M6-2]
uc007yio.2 mouse [Q8K1M6-5]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
10059
MGIiMGI:1921256 Dnm1l

Phylogenomic databases

GeneTreeiENSGT00940000155504
HOGENOMiHOG000161068
InParanoidiQ8K1M6
KOiK17065
OrthoDBi264244at2759
PhylomeDBiQ8K1M6
TreeFamiTF352031

Enzyme and pathway databases

ReactomeiR-MMU-75153 Apoptotic execution phase

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q8K1M6

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000022789 Expressed in 291 organ(s), highest expression level in brainstem
ExpressionAtlasiQ8K1M6 baseline and differential
GenevisibleiQ8K1M6 MM

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...

<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_MOUSE
<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: Q8K1M6
Secondary accession number(s): Q8BNQ5
, Q8BQ64, Q8CGD0, Q8K1A1
<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_and_isoforms">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: May 10, 2005
Last modified: June 5, 2019
This is version 156 of the entry and version 2 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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