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UniProtKB - O00429 (DNM1L_HUMAN)

Protein

Dynamin-1-like protein

Gene

DNM1L

Organism
Homo sapiens (Human)
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 (PubMed:29899447). 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 (PubMed:29899447). 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 (PubMed:26992161, PubMed:27301544, PubMed:27328748). 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.23 Publications
Isoform 1: Inhibits peroxisomal division when overexpressed.1 Publication
Isoform 4: Inhibits peroxisomal division when overexpressed.1 Publication

<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

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

GTPase activity is increased by binding to phospholipid membranes.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 – 40GTP1 Publication9
Nucleotide bindingi215 – 221GTP1 Publication7
Nucleotide bindingi246 – 249GTP1 Publication4

<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

  • BH2 domain binding Source: Ensembl
  • clathrin binding Source: Ensembl
  • GTPase activator activity Source: ParkinsonsUK-UCL
  • GTPase activity Source: UniProtKB
  • GTP binding Source: UniProtKB-KW
  • GTP-dependent protein binding Source: ParkinsonsUK-UCL
  • identical protein binding Source: IntAct
  • lipid binding Source: UniProtKB-KW
  • microtubule binding Source: GO_Central
  • protein-containing complex binding Source: Ensembl
  • protein homodimerization activity Source: UniProtKB
  • Rab GTPase binding Source: ParkinsonsUK-UCL
  • ubiquitin protein ligase binding Source: UniProtKB
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<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 processEndocytosis, Necrosis
LigandGTP-binding, Lipid-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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

SIGNOR Signaling Network Open Resource

More...SIGNORi		O00429

Protein family/group databases

Transport Classification Database

More...TCDBi		1.N.6.1.2 the mitochondrial inner/outer membrane fusion (mmf) family

<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):
Dnm1p/Vps1p-like protein
Short name:
DVLP
Dynamin family member proline-rich carboxyl-terminal domain less
Short name:
Dymple
Dynamin-like protein
Dynamin-like protein 4
Dynamin-like protein IV
Short name:
HdynIV
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:DLP1, 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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<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
  • UP000005640 <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 12

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000087470.17

Human Gene Nomenclature Database

More...HGNCi		HGNC:2973 DNM1L

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		603850 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_O00429

<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; 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 provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

May be associated with Alzheimer disease through amyloid-beta-induced increased S-nitrosylation of DNM1L, which triggers, directly or indirectly, excessive mitochondrial fission, synaptic loss and neuronal damage.1 Publication
Encephalopathy due to defective mitochondrial and peroxisomal fission 1 (EMPF1)7 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare autosomal dominant systemic disorder resulting in lack of neurologic development and death in infancy. After birth, infants present in the first week of life with poor feeding and neurologic impairment, including hypotonia, little spontaneous movement, no tendon reflexes, no response to light stimulation, and poor visual fixation. Other features include mildly elevated plasma concentration of very-long-chain fatty acids, lactic acidosis, microcephaly, deep-set eyes, optic atrophy and hypoplasia, and an abnormal gyral pattern in both frontal lobes associated with dysmyelination.
See also OMIM:614388
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_08087036S → G in EMPF1; autosomal recessive; impaired mitochondrial membrane fission; hypomorphic mutation retaining partial activity in mitochondrial membrane fission. 1 PublicationCorresponds to variant dbSNP:rs879255688EnsemblClinVar.1
Natural variantiVAR_076316362G → D in EMPF1; unknown pathological significance; unable to associate with MIEF2 into filaments forming the tubular structures that wrap around the scission site; presence of concentric cristae and/or increased dense granules in some mitochondria. 2 PublicationsCorresponds to variant dbSNP:rs879255685EnsemblClinVar.1
Natural variantiVAR_076317362G → S in EMPF1; the mutation acts in a dominant-negative manner; defects observed in mitochondrial fission; significant decrease in mitochondrial respiratory chain complex IV activity. 1 PublicationCorresponds to variant dbSNP:rs886037861EnsemblClinVar.1
Natural variantiVAR_063704395A → D in EMPF1; the mutation acts in a dominant-negative manner; defects observed in both mitochondrial and peroxisomal fission; reduced oligomerization, decreased mitochondrial recruitment. 2 PublicationsCorresponds to variant dbSNP:rs121908531EnsemblClinVar.1
Natural variantiVAR_076318403R → C in EMPF1; the mutation acts in a dominant-negative manner; reduced oligomerization; decreased mitochondrial recruitment; defects observed in mitochondrial fission. 1 PublicationCorresponds to variant dbSNP:rs863223953EnsemblClinVar.1
Natural variantiVAR_080872406L → S in EMPF1; impaired mitochondrial and peroxisomal membrane fission. 1 Publication1
Optic atrophy 5 (OPA5)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of optic atrophy, a disease characterized by progressive visual loss in association with a deficiency in the number of nerve fibers which arise in the retina and converge to form the optic disk, optic nerve, optic chiasm and optic tracts. OPA5 is an autosomal dominant non-syndromic form that manifests as slowly progressive visual loss with variable onset from the first to third decades. Additional ocular abnormalities may include central scotoma and dyschromatopsia.
See also OMIM:610708
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0808692E → A in OPA5; changed localization to mitochondrion; impaired mitochondrial membrane fission. 1 Publication1
Natural variantiVAR_080871192A → E in OPA5; changed localization to mitochondrion; impaired mitochondrial membrane fission. 1 Publication1

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>Mutagenesisi34Q → A: Abolishes GTP hydrolysis. 1 Publication1
Mutagenesisi38K → A: Loss of GTPase activity. Impairs mitochondrial division and induces changes in peroxisome morphology. No effect on oligomerization. Increase in sumoylation by SUMO3. 6 Publications1
Mutagenesisi38K → E: Overexpression delays protein secretion. 6 Publications1
Mutagenesisi39S → A: Abolishes GTP hydrolysis. 3 Publications1
Mutagenesisi39S → I: Decreased localization to the perinuclear region. 3 Publications1
Mutagenesisi39S → N: Reduces peroxisomal abundance. 3 Publications1
Mutagenesisi41V → F: Temperature-sensitive. Impairs mitochondrial division. 1 Publication1
Mutagenesisi59T → A: Abolishes GTP hydrolysis. Impairs mitochondrial division. Reduces peroxisomal abundance. 3 Publications1
Mutagenesisi146D → A: Abolishes GTP hydrolysis. 1 Publication1
Mutagenesisi149G → A: Abolishes GTP hydrolysis. 1 Publication1
Mutagenesisi190D → A: Unable to homooligomerize. Unable to associate with MIEF2 into filaments forming the tubular structures that wrap around the scission site. 1 Publication1
Mutagenesisi216K → A: Abolishes GTP hydrolysis. 1 Publication1
Mutagenesisi218D → A: Abolishes GTP hydrolysis. 1 Publication1
Mutagenesisi221D → A: Unable to homooligomerize. Unable to associate with MIEF2 into filaments forming the tubular structures that wrap around the scission site. 1 Publication1
Mutagenesisi281G → D: Temperature-sensitive. Impairs mitochondrial division. 1 Publication1
Mutagenesisi300C → A: No effect on S-nitrosylation. 1 Publication1
Mutagenesisi345C → A: No effect on S-nitrosylation. 1 Publication1
Mutagenesisi361C → A: No effect on S-nitrosylation. 1 Publication1
Mutagenesisi367C → A: No effect on S-nitrosylation. 1 Publication1
Mutagenesisi401 – 404GPRP → AAAA: Impairs formation of higher order oligomers, but not homodimerization. 1 Publication4
Mutagenesisi431C → A: No effect on S-nitrosylation. 1 Publication1
Mutagenesisi446C → A: No effect on S-nitrosylation. 1 Publication1
Mutagenesisi470C → A: No effect on S-nitrosylation. 1 Publication1
Mutagenesisi490E → A: Does not impair homodimerization and formation of higher order oligomers. 1 Publication1
Mutagenesisi490E → R: Impairs homodimerization and formation of higher order oligomers. 1 Publication1
Mutagenesisi505C → A: No effect on S-nitrosylation. 1 Publication1
Mutagenesisi532K → R: Some loss of sumoylation in B domain. Complete loss of sumoylation in B domain; when associated with R-535; R-558 and R-568. 1 Publication1
Mutagenesisi535K → R: Some loss of sumoylation in B domain. Complete loss of sumoylation in B domain; when associated with R-532; R-558 and R-568. 1 Publication1
Mutagenesisi558K → R: Some loss of sumoylation in B domain. Complete loss of sumoylation in B domain; when associated with R-532; R-535 and R-568. 1 Publication1
Mutagenesisi568K → R: Some loss of sumoylation in B domain. Complete loss of sumoylation in B domain; when associated with R-532; R-535 and R-558. 1 Publication1
Mutagenesisi594K → R: Some loss of sumoylation in the GED domain; Complete loss of sumoylation in the GED domain; when associated with R-597; R-606 and R-608. 1 Publication1
Mutagenesisi597K → R: Some loss of sumoylation in the GED domain; Complete loss of sumoylation in the GED domain; when associated with R-594; R-606 and R-608. 1 Publication1
Mutagenesisi606K → R: Some loss of sumoylation in the GED domain; Complete loss of sumoylation in the GED domain; when associated with R-594; R-597 and R-608. 1 Publication1
Mutagenesisi608K → R: Some loss of sumoylation in the GED domain; Complete loss of sumoylation in the GED domain; when associated with R-594; R-597 and R-606. 1 Publication1
Mutagenesisi616S → A: Little effect on mitochondrial morphology. Translocated to mitochondria. 1 Publication1
Mutagenesisi637S → A: Abolishes phosphorylation. Reduces interaction with MIEF1 and MIEF2. Promotes mitochondrial fission and cell vulnerability to apoptotic insults. Mostly mitochondrial. Disrupts, in vitro, binding to FIS1. 4 Publications1
Mutagenesisi637S → D: Impairs intramolecular interactions but not homooligomerization. Does not reduce interaction with MIEF1 and MIEF2. Impairs formation of higher order oligomers but not homodimerization. Unable to associate with MIEF2 into filaments forming the tubular structures that wrap around the scission site. Slight reduction in GTPase activity. Inhibits mitochondrial fission. Retained in the cytoplasm. 5 Publications1
Mutagenesisi644C → A: Abolishes S-nitrosylation. Reduced dimerization and no enhancement of GTPase activity. 1 Publication1
Mutagenesisi668K → E: Abolishes homodimerization and formation of higher order oligomers. 1 Publication1
Mutagenesisi679K → A: Diminishes intramolecular interaction between GTP-middle domain and GED domain but no effect on homooligomerization. Marked reduction in GTPase activity, in vitro. Decreased mitochondrial division. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...DisGeNETi		10059

MalaCards human disease database

More...MalaCardsi		DNM1L
MIMi610708 phenotype
614388 phenotype

Open Targets

More...OpenTargetsi		ENSG00000087470

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		98673 Autosomal dominant optic atrophy, classic form
330050 Lethal encephalopathy due to mitochondrial and peroxisomal fission defect

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA27441

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		DNM1L

<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_00002065661 – 736Dynamin-1-like proteinAdd BLAST736

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-acetylmethionineCombined sources1
Modified residuei529PhosphoserineCombined sources1
<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-linki532Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Cross-linki535Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei548PhosphoserineCombined sources1
Cross-linki558Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Cross-linki568Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
<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>Glycosylationi585O-linked (GlcNAc) threonineBy similarity1
Glycosylationi586O-linked (GlcNAc) threonineBy similarity1
Cross-linki594Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei597N6-acetyllysine; alternateBy similarity1
Cross-linki597Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Cross-linki606Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei607PhosphoserineCombined sources1
Cross-linki608Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei616Phosphoserine; by CDK1Combined sources2 Publications1
Modified residuei637Phosphoserine; by CAMK1 and PKA5 Publications1
Modified residuei644S-nitrosocysteine1 Publication1

<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-637 inhibits the GTPase activity, leading to a defect in mitochondrial fission promoting mitochondrial elongation. Dephosphorylated on this site by PPP3CA which promotes mitochondrial fission. Phosphorylation on Ser-616 activates the GTPase activity and promotes mitochondrial fission.6 Publications
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.3 Publications
S-nitrosylation increases DNM1L dimerization, mitochondrial fission and causes neuronal damage.1 Publication
Ubiquitination by MARCH5 affects mitochondrial morphology.2 Publications
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-637 (By similarity).By similarity

Keywords - PTMi

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

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		O00429

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		O00429

MaxQB - The MaxQuant DataBase

More...MaxQBi		O00429

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

More...PaxDbi		O00429

PeptideAtlas

More...PeptideAtlasi		O00429

PRoteomics IDEntifications database

More...PRIDEi		O00429

ProteomicsDB human proteome resource

More...ProteomicsDBi		47884
47885 [O00429-2]
47886 [O00429-3]
47887 [O00429-4]
47888 [O00429-5]
47889 [O00429-6]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		O00429

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

More...PhosphoSitePlusi		O00429

SwissPalm database of S-palmitoylation events

More...SwissPalmi		O00429

Miscellaneous databases

CutDB - Proteolytic event database

More...PMAP-CutDBi		O00429

<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

Ubiquitously expressed with highest levels found in skeletal muscles, heart, kidney and brain. Isoform 1 is brain-specific. Isoform 2 and isoform 3 are predominantly expressed in testis and skeletal muscles respectively. Isoform 4 is weakly expressed in brain, heart and kidney. Isoform 5 is dominantly expressed in liver, heart and kidney. Isoform 6 is expressed in neurons.5 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000087470 Expressed in 237 organ(s), highest expression level in intestine

CleanEx database of gene expression profiles

More...CleanExi		HS_DNM1L

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		O00429 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		O00429 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB009952
HPA039324

<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. Interacts with PGAM5; this interaction leads to dephosphorylation at Ser-656 and activation of GTPase activity and eventually to mitochondria fragmentation.17 Publications

<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

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		115370, 206 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		O00429

Database of interacting proteins

More...DIPi		DIP-42704N

Protein interaction database and analysis system

More...IntActi		O00429, 177 interactors

Molecular INTeraction database

More...MINTi		O00429

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000450399

<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

Secondary structure

1736
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3W6NX-ray2.00A/B1-329[»]
A/B709-736[»]
3W6OX-ray1.90A/B1-329[»]
A/B709-736[»]
3W6PX-ray1.70A/B1-329[»]
A/B709-736[»]
4BEJX-ray3.48A/B/C/D1-736[»]
4H1UX-ray2.30A1-327[»]
A711-736[»]
4H1VX-ray2.30A1-327[»]
A711-736[»]
5WP9electron microscopy4.22A/C/E/G/I/K/M/O1-736[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		O00429

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

More...SMRi		O00429

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...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 – 302Dynamin-type GPROSITE-ProRule annotationAdd BLAST281
Domaini644 – 735GEDPROSITE-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
Regioni146 – 149G3 motifPROSITE-ProRule annotation4
Regioni215 – 218G4 motifPROSITE-ProRule annotation4
Regioni245 – 248G5 motifPROSITE-ProRule annotation4
Regioni344 – 489Middle domain1 PublicationAdd BLAST146
Regioni448 – 685Interaction with GSK3B1 PublicationAdd BLAST238
Regioni502 – 569B domain1 PublicationAdd BLAST68
Regioni654 – 668Important for homodimerization1 PublicationAdd 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.1 Publication

<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

More...eggNOGi		KOG0446 Eukaryota
COG0699 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000155504

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000161068

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG107833

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		O00429

KEGG Orthology (KO)

More...KOi		K17065

Identification of Orthologs from Complete Genome Data

More...OMAi		NIMATQF

Database of Orthologous Groups

More...OrthoDBi		264244at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		O00429

TreeFam database of animal gene trees

More...TreeFami		TF352031

Family and domain databases

Conserved Domains Database

More...CDDi		cd08771 DLP_1, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.30.29.30, 1 hit

Integrated resource of protein families, domains and functional sites

More...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

More...PANTHERi		PTHR11566 PTHR11566, 1 hit
PTHR11566:SF39 PTHR11566:SF39, 1 hit

Pfam protein domain database

More...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

More...PRINTSi		PR00195 DYNAMIN

Simple Modular Architecture Research Tool; a protein domain database

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

Superfamily database of structural and functional annotation

More...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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (8+)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 8 <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 8 described isoforms and 10 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: O00429-1) [UniParc]FASTAAdd to basket
Also known as: HdynIV-WT, DLP1F

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
LPRGTGIVTR RPLILQLVHV SQEDKRKTTG EENGVEAEEW GKFLHTKNKL 
       110        120        130        140        150
YTDFDEIRQE IENETERISG NNKGVSPEPI HLKIFSPNVV NLTLVDLPGM 
       160        170        180        190        200
TKVPVGDQPK DIELQIRELI LRFISNPNSI ILAVTAANTD MATSEALKIS 
       210        220        230        240        250
REVDPDGRRT LAVITKLDLM DAGTDAMDVL MGRVIPVKLG IIGVVNRSQL 
       260        270        280        290        300
DINNKKSVTD SIRDEYAFLQ KKYPSLANRN GTKYLARTLN RLLMHHIRDC 
       310        320        330        340        350
LPELKTRINV LAAQYQSLLN SYGEPVDDKS ATLLQLITKF ATEYCNTIEG 
       360        370        380        390        400
TAKYIETSEL CGGARICYIF HETFGRTLES VDPLGGLNTI DILTAIRNAT 
       410        420        430        440        450
GPRPALFVPE VSFELLVKRQ IKRLEEPSLR CVELVHEEMQ RIIQHCSNYS 
       460        470        480        490        500
TQELLRFPKL HDAIVEVVTC LLRKRLPVTN EMVHNLVAIE LAYINTKHPD 
       510        520        530        540        550
FADACGLMNN NIEEQRRNRL ARELPSAVSR DKSSKVPSAL APASQEPSPA 
       560        570        580        590        600
ASAEADGKLI QDSRRETKNV ASGGGGVGDG VQEPTTGNWR GMLKTSKAEE 
       610        620        630        640        650
LLAEEKSKPI PIMPASPQKG HAVNLLDVPV PVARKLSARE QRDCEVIERL 
       660        670        680        690        700
IKSYFLIVRK NIQDSVPKAV MHFLVNHVKD TLQSELVGQL YKSSLLDDLL 
       710        720        730 
TESEDMAQRR KEAADMLKAL QGASQIIAEI RETHLW
Length:736
Mass (Da):81,877
Last modified:February 6, 2007 - 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:iF9521A376B785B71
GO
Isoform 4 (identifier: O00429-2) [UniParc]FASTAAdd to basket
Also known as: HdynIV-11, DLP1c

The sequence of this isoform differs from the canonical sequence as follows:
     559-569: Missing.

Show »
Length:725
Mass (Da):80,536
Checksum:i208E830E9F906B7F
GO
Isoform 2 (identifier: O00429-3) [UniParc]FASTAAdd to basket
Also known as: DLP1a

The sequence of this isoform differs from the canonical sequence as follows:
     533-558: Missing.

Show »
Length:710
Mass (Da):79,442
Checksum:i05BC4782DACC1C63
GO
Isoform 3 (identifier: O00429-4) [UniParc]FASTAAdd to basket
Also known as: HdynIV-37, DLP1b

The sequence of this isoform differs from the canonical sequence as follows:
     533-569: Missing.

Show »
Length:699
Mass (Da):78,100
Checksum:iCB252ECCC9871127
GO
Isoform 5 (identifier: O00429-5) [UniParc]FASTAAdd to basket
Also known as: HdynIV-26

The sequence of this isoform differs from the canonical sequence as follows:
     544-569: Missing.

Note: No experimental confirmation available.
Show »
Length:710
Mass (Da):79,109
Checksum:i0021B07297C5A6CC
GO
Isoform 6 (identifier: O00429-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     83-83: N → NDPATWKNSRHLSK

Show »
Length:749
Mass (Da):83,399
Checksum:i64E6658C90A577AA
GO
Isoform 7 (identifier: O00429-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-43: MEALIPVINK...QSSGKSSVLE → MFHKKINGKQ...NGVNFFTPKI
     44-246: Missing.

Note: No experimental confirmation available.
Show »
Length:533
Mass (Da):60,009
Checksum:i39FB7D0811EF0AF3
GO
Isoform 8 (identifier: O00429-8) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     83-83: N → NDPATWKNSRHLSK
     559-569: Missing.

Note: No experimental confirmation available.
Show »
Length:738
Mass (Da):82,057
Checksum:i04A6E66A8F236268
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 10 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G8JLD5G8JLD5_HUMAN
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>
B4DPZ9B4DPZ9_HUMAN
Dynamin-1-like protein
DNM1L
156Annotation 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>
B4DDQ3B4DDQ3_HUMAN
Dynamin-1-like protein
DNM1L
180Annotation 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>
F8VUJ9F8VUJ9_HUMAN
Dynamin-1-like protein
DNM1L
172Annotation 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>
F8VZ52F8VZ52_HUMAN
Dynamin-1-like protein
DNM1L
261Annotation 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>
F8W1W3F8W1W3_HUMAN
Dynamin-1-like protein
DNM1L
168Annotation 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>
F8VYL3F8VYL3_HUMAN
Dynamin-1-like protein
DNM1L
117Annotation 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>
F8VR28F8VR28_HUMAN
Dynamin-1-like protein
DNM1L
97Annotation 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>
H0YHY4H0YHY4_HUMAN
Dynamin-1-like protein
DNM1L
54Annotation 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>
H0YI79H0YI79_HUMAN
Dynamin-1-like protein
DNM1L
48Annotation 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>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence BAD92307 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

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 conflicti208R → C in AAC35283 (PubMed:9731200).Curated1
Sequence conflicti208R → C in AAD39541 (PubMed:10749171).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0808692E → A in OPA5; changed localization to mitochondrion; impaired mitochondrial membrane fission. 1 Publication1
Natural variantiVAR_08087036S → G in EMPF1; autosomal recessive; impaired mitochondrial membrane fission; hypomorphic mutation retaining partial activity in mitochondrial membrane fission. 1 PublicationCorresponds to variant dbSNP:rs879255688EnsemblClinVar.1
Natural variantiVAR_02244671S → T3 PublicationsCorresponds to variant dbSNP:rs1064610Ensembl.1
Natural variantiVAR_080871192A → E in OPA5; changed localization to mitochondrion; impaired mitochondrial membrane fission. 1 Publication1
Natural variantiVAR_076316362G → D in EMPF1; unknown pathological significance; unable to associate with MIEF2 into filaments forming the tubular structures that wrap around the scission site; presence of concentric cristae and/or increased dense granules in some mitochondria. 2 PublicationsCorresponds to variant dbSNP:rs879255685EnsemblClinVar.1
Natural variantiVAR_076317362G → S in EMPF1; the mutation acts in a dominant-negative manner; defects observed in mitochondrial fission; significant decrease in mitochondrial respiratory chain complex IV activity. 1 PublicationCorresponds to variant dbSNP:rs886037861EnsemblClinVar.1
Natural variantiVAR_063704395A → D in EMPF1; the mutation acts in a dominant-negative manner; defects observed in both mitochondrial and peroxisomal fission; reduced oligomerization, decreased mitochondrial recruitment. 2 PublicationsCorresponds to variant dbSNP:rs121908531EnsemblClinVar.1
Natural variantiVAR_076318403R → C in EMPF1; the mutation acts in a dominant-negative manner; reduced oligomerization; decreased mitochondrial recruitment; defects observed in mitochondrial fission. 1 PublicationCorresponds to variant dbSNP:rs863223953EnsemblClinVar.1
Natural variantiVAR_080872406L → S in EMPF1; impaired mitochondrial and peroxisomal membrane fission. 1 Publication1
Natural variantiVAR_030489426E → D. Corresponds to variant dbSNP:rs2389105Ensembl.1

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. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0545441 – 43MEALI…SSVLE → MFHKKINGKQQEKKMTLLHG KTQDTFLKGWKQKNGVNFFT PKI in isoform 7. 1 PublicationAdd BLAST43
Alternative sequenceiVSP_05454544 – 246Missing in isoform 7. 1 PublicationAdd BLAST203
Alternative sequenceiVSP_03909783N → NDPATWKNSRHLSK in isoform 6 and isoform 8. 2 Publications1
Alternative sequenceiVSP_013685533 – 569Missing in isoform 3. 3 PublicationsAdd BLAST37
Alternative sequenceiVSP_013686533 – 558Missing in isoform 2. 1 PublicationAdd BLAST26
Alternative sequenceiVSP_013687544 – 569Missing in isoform 5. 1 PublicationAdd BLAST26
Alternative sequenceiVSP_013688559 – 569Missing in isoform 4 and isoform 8. 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
AB006965 mRNA Translation: BAA22193.1
AF061795 mRNA Translation: AAC35283.1
AF000430 mRNA Translation: AAC23724.1
AF151685 mRNA Translation: AAD39541.1
AK299926 mRNA Translation: BAG61760.1
AK291094 mRNA Translation: BAF83783.1
AK294533 mRNA Translation: BAG57740.1
AB209070 mRNA Translation: BAD92307.1 Different initiation.
AC084824 Genomic DNA No translation available.
AC087588 Genomic DNA No translation available.
BC024590 mRNA Translation: AAH24590.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS61095.1 [O00429-6]
CCDS61096.1 [O00429-8]
CCDS61098.1 [O00429-2]
CCDS61099.1 [O00429-7]
CCDS8728.1 [O00429-4]
CCDS8729.1 [O00429-1]
CCDS8730.1 [O00429-3]

Protein sequence database of the Protein Information Resource

More...PIRi		JC5695

NCBI Reference Sequences

More...RefSeqi		NP_001265392.1, NM_001278463.1 [O00429-2]
NP_001265393.1, NM_001278464.1 [O00429-6]
NP_001265394.1, NM_001278465.1 [O00429-8]
NP_001265395.1, NM_001278466.1 [O00429-7]
NP_001317309.1, NM_001330380.1
NP_005681.2, NM_005690.4 [O00429-4]
NP_036192.2, NM_012062.4 [O00429-1]
NP_036193.2, NM_012063.3 [O00429-3]

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.556296

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000266481; ENSP00000266481; ENSG00000087470 [O00429-4]
ENST00000381000; ENSP00000370388; ENSG00000087470 [O00429-8]
ENST00000414834; ENSP00000404160; ENSG00000087470 [O00429-7]
ENST00000452533; ENSP00000415131; ENSG00000087470 [O00429-3]
ENST00000547312; ENSP00000448610; ENSG00000087470 [O00429-2]
ENST00000549701; ENSP00000450399; ENSG00000087470 [O00429-1]
ENST00000553257; ENSP00000449089; ENSG00000087470 [O00429-6]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		10059

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:10059

UCSC genome browser

More...UCSCi		uc001rld.4 human [O00429-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<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
AB006965 mRNA Translation: BAA22193.1
AF061795 mRNA Translation: AAC35283.1
AF000430 mRNA Translation: AAC23724.1
AF151685 mRNA Translation: AAD39541.1
AK299926 mRNA Translation: BAG61760.1
AK291094 mRNA Translation: BAF83783.1
AK294533 mRNA Translation: BAG57740.1
AB209070 mRNA Translation: BAD92307.1 Different initiation.
AC084824 Genomic DNA No translation available.
AC087588 Genomic DNA No translation available.
BC024590 mRNA Translation: AAH24590.1
CCDSiCCDS61095.1 [O00429-6]
CCDS61096.1 [O00429-8]
CCDS61098.1 [O00429-2]
CCDS61099.1 [O00429-7]
CCDS8728.1 [O00429-4]
CCDS8729.1 [O00429-1]
CCDS8730.1 [O00429-3]
PIRiJC5695
RefSeqiNP_001265392.1, NM_001278463.1 [O00429-2]
NP_001265393.1, NM_001278464.1 [O00429-6]
NP_001265394.1, NM_001278465.1 [O00429-8]
NP_001265395.1, NM_001278466.1 [O00429-7]
NP_001317309.1, NM_001330380.1
NP_005681.2, NM_005690.4 [O00429-4]
NP_036192.2, NM_012062.4 [O00429-1]
NP_036193.2, NM_012063.3 [O00429-3]
UniGeneiHs.556296

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3W6NX-ray2.00A/B1-329[»]
A/B709-736[»]
3W6OX-ray1.90A/B1-329[»]
A/B709-736[»]
3W6PX-ray1.70A/B1-329[»]
A/B709-736[»]
4BEJX-ray3.48A/B/C/D1-736[»]
4H1UX-ray2.30A1-327[»]
A711-736[»]
4H1VX-ray2.30A1-327[»]
A711-736[»]
5WP9electron microscopy4.22A/C/E/G/I/K/M/O1-736[»]
ProteinModelPortaliO00429
SMRiO00429
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115370, 206 interactors
CORUMiO00429
DIPiDIP-42704N
IntActiO00429, 177 interactors
MINTiO00429
STRINGi9606.ENSP00000450399

Protein family/group databases

TCDBi1.N.6.1.2 the mitochondrial inner/outer membrane fusion (mmf) family

PTM databases

iPTMnetiO00429
PhosphoSitePlusiO00429
SwissPalmiO00429

Polymorphism and mutation databases

BioMutaiDNM1L

Proteomic databases

EPDiO00429
jPOSTiO00429
MaxQBiO00429
PaxDbiO00429
PeptideAtlasiO00429
PRIDEiO00429
ProteomicsDBi47884
47885 [O00429-2]
47886 [O00429-3]
47887 [O00429-4]
47888 [O00429-5]
47889 [O00429-6]

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		10059
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000266481; ENSP00000266481; ENSG00000087470 [O00429-4]
ENST00000381000; ENSP00000370388; ENSG00000087470 [O00429-8]
ENST00000414834; ENSP00000404160; ENSG00000087470 [O00429-7]
ENST00000452533; ENSP00000415131; ENSG00000087470 [O00429-3]
ENST00000547312; ENSP00000448610; ENSG00000087470 [O00429-2]
ENST00000549701; ENSP00000450399; ENSG00000087470 [O00429-1]
ENST00000553257; ENSP00000449089; ENSG00000087470 [O00429-6]
GeneIDi10059
KEGGihsa:10059
UCSCiuc001rld.4 human [O00429-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		10059
DisGeNETi10059
EuPathDBiHostDB:ENSG00000087470.17

GeneCards: human genes, protein and diseases

More...GeneCardsi		DNM1L

H-Invitational Database, human transcriptome db

More...H-InvDBi		HIX0010537
HGNCiHGNC:2973 DNM1L
HPAiCAB009952
HPA039324
MalaCardsiDNM1L
MIMi603850 gene
610708 phenotype
614388 phenotype
neXtProtiNX_O00429
OpenTargetsiENSG00000087470
Orphaneti98673 Autosomal dominant optic atrophy, classic form
330050 Lethal encephalopathy due to mitochondrial and peroxisomal fission defect
PharmGKBiPA27441

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0446 Eukaryota
COG0699 LUCA
GeneTreeiENSGT00940000155504
HOGENOMiHOG000161068
HOVERGENiHBG107833
InParanoidiO00429
KOiK17065
OMAiNIMATQF
OrthoDBi264244at2759
PhylomeDBiO00429
TreeFamiTF352031

Enzyme and pathway databases

ReactomeiR-HSA-75153 Apoptotic execution phase
SIGNORiO00429

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		DNM1L human

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		DNM1L

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		10059
PMAP-CutDBiO00429

Protein Ontology

More...PROi		PR:O00429

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000087470 Expressed in 237 organ(s), highest expression level in intestine
CleanExiHS_DNM1L
ExpressionAtlasiO00429 baseline and differential
GenevisibleiO00429 HS

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_HUMAN
<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: O00429
Secondary accession number(s): A8K4X9
, B4DGC9, B4DSU8, J3KPI2, O14541, O60709, Q59GN9, Q7L6B3, Q8TBT7, Q9BWM1, Q9Y5J2
<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: February 6, 2007
Last modified: January 16, 2019
This is version 174 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
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<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

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
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