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Entry version 120 (07 Apr 2021)
Sequence version 1 (07 Mar 2006)
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Protein

Dynamin-1-like protein

Gene

DNM1L

Organism
Bos taurus (Bovine)
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 transcript 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. Acts downstream of PINK1 to promote mitochondrial fission in a PRKN-dependent manner. Plays an important role in mitochondrial fission during mitosis (By similarity). Through its function in mitochondrial division, ensures the survival of at least some types of postmitotic neurons, including Purkinje cells, by suppressing oxidative damage (By similarity). Required for normal brain development, including that of cerebellum (By similarity). 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 (By similarity). 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-650 is essential for the circadian control of mitochondrial ATP production (By similarity).By similarity

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

Regions

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

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

GO - Biological processi

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

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

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

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Dynamin-1-like protein (EC:3.6.5.5)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:DNM1L
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiBos taurus (Bovine)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9913 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaArtiodactylaRuminantiaPecoraBovidaeBovinaeBos
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000009136 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 5

Organism-specific databases

Vertebrate Gene Nomenclature Database

More...
VGNCi
VGNC:28142, 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

Keywords - Cellular componenti

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

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002849721 – 749Dynamin-1-like proteinAdd BLAST749

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1N-acetylmethionineBy similarity1
Modified residuei542PhosphoserineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki545Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Cross-linki548Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei561PhosphoserineBy similarity1
Cross-linki571Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Cross-linki581Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi598O-linked (GlcNAc) threonineBy similarity1
Glycosylationi599O-linked (GlcNAc) threonineBy similarity1
Cross-linki607Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei610N6-acetyllysine; alternateBy similarity1
Cross-linki610Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki619Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei620PhosphoserineBy similarity1
Cross-linki621Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei629Phosphoserine; by CDK1 and PINK1By similarity1
Modified residuei650Phosphoserine; by CAMK1 and PKABy similarity1
Modified residuei657S-nitrosocysteineBy similarity1

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

Phosphorylation/dephosphorylation events on two sites near the GED domain regulate mitochondrial fission. Phosphorylation on Ser-650 by CAMK1 and PKA 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-629 by CDK1 and PINK1 activates the GTPase activity and promotes mitochondrial fission. Phosphorylated in a circadian manner at Ser-650.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-650 (By similarity).By similarity

Keywords - PTMi

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

Proteomic databases

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

More...
PaxDbi
Q2KIA5

PeptideAtlas

More...
PeptideAtlasi
Q2KIA5

PRoteomics IDEntifications database

More...
PRIDEi
Q2KIA5

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSBTAG00000011395, Expressed in brain and 19 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q2KIA5, baseline and differential

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

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

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

Interacts with GSK3B and MARCHF5.

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 MFF; the interaction is inhinited by C11orf65/MFI.

Interacts with FIS1.

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

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

By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
9913.ENSBTAP00000037777

<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

More...
SMRi
Q2KIA5

Database of comparative protein structure models

More...
ModBasei
Search...

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini22 – 315Dynamin-type GPROSITE-ProRule annotationAdd BLAST294
Domaini657 – 748GEDPROSITE-ProRule annotationAdd BLAST92

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni32 – 39G1 motifPROSITE-ProRule annotation8
Regioni58 – 60G2 motifPROSITE-ProRule annotation3
Regioni159 – 162G3 motifPROSITE-ProRule annotation4
Regioni228 – 231G4 motifPROSITE-ProRule annotation4
Regioni258 – 261G5 motifPROSITE-ProRule annotation4
Regioni357 – 502Middle domainBy similarityAdd BLAST146
Regioni461 – 698Interaction with GSK3BBy similarityAdd BLAST238
Regioni515 – 582B domainBy similarityAdd BLAST68
Regioni667 – 681Important for homodimerizationBy similarityAdd BLAST15

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

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

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

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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0446, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000155504

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_008964_5_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q2KIA5

Identification of Orthologs from Complete Genome Data

More...
OMAi
KTRVNIM

Database of Orthologous Groups

More...
OrthoDBi
264244at2759

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
IPR001401, Dynamin_GTPase
IPR019762, Dynamin_GTPase_CS
IPR022812, Dynamin_SF
IPR000375, Dynamin_stalk
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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

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

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

Q2KIA5-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEALIPVINK LQDVFNTVGA DIIQLPQIVV VGTQSSGKSS VLESLVGRDL
60 70 80 90 100
LPRGTGIVTR RPLILQLVHV APEDKRKTTG EENDPATWKN SRHLSKGVEA
110 120 130 140 150
EEWGKFLHTK NKLYTDFDEI RQEIENETER ISGNNKGVSP EPIHLKIFSP
160 170 180 190 200
NVVNLTLVDL PGMTKVPVGD QPKDIELQIR ELILRFISNP NSIILAVTAA
210 220 230 240 250
NTDMATSEAL KISREVDPDG RRTLAVITKL DLMDAGTDAM DVLMGRVIPV
260 270 280 290 300
KLGIIGVVNR SQLDINNKKS VTDSIRDEYA FLQKKYPSLA NRNGTKYLAR
310 320 330 340 350
TLNRLLMHHI RDCLPELKTR INVLAAQYQS LLNSYGEPVD DKSATLLQLI
360 370 380 390 400
TKFATEYCNT IEGTAKYIET SELCGGARIC YIFHETFGRT LESVDPLGGL
410 420 430 440 450
NTIDILTAIR NATGPRPALF VPEVSFELLV KRQIKRLEEP SLRCVELVHE
460 470 480 490 500
EMQRIIQHCS NYSTQELLRF PKLHDAIVEV VTCLLRKRLP VTNEMVHNLV
510 520 530 540 550
AIELAYINTK HPDFADACGL MNNNIEEQRR NRLARELPSA VSRDKSSKVP
560 570 580 590 600
SALAPASQEP SPAASAEADG KLIQESRRET KNAASGGGGV GDAVQEPTTG
610 620 630 640 650
NWRGMLKTSK AEELLAEEKS KPIPIMPASP QKGHAVNLLD VPVPVARKLS
660 670 680 690 700
AREQRDCEVI ERLIKSYFLI VRKNIQDSVP KAVMHFLVNH VKDTLQSELV
710 720 730 740
GQLYKSSLLD DLLTESEDMA QRRKEAADML KALQGASQII AEIRETHLW
Length:749
Mass (Da):83,352
Last modified:March 7, 2006 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iBA90863E8BC8265B
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A3Q1M7W9A0A3Q1M7W9_BOVIN
Dynamin-1-like protein
DNM1L
709Annotation score:

Annotation score:3 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>

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
BC112710 mRNA Translation: AAI12711.1

NCBI Reference Sequences

More...
RefSeqi
NP_001039959.1, NM_001046494.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSBTAT00000037956; ENSBTAP00000037777; ENSBTAG00000011395

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
540892

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
bta:540892

<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
BC112710 mRNA Translation: AAI12711.1
RefSeqiNP_001039959.1, NM_001046494.2

3D structure databases

SMRiQ2KIA5
ModBaseiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000037777

Proteomic databases

PaxDbiQ2KIA5
PeptideAtlasiQ2KIA5
PRIDEiQ2KIA5

Genome annotation databases

EnsembliENSBTAT00000037956; ENSBTAP00000037777; ENSBTAG00000011395
GeneIDi540892
KEGGibta:540892

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
10059
VGNCiVGNC:28142, DNM1L

Phylogenomic databases

eggNOGiKOG0446, Eukaryota
GeneTreeiENSGT00940000155504
HOGENOMiCLU_008964_5_0_1
InParanoidiQ2KIA5
OMAiKTRVNIM
OrthoDBi264244at2759
TreeFamiTF352031

Gene expression databases

BgeeiENSBTAG00000011395, Expressed in brain and 19 other tissues
ExpressionAtlasiQ2KIA5, baseline and differential

Family and domain databases

CDDicd08771, DLP_1, 1 hit
Gene3Di2.30.29.30, 1 hit
InterProiView protein in InterPro
IPR030556, DNM1L
IPR001401, Dynamin_GTPase
IPR019762, Dynamin_GTPase_CS
IPR022812, Dynamin_SF
IPR000375, Dynamin_stalk
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

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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_BOVIN
<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: Q2KIA5
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: March 7, 2006
Last modified: April 7, 2021
This is version 120 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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

Keywords - Technical termi

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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