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Protein

Dynamin-1-like protein

Gene

DNM1L

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. 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). 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.20 Publications
Isoform 1: Inhibits peroxisomal division when overexpressed.1 Publication
Isoform 4: Inhibits peroxisomal division when overexpressed.1 Publication

Catalytic activityi

GTP + H2O = GDP + phosphate.2 Publications

Enzyme regulationi

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

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi32 – 40GTP1 Publication9
Nucleotide bindingi215 – 221GTP1 Publication7
Nucleotide bindingi246 – 249GTP1 Publication4

GO - Molecular functioni

  • 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 homodimerization activity Source: UniProtKB
  • Rab GTPase binding Source: ParkinsonsUK-UCL
  • ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  • cellular component disassembly involved in execution phase of apoptosis Source: Reactome
  • dynamin family protein polymerization involved in mitochondrial fission Source: UniProtKB
  • endocytosis Source: UniProtKB-KW
  • heart contraction Source: Ensembl
  • intracellular distribution of mitochondria Source: ParkinsonsUK-UCL
  • membrane fusion Source: UniProtKB
  • mitochondrial fission Source: UniProtKB
  • mitochondrial fragmentation involved in apoptotic process Source: UniProtKB
  • mitochondrial membrane fission Source: UniProtKB
  • mitochondrion morphogenesis Source: MGI
  • mitochondrion organization Source: ParkinsonsUK-UCL
  • necroptotic process Source: UniProtKB
  • peroxisome fission Source: UniProtKB
  • positive regulation of apoptotic process Source: UniProtKB
  • positive regulation of intrinsic apoptotic signaling pathway Source: UniProtKB
  • positive regulation of mitochondrial fission Source: ParkinsonsUK-UCL
  • positive regulation of protein secretion Source: UniProtKB
  • positive regulation of release of cytochrome c from mitochondria Source: UniProtKB
  • protein homotetramerization Source: UniProtKB
  • protein localization to mitochondrion Source: Ensembl
  • protein oligomerization Source: UniProtKB
  • regulation of ATP metabolic process Source: Ensembl
  • regulation of mitochondrion organization Source: UniProtKB
  • regulation of mitophagy Source: ParkinsonsUK-UCL
  • regulation of peroxisome organization Source: UniProtKB
  • regulation of protein oligomerization Source: UniProtKB
  • release of cytochrome c from mitochondria Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Endocytosis, Necrosis

Keywords - Ligandi

GTP-binding, Lipid-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS01578-MONOMER.
ReactomeiR-HSA-75153. Apoptotic execution phase.
SIGNORiO00429.

Names & Taxonomyi

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
Gene namesi
Name:DNM1L
Synonyms:DLP1, DRP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:2973. DNM1L.

Subcellular locationi

GO - Cellular componenti

  • brush border Source: Ensembl
  • cell junction Source: UniProtKB-KW
  • clathrin-coated pit Source: UniProtKB-SubCell
  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • endoplasmic reticulum Source: ParkinsonsUK-UCL
  • endoplasmic reticulum membrane Source: ParkinsonsUK-UCL
  • Golgi apparatus Source: UniProtKB
  • intracellular membrane-bounded organelle Source: HPA
  • membrane Source: UniProtKB
  • microtubule Source: UniProtKB
  • microtubule cytoskeleton Source: Ensembl
  • mitochondrial outer membrane Source: UniProtKB
  • mitochondrion Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB
  • peroxisome Source: UniProtKB
  • protein complex Source: UniProtKB
  • synaptic vesicle membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Involvement in diseasei

May be associated with Alzheimer disease through beta-amyloid-induced increased S-nitrosylation of DNM1L, which triggers, directly or indirectly, excessive mitochondrial fission, synaptic loss and neuronal damage.

Encephalopathy due to defective mitochondrial and peroxisomal fission 1 (EMPF1)4 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
Natural variantiVAR_076316362G → D in EMPF1; unknown pathological significance; presence of concentric cristae and/or increased dense granules in some mitochondria. 1 Publication1
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 Publication1
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 rs121908531dbSNPEnsembl.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 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
Mutagenesisi216K → A: Abolishes GTP hydrolysis. 1 Publication1
Mutagenesisi218D → A: Abolishes GTP hydrolysis. 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, but not intermolecular interactions. Slight reduction in GTPase activity. Does not reduce interaction with MIEF1 and MIEF2. Inhibits mitochondrial fission. Retained in cytoplasm. 4 Publications1
Mutagenesisi644C → A: Abolishes S-nitrosylation. Reduced dimerization and no enhancement of GTPase activity. 1 Publication1
Mutagenesisi668K → A: Abolishes homodimerization and formation of higher order oligomers. 1 Publication1
Mutagenesisi679K → A: Diminishes intermolecular interaction between GTP-middle domain and GED domain but no effect on oligomerization. Marked reduction in GTPase activity, in vitro. Decreased mitochondrial division. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi10059.
MalaCardsiDNM1L.
MIMi614388. phenotype.
OpenTargetsiENSG00000087470.
Orphaneti330050. Lethal encephalopathy due to mitochondrial and peroxisomal fission defect.
PharmGKBiPA27441.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002065661 – 736Dynamin-1-like proteinAdd BLAST736

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei529PhosphoserineCombined sources1
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
Glycosylationi585O-linked (GlcNAc)By similarity1
Glycosylationi586O-linked (GlcNAc)By 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

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

EPDiO00429.
MaxQBiO00429.
PaxDbiO00429.
PeptideAtlasiO00429.
PRIDEiO00429.

PTM databases

iPTMnetiO00429.
PhosphoSitePlusiO00429.
SwissPalmiO00429.

Miscellaneous databases

PMAP-CutDBO00429.

Expressioni

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

BgeeiENSG00000087470.
CleanExiHS_DNM1L.
ExpressionAtlasiO00429. baseline and differential.
GenevisibleiO00429. HS.

Organism-specific databases

HPAiCAB009952.
HPA039324.

Interactioni

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. Can also oligomerize to form multimeric ring-like structures. 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; 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

Binary interactionsi

WithEntry#Exp.IntActNotes
ESR1P033722EBI-724571,EBI-78473
LRRK2Q5S00711EBI-724571,EBI-5323863
MIEF1Q9NQG69EBI-724571,EBI-740987
MIEF2Q96C033EBI-724571,EBI-750153
SAMM50Q9Y5123EBI-724571,EBI-748409

GO - Molecular functioni

  • GTP-dependent protein binding Source: ParkinsonsUK-UCL
  • identical protein binding Source: IntAct
  • microtubule binding Source: GO_Central
  • protein homodimerization activity Source: UniProtKB
  • Rab GTPase binding Source: ParkinsonsUK-UCL
  • ubiquitin protein ligase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi115370. 60 interactors.
DIPiDIP-42704N.
IntActiO00429. 21 interactors.
MINTiMINT-1394198.
STRINGi9606.ENSP00000450399.

Structurei

Secondary structure

1736
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 18Combined sources14
Turni21 – 23Combined sources3
Beta strandi27 – 31Combined sources5
Helixi34 – 36Combined sources3
Helixi38 – 44Combined sources7
Beta strandi55 – 57Combined sources3
Beta strandi63 – 69Combined sources7
Beta strandi86 – 88Combined sources3
Beta strandi90 – 93Combined sources4
Helixi94 – 96Combined sources3
Helixi104 – 119Combined sources16
Beta strandi121 – 123Combined sources3
Beta strandi130 – 136Combined sources7
Beta strandi141 – 146Combined sources6
Helixi155 – 157Combined sources3
Helixi162 – 174Combined sources13
Beta strandi179 – 186Combined sources8
Helixi191 – 193Combined sources3
Helixi195 – 203Combined sources9
Beta strandi205 – 207Combined sources3
Beta strandi210 – 215Combined sources6
Helixi217 – 219Combined sources3
Beta strandi222 – 225Combined sources4
Helixi227 – 230Combined sources4
Beta strandi233 – 235Combined sources3
Beta strandi237 – 239Combined sources3
Beta strandi241 – 243Combined sources3
Helixi249 – 253Combined sources5
Helixi258 – 272Combined sources15
Turni274 – 276Combined sources3
Helixi277 – 279Combined sources3
Helixi282 – 317Combined sources36
Helixi329 – 349Combined sources21
Helixi363 – 371Combined sources9
Helixi373 – 380Combined sources8
Helixi389 – 399Combined sources11
Helixi409 – 420Combined sources12
Helixi421 – 424Combined sources4
Helixi425 – 440Combined sources16
Turni441 – 443Combined sources3
Helixi444 – 446Combined sources3
Helixi458 – 493Combined sources36
Helixi501 – 504Combined sources4
Helixi632 – 662Combined sources31
Helixi664 – 679Combined sources16
Helixi682 – 688Combined sources7
Helixi696 – 699Combined sources4
Helixi710 – 731Combined sources22

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[»]
ProteinModelPortaliO00429.
SMRiO00429.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini22 – 302Dynamin-type GAdd BLAST281
Domaini644 – 735GEDPROSITE-ProRule annotationAdd BLAST92

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 343GTPase domainAdd BLAST343
Regioni344 – 489Middle domainAdd BLAST146
Regioni448 – 685Interaction with GSK3BAdd BLAST238
Regioni502 – 569B domainAdd BLAST68
Regioni654 – 668Important for homodimerizationAdd BLAST15

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.

Sequence similaritiesi

Contains 1 GED domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0446. Eukaryota.
COG0699. LUCA.
GeneTreeiENSGT00760000119213.
HOGENOMiHOG000161068.
HOVERGENiHBG107833.
InParanoidiO00429.
KOiK17065.
OMAiGQEPTTG.
OrthoDBiEOG091G02TQ.
PhylomeDBiO00429.
TreeFamiTF352031.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR030556. 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.
[Graphical view]
PANTHERiPTHR11566. PTHR11566. 1 hit.
PTHR11566:SF39. PTHR11566:SF39. 1 hit.
PfamiPF01031. Dynamin_M. 1 hit.
PF00350. Dynamin_N. 1 hit.
PF02212. GED. 1 hit.
[Graphical view]
PRINTSiPR00195. DYNAMIN.
SMARTiSM00053. DYNc. 1 hit.
SM00302. GED. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00410. G_DYNAMIN_1. 1 hit.
PS51718. G_DYNAMIN_2. 1 hit.
PS51388. GED. 1 hit.
[Graphical view]

Sequences (8)i

Sequence statusi: Complete.

This entry describes 8 isoformsi produced by alternative splicing. AlignAdd to basket

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
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.
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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

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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_02244671S → T.3 PublicationsCorresponds to variant rs1064610dbSNPEnsembl.1
Natural variantiVAR_076316362G → D in EMPF1; unknown pathological significance; presence of concentric cristae and/or increased dense granules in some mitochondria. 1 Publication1
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 Publication1
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 rs121908531dbSNPEnsembl.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 Publication1
Natural variantiVAR_030489426E → D.Corresponds to variant rs2389105dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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:
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.

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]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

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[»]
ProteinModelPortaliO00429.
SMRiO00429.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115370. 60 interactors.
DIPiDIP-42704N.
IntActiO00429. 21 interactors.
MINTiMINT-1394198.
STRINGi9606.ENSP00000450399.

PTM databases

iPTMnetiO00429.
PhosphoSitePlusiO00429.
SwissPalmiO00429.

Proteomic databases

EPDiO00429.
MaxQBiO00429.
PaxDbiO00429.
PeptideAtlasiO00429.
PRIDEiO00429.

Protocols and materials databases

DNASUi10059.
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

CTDi10059.
DisGeNETi10059.
GeneCardsiDNM1L.
H-InvDBHIX0010537.
HGNCiHGNC:2973. DNM1L.
HPAiCAB009952.
HPA039324.
MalaCardsiDNM1L.
MIMi603850. gene.
614388. phenotype.
neXtProtiNX_O00429.
OpenTargetsiENSG00000087470.
Orphaneti330050. Lethal encephalopathy due to mitochondrial and peroxisomal fission defect.
PharmGKBiPA27441.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0446. Eukaryota.
COG0699. LUCA.
GeneTreeiENSGT00760000119213.
HOGENOMiHOG000161068.
HOVERGENiHBG107833.
InParanoidiO00429.
KOiK17065.
OMAiGQEPTTG.
OrthoDBiEOG091G02TQ.
PhylomeDBiO00429.
TreeFamiTF352031.

Enzyme and pathway databases

BioCyciZFISH:HS01578-MONOMER.
ReactomeiR-HSA-75153. Apoptotic execution phase.
SIGNORiO00429.

Miscellaneous databases

ChiTaRSiDNM1L. human.
GeneWikiiDNM1L.
GenomeRNAii10059.
PMAP-CutDBO00429.
PROiO00429.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000087470.
CleanExiHS_DNM1L.
ExpressionAtlasiO00429. baseline and differential.
GenevisibleiO00429. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR030556. 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.
[Graphical view]
PANTHERiPTHR11566. PTHR11566. 1 hit.
PTHR11566:SF39. PTHR11566:SF39. 1 hit.
PfamiPF01031. Dynamin_M. 1 hit.
PF00350. Dynamin_N. 1 hit.
PF02212. GED. 1 hit.
[Graphical view]
PRINTSiPR00195. DYNAMIN.
SMARTiSM00053. DYNc. 1 hit.
SM00302. GED. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00410. G_DYNAMIN_1. 1 hit.
PS51718. G_DYNAMIN_2. 1 hit.
PS51388. GED. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDNM1L_HUMAN
AccessioniPrimary (citable) accession number: O00429
Secondary accession number(s): A8K4X9
, B4DGC9, B4DSU8, J3KPI2, O14541, O60709, Q59GN9, Q7L6B3, Q8TBT7, Q9BWM1, Q9Y5J2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: February 6, 2007
Last modified: November 30, 2016
This is version 152 of the entry and version 2 of the sequence. [Complete history]
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.