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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.2 Publications
Isoform 1 and isoform 4 inhibit peroxisomal division when overexpressed.

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)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi32 – 409GTP1 Publication
Nucleotide bindingi215 – 2217GTP1 Publication
Nucleotide bindingi246 – 2494GTP1 Publication

GO - Molecular functioni

  • GTPase activity Source: UniProtKB
  • GTP binding Source: UniProtKB-KW
  • identical protein binding Source: IntAct
  • lipid binding Source: UniProtKB-KW
  • protein homodimerization activity Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  • cellular component disassembly involved in execution phase of apoptosis Source: Reactome
  • dynamin polymerization involved in mitochondrial fission Source: UniProtKB
  • endocytosis Source: UniProtKB-KW
  • heart contraction Source: Ensembl
  • 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
  • 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
  • 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

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
  • 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, lethal, due to defective mitochondrial and peroxisomal fission (EMPF)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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti362 – 3621G → D in EMPF; unknown pathological significance; presence of concentric cristae and/or increased dense granules in some mitochondria. 1 Publication
VAR_076316
Natural varianti362 – 3621G → S in EMPF; the mutation acts in a dominant-negative manner; defects observed in mitochondrial fission; significant decrease in mitochondrial respiratory chain complex IV activity. 1 Publication
VAR_076317
Natural varianti395 – 3951A → D in EMPF; the mutation acts in a dominant-negative manner; defects observed in both mitochondrial and peroxisomal fission; reduced oligomerization, decreased mitochondrial recruitment. 2 Publications
Corresponds to variant rs121908531 [ dbSNP | Ensembl ].
VAR_063704
Natural varianti403 – 4031R → C in EMPF; the mutation acts in a dominant-negative manner; reduced oligomerization; decreased mitochondrial recruitment; defects observed in mitochondrial fission. 1 Publication
VAR_076318

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi34 – 341Q → A: Abolishes GTP hydrolysis. 1 Publication
Mutagenesisi38 – 381K → A: Loss of GTPase activity. Impairs mitochondrial division and induces changes in peroxisome morphology. No effect on oligomerization. Increase in sumoylation by SUMO3. 6 Publications
Mutagenesisi38 – 381K → E: Overexpression delays protein secretion. 6 Publications
Mutagenesisi39 – 391S → A: Abolishes GTP hydrolysis. 3 Publications
Mutagenesisi39 – 391S → I: Decreased localization to the perinuclear region. 3 Publications
Mutagenesisi39 – 391S → N: Reduces peroxisomal abundance. 3 Publications
Mutagenesisi41 – 411V → F: Temperature-sensitive. Impairs mitochondrial division. 1 Publication
Mutagenesisi59 – 591T → A: Abolishes GTP hydrolysis. Impairs mitochondrial division. Reduces peroxisomal abundance. 3 Publications
Mutagenesisi146 – 1461D → A: Abolishes GTP hydrolysis. 1 Publication
Mutagenesisi149 – 1491G → A: Abolishes GTP hydrolysis. 1 Publication
Mutagenesisi216 – 2161K → A: Abolishes GTP hydrolysis. 1 Publication
Mutagenesisi218 – 2181D → A: Abolishes GTP hydrolysis. 1 Publication
Mutagenesisi281 – 2811G → D: Temperature-sensitive. Impairs mitochondrial division. 1 Publication
Mutagenesisi300 – 3001C → A: No effect on S-nitrosylation. 1 Publication
Mutagenesisi345 – 3451C → A: No effect on S-nitrosylation. 1 Publication
Mutagenesisi361 – 3611C → A: No effect on S-nitrosylation. 1 Publication
Mutagenesisi367 – 3671C → A: No effect on S-nitrosylation. 1 Publication
Mutagenesisi401 – 4044GPRP → AAAA: Impairs formation of higher order oligomers, but not homodimerization. 1 Publication
Mutagenesisi431 – 4311C → A: No effect on S-nitrosylation. 1 Publication
Mutagenesisi446 – 4461C → A: No effect on S-nitrosylation. 1 Publication
Mutagenesisi470 – 4701C → A: No effect on S-nitrosylation. 1 Publication
Mutagenesisi490 – 4901E → A: Does not impair homodimerization and formation of higher order oligomers. 1 Publication
Mutagenesisi490 – 4901E → R: Impairs homodimerization and formation of higher order oligomers. 1 Publication
Mutagenesisi505 – 5051C → A: No effect on S-nitrosylation. 1 Publication
Mutagenesisi532 – 5321K → 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 Publication
Mutagenesisi535 – 5351K → 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 Publication
Mutagenesisi558 – 5581K → 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 Publication
Mutagenesisi568 – 5681K → 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 Publication
Mutagenesisi594 – 5941K → 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 Publication
Mutagenesisi597 – 5971K → 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 Publication
Mutagenesisi606 – 6061K → 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 Publication
Mutagenesisi608 – 6081K → 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 Publication
Mutagenesisi616 – 6161S → A: Little effect on mitochondrial morphology. Translocated to mitochondria. 1 Publication
Mutagenesisi637 – 6371S → 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 Publications
Mutagenesisi637 – 6371S → 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 Publications
Mutagenesisi644 – 6441C → A: Abolishes S-nitrosylation. Reduced dimerization and no enhancement of GTPase activity. 1 Publication
Mutagenesisi668 – 6681K → A: Abolishes homodimerization and formation of higher order oligomers. 1 Publication
Mutagenesisi679 – 6791K → 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 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 736736Dynamin-1-like proteinPRO_0000206566Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei529 – 5291PhosphoserineCombined sources
Cross-linki532 – 532Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Cross-linki535 – 535Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residuei548 – 5481PhosphoserineCombined sources
Cross-linki558 – 558Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Cross-linki568 – 568Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Glycosylationi585 – 5851O-linked (GlcNAc)By similarity
Glycosylationi586 – 5861O-linked (GlcNAc)By similarity
Cross-linki594 – 594Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)Curated
Modified residuei597 – 5971N6-acetyllysine; alternateBy similarity
Cross-linki597 – 597Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Cross-linki606 – 606Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)Curated
Modified residuei607 – 6071PhosphoserineCombined sources
Cross-linki608 – 608Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residuei616 – 6161Phosphoserine; by CDK1Combined sources2 Publications
Modified residuei637 – 6371Phosphoserine; by CAMK1 and PKA5 Publications
Modified residuei644 – 6441S-nitrosocysteine1 Publication

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.
PhosphoSiteiO00429.
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

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein homodimerization activity Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi115370. 60 interactions.
DIPiDIP-42704N.
IntActiO00429. 19 interactions.
MINTiMINT-1394198.
STRINGi9606.ENSP00000450399.

Structurei

Secondary structure

1
736
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 1814Combined sources
Turni21 – 233Combined sources
Beta strandi27 – 315Combined sources
Helixi34 – 363Combined sources
Helixi38 – 447Combined sources
Beta strandi55 – 573Combined sources
Beta strandi63 – 697Combined sources
Beta strandi86 – 883Combined sources
Beta strandi90 – 934Combined sources
Helixi94 – 963Combined sources
Helixi104 – 11916Combined sources
Beta strandi121 – 1233Combined sources
Beta strandi130 – 1367Combined sources
Beta strandi141 – 1466Combined sources
Helixi155 – 1573Combined sources
Helixi162 – 17413Combined sources
Beta strandi179 – 1868Combined sources
Helixi191 – 1933Combined sources
Helixi195 – 2039Combined sources
Beta strandi205 – 2073Combined sources
Beta strandi210 – 2156Combined sources
Helixi217 – 2193Combined sources
Beta strandi222 – 2254Combined sources
Helixi227 – 2304Combined sources
Beta strandi233 – 2353Combined sources
Beta strandi237 – 2393Combined sources
Beta strandi241 – 2433Combined sources
Helixi249 – 2535Combined sources
Helixi258 – 27215Combined sources
Turni274 – 2763Combined sources
Helixi277 – 2793Combined sources
Helixi282 – 31736Combined sources
Helixi329 – 34921Combined sources
Helixi363 – 3719Combined sources
Helixi373 – 3808Combined sources
Helixi389 – 39911Combined sources
Helixi409 – 42012Combined sources
Helixi421 – 4244Combined sources
Helixi425 – 44016Combined sources
Turni441 – 4433Combined sources
Helixi444 – 4463Combined sources
Helixi458 – 49336Combined sources
Helixi501 – 5044Combined sources
Helixi632 – 66231Combined sources
Helixi664 – 67916Combined sources
Helixi682 – 6887Combined sources
Helixi710 – 73122Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-730.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 302281Dynamin-type GAdd
BLAST
Domaini644 – 73592GEDPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 343343GTPase domainAdd
BLAST
Regioni344 – 489146Middle domainAdd
BLAST
Regioni448 – 685238Interaction with GSK3BAdd
BLAST
Regioni502 – 56968B domainAdd
BLAST
Regioni654 – 66815Important for homodimerizationAdd
BLAST

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.
GeneTreeiENSGT00840000129895.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti208 – 2081R → C in AAC35283 (PubMed:9731200).Curated
Sequence conflicti208 – 2081R → C in AAD39541 (PubMed:10749171).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti71 – 711S → T.3 Publications
Corresponds to variant rs1064610 [ dbSNP | Ensembl ].
VAR_022446
Natural varianti362 – 3621G → D in EMPF; unknown pathological significance; presence of concentric cristae and/or increased dense granules in some mitochondria. 1 Publication
VAR_076316
Natural varianti362 – 3621G → S in EMPF; the mutation acts in a dominant-negative manner; defects observed in mitochondrial fission; significant decrease in mitochondrial respiratory chain complex IV activity. 1 Publication
VAR_076317
Natural varianti395 – 3951A → D in EMPF; the mutation acts in a dominant-negative manner; defects observed in both mitochondrial and peroxisomal fission; reduced oligomerization, decreased mitochondrial recruitment. 2 Publications
Corresponds to variant rs121908531 [ dbSNP | Ensembl ].
VAR_063704
Natural varianti403 – 4031R → C in EMPF; the mutation acts in a dominant-negative manner; reduced oligomerization; decreased mitochondrial recruitment; defects observed in mitochondrial fission. 1 Publication
VAR_076318
Natural varianti426 – 4261E → D.
Corresponds to variant rs2389105 [ dbSNP | Ensembl ].
VAR_030489

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4343MEALI…SSVLE → MFHKKINGKQQEKKMTLLHG KTQDTFLKGWKQKNGVNFFT PKI in isoform 7. 1 PublicationVSP_054544Add
BLAST
Alternative sequencei44 – 246203Missing in isoform 7. 1 PublicationVSP_054545Add
BLAST
Alternative sequencei83 – 831N → NDPATWKNSRHLSK in isoform 6 and isoform 8. 2 PublicationsVSP_039097
Alternative sequencei533 – 56937Missing in isoform 3. 3 PublicationsVSP_013685Add
BLAST
Alternative sequencei533 – 55826Missing in isoform 2. 1 PublicationVSP_013686Add
BLAST
Alternative sequencei544 – 56926Missing in isoform 5. 1 PublicationVSP_013687Add
BLAST
Alternative sequencei559 – 56911Missing in isoform 4 and isoform 8. 2 PublicationsVSP_013688Add
BLAST

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_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_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
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. Positions 1-730.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115370. 60 interactions.
DIPiDIP-42704N.
IntActiO00429. 19 interactions.
MINTiMINT-1394198.
STRINGi9606.ENSP00000450399.

PTM databases

iPTMnetiO00429.
PhosphoSiteiO00429.
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.
GeneCardsiDNM1L.
H-InvDBHIX0010537.
HGNCiHGNC:2973. DNM1L.
HPAiCAB009952.
HPA039324.
MalaCardsiDNM1L.
MIMi603850. gene.
614388. phenotype.
neXtProtiNX_O00429.
Orphaneti330050. Lethal encephalopathy due to mitochondrial and peroxisomal fission defect.
PharmGKBiPA27441.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0446. Eukaryota.
COG0699. LUCA.
GeneTreeiENSGT00840000129895.
HOGENOMiHOG000161068.
HOVERGENiHBG107833.
InParanoidiO00429.
KOiK17065.
OMAiGQEPTTG.
OrthoDBiEOG091G02TQ.
PhylomeDBiO00429.
TreeFamiTF352031.

Enzyme and pathway databases

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: September 7, 2016
This is version 149 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.