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UniProtKB - O00429 (DNM1L_HUMAN)

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Protein

Dynamin-1-like protein

Gene

DNM1L

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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

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

GO - Biological processi

  • cellular response to oxygen-glucose deprivation Source: Ensembl
  • cellular response to thapsigargin Source: Ensembl
  • dynamin family protein polymerization involved in mitochondrial fission Source: UniProtKB
  • endocytosis Source: UniProtKB-KW
  • execution phase of apoptosis Source: Reactome
  • 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
  • negative regulation of mitochondrial fusion Source: Ensembl
  • peroxisome fission Source: UniProtKB
  • positive regulation of apoptotic process Source: UniProtKB
  • positive regulation of dendritic spine morphogenesis Source: Ensembl
  • 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
  • positive regulation of synaptic vesicle endocytosis Source: Ensembl
  • positive regulation of synaptic vesicle exocytosis Source: Ensembl
  • protein complex oligomerization Source: UniProtKB
  • protein homotetramerization Source: UniProtKB
  • regulation of autophagy of mitochondrion Source: ParkinsonsUK-UCL
  • regulation of mitochondrion organization Source: UniProtKB
  • regulation of peroxisome organization Source: UniProtKB
  • regulation of protein oligomerization Source: UniProtKB
  • release of cytochrome c from mitochondria Source: UniProtKB
  • response to flavonoid Source: Ensembl
  • response to hypobaric hypoxia Source: Ensembl
  • synaptic vesicle recycling via endosome Source: Ensembl
View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionHydrolase
Biological processEndocytosis, Necrosis
LigandGTP-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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

EuPathDBiHostDB:ENSG00000087470.17
HGNCiHGNC:2973 DNM1L
MIMi603850 gene
neXtProtiNX_O00429

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

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

Pathology & Biotechi

Involvement in diseasei

May be associated with Alzheimer disease through amyloid-beta-induced increased S-nitrosylation of DNM1L, which triggers, directly or indirectly, excessive mitochondrial fission, synaptic loss and neuronal damage.1 Publication
Encephalopathy due to defective mitochondrial and peroxisomal fission 1 (EMPF1)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 PublicationCorresponds to variant dbSNP:rs879255685EnsemblClinVar.1
Natural variantiVAR_076317362G → S in EMPF1; the mutation acts in a dominant-negative manner; defects observed in mitochondrial fission; significant decrease in mitochondrial respiratory chain complex IV activity. 1 PublicationCorresponds to variant dbSNP:rs886037861EnsemblClinVar.1
Natural variantiVAR_063704395A → D in EMPF1; the mutation acts in a dominant-negative manner; defects observed in both mitochondrial and peroxisomal fission; reduced oligomerization, decreased mitochondrial recruitment. 2 PublicationsCorresponds to variant dbSNP:rs121908531EnsemblClinVar.1
Natural variantiVAR_076318403R → C in EMPF1; the mutation acts in a dominant-negative manner; reduced oligomerization; decreased mitochondrial recruitment; defects observed in mitochondrial fission. 1 PublicationCorresponds to variant dbSNP:rs863223953EnsemblClinVar.1

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

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
ProteomicsDBi47884
47885 [O00429-2]
47886 [O00429-3]
47887 [O00429-4]
47888 [O00429-5]
47889 [O00429-6]

PTM databases

iPTMnetiO00429
PhosphoSitePlusiO00429
SwissPalmiO00429

Miscellaneous databases

PMAP-CutDBiO00429

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

Show more details

GO - Molecular functioni

  • BH2 domain binding Source: Ensembl
  • clathrin binding Source: Ensembl
  • 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
View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi115370, 205 interactors
CORUMiO00429
DIPiDIP-42704N
IntActiO00429, 34 interactors
MINTiO00429
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
Helixi338 – 355Combined sources18
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
Helixi650 – 653Combined sources4
Turni655 – 657Combined sources3
Helixi658 – 660Combined sources3
Helixi663 – 692Combined sources30
Helixi693 – 699Combined sources7
Helixi712 – 732Combined sources21

3D structure databases

ProteinModelPortaliO00429
SMRiO00429
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni32 – 39G1 motifPROSITE-ProRule annotation8
Regioni58 – 60G2 motifPROSITE-ProRule annotation3
Regioni146 – 149G3 motifPROSITE-ProRule annotation4
Regioni215 – 218G4 motifPROSITE-ProRule annotation4
Regioni245 – 248G5 motifPROSITE-ProRule annotation4
Regioni344 – 489Middle 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

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

Phylogenomic databases

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

Family and domain databases

CDDicd08771 DLP_1, 1 hit
Gene3Di2.30.29.30, 1 hit
InterProiView protein in InterPro
IPR030556 DNM1L
IPR000375 Dynamin_central
IPR001401 Dynamin_GTPase
IPR019762 Dynamin_GTPase_CS
IPR022812 Dynamin_SF
IPR030381 G_DYNAMIN_dom
IPR003130 GED
IPR020850 GED_dom
IPR027417 P-loop_NTPase
IPR011993 PH-like_dom_sf
PANTHERiPTHR11566 PTHR11566, 1 hit
PTHR11566:SF39 PTHR11566:SF39, 1 hit
PfamiView protein in Pfam
PF01031 Dynamin_M, 1 hit
PF00350 Dynamin_N, 1 hit
PF02212 GED, 1 hit
PRINTSiPR00195 DYNAMIN
SMARTiView protein in SMART
SM00053 DYNc, 1 hit
SM00302 GED, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS00410 G_DYNAMIN_1, 1 hit
PS51718 G_DYNAMIN_2, 1 hit
PS51388 GED, 1 hit

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 → T3 PublicationsCorresponds to variant dbSNP:rs1064610Ensembl.1
Natural variantiVAR_076316362G → D in EMPF1; unknown pathological significance; presence of concentric cristae and/or increased dense granules in some mitochondria. 1 PublicationCorresponds to variant dbSNP:rs879255685EnsemblClinVar.1
Natural variantiVAR_076317362G → S in EMPF1; the mutation acts in a dominant-negative manner; defects observed in mitochondrial fission; significant decrease in mitochondrial respiratory chain complex IV activity. 1 PublicationCorresponds to variant dbSNP:rs886037861EnsemblClinVar.1
Natural variantiVAR_063704395A → D in EMPF1; the mutation acts in a dominant-negative manner; defects observed in both mitochondrial and peroxisomal fission; reduced oligomerization, decreased mitochondrial recruitment. 2 PublicationsCorresponds to variant dbSNP:rs121908531EnsemblClinVar.1
Natural variantiVAR_076318403R → C in EMPF1; the mutation acts in a dominant-negative manner; reduced oligomerization; decreased mitochondrial recruitment; defects observed in mitochondrial fission. 1 PublicationCorresponds to variant dbSNP:rs863223953EnsemblClinVar.1
Natural variantiVAR_030489426E → D. Corresponds to variant dbSNP:rs2389105Ensembl.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

Similar proteinsi

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 historyiIntegrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: February 6, 2007
Last modified: July 18, 2018
This is version 169 of the entry and version 2 of the sequence. See 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

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