Dnm1l
entrez
74006
canonical
uniprot
Q8K1M6
canonical
ensembl
ENSMUSG00000022789
resolver
ensp
ENSMUSP00000023477
resolver
ensp
ENSMUSP00000093945
resolver
ensp
ENSMUSP00000111415
resolver
ensp
ENSMUSP00000155155
resolver
ensp
ENSMUSP00000155429
resolver
ensp
ENSMUSP00000269511
resolver
ensp
ENSMUSP00000269512
resolver
ensp
ENSMUSP00000269513
resolver
ensp
ENSMUSP00000269514
resolver
ensp
ENSMUSP00000269515
resolver
ensp
ENSMUSP00000269516
resolver
ensp
ENSMUSP00000269517
resolver
ensp
ENSMUSP00000269518
resolver
ensp
ENSMUSP00000269521
resolver
ensp
ENSMUSP00000269523
resolver
ensp
ENSMUSP00000269525
resolver
ensp
ENSMUSP00000269529
resolver
ensp
ENSMUSP00000269533
resolver
ensp
ENSMUSP00000269558
resolver
ensp
ENSMUSP00000269570
resolver
enst
ENSMUST00000115749
resolver
genesymbol
Dnm1l
resolver
genesymbol_syn
Drp1
resolver
uniprot
A0A2U3TZ67
resolver
uniprot
E9PUD2
resolver
uniprot
Q8BNQ5
resolver
uniprot
Q8BQ64
resolver
uniprot
Q8CGD0
resolver
uniprot
Q8K1A1
resolver
uniprot_entry
A0A2U3TZ67_MOUSE
resolver
uniprot_entry
DNM1L_MOUSE
resolver
uniprot_sec
E9PUD2
resolver
uniprot_sec
Q8BNQ5
resolver
uniprot_sec
Q8BQ64
resolver
uniprot_sec
Q8CGD0
resolver
uniprot_sec
Q8K1A1
resolver
amino_acid_sequence
MEALIPVINKLQDVFNTVGADIIQLPQIVVVGTQSSGKSSVLESLVGRDLLPRGTGVVTRRPLILQLVHVSPEDKRKTTGEENGVEAEEWGKFLHTKNKLYTDFDEIRQEIENETERISGNNKGVSPEPIHLKVFSPNVVNLTLVDLPGMTKVPVGDQPKDIELQIRELILRFISNPNSIILAVTAANTDMATSEALKISREVDPDGRRTLAVITKLDLMDAGTDAMDVLMGRVIPVKLGIIGVVNRSQLDINNKKSVTDSIRDEYAFLQKKYPSLANRNGTKYLARTLNRLLMHHIRDCLPELKTRINVLAAQYQSLLNSYGEPVDDKSATLLQLITKFATEYCNTIEGTAKYIETSELCGGARICYIFHETFGRTLESVDPLGGLNTIDILTAIRNATGPRPALFVPEVSFELLVKRQIKRLEEPSLRCVELVHEEMQRIIQHCSNYSTQELLRFPKLHDAIVEVVTCLLRKRLPVTNEMVHNLVAIELAYINTKHPDFADACGLMNNNIEEQRRNRLARELPSAGSRDKSSKVPSALAPASQEPPPAASAEADGKLIQDNRRETKNVPSAGGGIGDGGQEPTTGNWRGMLKTSKAEELLAEEKSKPIPIMPASPQKGHAVNLLDVPVPVARKLSAREQRDCEVIERLIKSYFLIVRKNIQDSVPKAVMHFLVNHVKDTLQSELVGQLYKSSLLDDLLTESEDMAQRRKEAADMLKALQGASQIIAEIRETHLW
uniprot
proteins
ec_number
3.6.5.5
uniprot
proteins
function
FUNCTION: Functions in mitochondrial and peroxisomal division (PubMed:19578372, PubMed:19752021, PubMed:22564413, PubMed:23283981, PubMed:24508339, PubMed:29478834, PubMed:29853636, PubMed:32484300). 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 (PubMed:24508339). The specific recruitment at scission sites is mediated by membrane receptors like MFF, MIEF1 and MIEF2 for mitochondrial membranes (PubMed:23283981, PubMed:24508339). While the recruitment by the membrane receptors is GTP-dependent, the following hydrolysis of GTP induces the dissociation from the receptors and allows DNM1L filaments to curl into closed rings that are probably sufficient to sever a double membrane (PubMed:24508339). Acts downstream of PINK1 to promote mitochondrial fission in a PRKN-dependent manner (PubMed:32484300). Plays an important role in mitochondrial fission during mitosis (By similarity). Required for formation of endocytic vesicles (By similarity). Through its function in mitochondrial division, ensures the survival of at least some types of postmitotic neurons, including Purkinje cells, by suppressing oxidative damage (PubMed:19752021, PubMed:22564413). Required for normal brain development, including that of cerebellum (PubMed:19578372, PubMed:22564413). Facilitates developmentally regulated apoptosis during neural tube formation (PubMed:19578372). 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 (PubMed:19578372). 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 (By similarity). Required for programmed necrosis execution (By similarity). Rhythmic control of its activity following phosphorylation at Ser-637 is essential for the circadian control of mitochondrial ATP production (PubMed:29478834). {ECO:0000250|UniProtKB:O00429, ECO:0000269|PubMed:19578372, ECO:0000269|PubMed:19752021, ECO:0000269|PubMed:22564413, ECO:0000269|PubMed:23283981, ECO:0000269|PubMed:24508339, ECO:0000269|PubMed:29478834, ECO:0000269|PubMed:29853636, ECO:0000269|PubMed:32484300}.; FUNCTION: [Isoform 14]: Regulates postsynaptic clathrin-mediated endocytosis by positioning the endocytic zone at the postsynaptic density, independently of mitochondrial division. {ECO:0000269|PubMed:31603426}.
uniprot
proteins
mass_dalton
81825
uniprot
proteins
mutagenesis
MUTAGEN 59; /note="T->A: Abolishes GTP hydrolysis."; /evidence="ECO:0000269|PubMed:24508339"; MUTAGEN 616; /note="S->A: Loss of activity and phosphorylation. Unable to rescue aberrant mitochondrial fission in PINK1 null mutant neurons."; /evidence="ECO:0000269|PubMed:32484300"; MUTAGEN Q8K1M6-14:38; /note="K->A: Impairs lysosome localization. Impairs late endosome localization. Impairs cell membrane localization."; /evidence="ECO:0000269|PubMed:29853636"; MUTAGEN Q8K1M6-14:369; /note="G->D: Impairs lysosome localization. Impairs late endosome localization. Impairs cell membrane localization."; /evidence="ECO:0000269|PubMed:29853636
uniprot
proteins
post_translational_modification
PTM: Phosphorylation/dephosphorylation events on two sites near the GED domain regulate mitochondrial fission (By similarity). Phosphorylation on Ser-637 inhibits mitochondrial fission probably through preventing intramolecular interaction (By similarity). Dephosphorylated on this site by PPP3CA which promotes mitochondrial fission (By similarity). Phosphorylation on Ser-616 by Pink1 activates the GTPase activity and promotes mitochondrial fission (PubMed:32484300). Phosphorylated in a circadian manner at Ser-637 (By similarity). Dephosphorylated by PGAM5 (By similarity). {ECO:0000250|UniProtKB:O00429, ECO:0000269|PubMed:32484300}.; PTM: Sumoylated on various lysine residues within the B domain, probably by MUL1. Sumoylation positively regulates mitochondrial fission. Desumoylated by SENP5 during G2/M transition of mitosis. Appears to be linked to its catalytic activity (By similarity). {ECO:0000250}.; PTM: S-nitrosylation increases DNM1L dimerization, mitochondrial fission and causes neuronal damage. {ECO:0000250}.; PTM: O-GlcNAcylation augments the level of the GTP-bound active form of DNM1L and induces translocation from the cytoplasm to mitochondria in cardiomyocytes. It also decreases phosphorylation at Ser-637 (By similarity). {ECO:0000250|UniProtKB:O35303}.; PTM: Ubiquitination by MARCHF5 affects mitochondrial morphology. {ECO:0000250|UniProtKB:O00429}.
uniprot
proteins
protein_family
Dynamin/Fzo/YdjA family
uniprot
proteins
protein_family
TRAFAC class dynamin-like GTPase superfamily
uniprot
proteins
pubmed
14592431
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
19578372
uniprot
proteins
pubmed
19752021
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
22564413
uniprot
proteins
pubmed
23283981
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
24508339
uniprot
proteins
pubmed
29478834
uniprot
proteins
pubmed
29853636
uniprot
proteins
pubmed
30059978
uniprot
proteins
pubmed
31603426
uniprot
proteins
pubmed
32484300
uniprot
proteins
pubmed
9422767
uniprot
proteins
sequence_length
736
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:30059978}. Golgi apparatus {ECO:0000250|UniProtKB:O00429}. Endomembrane system {ECO:0000250|UniProtKB:O00429}. Mitochondrion outer membrane {ECO:0000269|PubMed:30059978, ECO:0000305|PubMed:29853636}; Peripheral membrane protein. Peroxisome {ECO:0000269|PubMed:29853636}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:O35303}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:O35303}. Note=Mainly cytosolic. Recruited by RALA and RALBP1 to mitochondrion during mitosis (By similarity). Translocated to the mitochondrial membrane through O-GlcNAcylation and interaction with FIS1. Colocalized with MARCHF5 at mitochondrial membrane. Localizes to mitochondria at sites of division. Localizes to mitochondria following necrosis induction. Recruited to the mitochondrial outer membrane by interaction with MIEF1. Mitochondrial recruitment is inhibited by C11orf65/MFI (PubMed:30059978). Associated with peroxisomal membranes, partly recruited there by PEX11B. May also be associated with endoplasmic reticulum tubules and cytoplasmic vesicles and found to be perinuclear. In some cell types, localizes to the Golgi complex (By similarity). Binds to phospholipid membranes. {ECO:0000250, ECO:0000250|UniProtKB:O00429, ECO:0000269|PubMed:30059978}.; SUBCELLULAR LOCATION: [Isoform 14]: Lysosome {ECO:0000269|PubMed:29853636}. Late endosome {ECO:0000269|PubMed:29853636}. Cell membrane {ECO:0000269|PubMed:29853636}; Peripheral membrane protein. Mitochondrion outer membrane {ECO:0000269|PubMed:29853636}; Peripheral membrane protein. Postsynaptic density {ECO:0000269|PubMed:31603426}. Note=Is recruited to existing interorganelle interfaces between mitochondria and lysosomes/ late endosomes (PubMed:29853636). GTP hydrolysis and oligomerization are required for its localization to lysosomes/late endosomes and the cell membrane (PubMed:29853636). {ECO:0000269|PubMed:29853636}.
uniprot
proteins