Dnm1l
entrez
114114
canonical
uniprot
O35303
canonical
ensembl
ENSRNOG00000001813
resolver
ensembl
ENSRNOG00055003188
resolver
ensembl
ENSRNOG00060002669
resolver
ensembl
ENSRNOG00065008527
resolver
ensp
ENSRNOP00000002482
resolver
ensp
ENSRNOP00000078603
resolver
ensp
ENSRNOP00000110808
resolver
enst
ENSRNOT00000002482
resolver
enst
ENSRNOT00000172935
resolver
genesymbol
Dnm1l
resolver
genesymbol_syn
Dlp1
resolver
genesymbol_syn
Drp1
resolver
uniprot
A0A8L2Q0G8
resolver
uniprot
A0ABK0LZ40
resolver
uniprot
O35318
resolver
uniprot
O35319
resolver
uniprot
O35320
resolver
uniprot
O35321
resolver
uniprot
O35322
resolver
uniprot
O35323
resolver
uniprot
Q5U2W1
resolver
uniprot
Q792T7
resolver
uniprot
Q9R234
resolver
uniprot
Q9R277
resolver
uniprot_entry
A0A8L2Q0G8_RAT
resolver
uniprot_entry
A0ABK0LZ40_RAT
resolver
uniprot_entry
DNM1L_RAT
resolver
uniprot_sec
O35318
resolver
uniprot_sec
O35319
resolver
uniprot_sec
O35320
resolver
uniprot_sec
O35321
resolver
uniprot_sec
O35322
resolver
uniprot_sec
O35323
resolver
uniprot_sec
Q5U2W1
resolver
uniprot_sec
Q792T7
resolver
uniprot_sec
Q9R234
resolver
uniprot_sec
Q9R277
resolver
amino_acid_sequence
MEALIPVINKLQDVFNTVGADIIQLPQIVVVGTQSSGKSSVLESLVGRDLLPRGTGVVTRRPLILQLVHVSPEDKRKTTGEENDPATWKNSRHLSKGVEAEEWGKFLHTKNKLYTDFDEIRQEIENETERISGNNKGVSPEPIHLKVFSPNVVNLTLVDLPGMTKVPVGDQPKDIELQIRELILRFISNPNSIILAVTAANTDMATSEALKISREVDPDGRRTLAVITKLDLMDAGTDAMDVLMGRVIPVKLGIIGVVNRSQLDINNKKSVTDSIRDEYAFLQKKYPSLANRNGTKYLARTLNRLLMHHIRDCLPELKTRINVLAAQYQSLLNSYGEPVDDKSATLLQLITKFATEYCNTIEGTAKYIETSELCGGARICYIFHETFGRTLESVDPLGGLNTIDILTAIRNATGPRPALFVPEVSFELLVKRQIKRLEEPSLRCVELVHEEMQRIIQHCSNYSTQELLRFPKLHDAIVEVVTCLLRKRLPVTNEMVHNLVAIELAYINTKHPDFADACGLMNNNIEEQRRNRLARELPSAVSRDKSSKVPSALAPASQEPSPAASAEADGKLIQDNRRETKNVASAGGGIGDGGRIGDGGQEPTTGNWRGMLKTSKAEELLAEEKSKPIPIMPASPQKGHAVNLLDVPVPVARKLSAREQRDCEVIERLIKSYFLIVRKNIQDSVPKAVMHFLVNHVKDTLQSELVGQLYKSSLLDDLLTESEDMAQRRKEAADMLKALQGASQIIAEIRETHLW
uniprot
proteins
ec_number
3.6.5.5
uniprot
proteins
function
FUNCTION: Functions in mitochondrial and peroxisomal division (PubMed:11553726, PubMed:12499366, PubMed:12861026, PubMed:17301055, PubMed:18250306). 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:11553726). The specific recruitment at scission sites is mediated by membrane receptors like MFF, MIEF1 and MIEF2 for mitochondrial membranes (By similarity). 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 (By similarity). Acts downstream of PINK1 to promote mitochondrial fission in a PRKN-dependent manner. Plays an important role in mitochondrial fission during mitosis (By similarity). Through its function in mitochondrial division, ensures the survival of at least some types of postmitotic neurons, including Purkinje cells, by suppressing oxidative damage (By similarity). Required for normal brain development, including that of cerebellum (By similarity). Facilitates developmentally regulated apoptosis during neural tube formation (By similarity). Required for a normal rate of cytochrome c release and caspase activation during apoptosis; this requirement may depend upon the cell type and the physiological apoptotic cues (By similarity). Required for formation of endocytic vesicles (PubMed:18250306, PubMed:23792689). 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 (PubMed:18250306, PubMed:23792689). Required for programmed necrosis execution (By similarity). Rhythmic control of its activity following phosphorylation at Ser-656 is essential for the circadian control of mitochondrial ATP production (By similarity). {ECO:0000250|UniProtKB:O00429, ECO:0000250|UniProtKB:Q8K1M6, ECO:0000269|PubMed:11553726, ECO:0000269|PubMed:12499366, ECO:0000269|PubMed:12861026, ECO:0000269|PubMed:17301055, ECO:0000269|PubMed:18250306, ECO:0000269|PubMed:23792689}.
uniprot
proteins
mass_dalton
83908
uniprot
proteins
mutagenesis
MUTAGEN 38; /note="K->A: Defective in GTP hydrolysis. Tubulates spherical liposomes. Impairs mitochondrial division. Decreases the BCL2L1-mediated induction of synapse number and size of synaptic vesicle clusters."; /evidence="ECO:0000269|PubMed:11553726, ECO:0000269|PubMed:18250306"; MUTAGEN 71; /note="S->A: No effect on mitotic phosphorylation."; /evidence="ECO:0000269|PubMed:17301055"; MUTAGEN 139; /note="S->A: No effect on mitotic phosphorylation."; /evidence="ECO:0000269|PubMed:17301055"; MUTAGEN 149; /note="S->A: No effect on mitotic phosphorylation."; /evidence="ECO:0000269|PubMed:17301055"; MUTAGEN 231; /note="D->N: Defective in GTP-binding."; /evidence="ECO:0000269|PubMed:11553726"; MUTAGEN 635; /note="S->A: Abolishes mitotic phosphorylation. Reduced mitotic mitochondrial fragmentation."; /evidence="ECO:0000269|PubMed:17301055
uniprot
proteins
post_translational_modification
PTM: Phosphorylation/dephosphorylation events on two sites near the GED domain regulate mitochondrial fission (By similarity). Phosphorylation on Ser-656 by CAMK1 and PKA inhibits the GTPase activity, leading to a defect in mitochondrial fission promoting mitochondrial elongation (By similarity). Dephosphorylated on this site by PPP3CA which promotes mitochondrial fission (By similarity). Phosphorylation on Ser-635 by PINK1 activates the GTPase activity and promotes mitochondrial fission (By similarity). Phosphorylation on Ser-635 by CDK1 also promotes mitochondrial fission (PubMed:17301055). Phosphorylated in a circadian manner at Ser-656 (By similarity). Dephosphorylated by PGAM5 (By similarity). {ECO:0000250|UniProtKB:O00429, ECO:0000269|PubMed:17301055}.; 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-656. {ECO:0000269|PubMed:17301055}.; 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
10679301
uniprot
proteins
pubmed
11553726
uniprot
proteins
pubmed
12499366
uniprot
proteins
pubmed
12861026
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17301055
uniprot
proteins
pubmed
18250306
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
22745122
uniprot
proteins
pubmed
23792689
uniprot
proteins
pubmed
28463107
uniprot
proteins
pubmed
9472031
uniprot
proteins
sequence_length
755
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12861026, ECO:0000269|PubMed:22745122}. Golgi apparatus {ECO:0000250|UniProtKB:O00429}. Endomembrane system {ECO:0000250|UniProtKB:O00429}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8K1M6}. Mitochondrion outer membrane {ECO:0000269|PubMed:12861026, ECO:0000269|PubMed:22745122}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8K1M6}. Peroxisome {ECO:0000269|PubMed:12499366}. Membrane, clathrin-coated pit {ECO:0000269|PubMed:23792689}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:23792689}. Note=Mainly cytosolic. Recruited by RALA and RALBP1 to mitochondrion during mitosis. 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 (By similarity). 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 (PubMed:23792689). In some cell types, localizes to the Golgi complex (By similarity). Binds to phospholipid membranes (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q8K1M6, ECO:0000269|PubMed:23792689}.
uniprot
proteins