DNM1L
entrez
10059
canonical
uniprot
O00429
canonical
ensembl
ENSG00000087470
resolver
ensp
ENSP00000266481
resolver
ensp
ENSP00000350948
resolver
ensp
ENSP00000370388
resolver
ensp
ENSP00000415131
resolver
ensp
ENSP00000448610
resolver
ensp
ENSP00000449089
resolver
ensp
ENSP00000450399
resolver
ensp
ENSP00000615680
resolver
genesymbol
DNM1L
resolver
genesymbol_syn
DLP1
resolver
genesymbol_syn
DRP1
resolver
hgnc
HGNC:2973
resolver
uniprot
A8K4X9
resolver
uniprot
B4DGC9
resolver
uniprot
B4DSU8
resolver
uniprot
B4DYR6
resolver
uniprot
G8JLD5
resolver
uniprot
J3KPI2
resolver
uniprot
O14541
resolver
uniprot
O60709
resolver
uniprot
Q59GN9
resolver
uniprot
Q7L6B3
resolver
uniprot
Q8TBT7
resolver
uniprot
Q9BWM1
resolver
uniprot
Q9Y5J2
resolver
uniprot_entry
B4DYR6_HUMAN
resolver
uniprot_entry
DNM1L_HUMAN
resolver
uniprot_sec
A8K4X9
resolver
uniprot_sec
B4DGC9
resolver
uniprot_sec
B4DSU8
resolver
uniprot_sec
G8JLD5
resolver
uniprot_sec
J3KPI2
resolver
uniprot_sec
O14541
resolver
uniprot_sec
O60709
resolver
uniprot_sec
Q59GN9
resolver
uniprot_sec
Q7L6B3
resolver
uniprot_sec
Q8TBT7
resolver
uniprot_sec
Q9BWM1
resolver
uniprot_sec
Q9Y5J2
resolver
activity_regulation
ACTIVITY REGULATION: GTPase activity is increased by binding to phospholipid membranes. {ECO:0000269|PubMed:23977156}.
uniprot
proteins
amino_acid_sequence
MEALIPVINKLQDVFNTVGADIIQLPQIVVVGTQSSGKSSVLESLVGRDLLPRGTGIVTRRPLILQLVHVSQEDKRKTTGEENGVEAEEWGKFLHTKNKLYTDFDEIRQEIENETERISGNNKGVSPEPIHLKIFSPNVVNLTLVDLPGMTKVPVGDQPKDIELQIRELILRFISNPNSIILAVTAANTDMATSEALKISREVDPDGRRTLAVITKLDLMDAGTDAMDVLMGRVIPVKLGIIGVVNRSQLDINNKKSVTDSIRDEYAFLQKKYPSLANRNGTKYLARTLNRLLMHHIRDCLPELKTRINVLAAQYQSLLNSYGEPVDDKSATLLQLITKFATEYCNTIEGTAKYIETSELCGGARICYIFHETFGRTLESVDPLGGLNTIDILTAIRNATGPRPALFVPEVSFELLVKRQIKRLEEPSLRCVELVHEEMQRIIQHCSNYSTQELLRFPKLHDAIVEVVTCLLRKRLPVTNEMVHNLVAIELAYINTKHPDFADACGLMNNNIEEQRRNRLARELPSAVSRDKSSKVPSALAPASQEPSPAASAEADGKLIQDSRRETKNVASGGGGVGDGVQEPTTGNWRGMLKTSKAEELLAEEKSKPIPIMPASPQKGHAVNLLDVPVPVARKLSAREQRDCEVIERLIKSYFLIVRKNIQDSVPKAVMHFLVNHVKDTLQSELVGQLYKSSLLDDLLTESEDMAQRRKEAADMLKALQGASQIIAEIRETHLW
uniprot
proteins
disease_involvement
DISEASE: Note=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. {ECO:0000269|PubMed:19342591}.; DISEASE: Encephalopathy due to defective mitochondrial and peroxisomal fission 1 (EMPF1) [MIM:614388]: A 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. {ECO:0000269|PubMed:17460227, ECO:0000269|PubMed:26604000, ECO:0000269|PubMed:26992161, ECO:0000269|PubMed:27145208, ECO:0000269|PubMed:27301544, ECO:0000269|PubMed:27328748, ECO:0000269|PubMed:29899447}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Optic atrophy 5 (OPA5) [MIM:610708]: A form of optic atrophy, a disease characterized by progressive visual loss in association with a deficiency in the number of nerve fibers which arise in the retina and converge to form the optic disk, optic nerve, optic chiasm and optic tracts. OPA5 is an autosomal dominant non-syndromic form that manifests as slowly progressive visual loss with variable onset from the first to third decades. Additional ocular abnormalities may include central scotoma and dyschromatopsia. {ECO:0000269|PubMed:28969390}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.6.5.5
uniprot
proteins
function
FUNCTION: Functions in mitochondrial and peroxisomal division (PubMed:11514614, PubMed:12499366, PubMed:17301055, PubMed:17460227, PubMed:17553808, PubMed:18695047, PubMed:18838687, PubMed:19342591, PubMed:19411255, PubMed:19638400, PubMed:23283981, PubMed:23530241, PubMed:23921378, PubMed:26992161, PubMed:27145208, PubMed:27145933, PubMed:27301544, PubMed:27328748, PubMed:29478834, PubMed:32439975, PubMed:32484300, PubMed:9570752, PubMed:9786947). 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:23530241, PubMed:23584531, PubMed:33850055). The specific recruitment at scission sites is mediated by membrane receptors like MFF, MIEF1 and MIEF2 for mitochondrial membranes (PubMed:23283981, PubMed:23921378, PubMed:29899447). 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:29899447). Acts downstream of PINK1 to promote mitochondrial fission in a PRKN-dependent manner (PubMed:32484300). Plays an important role in mitochondrial fission during mitosis (PubMed:19411255, PubMed:26992161, PubMed:27301544, PubMed:27328748). 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 (PubMed:17460227, PubMed:26992161, PubMed:27145208, PubMed:27301544, PubMed:27328748). 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:20688057, PubMed:23792689, PubMed:9570752). 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:17015472, PubMed:23792689). Required for programmed necrosis execution (PubMed:22265414). 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:Q8K1M6, ECO:0000269|PubMed:11514614, ECO:0000269|PubMed:12499366, ECO:0000269|PubMed:17015472, ECO:0000269|PubMed:17301055, ECO:0000269|PubMed:17460227, ECO:0000269|PubMed:17553808, ECO:0000269|PubMed:18695047, ECO:0000269|PubMed:18838687, ECO:0000269|PubMed:19342591, ECO:0000269|PubMed:19411255, ECO:0000269|PubMed:19638400, ECO:0000269|PubMed:20688057, ECO:0000269|PubMed:22265414, ECO:0000269|PubMed:23283981, ECO:0000269|PubMed:23530241, ECO:0000269|PubMed:23584531, ECO:0000269|PubMed:23792689, ECO:0000269|PubMed:23921378, ECO:0000269|PubMed:26992161, ECO:0000269|PubMed:27145208, ECO:0000269|PubMed:27145933, ECO:0000269|PubMed:27301544, ECO:0000269|PubMed:27328748, ECO:0000269|PubMed:29478834, ECO:0000269|PubMed:29899447, ECO:0000269|PubMed:32439975, ECO:0000269|PubMed:32484300, ECO:0000269|PubMed:33850055, ECO:0000269|PubMed:9570752, ECO:0000269|PubMed:9786947}.; FUNCTION: [Isoform 1]: Inhibits peroxisomal division when overexpressed. {ECO:0000269|PubMed:12618434}.; FUNCTION: [Isoform 4]: Inhibits peroxisomal division when overexpressed. {ECO:0000269|PubMed:12618434}.
uniprot
proteins
mass_dalton
81877
uniprot
proteins
mutagenesis
MUTAGEN 34; /note="Q->A: Abolishes GTP hydrolysis."; /evidence="ECO:0000269|PubMed:23977156"; MUTAGEN 38; /note="K->A: Loss of GTPase activity. Impairs mitochondrial division and induces changes in peroxisome morphology. No effect on oligomerization. Increase in sumoylation by SUMO3."; /evidence="ECO:0000269|PubMed:11514614, ECO:0000269|PubMed:12499366, ECO:0000269|PubMed:15208300, ECO:0000269|PubMed:19638400, ECO:0000269|PubMed:23977156, ECO:0000269|PubMed:32439975, ECO:0000269|PubMed:9570752"; MUTAGEN 38; /note="K->E: Overexpression delays protein secretion. Rescues fragmented or truncated mitochondria in PRKN- or PINK1-depleted cells."; /evidence="ECO:0000269|PubMed:11514614, ECO:0000269|PubMed:12499366, ECO:0000269|PubMed:15208300, ECO:0000269|PubMed:19638400, ECO:0000269|PubMed:23977156, ECO:0000269|PubMed:9570752"; MUTAGEN 39; /note="S->A: Abolishes GTP hydrolysis."; /evidence="ECO:0000269|PubMed:12618434, ECO:0000269|PubMed:23977156, ECO:0000269|PubMed:9422767"; MUTAGEN 39; /note="S->I: Decreased localization to the perinuclear region."; /evidence="ECO:0000269|PubMed:12618434, ECO:0000269|PubMed:23977156, ECO:0000269|PubMed:9422767"; MUTAGEN 39; /note="S->N: Reduces peroxisomal abundance."; /evidence="ECO:0000269|PubMed:12618434, ECO:0000269|PubMed:23977156, ECO:0000269|PubMed:9422767"; MUTAGEN 41; /note="V->F: Temperature-sensitive. Impairs mitochondrial division."; /evidence="ECO:0000269|PubMed:11514614"; MUTAGEN 59; /note="T->A: Abolishes GTP hydrolysis. Impairs mitochondrial division. Reduces peroxisomal abundance."; /evidence="ECO:0000269|PubMed:11514614, ECO:0000269|PubMed:12618434, ECO:0000269|PubMed:23977156"; MUTAGEN 146; /note="D->A: Abolishes GTP hydrolysis."; /evidence="ECO:0000269|PubMed:23977156"; MUTAGEN 149; /note="G->A: Abolishes GTP hydrolysis."; /evidence="ECO:0000269|PubMed:23977156"; MUTAGEN 190; /note="D->A: Unable to homooligomerize. Unable to associate with MIEF2 into filaments forming the tubular structures that wrap around the scission site."; /evidence="ECO:0000269|PubMed:29899447"; MUTAGEN 216; /note="K->A: Abolishes GTP hydrolysis."; /evidence="ECO:0000269|PubMed:23977156"; MUTAGEN 218; /note="D->A: Abolishes GTP hydrolysis."; /evidence="ECO:0000269|PubMed:23977156"; MUTAGEN 221; /note="D->A: Unable to homooligomerize. Unable to associate with MIEF2 into filaments forming the tubular structures that wrap around the scission site."; /evidence="ECO:0000269|PubMed:29899447"; MUTAGEN 281; /note="G->D: Temperature-sensitive. Impairs mitochondrial division."; /evidence="ECO:0000269|PubMed:11514614"; MUTAGEN 300; /note="C->A: No effect on S-nitrosylation."; /evidence="ECO:0000269|PubMed:19342591"; MUTAGEN 345; /note="C->A: No effect on S-nitrosylation."; /evidence="ECO:0000269|PubMed:19342591"; MUTAGEN 361; /note="C->A: No effect on S-nitrosylation."; /evidence="ECO:0000269|PubMed:19342591"; MUTAGEN 367; /note="C->A: No effect on S-nitrosylation."; /evidence="ECO:0000269|PubMed:19342591"; MUTAGEN 401..404; /note="GPRP->AAAA: Impairs formation of higher order oligomers, but not homodimerization."; /evidence="ECO:0000269|PubMed:23584531"; MUTAGEN 431; /note="C->A: No effect on S-nitrosylation."; /evidence="ECO:0000269|PubMed:19342591"; MUTAGEN 446; /note="C->A: No effect on S-nitrosylation."; /evidence="ECO:0000269|PubMed:19342591"; MUTAGEN 470; /note="C->A: No effect on S-nitrosylation."; /evidence="ECO:0000269|PubMed:19342591"; MUTAGEN 490; /note="E->A: Does not impair homodimerization and formation of higher order oligomers."; /evidence="ECO:0000269|PubMed:23584531"; MUTAGEN 490; /note="E->R: Impairs homodimerization and formation of higher order oligomers."; /evidence="ECO:0000269|PubMed:23584531"; MUTAGEN 505; /note="C->A: No effect on S-nitrosylation."; /evidence="ECO:0000269|PubMed:19342591"; MUTAGEN 532; /note="K->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."; /evidence="ECO:0000269|PubMed:19638400"; MUTAGEN 535; /note="K->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."; /evidence="ECO:0000269|PubMed:19638400"; MUTAGEN 558; /note="K->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."; /evidence="ECO:0000269|PubMed:19638400"; MUTAGEN 568; /note="K->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."; /evidence="ECO:0000269|PubMed:19638400"; MUTAGEN 594; /note="K->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."; /evidence="ECO:0000269|PubMed:19638400"; MUTAGEN 597; /note="K->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."; /evidence="ECO:0000269|PubMed:19638400"; MUTAGEN 606; /note="K->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."; /evidence="ECO:0000269|PubMed:19638400"; MUTAGEN 608; /note="K->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."; /evidence="ECO:0000269|PubMed:19638400"; MUTAGEN 616; /note="S->A: Loss of activity. Little effect on mitochondrial morphology. Translocated to mitochondria."; /evidence="ECO:0000269|PubMed:18838687, ECO:0000269|PubMed:32484300"; MUTAGEN 637; /note="S->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."; /evidence="ECO:0000269|PubMed:17553808, ECO:0000269|PubMed:18695047, ECO:0000269|PubMed:18838687, ECO:0000269|PubMed:23283981"; MUTAGEN 637; /note="S->D: Impairs intramolecular interactions but not homooligomerization. Does not reduce interaction with MIEF1 and MIEF2. Impairs formation of higher order oligomers but not homodimerization. Unable to associate with MIEF2 into filaments forming the tubular structures that wrap around the scission site. Slight reduction in GTPase activity. Inhibits mitochondrial fission. Retained in the cytoplasm."; /evidence="ECO:0000269|PubMed:17553808, ECO:0000269|PubMed:18695047, ECO:0000269|PubMed:18838687, ECO:0000269|PubMed:23283981, ECO:0000269|PubMed:29899447, ECO:0000269|PubMed:32439975"; MUTAGEN 644; /note="C->A: Abolishes S-nitrosylation. Reduced dimerization and no enhancement of GTPase activity."; /evidence="ECO:0000269|PubMed:19342591"; MUTAGEN 668; /note="K->E: Abolishes homodimerization and formation of higher order oligomers."; /evidence="ECO:0000269|PubMed:23584531"; MUTAGEN 679; /note="K->A: Diminishes intramolecular interaction between GTP-middle domain and GED domain but no effect on homooligomerization. Marked reduction in GTPase activity, in vitro. Decreased mitochondrial division."; /evidence="ECO:0000269|PubMed:15208300
uniprot
proteins
post_translational_modification
PTM: Phosphorylation/dephosphorylation events on two sites near the GED domain regulate mitochondrial fission (PubMed:17301055, PubMed:17553808, PubMed:18695047, PubMed:18838687, PubMed:23283981, PubMed:29478834, PubMed:33850055). Phosphorylation on Ser-637 by CAMK1 and PKA inhibits the GTPase activity, leading to a defect in mitochondrial fission promoting mitochondrial elongation (PubMed:17553808, PubMed:18695047, PubMed:23283981, PubMed:29478834). Dephosphorylated on this site by PPP3CA which promotes mitochondrial fission (PubMed:18838687). Phosphorylation on Ser-616 by CDK1 and PINK1 activates the GTPase activity and promotes mitochondrial fission (PubMed:18838687, PubMed:21822277, PubMed:32484300). Phosphorylated in a circadian manner at Ser-637 (PubMed:29478834). Dephosphorylated by PGAM5 (PubMed:32439975). {ECO:0000269|PubMed:17301055, ECO:0000269|PubMed:17553808, ECO:0000269|PubMed:18695047, ECO:0000269|PubMed:18838687, ECO:0000269|PubMed:21822277, ECO:0000269|PubMed:23283981, ECO:0000269|PubMed:29478834, ECO:0000269|PubMed:32439975, ECO:0000269|PubMed:32484300, ECO:0000269|PubMed:33850055}.; 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. {ECO:0000269|PubMed:19407830, ECO:0000269|PubMed:19411255, ECO:0000269|PubMed:19638400}.; PTM: S-nitrosylation increases DNM1L dimerization, mitochondrial fission and causes neuronal damage. {ECO:0000269|PubMed:19342591}.; PTM: Ubiquitination by MARCHF5 affects mitochondrial morphology. {ECO:0000269|PubMed:16874301, ECO:0000269|PubMed:16936636}.; 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}.
uniprot
proteins
protein_family
Dynamin/Fzo/YdjA family
uniprot
proteins
protein_family
TRAFAC class dynamin-like GTPase superfamily
uniprot
proteins
pubmed
10749171
uniprot
proteins
pubmed
11514614
uniprot
proteins
pubmed
12499366
uniprot
proteins
pubmed
12618434
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15208300
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16541075
uniprot
proteins
pubmed
16874301
uniprot
proteins
pubmed
16936636
uniprot
proteins
pubmed
17015472
uniprot
proteins
pubmed
17301055
uniprot
proteins
pubmed
17460227
uniprot
proteins
pubmed
17553808
uniprot
proteins
pubmed
17606867
uniprot
proteins
pubmed
18088087
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18695047
uniprot
proteins
pubmed
18838687
uniprot
proteins
pubmed
19342591
uniprot
proteins
pubmed
19407830
uniprot
proteins
pubmed
19411255
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19638400
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20688057
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21508961
uniprot
proteins
pubmed
21701560
uniprot
proteins
pubmed
21822277
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22265414
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23283981
uniprot
proteins
pubmed
23530241
uniprot
proteins
pubmed
23584531
uniprot
proteins
pubmed
23792689
uniprot
proteins
pubmed
23921378
uniprot
proteins
pubmed
23977156
uniprot
proteins
pubmed
24196833
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
26122121
uniprot
proteins
pubmed
26604000
uniprot
proteins
pubmed
26992161
uniprot
proteins
pubmed
27145208
uniprot
proteins
pubmed
27145933
uniprot
proteins
pubmed
27301544
uniprot
proteins
pubmed
27328748
uniprot
proteins
pubmed
28969390
uniprot
proteins
pubmed
29478834
uniprot
proteins
pubmed
29899447
uniprot
proteins
pubmed
32439975
uniprot
proteins
pubmed
32484300
uniprot
proteins
pubmed
33850055
uniprot
proteins
pubmed
9348079
uniprot
proteins
pubmed
9422767
uniprot
proteins
pubmed
9472031
uniprot
proteins
pubmed
9570752
uniprot
proteins
pubmed
9731200
uniprot
proteins
pubmed
9786947
uniprot
proteins
pubmed
9915810
uniprot
proteins
sequence_length
736
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:11514614, ECO:0000269|PubMed:12618434, ECO:0000269|PubMed:9786947}. Golgi apparatus {ECO:0000269|PubMed:20688057, ECO:0000269|PubMed:9348079, ECO:0000269|PubMed:9570752}. Endomembrane system {ECO:0000269|PubMed:11514614, ECO:0000269|PubMed:9348079, ECO:0000269|PubMed:9472031, ECO:0000269|PubMed:9570752}; Peripheral membrane protein. Mitochondrion outer membrane {ECO:0000269|PubMed:26122121, ECO:0000269|PubMed:27145208, ECO:0000269|PubMed:27145933, ECO:0000269|PubMed:28969390}; Peripheral membrane protein. Peroxisome {ECO:0000269|PubMed:12499366, ECO:0000269|PubMed:12618434}. 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 (PubMed:21822277). Translocated to the mitochondrial membrane through O-GlcNAcylation and interaction with FIS1. Colocalized with MARCHF5 at mitochondrial membrane (PubMed:17606867). Localizes to mitochondria at sites of division (PubMed:15208300). 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:9422767, PubMed:9570752). 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:15208300, ECO:0000269|PubMed:17606867, ECO:0000269|PubMed:21822277, ECO:0000269|PubMed:9422767, ECO:0000269|PubMed:9570752}.
uniprot
proteins