O00429 · DNM1L_HUMAN
- ProteinDynamin-1-like protein
- GeneDNM1L
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids736 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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).
Isoform 1
Isoform 4
Catalytic activity
- GTP + H2O = GDP + H+ + phosphate
Activity regulation
Features
Showing features for binding site.
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Necessary for mitochondrial and peroxisomal division. Sufficient for membrane fission. Organizes into membrane-associated scaffolds that wrap around a tubule and utilizes GTP hydrolysis to constrict and sever the tubule.
Names & Taxonomy
Protein names
- Recommended nameDynamin-1-like protein
- EC number
- Alternative names
Gene names
- Community suggested namesDynamin-1-like protein;DNM1L.
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO00429
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
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).
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Encephalopathy due to defective mitochondrial and peroxisomal fission 1 (EMPF1)
- Note
- 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 alsoMIM:614388
Natural variants in EMPF1
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_080870 | 36 | S>G | in EMPF1; autosomal recessive; impaired mitochondrial membrane fission; hypomorphic mutation retaining partial activity in mitochondrial membrane fission; dbSNP:rs879255688 | |
VAR_076316 | 362 | G>D | in EMPF1; uncertain significance; unable to associate with MIEF2 into filaments forming the tubular structures that wrap around the scission site; presence of concentric cristae and/or increased dense granules in some mitochondria; dbSNP:rs879255685 | |
VAR_076317 | 362 | G>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; dbSNP:rs886037861 | |
VAR_063704 | 395 | A>D | in EMPF1; the mutation acts in a dominant-negative manner; defects observed in both mitochondrial and peroxisomal fission; reduced oligomerization, decreased mitochondrial recruitment; dbSNP:rs121908531 | |
VAR_076318 | 403 | R>C | in EMPF1; the mutation acts in a dominant-negative manner; reduced oligomerization; decreased mitochondrial recruitment; defects observed in mitochondrial fission; dbSNP:rs863223953 | |
VAR_080872 | 406 | L>S | in EMPF1; impaired mitochondrial and peroxisomal membrane fission |
Optic atrophy 5 (OPA5)
- Note
- DescriptionA 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.
- See alsoMIM:610708
Natural variants in OPA5
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_080869 | 2 | E>A | in OPA5; changed localization to mitochondrion; impaired mitochondrial membrane fission; dbSNP:rs1555229948 | |
VAR_080871 | 192 | A>E | in OPA5; changed localization to mitochondrion; impaired mitochondrial membrane fission; dbSNP:rs1555119216 |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_080869 | 2 | in OPA5; changed localization to mitochondrion; impaired mitochondrial membrane fission; dbSNP:rs1555229948 | |||
Sequence: E → A | ||||||
Mutagenesis | 34 | Abolishes GTP hydrolysis. | ||||
Sequence: Q → A | ||||||
Natural variant | VAR_080870 | 36 | in EMPF1; autosomal recessive; impaired mitochondrial membrane fission; hypomorphic mutation retaining partial activity in mitochondrial membrane fission; dbSNP:rs879255688 | |||
Sequence: S → G | ||||||
Mutagenesis | 38 | Loss of GTPase activity. Impairs mitochondrial division and induces changes in peroxisome morphology. No effect on oligomerization. Increase in sumoylation by SUMO3. | ||||
Sequence: K → A | ||||||
Mutagenesis | 38 | Overexpression delays protein secretion. Rescues fragmented or truncated mitochondria in PRKN- or PINK1-depleted cells. | ||||
Sequence: K → E | ||||||
Mutagenesis | 39 | Abolishes GTP hydrolysis. | ||||
Sequence: S → A | ||||||
Mutagenesis | 39 | Decreased localization to the perinuclear region. | ||||
Sequence: S → I | ||||||
Mutagenesis | 39 | Reduces peroxisomal abundance. | ||||
Sequence: S → N | ||||||
Mutagenesis | 41 | Temperature-sensitive. Impairs mitochondrial division. | ||||
Sequence: V → F | ||||||
Mutagenesis | 59 | Abolishes GTP hydrolysis. Impairs mitochondrial division. Reduces peroxisomal abundance. | ||||
Sequence: T → A | ||||||
Natural variant | VAR_022446 | 71 | in dbSNP:rs1064610 | |||
Sequence: S → T | ||||||
Mutagenesis | 146 | Abolishes GTP hydrolysis. | ||||
Sequence: D → A | ||||||
Mutagenesis | 149 | Abolishes GTP hydrolysis. | ||||
Sequence: G → A | ||||||
Mutagenesis | 190 | Unable to homooligomerize. Unable to associate with MIEF2 into filaments forming the tubular structures that wrap around the scission site. | ||||
Sequence: D → A | ||||||
Natural variant | VAR_080871 | 192 | in OPA5; changed localization to mitochondrion; impaired mitochondrial membrane fission; dbSNP:rs1555119216 | |||
Sequence: A → E | ||||||
Mutagenesis | 216 | Abolishes GTP hydrolysis. | ||||
Sequence: K → A | ||||||
Mutagenesis | 218 | Abolishes GTP hydrolysis. | ||||
Sequence: D → A | ||||||
Mutagenesis | 221 | Unable to homooligomerize. Unable to associate with MIEF2 into filaments forming the tubular structures that wrap around the scission site. | ||||
Sequence: D → A | ||||||
Mutagenesis | 281 | Temperature-sensitive. Impairs mitochondrial division. | ||||
Sequence: G → D | ||||||
Mutagenesis | 300 | No effect on S-nitrosylation. | ||||
Sequence: C → A | ||||||
Mutagenesis | 345 | No effect on S-nitrosylation. | ||||
Sequence: C → A | ||||||
Mutagenesis | 361 | No effect on S-nitrosylation. | ||||
Sequence: C → A | ||||||
Natural variant | VAR_076316 | 362 | in EMPF1; uncertain significance; unable to associate with MIEF2 into filaments forming the tubular structures that wrap around the scission site; presence of concentric cristae and/or increased dense granules in some mitochondria; dbSNP:rs879255685 | |||
Sequence: G → D | ||||||
Natural variant | VAR_076317 | 362 | in EMPF1; the mutation acts in a dominant-negative manner; defects observed in mitochondrial fission; significant decrease in mitochondrial respiratory chain complex IV activity; dbSNP:rs886037861 | |||
Sequence: G → S | ||||||
Mutagenesis | 367 | No effect on S-nitrosylation. | ||||
Sequence: C → A | ||||||
Natural variant | VAR_063704 | 395 | in EMPF1; the mutation acts in a dominant-negative manner; defects observed in both mitochondrial and peroxisomal fission; reduced oligomerization, decreased mitochondrial recruitment; dbSNP:rs121908531 | |||
Sequence: A → D | ||||||
Mutagenesis | 401-404 | Impairs formation of higher order oligomers, but not homodimerization. | ||||
Sequence: GPRP → AAAA | ||||||
Natural variant | VAR_076318 | 403 | in EMPF1; the mutation acts in a dominant-negative manner; reduced oligomerization; decreased mitochondrial recruitment; defects observed in mitochondrial fission; dbSNP:rs863223953 | |||
Sequence: R → C | ||||||
Natural variant | VAR_080872 | 406 | in EMPF1; impaired mitochondrial and peroxisomal membrane fission | |||
Sequence: L → S | ||||||
Natural variant | VAR_030489 | 426 | in dbSNP:rs2389105 | |||
Sequence: E → D | ||||||
Mutagenesis | 431 | No effect on S-nitrosylation. | ||||
Sequence: C → A | ||||||
Mutagenesis | 446 | No effect on S-nitrosylation. | ||||
Sequence: C → A | ||||||
Mutagenesis | 470 | No effect on S-nitrosylation. | ||||
Sequence: C → A | ||||||
Mutagenesis | 490 | Does not impair homodimerization and formation of higher order oligomers. | ||||
Sequence: E → A | ||||||
Mutagenesis | 490 | Impairs homodimerization and formation of higher order oligomers. | ||||
Sequence: E → R | ||||||
Mutagenesis | 505 | No effect on S-nitrosylation. | ||||
Sequence: C → A | ||||||
Mutagenesis | 532 | Some loss of sumoylation in B domain. Complete loss of sumoylation in B domain; when associated with R-535; R-558 and R-568. | ||||
Sequence: K → R | ||||||
Mutagenesis | 535 | Some loss of sumoylation in B domain. Complete loss of sumoylation in B domain; when associated with R-532; R-558 and R-568. | ||||
Sequence: K → R | ||||||
Mutagenesis | 558 | Some loss of sumoylation in B domain. Complete loss of sumoylation in B domain; when associated with R-532; R-535 and R-568. | ||||
Sequence: K → R | ||||||
Mutagenesis | 568 | Some loss of sumoylation in B domain. Complete loss of sumoylation in B domain; when associated with R-532; R-535 and R-558. | ||||
Sequence: K → R | ||||||
Mutagenesis | 594 | 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. | ||||
Sequence: K → R | ||||||
Mutagenesis | 597 | 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. | ||||
Sequence: K → R | ||||||
Mutagenesis | 606 | 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. | ||||
Sequence: K → R | ||||||
Mutagenesis | 608 | 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. | ||||
Sequence: K → R | ||||||
Mutagenesis | 616 | Loss of activity. Little effect on mitochondrial morphology. Translocated to mitochondria. | ||||
Sequence: S → A | ||||||
Mutagenesis | 637 | 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. | ||||
Sequence: S → A | ||||||
Mutagenesis | 637 | 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. | ||||
Sequence: S → D | ||||||
Mutagenesis | 644 | Abolishes S-nitrosylation. Reduced dimerization and no enhancement of GTPase activity. | ||||
Sequence: C → A | ||||||
Mutagenesis | 668 | Abolishes homodimerization and formation of higher order oligomers. | ||||
Sequence: K → E | ||||||
Mutagenesis | 679 | 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. | ||||
Sequence: K → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 609 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for modified residue, chain, modified residue (large scale data), cross-link, glycosylation.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue | 1 | UniProt | N-acetylmethionine | ||||
Sequence: M | |||||||
Chain | PRO_0000206566 | 1-736 | UniProt | Dynamin-1-like protein | |||
Sequence: MEALIPVINKLQDVFNTVGADIIQLPQIVVVGTQSSGKSSVLESLVGRDLLPRGTGIVTRRPLILQLVHVSQEDKRKTTGEENGVEAEEWGKFLHTKNKLYTDFDEIRQEIENETERISGNNKGVSPEPIHLKIFSPNVVNLTLVDLPGMTKVPVGDQPKDIELQIRELILRFISNPNSIILAVTAANTDMATSEALKISREVDPDGRRTLAVITKLDLMDAGTDAMDVLMGRVIPVKLGIIGVVNRSQLDINNKKSVTDSIRDEYAFLQKKYPSLANRNGTKYLARTLNRLLMHHIRDCLPELKTRINVLAAQYQSLLNSYGEPVDDKSATLLQLITKFATEYCNTIEGTAKYIETSELCGGARICYIFHETFGRTLESVDPLGGLNTIDILTAIRNATGPRPALFVPEVSFELLVKRQIKRLEEPSLRCVELVHEEMQRIIQHCSNYSTQELLRFPKLHDAIVEVVTCLLRKRLPVTNEMVHNLVAIELAYINTKHPDFADACGLMNNNIEEQRRNRLARELPSAVSRDKSSKVPSALAPASQEPSPAASAEADGKLIQDSRRETKNVASGGGGVGDGVQEPTTGNWRGMLKTSKAEELLAEEKSKPIPIMPASPQKGHAVNLLDVPVPVARKLSAREQRDCEVIERLIKSYFLIVRKNIQDSVPKAVMHFLVNHVKDTLQSELVGQLYKSSLLDDLLTESEDMAQRRKEAADMLKALQGASQIIAEIRETHLW | |||||||
Modified residue (large scale data) | 126 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 526 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 529 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 529 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 532 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) | ||||
Sequence: K | |||||||
Cross-link | 535 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 544 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 548 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 548 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 558 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) | ||||
Sequence: K | |||||||
Cross-link | 568 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 572 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Glycosylation | 585 | UniProt | O-linked (GlcNAc) threonine | ||||
Sequence: T | |||||||
Glycosylation | 586 | UniProt | O-linked (GlcNAc) threonine | ||||
Sequence: T | |||||||
Cross-link | 594 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) | ||||
Sequence: K | |||||||
Modified residue | 597 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 597 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate | ||||
Sequence: K | |||||||
Cross-link | 606 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) | ||||
Sequence: K | |||||||
Modified residue | 607 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 607 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 608 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) | ||||
Sequence: K | |||||||
Modified residue | 616 | UniProt | Phosphoserine; by CDK1 and PINK1 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 616 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 637 | UniProt | Phosphoserine; by CAMK1 and PKA | ||||
Sequence: S | |||||||
Modified residue | 644 | UniProt | S-nitrosocysteine | ||||
Sequence: C |
Post-translational modification
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).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
Oligomerizes in a GTP-dependent manner to form membrane-associated tubules with a spiral pattern (PubMed:23584531).
Interacts with GSK3B and MARCHF5 (PubMed:10749171, PubMed:16874301, PubMed:16936636, PubMed:9731200).
Interacts (via the GTPase and B domains) with UBE2I; the interaction promotes sumoylation of DNM1L, mainly in its B domain (PubMed:19638400).
Interacts with PPP3CA; the interaction dephosphorylates DNM1L and regulates its transition to mitochondria (PubMed:18838687).
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 (PubMed:23792689).
Interacts with MFF; the interaction is inhibited by C11orf65/MFI (By similarity).
Interacts with FIS1; may form part of a larger protein complex at the endoplasmic reticulum-mitochondrial interface during mitochondrial fission (PubMed:18695047, PubMed:24196833).
Interacts with CANX (PubMed:24196833).
Interacts with BCAP31 (PubMed:24196833).
Interacts with MIEF2 and MIEF1; GTP-dependent, regulates GTP hydrolysis and DNM1L oligomerization (PubMed:21508961).
Interacts with PGAM5; this interaction leads to dephosphorylation at Ser-656 and activation of GTPase activity and eventually to mitochondria fragmentation (PubMed:22265414).
Interacts with RALBP1; during mitosis, recruits DNM1L to the mitochondrion and mediates its activation by the mitotic kinase cyclin B-CDK1 (PubMed:21822277).
Interacts with FUNDC1; this interaction recruits DNM1L/DRP1 at ER-mitochondria contact sites (PubMed:27145933).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O00429 | ATAD3A Q9NVI7 | 4 | EBI-724571, EBI-352007 | |
BINARY | O00429 | ATAD3A Q9NVI7-2 | 5 | EBI-724571, EBI-5456381 | |
BINARY | O00429 | DNM1L O00429 | 2 | EBI-724571, EBI-724571 | |
BINARY | O00429 | ESR1 P03372 | 2 | EBI-724571, EBI-78473 | |
BINARY | O00429 | FIS1 Q9Y3D6 | 2 | EBI-724571, EBI-3385283 | |
BINARY | O00429 | LRRK2 Q5S007 | 16 | EBI-724571, EBI-5323863 | |
BINARY | O00429 | MFF Q9GZY8 | 3 | EBI-724571, EBI-11420856 | |
BINARY | O00429 | MIEF1 Q9NQG6 | 11 | EBI-724571, EBI-740987 | |
BINARY | O00429 | MIEF2 Q96C03 | 5 | EBI-724571, EBI-750153 | |
BINARY | O00429 | SAMM50 Q9Y512 | 3 | EBI-724571, EBI-748409 | |
BINARY | O00429 | SCRIB Q14160 | 2 | EBI-724571, EBI-357345 | |
BINARY | O00429-3 | DNM1L O00429-3 | 8 | EBI-6896746, EBI-6896746 | |
BINARY | O00429-3 | LRRK2 Q5S007 | 2 | EBI-6896746, EBI-5323863 | |
BINARY | O00429-3 | MAGEB6 Q8N7X4 | 3 | EBI-6896746, EBI-6447163 | |
BINARY | O00429-3 | MPC2 O95563 | 3 | EBI-6896746, EBI-719403 | |
BINARY | O00429-3 | TGM2 P21980-2 | 3 | EBI-6896746, EBI-25842075 | |
BINARY | O00429-3 | ZNHIT1 O43257 | 3 | EBI-6896746, EBI-347522 | |
BINARY | O00429-4 | DNM1L O00429-4 | 2 | EBI-4420450, EBI-4420450 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 22-302 | Dynamin-type G | ||||
Sequence: IIQLPQIVVVGTQSSGKSSVLESLVGRDLLPRGTGIVTRRPLILQLVHVSQEDKRKTTGEENGVEAEEWGKFLHTKNKLYTDFDEIRQEIENETERISGNNKGVSPEPIHLKIFSPNVVNLTLVDLPGMTKVPVGDQPKDIELQIRELILRFISNPNSIILAVTAANTDMATSEALKISREVDPDGRRTLAVITKLDLMDAGTDAMDVLMGRVIPVKLGIIGVVNRSQLDINNKKSVTDSIRDEYAFLQKKYPSLANRNGTKYLARTLNRLLMHHIRDCLP | ||||||
Region | 32-39 | G1 motif | ||||
Sequence: GTQSSGKS | ||||||
Region | 58-60 | G2 motif | ||||
Sequence: VTR | ||||||
Region | 146-149 | G3 motif | ||||
Sequence: DLPG | ||||||
Region | 215-218 | G4 motif | ||||
Sequence: TKLD | ||||||
Region | 245-248 | G5 motif | ||||
Sequence: VNRS | ||||||
Region | 344-489 | Middle domain | ||||
Sequence: YCNTIEGTAKYIETSELCGGARICYIFHETFGRTLESVDPLGGLNTIDILTAIRNATGPRPALFVPEVSFELLVKRQIKRLEEPSLRCVELVHEEMQRIIQHCSNYSTQELLRFPKLHDAIVEVVTCLLRKRLPVTNEMVHNLVAI | ||||||
Region | 448-685 | Interaction with GSK3B | ||||
Sequence: NYSTQELLRFPKLHDAIVEVVTCLLRKRLPVTNEMVHNLVAIELAYINTKHPDFADACGLMNNNIEEQRRNRLARELPSAVSRDKSSKVPSALAPASQEPSPAASAEADGKLIQDSRRETKNVASGGGGVGDGVQEPTTGNWRGMLKTSKAEELLAEEKSKPIPIMPASPQKGHAVNLLDVPVPVARKLSAREQRDCEVIERLIKSYFLIVRKNIQDSVPKAVMHFLVNHVKDTLQSE | ||||||
Region | 502-569 | B domain | ||||
Sequence: ADACGLMNNNIEEQRRNRLARELPSAVSRDKSSKVPSALAPASQEPSPAASAEADGKLIQDSRRETKN | ||||||
Region | 523-590 | Disordered | ||||
Sequence: ELPSAVSRDKSSKVPSALAPASQEPSPAASAEADGKLIQDSRRETKNVASGGGGVGDGVQEPTTGNWR | ||||||
Domain | 644-735 | GED | ||||
Sequence: CEVIERLIKSYFLIVRKNIQDSVPKAVMHFLVNHVKDTLQSELVGQLYKSSLLDDLLTESEDMAQRRKEAADMLKALQGASQIIAEIRETHL | ||||||
Region | 654-668 | Important for homodimerization | ||||
Sequence: YFLIVRKNIQDSVPK |
Domain
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 9 isoforms produced by Alternative splicing.
O00429-1
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.
- Name1
- SynonymsHdynIV-WT, DLP1F
- Length736
- Mass (Da)81,877
- Last updated2007-02-06 v2
- ChecksumF9521A376B785B71
O00429-2
- Name4
- SynonymsHdynIV-11, DLP1c
- Differences from canonical
- 559-569: Missing
O00429-3
- Name2
- SynonymsDLP1a
- Differences from canonical
- 533-558: Missing
O00429-4
- Name3
- SynonymsHdynIV-37, DLP1b
- Differences from canonical
- 533-569: Missing
O00429-5
- Name5
- SynonymsHdynIV-26
- Differences from canonical
- 544-569: Missing
O00429-6
- Name6
- Differences from canonical
- 83-83: N → NDPATWKNSRHLSK
O00429-7
- Name7
O00429-8
- Name8
O00429-9
- Name9
Computationally mapped potential isoform sequences
There are 23 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H0YHY4 | H0YHY4_HUMAN | DNM1L | 88 | ||
H0YI79 | H0YI79_HUMAN | DNM1L | 504 | ||
F8VZ52 | F8VZ52_HUMAN | DNM1L | 696 | ||
F8VYL3 | F8VYL3_HUMAN | DNM1L | 117 | ||
F8VUJ9 | F8VUJ9_HUMAN | DNM1L | 719 | ||
F8VR28 | F8VR28_HUMAN | DNM1L | 97 | ||
B4DPZ9 | B4DPZ9_HUMAN | DNM1L | 156 | ||
F8W1W3 | F8W1W3_HUMAN | DNM1L | 168 | ||
B4DDQ3 | B4DDQ3_HUMAN | DNM1L | 180 | ||
A0A8V8TRA9 | A0A8V8TRA9_HUMAN | DNM1L | 104 | ||
A0A8V8TQT5 | A0A8V8TQT5_HUMAN | DNM1L | 587 | ||
A0A8V8TQV1 | A0A8V8TQV1_HUMAN | DNM1L | 140 | ||
A0A994J6L3 | A0A994J6L3_HUMAN | DNM1L | 148 | ||
A0A994J6L8 | A0A994J6L8_HUMAN | DNM1L | 576 | ||
A0A994J691 | A0A994J691_HUMAN | DNM1L | 103 | ||
A0A994J696 | A0A994J696_HUMAN | DNM1L | 563 | ||
A0A994J6A0 | A0A994J6A0_HUMAN | DNM1L | 409 | ||
A0A994J3M8 | A0A994J3M8_HUMAN | DNM1L | 602 | ||
A0A994J402 | A0A994J402_HUMAN | DNM1L | 576 | ||
A0A994J409 | A0A994J409_HUMAN | DNM1L | 194 | ||
A0A994J3F1 | A0A994J3F1_HUMAN | DNM1L | 181 | ||
A0A994J3G1 | A0A994J3G1_HUMAN | DNM1L | 386 | ||
A0A994J3G5 | A0A994J3G5_HUMAN | DNM1L | 561 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_054544 | 1-43 | in isoform 7 | |||
Sequence: MEALIPVINKLQDVFNTVGADIIQLPQIVVVGTQSSGKSSVLE → MFHKKINGKQQEKKMTLLHGKTQDTFLKGWKQKNGVNFFTPKI | ||||||
Alternative sequence | VSP_054545 | 44-246 | in isoform 7 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_039097 | 83 | in isoform 6, isoform 8 and isoform 9 | |||
Sequence: N → NDPATWKNSRHLSK | ||||||
Sequence conflict | 208 | in Ref. 2; AAC35283 and 4; AAD39541 | ||||
Sequence: R → C | ||||||
Alternative sequence | VSP_013686 | 533-558 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_013685 | 533-569 | in isoform 3 and isoform 9 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_013687 | 544-569 | in isoform 5 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_013688 | 559-569 | in isoform 4 and isoform 8 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB006965 EMBL· GenBank· DDBJ | BAA22193.1 EMBL· GenBank· DDBJ | mRNA | ||
AF061795 EMBL· GenBank· DDBJ | AAC35283.1 EMBL· GenBank· DDBJ | mRNA | ||
AF000430 EMBL· GenBank· DDBJ | AAC23724.1 EMBL· GenBank· DDBJ | mRNA | ||
AF151685 EMBL· GenBank· DDBJ | AAD39541.1 EMBL· GenBank· DDBJ | mRNA | ||
AK299926 EMBL· GenBank· DDBJ | BAG61760.1 EMBL· GenBank· DDBJ | mRNA | ||
AK291094 EMBL· GenBank· DDBJ | BAF83783.1 EMBL· GenBank· DDBJ | mRNA | ||
AK294533 EMBL· GenBank· DDBJ | BAG57740.1 EMBL· GenBank· DDBJ | mRNA | ||
AB209070 EMBL· GenBank· DDBJ | BAD92307.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AC084824 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC087588 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC024590 EMBL· GenBank· DDBJ | AAH24590.1 EMBL· GenBank· DDBJ | mRNA |