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O00429

- DNM1L_HUMAN

UniProt

O00429 - DNM1L_HUMAN

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Protein

Dynamin-1-like protein

Gene
DNM1L, DLP1, DRP1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - 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. Also required for mitochondrial fission during mitosis. 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 and isoform 4 inhibit peroxisomal division when overexpressed.20 Publications

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)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi32 – 398GTP
Nucleotide bindingi146 – 1505GTP
Nucleotide bindingi215 – 2184GTP
Nucleotide bindingi246 – 2494GTP

GO - Molecular functioni

  1. GTPase activity Source: UniProtKB
  2. GTP binding Source: UniProtKB-KW
  3. identical protein binding Source: IntAct
  4. lipid binding Source: UniProtKB-KW
  5. protein binding Source: UniProtKB
  6. protein homodimerization activity Source: UniProtKB
  7. ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  1. apoptotic process Source: Reactome
  2. cellular component disassembly involved in execution phase of apoptosis Source: Reactome
  3. dynamin polymerization involved in mitochondrial fission Source: UniProtKB
  4. endocytosis Source: UniProtKB-KW
  5. GTP catabolic process Source: UniProtKB
  6. membrane fission involved in mitochondrial fission Source: UniProtKB
  7. membrane fusion Source: UniProtKB
  8. mitochondrial fission Source: UniProtKB
  9. mitochondrial fragmentation involved in apoptotic process Source: UniProtKB
  10. mitochondrion morphogenesis Source: MGI
  11. necroptotic process Source: UniProtKB
  12. peroxisome fission Source: UniProtKB
  13. positive regulation of apoptotic process Source: UniProtKB
  14. positive regulation of intrinsic apoptotic signaling pathway Source: UniProtKB
  15. positive regulation of mitochondrial fission Source: BHF-UCL
  16. positive regulation of protein secretion Source: UniProtKB
  17. positive regulation of release of cytochrome c from mitochondria Source: UniProtKB
  18. protein homotetramerization Source: UniProtKB
  19. regulation of mitochondrion organization Source: UniProtKB
  20. regulation of peroxisome organization Source: UniProtKB
  21. regulation of protein oligomerization Source: UniProtKB
  22. release of cytochrome c from mitochondria Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Endocytosis, Necrosis

Keywords - Ligandi

GTP-binding, Lipid-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_995. Apoptotic execution phase.

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:2973. DNM1L.

Subcellular locationi

Cytoplasmcytosol. Golgi apparatus. Endomembrane system; Peripheral membrane protein. Mitochondrion outer membrane; Peripheral membrane protein. Peroxisome. Membraneclathrin-coated pit By similarity. Cytoplasmic vesiclesecretory vesiclesynaptic vesicle membrane By similarity
Note: Mainly cytosolic. Translocated to the mitochondrial membrane through O-GlcNAcylation and interaction with FIS1. Recruited to the mitochondrial outer membrane by interaction with MIEF1. Colocalized with MARCH5 at mitochondrial membrane. Localizes to mitochondria at sites of division. Localizes to mitochondria following necrosis induction. 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. Binds to phospholipid membranes.15 Publications

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. coated pit Source: UniProtKB-SubCell
  3. cytoplasm Source: UniProtKB
  4. cytosol Source: UniProtKB
  5. Golgi apparatus Source: UniProtKB
  6. intracellular membrane-bounded organelle Source: HPA
  7. microtubule Source: UniProtKB
  8. mitochondrial outer membrane Source: UniProtKB
  9. mitochondrion Source: UniProtKB
  10. perinuclear region of cytoplasm Source: UniProtKB
  11. peroxisome Source: UniProtKB
  12. protein complex Source: UniProtKB
  13. synaptic vesicle membrane Source: UniProtKB-SubCell
Complete GO annotation...

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 beta-amyloid-induced increased S-nitrosylation of DNM1L, which triggers, directly or indirectly, excessive mitochondrial fission, synaptic loss and neuronal damage.1 Publication
Encephalopathy, lethal, due to defective mitochondrial and peroxisomal fission (EMPF) [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.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti395 – 3951A → D in EMPF; the mutation acts in a dominant-negative manner; defects observed in both mitochondrial and peroxisomal fission. 1 Publication
VAR_063704

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi34 – 341Q → A: Abolishes GTP hydrolysis. 1 Publication
Mutagenesisi38 – 381K → A: Loss of GTPase activity. Impairs mitochondrial division and induces changes in peroxisome morphology. No effect on oligomerization. Increase in sumoylation by SUMO3. 6 Publications
Mutagenesisi38 – 381K → E: Overexpression delays protein secretion. 6 Publications
Mutagenesisi39 – 391S → A: Abolishes GTP hydrolysis. 3 Publications
Mutagenesisi39 – 391S → I: Decreased localization to the perinuclear region. 3 Publications
Mutagenesisi39 – 391S → N: Reduces peroxisomal abundance. 3 Publications
Mutagenesisi41 – 411V → F: Temperature-sensitive. Impairs mitochondrial division. 1 Publication
Mutagenesisi59 – 591T → A: Abolishes GTP hydrolysis. Impairs mitochondrial division. Reduces peroxisomal abundance. 3 Publications
Mutagenesisi146 – 1461D → A: Abolishes GTP hydrolysis. 1 Publication
Mutagenesisi149 – 1491G → A: Abolishes GTP hydrolysis. 1 Publication
Mutagenesisi216 – 2161K → A: Abolishes GTP hydrolysis. 1 Publication
Mutagenesisi218 – 2181D → A: Abolishes GTP hydrolysis. 1 Publication
Mutagenesisi281 – 2811G → D: Temperature-sensitive. Impairs mitochondrial division. 1 Publication
Mutagenesisi300 – 3001C → A: No effect on S-nitrosylation. 1 Publication
Mutagenesisi345 – 3451C → A: No effect on S-nitrosylation. 1 Publication
Mutagenesisi361 – 3611C → A: No effect on S-nitrosylation. 1 Publication
Mutagenesisi367 – 3671C → A: No effect on S-nitrosylation. 1 Publication
Mutagenesisi401 – 4044GPRP → AAAA: Impairs formation of higher order oligomers, but not homodimerization. 1 Publication
Mutagenesisi431 – 4311C → A: No effect on S-nitrosylation. 1 Publication
Mutagenesisi446 – 4461C → A: No effect on S-nitrosylation. 1 Publication
Mutagenesisi470 – 4701C → A: No effect on S-nitrosylation. 1 Publication
Mutagenesisi490 – 4901E → A: Does not impair homodimerization and formation of higher order oligomers. 1 Publication
Mutagenesisi490 – 4901E → R: Impairs homodimerization and formation of higher order oligomers. 1 Publication
Mutagenesisi505 – 5051C → A: No effect on S-nitrosylation. 1 Publication
Mutagenesisi532 – 5321K → 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 Publication
Mutagenesisi535 – 5351K → 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 Publication
Mutagenesisi558 – 5581K → 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 Publication
Mutagenesisi568 – 5681K → 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 Publication
Mutagenesisi594 – 5941K → 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 Publication
Mutagenesisi597 – 5971K → 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 Publication
Mutagenesisi606 – 6061K → 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 Publication
Mutagenesisi608 – 6081K → 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 Publication
Mutagenesisi616 – 6161S → A: Little effect on mitochondrial morphology. Translocated to mitochondria. 1 Publication
Mutagenesisi637 – 6371S → 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 Publications
Mutagenesisi637 – 6371S → 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 Publications
Mutagenesisi644 – 6441C → A: Abolishes S-nitrosylation. Reduced dimerization and no enhancement of GTPase activity. 1 Publication
Mutagenesisi668 – 6681K → A: Abolishes homodimerization and formation of higher order oligomers. 1 Publication
Mutagenesisi679 – 6791K → 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 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi614388. phenotype.
Orphaneti330050. Lethal encephalopathy due to mitochondrial and peroxisomal fission defect.
PharmGKBiPA27441.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 736736Dynamin-1-like proteinPRO_0000206566Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine2 Publications
Cross-linki532 – 532Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Cross-linki535 – 535Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei548 – 5481Phosphoserine1 Publication
Cross-linki558 – 558Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Cross-linki568 – 568Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Glycosylationi585 – 5851O-linked (GlcNAc) By similarity
Glycosylationi586 – 5861O-linked (GlcNAc) By similarity
Cross-linki594 – 594Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Inferred
Modified residuei597 – 5971N6-acetyllysine; alternate By similarity
Cross-linki597 – 597Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate1 Publication
Cross-linki606 – 606Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Inferred
Modified residuei607 – 6071Phosphoserine1 Publication
Cross-linki608 – 608Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei616 – 6161Phosphoserine; by CDK16 Publications
Modified residuei637 – 6371Phosphoserine; by CAMK1 and PKA4 Publications
Modified residuei644 – 6441S-nitrosocysteine1 Publication

Post-translational modificationi

Phosphorylation/dephosphorylation events on two sites near the GED domain regulate mitochondrial fission. Phosphorylation on Ser-637 inhibits mitochondrial fission probably through preventing intramolecular interaction. Dephosphorylated on this site by PPP3CA which promotes mitochondrial fission. Phosphorylation on Ser-616 also promotes mitochondrial fission.5 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.
Ubiquitination by MARCH5 affects mitochondrial morphology.
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.

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Phosphoprotein, S-nitrosylation, Ubl conjugation

Proteomic databases

MaxQBiO00429.
PaxDbiO00429.
PRIDEiO00429.

PTM databases

PhosphoSiteiO00429.

Miscellaneous databases

PMAP-CutDBO00429.

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

ArrayExpressiO00429.
BgeeiO00429.
CleanExiHS_DNM1L.
GenevestigatoriO00429.

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.19 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ESR1P033722EBI-724571,EBI-78473
LRRK2Q5S00711EBI-724571,EBI-5323863
MIEF1Q9NQG69EBI-724571,EBI-740987
MIEF2Q96C033EBI-724571,EBI-750153

Protein-protein interaction databases

BioGridi115370. 35 interactions.
DIPiDIP-42704N.
IntActiO00429. 12 interactions.
MINTiMINT-1394198.
STRINGi9606.ENSP00000266481.

Structurei

Secondary structure

1
736
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 1814
Turni21 – 233
Beta strandi27 – 315
Helixi34 – 363
Helixi38 – 447
Beta strandi55 – 573
Beta strandi63 – 697
Beta strandi86 – 883
Beta strandi90 – 934
Helixi94 – 963
Helixi104 – 11916
Beta strandi121 – 1233
Beta strandi130 – 1367
Beta strandi141 – 1466
Helixi155 – 1573
Helixi162 – 17413
Beta strandi179 – 1868
Helixi191 – 1933
Helixi195 – 2039
Beta strandi205 – 2073
Beta strandi210 – 2156
Helixi217 – 2193
Beta strandi222 – 2254
Helixi227 – 2304
Beta strandi233 – 2353
Beta strandi237 – 2393
Beta strandi241 – 2433
Helixi249 – 2535
Helixi258 – 27215
Turni274 – 2763
Helixi277 – 2793
Helixi282 – 31736
Helixi329 – 34921
Helixi363 – 3719
Helixi373 – 3808
Helixi389 – 39911
Helixi409 – 42012
Helixi421 – 4244
Helixi425 – 44016
Turni441 – 4433
Helixi444 – 4463
Helixi458 – 49336
Helixi501 – 5044
Helixi632 – 66231
Helixi664 – 67916
Helixi682 – 6887
Helixi710 – 73122

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3W6NX-ray2.00A/B1-329[»]
A/B709-736[»]
3W6OX-ray1.90A/B1-329[»]
A/B709-736[»]
3W6PX-ray1.70A/B1-329[»]
A/B709-736[»]
4BEJX-ray3.48A/B/C/D1-736[»]
4H1UX-ray2.30A1-327[»]
A711-736[»]
4H1VX-ray2.30A1-327[»]
A711-736[»]
ProteinModelPortaliO00429.
SMRiO00429. Positions 1-504, 642-729.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 302281Dynamin-type GAdd
BLAST
Domaini644 – 73592GEDAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 343343GTPase domainAdd
BLAST
Regioni344 – 489146Middle domainAdd
BLAST
Regioni448 – 685238Interaction with GSK3BAdd
BLAST
Regioni502 – 56968B domainAdd
BLAST
Regioni654 – 66815Important for homodimerizationAdd
BLAST

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.1 Publication

Sequence similaritiesi

Contains 1 GED domain.

Phylogenomic databases

eggNOGiCOG0699.
HOGENOMiHOG000161068.
HOVERGENiHBG107833.
KOiK17065.
OMAiRDKSYKV.
OrthoDBiEOG7GJ6CB.
PhylomeDBiO00429.
TreeFamiTF352031.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR000375. Dynamin_central.
IPR001401. Dynamin_GTPase.
IPR019762. Dynamin_GTPase_CS.
IPR022812. Dynamin_SF.
IPR003130. GED.
IPR020850. GTPase_effector_domain_GED.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11566. PTHR11566. 1 hit.
PfamiPF01031. Dynamin_M. 1 hit.
PF00350. Dynamin_N. 1 hit.
PF02212. GED. 1 hit.
[Graphical view]
PRINTSiPR00195. DYNAMIN.
SMARTiSM00053. DYNc. 1 hit.
SM00302. GED. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00410. G_DYNAMIN_1. 1 hit.
PS51718. G_DYNAMIN_2. 1 hit.
PS51388. GED. 1 hit.
[Graphical view]

Sequences (8)i

Sequence statusi: Complete.

This entry describes 8 isoformsi produced by alternative splicing. Align

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

MEALIPVINK LQDVFNTVGA DIIQLPQIVV VGTQSSGKSS VLESLVGRDL    50
LPRGTGIVTR RPLILQLVHV SQEDKRKTTG EENGVEAEEW GKFLHTKNKL 100
YTDFDEIRQE IENETERISG NNKGVSPEPI HLKIFSPNVV NLTLVDLPGM 150
TKVPVGDQPK DIELQIRELI LRFISNPNSI ILAVTAANTD MATSEALKIS 200
REVDPDGRRT LAVITKLDLM DAGTDAMDVL MGRVIPVKLG IIGVVNRSQL 250
DINNKKSVTD SIRDEYAFLQ KKYPSLANRN GTKYLARTLN RLLMHHIRDC 300
LPELKTRINV LAAQYQSLLN SYGEPVDDKS ATLLQLITKF ATEYCNTIEG 350
TAKYIETSEL CGGARICYIF HETFGRTLES VDPLGGLNTI DILTAIRNAT 400
GPRPALFVPE VSFELLVKRQ IKRLEEPSLR CVELVHEEMQ RIIQHCSNYS 450
TQELLRFPKL HDAIVEVVTC LLRKRLPVTN EMVHNLVAIE LAYINTKHPD 500
FADACGLMNN NIEEQRRNRL ARELPSAVSR DKSSKVPSAL APASQEPSPA 550
ASAEADGKLI QDSRRETKNV ASGGGGVGDG VQEPTTGNWR GMLKTSKAEE 600
LLAEEKSKPI PIMPASPQKG HAVNLLDVPV PVARKLSARE QRDCEVIERL 650
IKSYFLIVRK NIQDSVPKAV MHFLVNHVKD TLQSELVGQL YKSSLLDDLL 700
TESEDMAQRR KEAADMLKAL QGASQIIAEI RETHLW 736
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.

Show »
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 BAD92307.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti71 – 711S → T.3 Publications
Corresponds to variant rs1064610 [ dbSNP | Ensembl ].
VAR_022446
Natural varianti395 – 3951A → D in EMPF; the mutation acts in a dominant-negative manner; defects observed in both mitochondrial and peroxisomal fission. 1 Publication
VAR_063704
Natural varianti426 – 4261E → D.
Corresponds to variant rs2389105 [ dbSNP | Ensembl ].
VAR_030489

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4343MEALI…SSVLE → MFHKKINGKQQEKKMTLLHG KTQDTFLKGWKQKNGVNFFT PKI in isoform 7. VSP_054544Add
BLAST
Alternative sequencei44 – 246203Missing in isoform 7. VSP_054545Add
BLAST
Alternative sequencei83 – 831N → NDPATWKNSRHLSK in isoform 6 and isoform 8. VSP_039097
Alternative sequencei533 – 56937Missing in isoform 3. VSP_013685Add
BLAST
Alternative sequencei533 – 55826Missing in isoform 2. VSP_013686Add
BLAST
Alternative sequencei544 – 56926Missing in isoform 5. VSP_013687Add
BLAST
Alternative sequencei559 – 56911Missing in isoform 4 and isoform 8. VSP_013688Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti208 – 2081R → C in AAC35283. 1 Publication
Sequence conflicti208 – 2081R → C in AAD39541. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_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.
ENST00000414834; ENSP00000404160; ENSG00000087470.
ENST00000452533; ENSP00000415131; ENSG00000087470. [O00429-3]
ENST00000547312; ENSP00000448610; ENSG00000087470. [O00429-2]
ENST00000549701; ENSP00000450399; ENSG00000087470. [O00429-1]
ENST00000553257; ENSP00000449089; ENSG00000087470. [O00429-6]
GeneIDi10059.
KEGGihsa:10059.
UCSCiuc001rld.2. human. [O00429-1]
uc001rle.2. human. [O00429-3]
uc001rlf.2. human. [O00429-4]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS61095.1. [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 ]
PIRi JC5695.
RefSeqi NP_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_005681.2. NM_005690.4. [O00429-4 ]
NP_036192.2. NM_012062.4. [O00429-1 ]
NP_036193.2. NM_012063.3. [O00429-3 ]
UniGenei Hs.556296.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3W6N X-ray 2.00 A/B 1-329 [» ]
A/B 709-736 [» ]
3W6O X-ray 1.90 A/B 1-329 [» ]
A/B 709-736 [» ]
3W6P X-ray 1.70 A/B 1-329 [» ]
A/B 709-736 [» ]
4BEJ X-ray 3.48 A/B/C/D 1-736 [» ]
4H1U X-ray 2.30 A 1-327 [» ]
A 711-736 [» ]
4H1V X-ray 2.30 A 1-327 [» ]
A 711-736 [» ]
ProteinModelPortali O00429.
SMRi O00429. Positions 1-504, 642-729.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115370. 35 interactions.
DIPi DIP-42704N.
IntActi O00429. 12 interactions.
MINTi MINT-1394198.
STRINGi 9606.ENSP00000266481.

PTM databases

PhosphoSitei O00429.

Proteomic databases

MaxQBi O00429.
PaxDbi O00429.
PRIDEi O00429.

Protocols and materials databases

DNASUi 10059.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000266481 ; ENSP00000266481 ; ENSG00000087470 . [O00429-4 ]
ENST00000381000 ; ENSP00000370388 ; ENSG00000087470 .
ENST00000414834 ; ENSP00000404160 ; ENSG00000087470 .
ENST00000452533 ; ENSP00000415131 ; ENSG00000087470 . [O00429-3 ]
ENST00000547312 ; ENSP00000448610 ; ENSG00000087470 . [O00429-2 ]
ENST00000549701 ; ENSP00000450399 ; ENSG00000087470 . [O00429-1 ]
ENST00000553257 ; ENSP00000449089 ; ENSG00000087470 . [O00429-6 ]
GeneIDi 10059.
KEGGi hsa:10059.
UCSCi uc001rld.2. human. [O00429-1 ]
uc001rle.2. human. [O00429-3 ]
uc001rlf.2. human. [O00429-4 ]

Organism-specific databases

CTDi 10059.
GeneCardsi GC12P032832.
H-InvDB HIX0010537.
HGNCi HGNC:2973. DNM1L.
HPAi CAB009952.
HPA039324.
MIMi 603850. gene.
614388. phenotype.
neXtProti NX_O00429.
Orphaneti 330050. Lethal encephalopathy due to mitochondrial and peroxisomal fission defect.
PharmGKBi PA27441.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0699.
HOGENOMi HOG000161068.
HOVERGENi HBG107833.
KOi K17065.
OMAi RDKSYKV.
OrthoDBi EOG7GJ6CB.
PhylomeDBi O00429.
TreeFami TF352031.

Enzyme and pathway databases

Reactomei REACT_995. Apoptotic execution phase.

Miscellaneous databases

ChiTaRSi DNM1L. human.
GeneWikii DNM1L.
GenomeRNAii 10059.
NextBioi 35471718.
PMAP-CutDB O00429.
PROi O00429.
SOURCEi Search...

Gene expression databases

ArrayExpressi O00429.
Bgeei O00429.
CleanExi HS_DNM1L.
Genevestigatori O00429.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR000375. Dynamin_central.
IPR001401. Dynamin_GTPase.
IPR019762. Dynamin_GTPase_CS.
IPR022812. Dynamin_SF.
IPR003130. GED.
IPR020850. GTPase_effector_domain_GED.
IPR027417. P-loop_NTPase.
[Graphical view ]
PANTHERi PTHR11566. PTHR11566. 1 hit.
Pfami PF01031. Dynamin_M. 1 hit.
PF00350. Dynamin_N. 1 hit.
PF02212. GED. 1 hit.
[Graphical view ]
PRINTSi PR00195. DYNAMIN.
SMARTi SM00053. DYNc. 1 hit.
SM00302. GED. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
PROSITEi PS00410. G_DYNAMIN_1. 1 hit.
PS51718. G_DYNAMIN_2. 1 hit.
PS51388. GED. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and subcellular localization of a novel mammalian dynamin-related protein homologous to yeast Vps1p and Dnm1p."
    Shin H.-W., Shinotsuka C., Torii S., Murakami K., Nakayama K.
    J. Biochem. 122:525-530(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
    Tissue: Hepatoma.
  2. "Human dynamin-like protein interacts with the glycogen synthase kinase 3beta."
    Hong Y.-R., Chen C.-H., Cheng D.-S., Howng S.-L., Chow C.-C.
    Biochem. Biophys. Res. Commun. 249:697-703(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), VARIANT THR-71, TISSUE SPECIFICITY, INTERACTION WITH GSK3B.
    Tissue: Liver.
  3. "Identification and functional characterization of a novel human protein highly related to the yeast dynamin-like GTPase Vps1p."
    Imoto M., Tachibana I., Urrutia R.
    J. Cell Sci. 111:1341-1349(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT THR-71, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-38, FUNCTION.
    Tissue: Brain.
  4. "Differential expression of four human dynamin-like protein variants in brain tumors."
    Chen C.-H., Howng S.-L., Hwang S.-L., Chou C.-K., Liao C.-H., Hong Y.-R.
    DNA Cell Biol. 19:189-194(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3; 4 AND 5), VARIANT THR-71, TISSUE SPECIFICITY, INTERACTION WITH GSK3B.
    Tissue: Brain.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 6 AND 7).
    Tissue: Amygdala and Brain.
  6. "Homo sapiens protein coding cDNA."
    Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8).
    Tissue: Brain.
  7. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 27-736 (ISOFORM 1).
    Tissue: Lung.
  9. "Dymple, a novel dynamin-like high molecular weight GTPase lacking a proline-rich carboxyl-terminal domain in mammalian cells."
    Kamimoto T., Nagai Y., Onogi H., Muro Y., Wakabayashi T., Hagiwara M.
    J. Biol. Chem. 273:1044-1051(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF SER-39, TISSUE SPECIFICITY, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
  10. "A novel dynamin-like protein associates with cytoplasmic vesicles and tubules of the endoplasmic reticulum in mammalian cells."
    Yoon Y., Pitts K.R., Dahan S., McNiven M.A.
    J. Cell Biol. 140:779-793(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  11. "A human dynamin-related protein controls the distribution of mitochondria."
    Smirnova E., Shurland D.-L., Ryazantsev S.N., van der Bliek A.M.
    J. Cell Biol. 143:351-358(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION.
  12. "Intermolecular and interdomain interactions of a dynamin-related GTP-binding protein, Dnm1p/Vps1p-like protein."
    Shin H.-W., Takatsu H., Mukai H., Munekata E., Murakami K., Nakayama K.
    J. Biol. Chem. 274:2780-2785(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: OLIGOMERIZATION.
  13. "Dynamin-related protein Drp1 is required for mitochondrial division in mammalian cells."
    Smirnova E., Griparic L., Shurland D.-L., van der Bliek A.M.
    Mol. Biol. Cell 12:2245-2256(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-38; VAL-41; THR-59 AND GLY-281, OLIGOMERIZATION.
  14. Cited for: MUTAGENESIS OF LYS-38, SUBCELLULAR LOCATION, FUNCTION.
  15. "The dynamin-like GTPase DLP1 is essential for peroxisome division and is recruited to peroxisomes in part by PEX11."
    Li X., Gould S.J.
    J. Biol. Chem. 278:17012-17020(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF SER-39 AND THR-59, FUNCTION, SUBCELLULAR LOCATION.
  16. "Intra- and intermolecular domain interactions of the C-terminal GTPase effector domain of the multimeric dynamin-like GTPase Drp1."
    Zhu P.P., Patterson A., Stadler J., Seeburg D.P., Sheng M., Blackstone C.
    J. Biol. Chem. 279:35967-35974(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF STRUCTURAL DOMAINS, OLIGOMERIZATION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-38 AND LYS-679.
  17. "A novel mitochondrial ubiquitin ligase plays a critical role in mitochondrial dynamics."
    Yonashiro R., Ishido S., Kyo S., Fukuda T., Goto E., Matsuki Y., Ohmura-Hoshino M., Sada K., Hotta H., Yamamura H., Inatome R., Yanagi S.
    EMBO J. 25:3618-3626(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION BY MARCH5, INTERACTION WITH MARCH5.
  18. "MARCH-V is a novel mitofusin 2- and Drp1-binding protein able to change mitochondrial morphology."
    Nakamura N., Kimura Y., Tokuda M., Honda S., Hirose S.
    EMBO Rep. 7:1019-1022(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION BY MARCH5, INTERACTION WITH MARCH5.
  19. "Inhibiting the mitochondrial fission machinery does not prevent Bax/Bak-dependent apoptosis."
    Parone P.A., James D.I., Da Cruz S., Mattenberger Y., Donze O., Barja F., Martinou J.C.
    Mol. Cell. Biol. 26:7397-7408(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  20. "Mitotic phosphorylation of dynamin-related GTPase Drp1 participates in mitochondrial fission."
    Taguchi N., Ishihara N., Jofuku A., Oka T., Mihara K.
    J. Biol. Chem. 282:11521-11529(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, FUNCTION.
  21. "Cyclic AMP-dependent protein kinase phosphorylation of Drp1 regulates its GTPase activity and mitochondrial morphology."
    Chang C.R., Blackstone C.
    J. Biol. Chem. 282:21583-21587(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-637, FUNCTION, SUBUNIT, MUTAGENESIS OF SER-637.
  22. "The mitochondrial E3 ubiquitin ligase MARCH5 is required for Drp1 dependent mitochondrial division."
    Karbowski M., Neutzner A., Youle R.J.
    J. Cell Biol. 178:71-84(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  23. Cited for: FUNCTION, VARIANT EMPF ASP-395, CHARACTERIZATION OF VARIANT EMPF ASP-395.
  24. "CaM kinase I alpha-induced phosphorylation of Drp1 regulates mitochondrial morphology."
    Han X.J., Lu Y.F., Li S.A., Kaitsuka T., Sato Y., Tomizawa K., Nairn A.C., Takei K., Matsui H., Matsushita M.
    J. Cell Biol. 182:573-585(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-637, FUNCTION, INTERACTION WITH FIS1, MUTAGENESIS OF SER-637.
  25. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-616, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  26. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-548; SER-607 AND SER-616, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  27. Cited for: PHOSPHORYLATION AT SER-616 AND SER-637, INTERACTION WITH PPP3CA, DEPHOSPHORYLATION, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-616 AND SER-637.
  28. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  29. "MAPL is a new mitochondrial SUMO E3 ligase that regulates mitochondrial fission."
    Braschi E., Zunino R., McBride H.M.
    EMBO Rep. 10:748-754(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION BY MUL1.
  30. "SUMOylation of the mitochondrial fission protein Drp1 occurs at multiple nonconsensus sites within the B domain and is linked to its activity cycle."
    Figueroa-Romero C., Iniguez-Lluhi J.A., Stadler J., Chang C.R., Arnoult D., Keller P.J., Hong Y., Blackstone C., Feldman E.L.
    FASEB J. 23:3917-3927(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-532; LYS-535; LYS-558; LYS-568; LYS-594; LYS-597; LYS-606 AND LYS-608, INTERACTION WITH UBE2I, FUNCTION, MUTAGENESIS OF LYS-38; LYS-532; LYS-535; LYS-558; LYS-568; LYS-594; LYS-597; LYS-606 AND LYS-608.
  31. "Translocation of SenP5 from the nucleoli to the mitochondria modulates DRP1-dependent fission during mitosis."
    Zunino R., Braschi E., Xu L., McBride H.M.
    J. Biol. Chem. 284:17783-17795(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION, DESUMOYLATION, FUNCTION.
  32. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-616, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  33. "S-nitrosylation of Drp1 mediates beta-amyloid-related mitochondrial fission and neuronal injury."
    Cho D.H., Nakamura T., Fang J., Cieplak P., Godzik A., Gu Z., Lipton S.A.
    Science 324:102-105(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: S-NITROSYLATION AT CYS-644, FUNCTION, ASSOCIATION WITH ALZHEIMER DISEASE, MUTAGENESIS OF CYS-300; CYS-345; CYS-361; CYS-367; CYS-431; CYS-446; CYS-470; CYS-505 AND CYS-644.
  34. "Dynamin-like protein 1 at the Golgi complex: A novel component of the sorting/targeting machinery en route to the plasma membrane."
    Bonekamp N.A., Vormund K., Jacob R., Schrader M.
    Exp. Cell Res. 316:3454-3467(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE FUNCTION, SUBCELLULAR LOCATION.
  35. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-616, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  36. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  37. "MiD49 and MiD51, new components of the mitochondrial fission machinery."
    Palmer C.S., Osellame L.D., Laine D., Koutsopoulos O.S., Frazier A.E., Ryan M.T.
    EMBO Rep. 12:565-573(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MIEF2 AND MIEF1.
  38. "Human MIEF1 recruits Drp1 to mitochondrial outer membranes and promotes mitochondrial fusion rather than fission."
    Zhao J., Liu T., Jin S., Wang X., Qu M., Uhlen P., Tomilin N., Shupliakov O., Lendahl U., Nister M.
    EMBO J. 30:2762-2778(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MIEF1.
  39. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-616, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  40. "The mitochondrial phosphatase PGAM5 functions at the convergence point of multiple necrotic death pathways."
    Wang Z., Jiang H., Chen S., Du F., Wang X.
    Cell 148:228-243(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PGAM5, SUBCELLULAR LOCATION.
  41. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  42. "MiD49 and MiD51 can act independently of Mff and Fis1 in Drp1 recruitment and are specific for mitochondrial fission."
    Palmer C.S., Elgass K.D., Parton R.G., Osellame L.D., Stojanovski D., Ryan M.T.
    J. Biol. Chem. 288:27584-27593(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  43. "Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial fission."
    Loson O.C., Song Z., Chen H., Chan D.C.
    Mol. Biol. Cell 24:659-667(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MIEF2 AND MIEF1, PHOSPHORYLATION AT SER-637, MUTAGENESIS OF SER-637.
  44. "A Bcl-xL-Drp1 complex regulates synaptic vesicle membrane dynamics during endocytosis."
    Li H., Alavian K.N., Lazrove E., Mehta N., Jones A., Zhang P., Licznerski P., Graham M., Uo T., Guo J., Rahner C., Duman R.S., Morrison R.S., Jonas E.A.
    Nat. Cell Biol. 15:773-785(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BCL2L1.
  45. "Interchangeable adaptors regulate mitochondrial dynamin assembly for membrane scission."
    Koirala S., Guo Q., Kalia R., Bui H.T., Eckert D.M., Frost A., Shaw J.M.
    Proc. Natl. Acad. Sci. U.S.A. 110:E1342-E1351(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MIEF2, SUBUNIT.
  46. "Structural insights into oligomerization and mitochondrial remodelling of dynamin 1-like protein."
    Frohlich C., Grabiger S., Schwefel D., Faelber K., Rosenbaum E., Mears J., Rocks O., Daumke O.
    EMBO J. 32:1280-1292(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.48 ANGSTROMS), FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF 401-GLY--PRO-404; GLU-490 AND LYS-668, LIPID-BINDING.
  47. "Functional mapping of human dynamin-1-like GTPase domain based on x-ray structure analyses."
    Wenger J., Klinglmayr E., Frohlich C., Eibl C., Gimeno A., Hessenberger M., Puehringer S., Daumke O., Goettig P.
    PLoS ONE 8:E71835-E71835(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-327 AND 711-736 IN COMPLEX WITH GTP ANALOGS, CATALYTIC ACTIVITY, MUTAGENESIS OF GLN-34; LYS-38; SER-39; THR-59; ASP-146; GLY-149; LYS-216 AND ASP-218, ENZYME REGULATION, SUBUNIT.

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 historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: February 6, 2007
Last modified: September 3, 2014
This is version 127 of the entry and version 2 of the sequence. [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

External Data

Dasty 3

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