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Q8K1M6

- DNM1L_MOUSE

UniProt

Q8K1M6 - DNM1L_MOUSE

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Protein

Dynamin-1-like protein

Gene

Dnm1l

Organism
Mus musculus (Mouse)
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.5 Publications

Catalytic activityi

GTP + H2O = GDP + phosphate.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi32 – 398GTPBy similarity
Nucleotide bindingi152 – 1565GTPBy similarity
Nucleotide bindingi221 – 2244GTPBy similarity

GO - Molecular functioni

  1. GTPase activity Source: UniProtKB
  2. GTP binding Source: UniProtKB-KW
  3. lipid binding Source: UniProtKB-KW
  4. protein homodimerization activity Source: UniProtKB

GO - Biological processi

  1. dynamin polymerization involved in mitochondrial fission Source: UniProtKB
  2. endocytosis Source: UniProtKB-KW
  3. GTP catabolic process Source: UniProtKB
  4. membrane fission involved in mitochondrial fission Source: Ensembl
  5. membrane fusion Source: Ensembl
  6. mitochondrial fission Source: UniProtKB
  7. mitochondrial fragmentation involved in apoptotic process Source: Ensembl
  8. mitochondrion morphogenesis Source: Ensembl
  9. necroptotic process Source: UniProtKB
  10. peroxisome fission Source: UniProtKB
  11. positive regulation of apoptotic process Source: Ensembl
  12. positive regulation of intrinsic apoptotic signaling pathway Source: Ensembl
  13. positive regulation of protein secretion Source: Ensembl
  14. positive regulation of release of cytochrome c from mitochondria Source: Ensembl
  15. protein homotetramerization Source: Ensembl
  16. protein localization to mitochondrion Source: MGI
  17. regulation of peroxisome organization Source: Ensembl
  18. regulation of protein oligomerization Source: Ensembl
  19. release of cytochrome c from mitochondria Source: Ensembl
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_207035. Apoptotic execution phase.

Names & Taxonomyi

Protein namesi
Recommended name:
Dynamin-1-like protein (EC:3.6.5.5)
Alternative name(s):
Dynamin family member proline-rich carboxyl-terminal domain less
Short name:
Dymple
Dynamin-related protein 1
Gene namesi
Name:Dnm1l
Synonyms:Drp1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 16

Organism-specific databases

MGIiMGI:1921256. Dnm1l.

Subcellular locationi

Cytoplasmcytosol. Golgi apparatus By similarity. Endomembrane system; Peripheral membrane protein. Mitochondrion outer membrane; Peripheral membrane protein. Peroxisome By similarity. 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. 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 (By similarity). Recruited to the mitochondrial outer membrane by interaction with MIEF1. Binds to phospholipid membranes.By similarity

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. coated pit Source: UniProtKB-KW
  3. cytoplasmic vesicle Source: UniProtKB-KW
  4. cytosol Source: UniProtKB
  5. Golgi apparatus Source: UniProtKB-KW
  6. microtubule Source: Ensembl
  7. mitochondrial outer membrane Source: MGI
  8. mitochondrion Source: UniProtKB
  9. perinuclear region of cytoplasm Source: Ensembl
  10. peroxisome Source: UniProtKB
  11. synapse Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Coated pit, Cytoplasm, Cytoplasmic vesicle, Golgi apparatus, Membrane, Mitochondrion, Mitochondrion outer membrane, Peroxisome, Synapse

Pathology & Biotechi

Disruption phenotypei

Mutant mice show severe developmental abnormalities and die between 10.5 and 12.5 dpc. Compared to wild-type littermates, mutant embryos at 9.5-11.5 dpc have a significantly smaller body size, pulsing, but less developed cardiac structures, a poorly developed liver and a thinner neural tube cell layer. They lack trophoblastic giant cell layer in the placenta. Primary cultures of mutant neuronal cells have severe defects in synapse formation and high sensitivity to Ca2+-dependent apoptosis. Within cerebellar neurons, Purkinje cells are particularly sensitive to Dnm1l ablation. Conditional knockout in postmitotic Purkinje cells leads to 40% neuronal degeneration after 3 months and 90% after 6 months.3 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi59 – 591T → A: Abolishes GTP hydrolysis. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 742742Dynamin-1-like proteinPRO_0000206567Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Cross-linki538 – 538Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Cross-linki541 – 541Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Cross-linki564 – 564Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Cross-linki574 – 574Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Glycosylationi591 – 5911O-linked (GlcNAc)By similarity
Glycosylationi592 – 5921O-linked (GlcNAc)By similarity
Cross-linki600 – 600Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei603 – 6031N6-acetyllysine; alternate1 Publication
Cross-linki603 – 603Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki612 – 612Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei613 – 6131PhosphoserineBy similarity
Cross-linki614 – 614Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei622 – 6221Phosphoserine; by CDK1By similarity
Modified residuei643 – 6431Phosphoserine; by CAMK1 and PKABy similarity
Modified residuei650 – 6501S-nitrosocysteineBy similarity

Post-translational modificationi

Phosphorylation/dephosphorylation events on two sites near the GED domain regulate mitochondrial fission. Phosphorylation on Ser-643 inhibits mitochondrial fission probably through preventing intramolecular interaction. Dephosphorylated on this site by PPP3CA which promotes mitochondrial fission. Phosphorylation on Ser-622 also promotes mitochondrial fission (By similarity).By similarity
Sumoylated on various lysine residues within the B domain, probably by MUL1. Sumoylation positively regulates mitochondrial fission. Desumoylated by SENP5 during G2/M transition of mitosis. Appears to be linked to its catalytic activity (By similarity).By similarity
S-nitrosylation increases DNM1L dimerization, mitochondrial fission and causes neuronal damage.By similarity
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-643 (By similarity).By similarity

Keywords - PTMi

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

Proteomic databases

MaxQBiQ8K1M6.
PaxDbiQ8K1M6.
PRIDEiQ8K1M6.

PTM databases

PhosphoSiteiQ8K1M6.

Expressioni

Tissue specificityi

Expressed in the cerebellum and in several regions of the cerebrum and diencephalon. Strongly expressed in the cerebellar Purkinje cells and in the pontile giant neurons.1 Publication

Gene expression databases

BgeeiQ8K1M6.
CleanExiMM_DNM1L.
ExpressionAtlasiQ8K1M6. baseline and differential.
GenevestigatoriQ8K1M6.

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. Interacts with PGAM5; this interaction leads to dephosphorylation at Ser-656 and activation of GTPase activity and eventually to mitochondria fragmentation (By similarity). Interacts with MIEF1; this regulates GTP hydrolysis and DNM1L oligomerization.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Lrrk2Q5S0064EBI-2365792,EBI-2693710

Protein-protein interaction databases

BioGridi216417. 6 interactions.
DIPiDIP-54818N.
IntActiQ8K1M6. 6 interactions.
MINTiMINT-1858955.

Structurei

3D structure databases

ProteinModelPortaliQ8K1M6.
SMRiQ8K1M6. Positions 1-510, 648-735.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 308287Dynamin-type GAdd
BLAST
Domaini650 – 74192GEDPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 349349GTPase domainBy similarityAdd
BLAST
Regioni1 – 349349N-terminal dimerization domainBy similarityAdd
BLAST
Regioni350 – 495146Middle domainBy similarityAdd
BLAST
Regioni454 – 691238Interaction with GSK3BBy similarityAdd
BLAST
Regioni454 – 654201Interaction with GSK3BBy similarityAdd
BLAST
Regioni508 – 57568B domainBy similarityAdd
BLAST
Regioni548 – 742195C-terminal dimerization domainBy similarityAdd
BLAST
Regioni660 – 67415Important for homodimerizationBy similarityAdd
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.By similarity

Sequence similaritiesi

Contains 1 GED domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0699.
GeneTreeiENSGT00760000119213.
HOGENOMiHOG000161068.
HOVERGENiHBG107833.
InParanoidiQ8K1M6.
KOiK17065.
OMAiSANTDMA.
OrthoDBiEOG7GJ6CB.
PhylomeDBiQ8K1M6.
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 (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8K1M6) [UniParc]FASTAAdd to Basket

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

        10         20         30         40         50
MEALIPVINK LQDVFNTVGA DIIQLPQIVV VGTQSSGKSS VLESLVGRDL
60 70 80 90 100
LPRGTGVVTR RPLILQLVHV SPEDKRKTTG EENGKFQSWR VEAEEWGKFL
110 120 130 140 150
HTKNKLYTDF DEIRQEIENE TERISGNNKG VSPEPIHLKV FSPNVVNLTL
160 170 180 190 200
VDLPGMTKVP VGDQPKDIEL QIRELILRFI SNPNSIILAV TAANTDMATS
210 220 230 240 250
EALKISREVD PDGRRTLAVI TKLDLMDAGT DAMDVLMGRV IPVKLGIIGV
260 270 280 290 300
VNRSQLDINN KKSVTDSIRD EYAFLQKKYP SLANRNGTKY LARTLNRLLM
310 320 330 340 350
HHIRDCLPEL KTRINVLAAQ YQSLLNSYGE PVDDKSATLL QLITKFATEY
360 370 380 390 400
CNTIEGTAKY IETSELCGGA RICYIFHETF GRTLESVDPL GGLNTIDILT
410 420 430 440 450
AIRNATGPRP ALFVPEVSFE LLVKRQIKRL EEPSLRCVEL VHEEMQRIIQ
460 470 480 490 500
HCSNYSTQEL LRFPKLHDAI VEVVTCLLRK RLPVTNEMVH NLVAIELAYI
510 520 530 540 550
NTKHPDFADA CGLMNNNIEE QRRNRLAREL PSAGSRDKSS KVPSALAPAS
560 570 580 590 600
QEPPPAASAE ADGKLIQDNR RETKNVPSAG GGIGDGGQEP TTGNWRGMLK
610 620 630 640 650
TSKAEELLAE EKSKPIPIMP ASPQKGHAVN LLDVPVPVAR KLSAREQRDC
660 670 680 690 700
EVIERLIKSY FLIVRKNIQD SVPKAVMHFL VNHVKDTLQS ELVGQLYKSS
710 720 730 740
LLDDLLTESE DMAQRRKEAA DMLKALQGAS QIIAEIRETH LW

Note: No experimental confirmation available.

Length:742
Mass (Da):82,658
Last modified:May 10, 2005 - v2
Checksum:i5A8679B61A444847
GO
Isoform 2 (identifier: Q8K1M6-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     539-564: Missing.

Show »
Length:716
Mass (Da):80,212
Checksum:i3C922A7A135B9A37
GO
Isoform 3 (identifier: Q8K1M6-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     85-90: Missing.
     539-575: Missing.

Show »
Length:699
Mass (Da):78,011
Checksum:i68ED85D93914B4DC
GO
Isoform 4 (identifier: Q8K1M6-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-104: Missing.
     105-105: K → M
     539-564: Missing.

Show »
Length:612
Mass (Da):68,701
Checksum:iC5D0BCE4B4622502
GO
Isoform 5 (identifier: Q8K1M6-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     85-90: Missing.
     214-227: RRTLAVITKLDLMD → KGRCLYLMDVDLQW
     228-742: Missing.

Show »
Length:221
Mass (Da):24,488
Checksum:i29C66A3A04924F55
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti165 – 1651P → L in BAC06576. (PubMed:14592431)Curated
Sequence conflicti320 – 3201Q → R in BAC06576. (PubMed:14592431)Curated
Sequence conflicti519 – 5191E → A in BAC34640. (PubMed:16141072)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 104104Missing in isoform 4. 1 PublicationVSP_013689Add
BLAST
Alternative sequencei85 – 906Missing in isoform 3 and isoform 5. 2 PublicationsVSP_013690
Alternative sequencei105 – 1051K → M in isoform 4. 1 PublicationVSP_013691
Alternative sequencei214 – 22714RRTLA…LDLMD → KGRCLYLMDVDLQW in isoform 5. CuratedVSP_013692Add
BLAST
Alternative sequencei228 – 742515Missing in isoform 5. CuratedVSP_013693Add
BLAST
Alternative sequencei539 – 57537Missing in isoform 3. 2 PublicationsVSP_013694Add
BLAST
Alternative sequencei539 – 56426Missing in isoform 2 and isoform 4. 2 PublicationsVSP_013695Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB079133 mRNA. Translation: BAC06576.1.
AK051443 mRNA. Translation: BAC34640.1.
AK080871 mRNA. Translation: BAC38054.1.
BC027538 mRNA. Translation: AAH27538.1.
BC040777 mRNA. Translation: AAH40777.1.
BC079635 mRNA. Translation: AAH79635.1.
CF914619 mRNA. No translation available.
CCDSiCCDS27984.1. [Q8K1M6-3]
CCDS70689.1. [Q8K1M6-2]
RefSeqiNP_001021118.1. NM_001025947.2. [Q8K1M6-3]
NP_001263269.1. NM_001276340.1. [Q8K1M6-2]
NP_001263270.1. NM_001276341.1. [Q8K1M6-4]
NP_690029.2. NM_152816.3.
XP_006522694.1. XM_006522631.1. [Q8K1M6-1]
UniGeneiMm.218820.

Genome annotation databases

EnsembliENSMUST00000023477; ENSMUSP00000023477; ENSMUSG00000022789. [Q8K1M6-3]
ENSMUST00000115749; ENSMUSP00000111415; ENSMUSG00000022789. [Q8K1M6-2]
GeneIDi74006.
KEGGimmu:74006.
UCSCiuc007yij.1. mouse. [Q8K1M6-1]
uc007yik.1. mouse. [Q8K1M6-4]
uc007yim.1. mouse. [Q8K1M6-3]
uc007yin.1. mouse. [Q8K1M6-2]
uc007yio.1. mouse. [Q8K1M6-5]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB079133 mRNA. Translation: BAC06576.1 .
AK051443 mRNA. Translation: BAC34640.1 .
AK080871 mRNA. Translation: BAC38054.1 .
BC027538 mRNA. Translation: AAH27538.1 .
BC040777 mRNA. Translation: AAH40777.1 .
BC079635 mRNA. Translation: AAH79635.1 .
CF914619 mRNA. No translation available.
CCDSi CCDS27984.1. [Q8K1M6-3 ]
CCDS70689.1. [Q8K1M6-2 ]
RefSeqi NP_001021118.1. NM_001025947.2. [Q8K1M6-3 ]
NP_001263269.1. NM_001276340.1. [Q8K1M6-2 ]
NP_001263270.1. NM_001276341.1. [Q8K1M6-4 ]
NP_690029.2. NM_152816.3.
XP_006522694.1. XM_006522631.1. [Q8K1M6-1 ]
UniGenei Mm.218820.

3D structure databases

ProteinModelPortali Q8K1M6.
SMRi Q8K1M6. Positions 1-510, 648-735.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 216417. 6 interactions.
DIPi DIP-54818N.
IntActi Q8K1M6. 6 interactions.
MINTi MINT-1858955.

Chemistry

ChEMBLi CHEMBL2331072.

PTM databases

PhosphoSitei Q8K1M6.

Proteomic databases

MaxQBi Q8K1M6.
PaxDbi Q8K1M6.
PRIDEi Q8K1M6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000023477 ; ENSMUSP00000023477 ; ENSMUSG00000022789 . [Q8K1M6-3 ]
ENSMUST00000115749 ; ENSMUSP00000111415 ; ENSMUSG00000022789 . [Q8K1M6-2 ]
GeneIDi 74006.
KEGGi mmu:74006.
UCSCi uc007yij.1. mouse. [Q8K1M6-1 ]
uc007yik.1. mouse. [Q8K1M6-4 ]
uc007yim.1. mouse. [Q8K1M6-3 ]
uc007yin.1. mouse. [Q8K1M6-2 ]
uc007yio.1. mouse. [Q8K1M6-5 ]

Organism-specific databases

CTDi 10059.
MGIi MGI:1921256. Dnm1l.

Phylogenomic databases

eggNOGi COG0699.
GeneTreei ENSGT00760000119213.
HOGENOMi HOG000161068.
HOVERGENi HBG107833.
InParanoidi Q8K1M6.
KOi K17065.
OMAi SANTDMA.
OrthoDBi EOG7GJ6CB.
PhylomeDBi Q8K1M6.
TreeFami TF352031.

Enzyme and pathway databases

Reactomei REACT_207035. Apoptotic execution phase.

Miscellaneous databases

NextBioi 339508.
PROi Q8K1M6.
SOURCEi Search...

Gene expression databases

Bgeei Q8K1M6.
CleanExi MM_DNM1L.
ExpressionAtlasi Q8K1M6. baseline and differential.
Genevestigatori Q8K1M6.

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. "Stage-specific enhanced expression of mitochondrial fusion and fission factors during spermatogenesis in rat testis."
    Honda S., Hirose S.
    Biochem. Biophys. Res. Commun. 311:424-432(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Osteoclast.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Strain: C57BL/6J.
    Tissue: Adipose tissue and Spinal ganglion.
  3. "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] (ISOFORMS 3 AND 4).
    Strain: C57BL/6.
    Tissue: Brain, Mammary gland and Thymus.
  4. "Construction of long-transcript enriched cDNA libraries from submicrogram amounts of total RNAs by a universal PCR amplification method."
    Piao Y., Ko N.T., Lim M.K., Ko M.S.H.
    Genome Res. 11:1553-1558(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 448-659 (ISOFORM 1).
  5. Lubec G., Klug S.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 626-640 AND 725-737, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Hippocampus.
  6. "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: TISSUE SPECIFICITY.
  7. "The dynamin-related GTPase Drp1 is required for embryonic and brain development in mice."
    Wakabayashi J., Zhang Z., Wakabayashi N., Tamura Y., Fukaya M., Kensler T.W., Iijima M., Sesaki H.
    J. Cell Biol. 186:805-816(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, CONDITIONAL KNOCKOUT IN PURKINJE CELLS.
  8. "Mitochondrial fission factor Drp1 is essential for embryonic development and synapse formation in mice."
    Ishihara N., Nomura M., Jofuku A., Kato H., Suzuki S.O., Masuda K., Otera H., Nakanishi Y., Nonaka I., Goto Y., Taguchi N., Morinaga H., Maeda M., Takayanagi R., Yokota S., Mihara K.
    Nat. Cell Biol. 11:958-966(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  9. "Mitochondrial division ensures the survival of postmitotic neurons by suppressing oxidative damage."
    Kageyama Y., Zhang Z., Roda R., Fukaya M., Wakabayashi J., Wakabayashi N., Kensler T.W., Reddy P.H., Iijima M., Sesaki H.
    J. Cell Biol. 197:535-551(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, CONDITIONAL KNOCKOUT IN PURKINJE CELLS.
  10. "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, SUBCELLULAR LOCATION.
  11. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-603, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  12. "The mitochondrial fission receptor Mid51 requires ADP as a cofactor."
    Loson O.C., Liu R., Rome M.E., Meng S., Kaiser J.T., Shan S.O., Chan D.C.
    Structure 22:367-377(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-59, CATALYTIC ACTIVITY, INTERACTION WITH MIEF1.

Entry informationi

Entry nameiDNM1L_MOUSE
AccessioniPrimary (citable) accession number: Q8K1M6
Secondary accession number(s): Q8BNQ5
, Q8BQ64, Q8CGD0, Q8K1A1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: May 10, 2005
Last modified: October 29, 2014
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3