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Q8K1M6

- DNM1L_MOUSE

UniProt

Q8K1M6 - DNM1L_MOUSE

Protein

Dynamin-1-like protein

Gene

Dnm1l

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 2 (10 May 2005)
      Previous versions | rss
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    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 binding Source: IntAct
    5. 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. mitochondrial fission Source: UniProtKB
    5. necroptotic process Source: UniProtKB
    6. peroxisome fission Source: UniProtKB
    7. protein localization to mitochondrion Source: MGI

    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-SubCell
    3. cytosol Source: UniProtKB
    4. Golgi apparatus Source: UniProtKB-SubCell
    5. mitochondrial outer membrane Source: MGI
    6. mitochondrion Source: UniProtKB
    7. peroxisome Source: UniProtKB
    8. synaptic vesicle membrane Source: UniProtKB-SubCell

    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

    ArrayExpressiQ8K1M6.
    BgeeiQ8K1M6.
    CleanExiMM_DNM1L.
    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.
    GeneTreeiENSGT00740000115284.
    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: Q8K1M6-1) [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

    MEALIPVINK LQDVFNTVGA DIIQLPQIVV VGTQSSGKSS VLESLVGRDL    50
    LPRGTGVVTR RPLILQLVHV SPEDKRKTTG EENGKFQSWR VEAEEWGKFL 100
    HTKNKLYTDF DEIRQEIENE TERISGNNKG VSPEPIHLKV FSPNVVNLTL 150
    VDLPGMTKVP VGDQPKDIEL QIRELILRFI SNPNSIILAV TAANTDMATS 200
    EALKISREVD PDGRRTLAVI TKLDLMDAGT DAMDVLMGRV IPVKLGIIGV 250
    VNRSQLDINN KKSVTDSIRD EYAFLQKKYP SLANRNGTKY LARTLNRLLM 300
    HHIRDCLPEL KTRINVLAAQ YQSLLNSYGE PVDDKSATLL QLITKFATEY 350
    CNTIEGTAKY IETSELCGGA RICYIFHETF GRTLESVDPL GGLNTIDILT 400
    AIRNATGPRP ALFVPEVSFE LLVKRQIKRL EEPSLRCVEL VHEEMQRIIQ 450
    HCSNYSTQEL LRFPKLHDAI VEVVTCLLRK RLPVTNEMVH NLVAIELAYI 500
    NTKHPDFADA CGLMNNNIEE QRRNRLAREL PSAGSRDKSS KVPSALAPAS 550
    QEPPPAASAE ADGKLIQDNR RETKNVPSAG GGIGDGGQEP TTGNWRGMLK 600
    TSKAEELLAE EKSKPIPIMP ASPQKGHAVN LLDVPVPVAR KLSAREQRDC 650
    EVIERLIKSY FLIVRKNIQD SVPKAVMHFL VNHVKDTLQS ELVGQLYKSS 700
    LLDDLLTESE DMAQRRKEAA DMLKALQGAS QIIAEIRETH LW 742

    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 ENSGT00740000115284.
    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

    ArrayExpressi Q8K1M6.
    Bgeei Q8K1M6.
    CleanExi MM_DNM1L.
    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

    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 1, 2014
    This is version 110 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