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O00429

- DNM1L_HUMAN

UniProt

O00429 - DNM1L_HUMAN

Protein

Dynamin-1-like protein

Gene

DNM1L

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 2 (06 Feb 2007)
      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.
    Isoform 1 and isoform 4 inhibit peroxisomal division when overexpressed.

    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

    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.

    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. membrane Source: UniProtKB
    8. microtubule Source: UniProtKB
    9. mitochondrial outer membrane Source: UniProtKB
    10. mitochondrion Source: UniProtKB
    11. perinuclear region of cytoplasm Source: UniProtKB
    12. peroxisome Source: UniProtKB
    13. protein complex Source: UniProtKB
    14. 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

    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.
    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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.
    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)
    Cross-linki535 – 535Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei548 – 5481Phosphoserine2 Publications
    Cross-linki558 – 558Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Cross-linki568 – 568Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    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)Curated
    Modified residuei597 – 5971N6-acetyllysine; alternateBy similarity
    Cross-linki597 – 597Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
    Cross-linki606 – 606Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)Curated
    Modified residuei607 – 6071Phosphoserine2 Publications
    Cross-linki608 – 608Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei616 – 6161Phosphoserine; by CDK17 Publications
    Modified residuei637 – 6371Phosphoserine; by CAMK1 and PKA5 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.10 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.1 Publication
    Ubiquitination by MARCH5 affects mitochondrial morphology.2 Publications
    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.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.16 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. 36 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini22 – 302281Dynamin-type GAdd
    BLAST
    Domaini644 – 73592GEDPROSITE-ProRule annotationAdd
    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.

    Sequence similaritiesi

    Contains 1 GED domain.PROSITE-ProRule annotation

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti208 – 2081R → C in AAC35283. (PubMed:9731200)Curated
    Sequence conflicti208 – 2081R → C in AAD39541. (PubMed:10749171)Curated

    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. 1 PublicationVSP_054544Add
    BLAST
    Alternative sequencei44 – 246203Missing in isoform 7. 1 PublicationVSP_054545Add
    BLAST
    Alternative sequencei83 – 831N → NDPATWKNSRHLSK in isoform 6 and isoform 8. 2 PublicationsVSP_039097
    Alternative sequencei533 – 56937Missing in isoform 3. 3 PublicationsVSP_013685Add
    BLAST
    Alternative sequencei533 – 55826Missing in isoform 2. 1 PublicationVSP_013686Add
    BLAST
    Alternative sequencei544 – 56926Missing in isoform 5. 1 PublicationVSP_013687Add
    BLAST
    Alternative sequencei559 – 56911Missing in isoform 4 and isoform 8. 2 PublicationsVSP_013688Add
    BLAST

    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. [O00429-8]
    ENST00000414834; ENSP00000404160; ENSG00000087470. [O00429-7]
    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. 36 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 . [O00429-8 ]
    ENST00000414834 ; ENSP00000404160 ; ENSG00000087470 . [O00429-7 ]
    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

    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: October 1, 2014
    This is version 128 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