Details for: DNM1L

Gene ID: 10059

Symbol: DNM1L

Ensembl ID: ENSG00000087470

Description: dynamin 1 like

Associated with

Other Information

Genular Protein ID: 2820353759

Symbol: DNM1L_HUMAN

Name: Dynamin-1-like protein

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 9348079

Title: Identification and subcellular localization of a novel mammalian dynamin-related protein homologous to yeast Vps1p and Dnm1p.

PubMed ID: 9348079

DOI: 10.1093/oxfordjournals.jbchem.a021784

PubMed ID: 9731200

Title: Human dynamin-like protein interacts with the glycogen synthase kinase 3beta.

PubMed ID: 9731200

DOI: 10.1006/bbrc.1998.9253

PubMed ID: 9570752

Title: Identification and functional characterization of a novel human protein highly related to the yeast dynamin-like GTPase Vps1p.

PubMed ID: 9570752

DOI: 10.1242/jcs.111.10.1341

PubMed ID: 10749171

Title: Differential expression of four human dynamin-like protein variants in brain tumors.

PubMed ID: 10749171

DOI: 10.1089/104454900314573

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 16541075

Title: The finished DNA sequence of human chromosome 12.

PubMed ID: 16541075

DOI: 10.1038/nature04569

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 9422767

Title: Dymple, a novel dynamin-like high molecular weight GTPase lacking a proline-rich carboxyl-terminal domain in mammalian cells.

PubMed ID: 9422767

DOI: 10.1074/jbc.273.2.1044

PubMed ID: 9472031

Title: A novel dynamin-like protein associates with cytoplasmic vesicles and tubules of the endoplasmic reticulum in mammalian cells.

PubMed ID: 9472031

DOI: 10.1083/jcb.140.4.779

PubMed ID: 9786947

Title: A human dynamin-related protein controls the distribution of mitochondria.

PubMed ID: 9786947

DOI: 10.1083/jcb.143.2.351

PubMed ID: 9915810

Title: Intermolecular and interdomain interactions of a dynamin-related GTP-binding protein, Dnm1p/Vps1p-like protein.

PubMed ID: 9915810

DOI: 10.1074/jbc.274.5.2780

PubMed ID: 11514614

Title: Dynamin-related protein Drp1 is required for mitochondrial division in mammalian cells.

PubMed ID: 11514614

DOI: 10.1091/mbc.12.8.2245

PubMed ID: 12499366

Title: Dynamin-like protein 1 is involved in peroxisomal fission.

PubMed ID: 12499366

DOI: 10.1074/jbc.m211761200

PubMed ID: 12618434

Title: The dynamin-like GTPase DLP1 is essential for peroxisome division and is recruited to peroxisomes in part by PEX11.

PubMed ID: 12618434

DOI: 10.1074/jbc.m212031200

PubMed ID: 15208300

Title: Intra- and intermolecular domain interactions of the C-terminal GTPase effector domain of the multimeric dynamin-like GTPase Drp1.

PubMed ID: 15208300

DOI: 10.1074/jbc.m404105200

PubMed ID: 16874301

Title: A novel mitochondrial ubiquitin ligase plays a critical role in mitochondrial dynamics.

PubMed ID: 16874301

DOI: 10.1038/sj.emboj.7601249

PubMed ID: 16936636

Title: MARCH-V is a novel mitofusin 2- and Drp1-binding protein able to change mitochondrial morphology.

PubMed ID: 16936636

DOI: 10.1038/sj.embor.7400790

PubMed ID: 17015472

Title: Inhibiting the mitochondrial fission machinery does not prevent Bax/Bak-dependent apoptosis.

PubMed ID: 17015472

DOI: 10.1128/mcb.02282-05

PubMed ID: 17301055

Title: Mitotic phosphorylation of dynamin-related GTPase Drp1 participates in mitochondrial fission.

PubMed ID: 17301055

DOI: 10.1074/jbc.m607279200

PubMed ID: 17553808

Title: Cyclic AMP-dependent protein kinase phosphorylation of Drp1 regulates its GTPase activity and mitochondrial morphology.

PubMed ID: 17553808

DOI: 10.1074/jbc.c700083200

PubMed ID: 17606867

Title: The mitochondrial E3 ubiquitin ligase MARCH5 is required for Drp1 dependent mitochondrial division.

PubMed ID: 17606867

DOI: 10.1083/jcb.200611064

PubMed ID: 17460227

Title: A lethal defect of mitochondrial and peroxisomal fission.

PubMed ID: 17460227

DOI: 10.1056/nejmoa064436

PubMed ID: 18695047

Title: CaM kinase I alpha-induced phosphorylation of Drp1 regulates mitochondrial morphology.

PubMed ID: 18695047

DOI: 10.1083/jcb.200802164

PubMed ID: 18088087

Title: Phosphoproteome of resting human platelets.

PubMed ID: 18088087

DOI: 10.1021/pr0704130

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 18838687

Title: Dephosphorylation by calcineurin regulates translocation of Drp1 to mitochondria.

PubMed ID: 18838687

DOI: 10.1073/pnas.0808249105

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19407830

Title: MAPL is a new mitochondrial SUMO E3 ligase that regulates mitochondrial fission.

PubMed ID: 19407830

DOI: 10.1038/embor.2009.86

PubMed ID: 19638400

Title: SUMOylation of the mitochondrial fission protein Drp1 occurs at multiple nonconsensus sites within the B domain and is linked to its activity cycle.

PubMed ID: 19638400

DOI: 10.1096/fj.09-136630

PubMed ID: 19411255

Title: Translocation of SenP5 from the nucleoli to the mitochondria modulates DRP1-dependent fission during mitosis.

PubMed ID: 19411255

DOI: 10.1074/jbc.m901902200

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 19342591

Title: S-nitrosylation of Drp1 mediates beta-amyloid-related mitochondrial fission and neuronal injury.

PubMed ID: 19342591

DOI: 10.1126/science.1171091

PubMed ID: 20688057

Title: Dynamin-like protein 1 at the Golgi complex: A novel component of the sorting/targeting machinery en route to the plasma membrane.

PubMed ID: 20688057

DOI: 10.1016/j.yexcr.2010.07.020

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21508961

Title: MiD49 and MiD51, new components of the mitochondrial fission machinery.

PubMed ID: 21508961

DOI: 10.1038/embor.2011.54

PubMed ID: 21701560

Title: Human MIEF1 recruits Drp1 to mitochondrial outer membranes and promotes mitochondrial fusion rather than fission.

PubMed ID: 21701560

DOI: 10.1038/emboj.2011.198

PubMed ID: 21822277

Title: RALA and RALBP1 regulate mitochondrial fission at mitosis.

PubMed ID: 21822277

DOI: 10.1038/ncb2310

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 22265414

Title: The mitochondrial phosphatase PGAM5 functions at the convergence point of multiple necrotic death pathways.

PubMed ID: 22265414

DOI: 10.1016/j.cell.2011.11.030

PubMed ID: 22223895

Title: Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.

PubMed ID: 22223895

DOI: 10.1074/mcp.m111.015131

PubMed ID: 23921378

Title: MiD49 and MiD51 can act independently of Mff and Fis1 in Drp1 recruitment and are specific for mitochondrial fission.

PubMed ID: 23921378

DOI: 10.1074/jbc.m113.479873

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 23283981

Title: Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial fission.

PubMed ID: 23283981

DOI: 10.1091/mbc.e12-10-0721

PubMed ID: 23792689

Title: A Bcl-xL-Drp1 complex regulates synaptic vesicle membrane dynamics during endocytosis.

PubMed ID: 23792689

DOI: 10.1038/ncb2791

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 24196833

Title: Mutations in Fis1 disrupt orderly disposal of defective mitochondria.

PubMed ID: 24196833

DOI: 10.1091/mbc.e13-09-0525

PubMed ID: 26122121

Title: Signal transducer and activator of transcription 2 deficiency is a novel disorder of mitochondrial fission.

PubMed ID: 26122121

DOI: 10.1093/brain/awv182

PubMed ID: 23530241

Title: Interchangeable adaptors regulate mitochondrial dynamin assembly for membrane scission.

PubMed ID: 23530241

DOI: 10.1073/pnas.1300855110

PubMed ID: 29478834

Title: Circadian control of DRP1 activity regulates mitochondrial dynamics and bioenergetics.

PubMed ID: 29478834

DOI: 10.1016/j.cmet.2018.01.011

PubMed ID: 32484300

Title: PINK1 phosphorylates Drp1S616 to regulate mitophagy-independent mitochondrial dynamics.

PubMed ID: 32484300

DOI: 10.15252/embr.201948686

PubMed ID: 33850055

Title: DDAH2 suppresses RLR-MAVS-mediated innate antiviral immunity by stimulating nitric oxide-activated, Drp1-induced mitochondrial fission.

PubMed ID: 33850055

DOI: 10.1126/scisignal.abc7931

PubMed ID: 23584531

Title: Structural insights into oligomerization and mitochondrial remodelling of dynamin 1-like protein.

PubMed ID: 23584531

DOI: 10.1038/emboj.2013.74

PubMed ID: 23977156

Title: Functional mapping of human dynamin-1-like GTPase domain based on x-ray structure analyses.

PubMed ID: 23977156

DOI: 10.1371/journal.pone.0071835

PubMed ID: 29899447

Title: Structural basis of mitochondrial receptor binding and constriction by DRP1.

PubMed ID: 29899447

DOI: 10.1038/s41586-018-0211-2

PubMed ID: 26604000

Title: DNM1L-related mitochondrial fission defect presenting as refractory epilepsy.

PubMed ID: 26604000

DOI: 10.1038/ejhg.2015.243

PubMed ID: 27145208

Title: A novel de novo dominant negative mutation in DNM1L impairs mitochondrial fission and presents as childhood epileptic encephalopathy.

PubMed ID: 27145208

DOI: 10.1002/ajmg.a.37721

PubMed ID: 26992161

Title: Postnatal microcephaly and pain insensitivity due to a de novo heterozygous DNM1L mutation causing impaired mitochondrial fission and function.

PubMed ID: 26992161

DOI: 10.1002/ajmg.a.37624

PubMed ID: 27301544

Title: DNM1L-related encephalopathy in infancy with Leigh syndrome-like phenotype and suppression-burst.

PubMed ID: 27301544

DOI: 10.1111/cge.12805

PubMed ID: 27328748

Title: Biallelic Mutations in DNM1L are Associated with a Slowly Progressive Infantile Encephalopathy.

PubMed ID: 27328748

DOI: 10.1002/humu.23033

PubMed ID: 28969390

Title: Mutations in DNM1L, as in OPA1, result indominant optic atrophy despite opposite effectson mitochondrial fusion and fission.

PubMed ID: 28969390

DOI: 10.1093/brain/awx219

Sequence Information:

  • Length: 736
  • Mass: 81877
  • Checksum: F9521A376B785B71
  • Sequence:
  • MEALIPVINK LQDVFNTVGA DIIQLPQIVV VGTQSSGKSS VLESLVGRDL LPRGTGIVTR 
    RPLILQLVHV SQEDKRKTTG EENGVEAEEW GKFLHTKNKL YTDFDEIRQE IENETERISG 
    NNKGVSPEPI HLKIFSPNVV NLTLVDLPGM TKVPVGDQPK DIELQIRELI LRFISNPNSI 
    ILAVTAANTD MATSEALKIS REVDPDGRRT LAVITKLDLM DAGTDAMDVL MGRVIPVKLG 
    IIGVVNRSQL DINNKKSVTD SIRDEYAFLQ KKYPSLANRN GTKYLARTLN RLLMHHIRDC 
    LPELKTRINV LAAQYQSLLN SYGEPVDDKS ATLLQLITKF ATEYCNTIEG TAKYIETSEL 
    CGGARICYIF HETFGRTLES VDPLGGLNTI DILTAIRNAT GPRPALFVPE VSFELLVKRQ 
    IKRLEEPSLR CVELVHEEMQ RIIQHCSNYS TQELLRFPKL HDAIVEVVTC LLRKRLPVTN 
    EMVHNLVAIE LAYINTKHPD FADACGLMNN NIEEQRRNRL ARELPSAVSR DKSSKVPSAL 
    APASQEPSPA ASAEADGKLI QDSRRETKNV ASGGGGVGDG VQEPTTGNWR GMLKTSKAEE 
    LLAEEKSKPI PIMPASPQKG HAVNLLDVPV PVARKLSARE QRDCEVIERL IKSYFLIVRK 
    NIQDSVPKAV MHFLVNHVKD TLQSELVGQL YKSSLLDDLL TESEDMAQRR KEAADMLKAL 
    QGASQIIAEI RETHLW

Genular Protein ID: 3884563909

Symbol: B4DYR6_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Sequence Information:

  • Length: 763
  • Mass: 85378
  • Checksum: 5981338137BA8A21
  • Sequence:
  • MACREGAGSR RARSNGCRLP RRGRRRGGRR RTVGPGPIHC RGRRALGPRV FRVMEALIPV 
    INKLQDVFNT VGADIIQLPQ IVVVGTQSSG KSSVLESLVG RDLLPRGTGI VTRRPLILQL 
    VHVSQEDKRK TTGEENGVEA EEWGKFLHTK NKLYTDFDEI RQEIENETER ISGNNKGVSP 
    EPIHLKIFSP NVVNLTLVDL PGMTKVPVGD QPKDIELQIR ELILRFISNP NSIILAVTAA 
    NTDMATSEAL KISREVDPDG RRTLAVITKL DLMDAGTDAM DVLMGRVIPV KLGIIGVVNR 
    SQLDINNKKS VTDSIRDEYA FLQKKYPSLA NRNGTKYLAR TLNRLLMHHI RDCLPELKTR 
    INVLAAQYQS LLNSYGEPVD DKSATLLQLI TKFATEYCNT IEGTAKYIET SELCGGARIC 
    YIFHETFGRT LESVDPLGGL NTIDILTAIR NATGPRPALF VPEVSFELLV KRQIKRLEEP 
    SLRCVELVHE EMQRIIQHCS NYSTQELLRF PKLHDAIVEV VTCLLRKRLP VTNEMVHNLV 
    AIELAYINTK HPDFADACGL MNNNIEEQRR NRLARELPSA VSRDKLIQDS RRETKNVASG 
    GGGAGDGVQE PTTGNWRGML KTSKAEELLA EEKSKPIPIM PASPQKGHAV NLLDVPVPVA 
    RKLSAREQRD CEVIERLIKS YFLIVRKNIQ DSVPKAVMHF LVNHVKDTLQ SELVGQLYKS 
    SLLDDLLTES EDMAQRRKEA TDMLKALQGA SQIIAEIRET HLW

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.