Dynamin 1

PDB rendering based on 1dyn.
Symbols DNM1; DNM
External IDs OMIM602377 MGI107384 HomoloGene123905 GeneCards: DNM1 Gene
EC number
RNA expression pattern
PBB GE DNM1 215116 s at tn.png
More reference expression data
Species Human Mouse
Entrez 1759 13429
Ensembl ENSG00000106976 ENSMUSG00000026825
UniProt Q05193 Q6PDM5
RefSeq (mRNA) NM_001005336.1 NM_010065.2
RefSeq (protein) NP_001005336.1 NP_034195.2
Location (UCSC) Chr 9:
130.97 – 131.02 Mb
Chr 2:
32.16 – 32.21 Mb
PubMed search [1] [2]

Dynamin-1 is a protein that in humans is encoded by the DNM1 gene.[1][2]

This gene encodes a member of the dynamin subfamily of GTP-binding proteins. The encoded protein possesses unique mechanochemical properties used to tubulate and sever membranes, and is involved in clathrin-mediated endocytosis and other vesicular trafficking processes. Actin and other cytoskeletal proteins act as binding partners for the encoded protein, which can also self-assemble leading to stimulation of GTPase activity. More than sixty highly conserved copies of the 3' region of this gene are found elsewhere in the genome, particularly on chromosomes Y and 15. Alternatively spliced transcript variants encoding different isoforms have been described.[3]


DNM1 has been shown to interact with Amphiphysin,[4][5][6][7][8] FNBP1,[9] NCK1,[10] PACSIN1,[9][11] Grb2[12][13] and SH3GL2.[4][14]


  1. ^ Obar RA, Collins CA, Hammarback JA, Shpetner HS, Vallee RB (Oct 1990). "Molecular cloning of the microtubule-associated mechanochemical enzyme dynamin reveals homology with a new family of GTP-binding proteins". Nature 347 (6290): 256–61. doi:10.1038/347256a0. PMID 2144893. 
  2. ^ Newman-Smith ED, Shurland DL, van der Bliek AM (Jul 1997). "Assignment of the dynamin-1 gene (DNM1) to human chromosome 9q34 by fluorescence in situ hybridization and somatic cell hybrid analysis". Genomics 41 (2): 286–9. doi:10.1006/geno.1996.4596. PMID 9143509. 
  3. ^ "Entrez Gene: DNM1 dynamin 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1759. 
  4. ^ a b Micheva, K D; Kay B K, McPherson P S (Oct. 1997). "Synaptojanin forms two separate complexes in the nerve terminal. Interactions with endophilin and amphiphysin". J. Biol. Chem. (UNITED STATES) 272 (43): 27239–45. doi:10.1074/jbc.272.43.27239. ISSN 0021-9258. PMID 9341169. 
  5. ^ Wigge, P; Köhler K, Vallis Y, Doyle C A, Owen D, Hunt S P, McMahon H T (Oct. 1997). "Amphiphysin heterodimers: potential role in clathrin-mediated endocytosis". Mol. Biol. Cell (UNITED STATES) 8 (10): 2003–15. ISSN 1059-1524. PMC 25662. PMID 9348539. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=25662. 
  6. ^ McMahon, H T; Wigge P, Smith C (Aug. 1997). "Clathrin interacts specifically with amphiphysin and is displaced by dynamin". FEBS Lett. (NETHERLANDS) 413 (2): 319–22. doi:10.1016/S0014-5793(97)00928-9. ISSN 0014-5793. PMID 9280305. 
  7. ^ Chen-Hwang, Mo-Chou; Chen Huey-Ru, Elzinga Marshall, Hwang Yu-Wen (May. 2002). "Dynamin is a minibrain kinase/dual specificity Yak1-related kinase 1A substrate". J. Biol. Chem. (United States) 277 (20): 17597–604. doi:10.1074/jbc.M111101200. ISSN 0021-9258. PMID 11877424. 
  8. ^ Grabs, D; Slepnev V I, Songyang Z, David C, Lynch M, Cantley L C, De Camilli P (May. 1997). "The SH3 domain of amphiphysin binds the proline-rich domain of dynamin at a single site that defines a new SH3 binding consensus sequence". J. Biol. Chem. (UNITED STATES) 272 (20): 13419–25. doi:10.1074/jbc.272.20.13419. ISSN 0021-9258. PMID 9148966. 
  9. ^ a b Kamioka, Yuji; Fukuhara Shigetomo, Sawa Hirofumi, Nagashima Kazuo, Masuda Michitaka, Matsuda Michiyuki, Mochizuki Naoki (Sep. 2004). "A novel dynamin-associating molecule, formin-binding protein 17, induces tubular membrane invaginations and participates in endocytosis". J. Biol. Chem. (United States) 279 (38): 40091–9. doi:10.1074/jbc.M404899200. ISSN 0021-9258. PMID 15252009. 
  10. ^ Wunderlich, L; Faragó A, Buday L (Jan. 1999). "Characterization of interactions of Nck with Sos and dynamin". Cell. Signal. (ENGLAND) 11 (1): 25–9. doi:10.1016/S0898-6568(98)00027-8. ISSN 0898-6568. PMID 10206341. 
  11. ^ Modregger, J; Ritter B, Witter B, Paulsson M, Plomann M (Dec. 2000). "All three PACSIN isoforms bind to endocytic proteins and inhibit endocytosis". J. Cell. Sci. (ENGLAND) 113 Pt 24: 4511–21. ISSN 0021-9533. PMID 11082044. 
  12. ^ Miki, H; Miura K, Matuoka K, Nakata T, Hirokawa N, Orita S, Kaibuchi K, Takai Y, Takenawa T (Feb. 1994). "Association of Ash/Grb-2 with dynamin through the Src homology 3 domain". J. Biol. Chem. (UNITED STATES) 269 (8): 5489–92. ISSN 0021-9258. PMID 8119878. 
  13. ^ Sastry, L; Cao T, King C R (Jan. 1997). "Multiple Grb2-protein complexes in human cancer cells". Int. J. Cancer (UNITED STATES) 70 (2): 208–13. doi:10.1002/(SICI)1097-0215(19970117)70:2<208::AID-IJC12>3.0.CO;2-E. ISSN 0020-7136. PMID 9009162. 
  14. ^ Modregger, Jan; Schmidt Anne A, Ritter Brigitte, Huttner Wieland B, Plomann Markus (Feb. 2003). "Characterization of Endophilin B1b, a brain-specific membrane-associated lysophosphatidic acid acyl transferase with properties distinct from endophilin A1". J. Biol. Chem. (United States) 278 (6): 4160–7. doi:10.1074/jbc.M208568200. ISSN 0021-9258. PMID 12456676. 

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