DNM1

DNM1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
Aliases DNM1, Dynamin-1, DNM, EIEE31, dynamin 1
External IDs MGI: 107384 HomoloGene: 123905 GeneCards: DNM1
Genetically Related Diseases
attention deficit hyperactivity disorder[1]
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez

1759

13429

Ensembl

ENSG00000106976

ENSMUSG00000026825

UniProt

Q05193

P39053

RefSeq (mRNA)

NM_001005336
NM_001288737
NM_001288738
NM_001288739
NM_004408

NM_001301737
NM_010065

RefSeq (protein)

NP_001005336.1
NP_001275666.1
NP_001275667.1
NP_001275668.1
NP_004399.2

NP_001288666.1
NP_034195.2

Location (UCSC) Chr 9: 128.2 – 128.26 Mb Chr 2: 32.31 – 32.35 Mb
PubMed search [2] [3]
Wikidata
View/Edit HumanView/Edit Mouse

Dynamin-1 is a protein that in humans is encoded by the DNM1 gene.[4][5]

Function

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.[6]

Interactions

DNM1 has been shown to interact with:

References

Wikimedia Commons has media related to Dynamin 1.
  1. ↑ "Diseases that are genetically associated with DNM1 view/edit references on wikidata".
  2. ↑ "Human PubMed Reference:".
  3. ↑ "Mouse PubMed Reference:".
  4. ↑ Obar RA, Collins CA, Hammarback JA, Shpetner HS, Vallee RB (October 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.
  5. ↑ Newman-Smith ED, Shurland DL, van der Bliek AM (July 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.
  6. ↑ "Entrez Gene: DNM1 dynamin 1".
  7. 1 2 Micheva KD, Kay BK, McPherson PS (October 1997). "Synaptojanin forms two separate complexes in the nerve terminal. Interactions with endophilin and amphiphysin". J. Biol. Chem. 272 (43): 27239–45. doi:10.1074/jbc.272.43.27239. PMID 9341169.
  8. ↑ Wigge P, Köhler K, Vallis Y, Doyle CA, Owen D, Hunt SP, McMahon HT (October 1997). "Amphiphysin heterodimers: potential role in clathrin-mediated endocytosis". Mol. Biol. Cell. 8 (10): 2003–15. doi:10.1091/mbc.8.10.2003. PMC 25662Freely accessible. PMID 9348539.
  9. ↑ McMahon HT, Wigge P, Smith C (August 1997). "Clathrin interacts specifically with amphiphysin and is displaced by dynamin". FEBS Lett. 413 (2): 319–22. doi:10.1016/s0014-5793(97)00928-9. PMID 9280305.
  10. ↑ Chen-Hwang MC, Chen HR, Elzinga M, Hwang YW (May 2002). "Dynamin is a minibrain kinase/dual specificity Yak1-related kinase 1A substrate". J. Biol. Chem. 277 (20): 17597–604. doi:10.1074/jbc.M111101200. PMID 11877424.
  11. ↑ Grabs D, Slepnev VI, Songyang Z, David C, Lynch M, Cantley LC, 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. 272 (20): 13419–25. doi:10.1074/jbc.272.20.13419. PMID 9148966.
  12. 1 2 Kamioka Y, Fukuhara S, Sawa H, Nagashima K, Masuda M, Matsuda M, Mochizuki N (September 2004). "A novel dynamin-associating molecule, formin-binding protein 17, induces tubular membrane invaginations and participates in endocytosis". J. Biol. Chem. 279 (38): 40091–9. doi:10.1074/jbc.M404899200. PMID 15252009.
  13. ↑ Miki H, Miura K, Matuoka K, Nakata T, Hirokawa N, Orita S, Kaibuchi K, Takai Y, Takenawa T (February 1994). "Association of Ash/Grb-2 with dynamin through the Src homology 3 domain". J. Biol. Chem. 269 (8): 5489–92. PMID 8119878.
  14. ↑ Sastry L, Cao T, King CR (January 1997). "Multiple Grb2-protein complexes in human cancer cells". Int. J. Cancer. 70 (2): 208–13. doi:10.1002/(sici)1097-0215(19970117)70:2<208::aid-ijc12>3.0.co;2-e. PMID 9009162.
  15. ↑ Wunderlich L, Faragó A, Buday L (January 1999). "Characterization of interactions of Nck with Sos and dynamin". Cell. Signal. 11 (1): 25–9. doi:10.1016/s0898-6568(98)00027-8. PMID 10206341.
  16. ↑ Modregger J, Ritter B, Witter B, Paulsson M, Plomann M (December 2000). "All three PACSIN isoforms bind to endocytic proteins and inhibit endocytosis". J. Cell. Sci. 113 (24): 4511–21. PMID 11082044.
  17. ↑ Modregger J, Schmidt AA, Ritter B, Huttner WB, Plomann M (February 2003). "Characterization of Endophilin B1b, a brain-specific membrane-associated lysophosphatidic acid acyl transferase with properties distinct from endophilin A1". J. Biol. Chem. 278 (6): 4160–7. doi:10.1074/jbc.M208568200. PMID 12456676.

Further reading

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