DNM1

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DNM1
Protein DNM1 PDB 1dyn.png
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesDNM1, Dynamin-1, DNM, EIEE31, dynamin 1
External IDsOMIM: 602377 MGI: 107384 HomoloGene: 123905 GeneCards: DNM1
Gene location (Human)
Chromosome 9 (human)
Chr.Chromosome 9 (human)[1]
Chromosome 9 (human)
Genomic location for DNM1
Genomic location for DNM1
Band9q34.11Start128,191,655 bp[1]
End128,255,248 bp[1]
RNA expression pattern
PBB GE DNM1 215116 s at fs.png
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001301737
NM_010065
NM_001368679

RefSeq (protein)

NP_001005336
NP_001275666
NP_001275667
NP_001275668
NP_004399

NP_001288666
NP_034195
NP_001355608

Location (UCSC)Chr 9: 128.19 – 128.26 MbChr 2: 32.31 – 32.35 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Dynamin-1 is a protein that in humans is encoded by the DNM1 gene.[5][6]

Function[edit]

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.[7]

Interactions[edit]

DNM1 has been shown to interact with:

References[edit]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000106976 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000026825 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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.
  6. ^ 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.
  7. ^ "Entrez Gene: DNM1 dynamin 1".
  8. ^ a b 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.
  9. ^ 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 25662. PMID 9348539.
  10. ^ 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.
  11. ^ 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.
  12. ^ 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.
  13. ^ a b 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.
  14. ^ 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.
  15. ^ 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.
  16. ^ 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.
  17. ^ 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.
  18. ^ 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[edit]