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{{Infobox_gene}}
{{PBB_Controls
'''Dynamin-1''' is a [[protein]] that in humans is encoded by the ''DNM1'' [[gene]].<ref name="pmid2144893">{{cite journal | vauthors = Obar RA, Collins CA, Hammarback JA, Shpetner HS, Vallee RB | title = Molecular cloning of the microtubule-associated mechanochemical enzyme dynamin reveals homology with a new family of GTP-binding proteins | journal = Nature | volume = 347 | issue = 6290 | pages = 256–61 |date=October 1990 | pmid = 2144893 | pmc =  | doi = 10.1038/347256a0 }}</ref><ref name="pmid9143509">{{cite journal | vauthors = Newman-Smith ED, Shurland DL, van der Bliek AM | title = Assignment of the dynamin-1 gene (DNM1) to human chromosome 9q34 by fluorescence in situ hybridization and somatic cell hybrid analysis | journal = Genomics | volume = 41 | issue = 2 | pages = 286–9 |date=July 1997 | pmid = 9143509 | pmc = | doi = 10.1006/geno.1996.4596 }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_DNM1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1dyn.
| PDB = {{PDB2|1dyn}}, {{PDB2|2aka}}, {{PDB2|2dyn}}
| Name = Dynamin 1
| HGNCid = 2972
| Symbol = DNM1
| AltSymbols =; DNM
| OMIM = 602377
| ECnumber = 
| Homologene = 68397
| MGIid = 107384
| GeneAtlas_image1 = PBB_GE_DNM1_215116_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003774 |text = motor activity}} {{GNF_GO|id=GO:0003924 |text = GTPase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005525 |text = GTP binding}} {{GNF_GO|id=GO:0016301 |text = kinase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005874 |text = microtubule}} {{GNF_GO|id=GO:0005905 |text = coated pit}}
| Process = {{GNF_GO|id=GO:0006897 |text = endocytosis}} {{GNF_GO|id=GO:0006898 |text = receptor-mediated endocytosis}} {{GNF_GO|id=GO:0007268 |text = synaptic transmission}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1759
    | Hs_Ensembl = ENSG00000106976
    | Hs_RefseqProtein = NP_001005336
    | Hs_RefseqmRNA = NM_001005336
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 9
    | Hs_GenLoc_start = 130005479
    | Hs_GenLoc_end = 130057348
    | Hs_Uniprot = Q05193
    | Mm_EntrezGene = 13429
    | Mm_Ensembl = ENSMUSG00000026825
    | Mm_RefseqmRNA = NM_010065
    | Mm_RefseqProtein = NP_034195
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 2
    | Mm_GenLoc_start = 32130480
    | Mm_GenLoc_end = 32175293
    | Mm_Uniprot = Q6PDM5
  }}
}}
'''Dynamin 1''', also known as '''DNM1''', is a human [[gene]].


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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.<ref>{{cite web | title = Entrez Gene: DNM1 dynamin 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1759| accessdate = }}</ref>
{{PBB_Summary
| section_title =
| summary_text = 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.<ref>{{cite web | title = Entrez Gene: DNM1 dynamin 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1759| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
DNM1 has been shown to [[Protein-protein interaction|interact]] with:
{{div col|colwidth=20em}}
* [[Amphiphysin|AMPH]],<ref name = pmid9341169>{{cite journal | date = October 1997 | vauthors = Micheva KD, Kay BK, McPherson PS | title = Synaptojanin forms two separate complexes in the nerve terminal. Interactions with endophilin and amphiphysin | journal = J. Biol. Chem. | volume = 272 | issue = 43 | pages = 27239–45 | pmid = 9341169 | doi = 10.1074/jbc.272.43.27239}}</ref><ref name = pmid9348539>{{cite journal | date = October 1997 | vauthors = Wigge P, Köhler K, Vallis Y, Doyle CA, Owen D, Hunt SP, McMahon HT | title = Amphiphysin heterodimers: potential role in clathrin-mediated endocytosis | journal = Mol. Biol. Cell | volume = 8 | issue = 10 | pages = 2003–15 | pmid = 9348539 | pmc = 25662 | doi = 10.1091/mbc.8.10.2003}}</ref><ref name = pmid9280305>{{cite journal | date = August 1997 | vauthors = McMahon HT, Wigge P, Smith C | title = Clathrin interacts specifically with amphiphysin and is displaced by dynamin | journal = FEBS Lett. | volume = 413 | issue = 2 | pages = 319–22 | pmid = 9280305 | doi = 10.1016/s0014-5793(97)00928-9}}</ref><ref name = pmid11877424>{{cite journal | date = May 2002 | vauthors = Chen-Hwang MC, Chen HR, Elzinga M, Hwang YW | title = Dynamin is a minibrain kinase/dual specificity Yak1-related kinase 1A substrate | journal = J. Biol. Chem. | volume = 277 | issue = 20 | pages = 17597–604 | pmid = 11877424 | doi = 10.1074/jbc.M111101200}}</ref><ref name = pmid9148966>{{cite journal | date = May 1997 | vauthors = Grabs D, Slepnev VI, Songyang Z, David C, Lynch M, Cantley LC, De Camilli P | title = The SH3 domain of amphiphysin binds the proline-rich domain of dynamin at a single site that defines a new SH3 binding consensus sequence | journal = J. Biol. Chem. | volume = 272 | issue = 20 | pages = 13419–25 | pmid = 9148966 | doi = 10.1074/jbc.272.20.13419}}</ref>
* [[FNBP1]],<ref name = pmid15252009>{{cite journal | date = September 2004 | vauthors = Kamioka Y, Fukuhara S, Sawa H, Nagashima K, Masuda M, Matsuda M, Mochizuki N | title = A novel dynamin-associating molecule, formin-binding protein 17, induces tubular membrane invaginations and participates in endocytosis | journal = J. Biol. Chem. | volume = 279 | issue = 38 | pages = 40091–9 | pmid = 15252009 | doi = 10.1074/jbc.M404899200}}</ref>
* [[Grb2]]<ref name = pmid8119878>{{cite journal  | date = February 1994 | vauthors = Miki H, Miura K, Matuoka K, Nakata T, Hirokawa N, Orita S, Kaibuchi K, Takai Y, Takenawa T | title = Association of Ash/Grb-2 with dynamin through the Src homology 3 domain | journal = J. Biol. Chem. | volume = 269 | issue = 8 | pages = 5489–92 | pmid = 8119878 | doi = }}</ref><ref name = pmid9009162>{{cite journal | date = January 1997 | vauthors = Sastry L, Cao T, King CR | title = Multiple Grb2-protein complexes in human cancer cells | journal = Int. J. Cancer | volume = 70 | issue = 2 | pages = 208–13 | pmid = 9009162 | doi = 10.1002/(sici)1097-0215(19970117)70:2<208::aid-ijc12>3.0.co;2-e}}</ref>
* [[NCK1]],<ref name = pmid10206341>{{cite journal | date = January 1999 | vauthors = Wunderlich L, Faragó A, Buday L | title = Characterization of interactions of Nck with Sos and dynamin | journal = Cell. Signal. | volume = 11 | issue = 1 | pages = 25–9 | pmid = 10206341 | doi = 10.1016/s0898-6568(98)00027-8}}</ref>
* [[PACSIN1]],<ref name = pmid15252009/><ref name = pmid11082044>{{cite journal | date = December 2000 | vauthors = Modregger J, Ritter B, Witter B, Paulsson M, Plomann M | title = All three PACSIN isoforms bind to endocytic proteins and inhibit endocytosis | journal = J. Cell Sci. | volume = 113 | issue = 24| pages = 4511–21 | pmid = 11082044 | doi = }}</ref>  and
* [[SH3GL2]].<ref name = pmid9341169/><ref name = pmid12456676>{{cite journal | date = February 2003 | vauthors = Modregger J, Schmidt AA, Ritter B, Huttner WB, Plomann M | title = Characterization of Endophilin B1b, a brain-specific membrane-associated lysophosphatidic acid acyl transferase with properties distinct from endophilin A1 | journal = J. Biol. Chem. | volume = 278 | issue = 6 | pages = 4160–7 | pmid = 12456676 | doi = 10.1074/jbc.M208568200}}</ref>
{{Div col end}}
 
== References ==
{{Commons category|Dynamin 1}}
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
*{{cite journal  | author=Sever S |title=Dynamin and endocytosis. |journal=Curr. Opin. Cell Biol. |volume=14 |issue= 4 |pages= 463–7 |year= 2003 |pmid= 12383797 |doi=10.1016/S0955-0674(02)00347-2 }}
| citations =
*{{cite journal  | vauthors=Wiejak J, Wyroba E |title=Dynamin: characteristics, mechanism of action and function. |journal=Cell. Mol. Biol. Lett. |volume=7 |issue= 4 |pages= 1073–80 |year= 2003 |pmid= 12511974 |doi=  }}
*{{cite journal  | author=Sever S |title=Dynamin and endocytosis. |journal=Curr. Opin. Cell Biol. |volume=14 |issue= 4 |pages= 463-7 |year= 2003 |pmid= 12383797 |doi=  }}
*{{cite journal  | vauthors=Orth JD, McNiven MA |title=Dynamin at the actin-membrane interface. |journal=Curr. Opin. Cell Biol. |volume=15 |issue= 1 |pages= 31–9 |year= 2003 |pmid= 12517701 |doi=10.1016/S0955-0674(02)00010-8  }}
*{{cite journal  | author=Wiejak J, Wyroba E |title=Dynamin: characteristics, mechanism of action and function. |journal=Cell. Mol. Biol. Lett. |volume=7 |issue= 4 |pages= 1073-80 |year= 2003 |pmid= 12511974 |doi=  }}
*{{cite journal  | vauthors=Timm D, Salim K, Gout I |title=Crystal structure of the pleckstrin homology domain from dynamin. |journal=Nat. Struct. Biol. |volume=1 |issue= 11 |pages= 782–8 |year= 1995 |pmid= 7634088 |doi=10.1038/nsb1194-782  |display-authors=etal}}
*{{cite journal  | author=Orth JD, McNiven MA |title=Dynamin at the actin-membrane interface. |journal=Curr. Opin. Cell Biol. |volume=15 |issue= 1 |pages= 31-9 |year= 2003 |pmid= 12517701 |doi= }}
*{{cite journal  | vauthors=Downing AK, Driscoll PC, Gout I |title=Three-dimensional solution structure of the pleckstrin homology domain from dynamin. |journal=Curr. Biol. |volume=4 |issue= 10 |pages= 884–91 |year= 1995 |pmid= 7850421 |doi=10.1016/S0960-9822(00)00197-4 |display-authors=etal}}
*{{cite journal  | author=Obar RA, Collins CA, Hammarback JA, ''et al.'' |title=Molecular cloning of the microtubule-associated mechanochemical enzyme dynamin reveals homology with a new family of GTP-binding proteins. |journal=Nature |volume=347 |issue= 6290 |pages= 256-61 |year= 1990 |pmid= 2144893 |doi= 10.1038/347256a0 }}
*{{cite journal  | vauthors=Ferguson KM, Lemmon MA, Schlessinger J, Sigler PB |title=Crystal structure at 2.2 A resolution of the pleckstrin homology domain from human dynamin. |journal=Cell |volume=79 |issue= 2 |pages= 199–209 |year= 1994 |pmid= 7954789 |doi=10.1016/0092-8674(94)90190-2  }}
*{{cite journal  | author=Timm D, Salim K, Gout I, ''et al.'' |title=Crystal structure of the pleckstrin homology domain from dynamin. |journal=Nat. Struct. Biol. |volume=1 |issue= 11 |pages= 782-8 |year= 1995 |pmid= 7634088 |doi=  }}
*{{cite journal  | vauthors=van der Bliek AM, Redelmeier TE, Damke H |title=Mutations in human dynamin block an intermediate stage in coated vesicle formation. |journal=J. Cell Biol. |volume=122 |issue= 3 |pages= 553–63 |year= 1993 |pmid= 8101525 |doi=10.1083/jcb.122.3.553  | pmc=2119674 |display-authors=etal}}
*{{cite journal  | author=Downing AK, Driscoll PC, Gout I, ''et al.'' |title=Three-dimensional solution structure of the pleckstrin homology domain from dynamin. |journal=Curr. Biol. |volume=4 |issue= 10 |pages= 884-91 |year= 1995 |pmid= 7850421 |doi= }}
*{{cite journal  | vauthors=Miki H, Miura K, Matuoka K |title=Association of Ash/Grb-2 with dynamin through the Src homology 3 domain. |journal=J. Biol. Chem. |volume=269 |issue= 8 |pages= 5489–92 |year= 1994 |pmid= 8119878 |doi=  |display-authors=etal}}
*{{cite journal  | author=Ferguson KM, Lemmon MA, Schlessinger J, Sigler PB |title=Crystal structure at 2.2 A resolution of the pleckstrin homology domain from human dynamin. |journal=Cell |volume=79 |issue= 2 |pages= 199-209 |year= 1994 |pmid= 7954789 |doi=  }}
*{{cite journal  | vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8  }}
*{{cite journal  | author=van der Bliek AM, Redelmeier TE, Damke H, ''et al.'' |title=Mutations in human dynamin block an intermediate stage in coated vesicle formation. |journal=J. Cell Biol. |volume=122 |issue= 3 |pages= 553-63 |year= 1993 |pmid= 8101525 |doi=  }}
*{{cite journal  | vauthors=Sontag JM, Fykse EM, Ushkaryov Y |title=Differential expression and regulation of multiple dynamins. |journal=J. Biol. Chem. |volume=269 |issue= 6 |pages= 4547–54 |year= 1994 |pmid= 8308025 |doi=  |display-authors=etal}}
*{{cite journal  | author=Miki H, Miura K, Matuoka K, ''et al.'' |title=Association of Ash/Grb-2 with dynamin through the Src homology 3 domain. |journal=J. Biol. Chem. |volume=269 |issue= 8 |pages= 5489-92 |year= 1994 |pmid= 8119878 |doi= }}
*{{cite journal  | vauthors=Grabs D, Slepnev VI, Songyang Z |title=The SH3 domain of amphiphysin binds the proline-rich domain of dynamin at a single site that defines a new SH3 binding consensus sequence. |journal=J. Biol. Chem. |volume=272 |issue= 20 |pages= 13419–25 |year= 1997 |pmid= 9148966 |doi=10.1074/jbc.272.20.13419 |display-authors=etal}}
*{{cite journal  | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi=  }}
*{{cite journal  | vauthors=Ramjaun AR, Micheva KD, Bouchelet I, McPherson PS |title=Identification and characterization of a nerve terminal-enriched amphiphysin isoform. |journal=J. Biol. Chem. |volume=272 |issue= 26 |pages= 16700–6 |year= 1997 |pmid= 9195986 |doi=10.1074/jbc.272.26.16700  }}
*{{cite journal  | author=Sontag JM, Fykse EM, Ushkaryov Y, ''et al.'' |title=Differential expression and regulation of multiple dynamins. |journal=J. Biol. Chem. |volume=269 |issue= 6 |pages= 4547-54 |year= 1994 |pmid= 8308025 |doi=  }}
*{{cite journal  | vauthors=Ringstad N, Nemoto Y, De Camilli P |title=The SH3p4/Sh3p8/SH3p13 protein family: binding partners for synaptojanin and dynamin via a Grb2-like Src homology 3 domain. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 16 |pages= 8569–74 |year= 1997 |pmid= 9238017 |doi=10.1073/pnas.94.16.8569  | pmc=23017 }}
*{{cite journal  | author=Newman-Smith ED, Shurland DL, van der Bliek AM |title=Assignment of the dynamin-1 gene (DNM1) to human chromosome 9q34 by fluorescence in situ hybridization and somatic cell hybrid analysis. |journal=Genomics |volume=41 |issue= 2 |pages= 286-9 |year= 1997 |pmid= 9143509 |doi= 10.1006/geno.1996.4596 }}
*{{cite journal  | vauthors=McMahon HT, Wigge P, Smith C |title=Clathrin interacts specifically with amphiphysin and is displaced by dynamin. |journal=FEBS Lett. |volume=413 |issue= 2 |pages= 319–22 |year= 1997 |pmid= 9280305 |doi=10.1016/S0014-5793(97)00928-9 }}
*{{cite journal  | author=Grabs D, Slepnev VI, Songyang Z, ''et al.'' |title=The SH3 domain of amphiphysin binds the proline-rich domain of dynamin at a single site that defines a new SH3 binding consensus sequence. |journal=J. Biol. Chem. |volume=272 |issue= 20 |pages= 13419-25 |year= 1997 |pmid= 9148966 |doi=  }}
*{{cite journal  | vauthors=Wigge P, Köhler K, Vallis Y |title=Amphiphysin heterodimers: potential role in clathrin-mediated endocytosis. |journal=Mol. Biol. Cell |volume=8 |issue= 10 |pages= 2003–15 |year= 1997 |pmid= 9348539 |doi=  10.1091/mbc.8.10.2003| pmc=25662  |display-authors=etal}}
*{{cite journal  | author=Ramjaun AR, Micheva KD, Bouchelet I, McPherson PS |title=Identification and characterization of a nerve terminal-enriched amphiphysin isoform. |journal=J. Biol. Chem. |volume=272 |issue= 26 |pages= 16700-6 |year= 1997 |pmid= 9195986 |doi=  }}
*{{cite journal  | vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3  |display-authors=etal}}
*{{cite journal  | author=Ringstad N, Nemoto Y, De Camilli P |title=The SH3p4/Sh3p8/SH3p13 protein family: binding partners for synaptojanin and dynamin via a Grb2-like Src homology 3 domain. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 16 |pages= 8569-74 |year= 1997 |pmid= 9238017 |doi=  }}
*{{cite journal  | vauthors=Witke W, Podtelejnikov AV, Di Nardo A |title=In mouse brain profilin I and profilin II associate with regulators of the endocytic pathway and actin assembly. |journal=EMBO J. |volume=17 |issue= 4 |pages= 967–76 |year= 1998 |pmid= 9463375 |doi= 10.1093/emboj/17.4.967 | pmc=1170446 |display-authors=etal}}
*{{cite journal  | author=McMahon HT, Wigge P, Smith C |title=Clathrin interacts specifically with amphiphysin and is displaced by dynamin. |journal=FEBS Lett. |volume=413 |issue= 2 |pages= 319-22 |year= 1997 |pmid= 9280305 |doi= }}
*{{cite journal  | vauthors=Slepnev VI, Ochoa GC, Butler MH |title=Role of phosphorylation in regulation of the assembly of endocytic coat complexes. |journal=Science |volume=281 |issue= 5378 |pages= 821–4 |year= 1998 |pmid= 9694653 |doi=10.1126/science.281.5378.821 |display-authors=etal}}
*{{cite journal  | author=Wigge P, Köhler K, Vallis Y, ''et al.'' |title=Amphiphysin heterodimers: potential role in clathrin-mediated endocytosis. |journal=Mol. Biol. Cell |volume=8 |issue= 10 |pages= 2003-15 |year= 1997 |pmid= 9348539 |doi=  }}
*{{cite journal  | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi=  }}
*{{cite journal  | author=Witke W, Podtelejnikov AV, Di Nardo A, ''et al.'' |title=In mouse brain profilin I and profilin II associate with regulators of the endocytic pathway and actin assembly. |journal=EMBO J. |volume=17 |issue= 4 |pages= 967-76 |year= 1998 |pmid= 9463375 |doi= 10.1093/emboj/17.4.967 }}
*{{cite journal  | author=Slepnev VI, Ochoa GC, Butler MH, ''et al.'' |title=Role of phosphorylation in regulation of the assembly of endocytic coat complexes. |journal=Science |volume=281 |issue= 5378 |pages= 821-4 |year= 1998 |pmid= 9694653 |doi=  }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{PDB Gallery|geneid=1759}}
{{WikiDoc Sources}}
{{Vesicular transport proteins}}

Latest revision as of 19:45, 8 November 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

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RefSeq (protein)

n/a

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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

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.[3]

Interactions

DNM1 has been shown to interact with:

References

  1. ↑ 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.
  2. ↑ 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.
  3. ↑ "Entrez Gene: DNM1 dynamin 1".
  4. ↑ 4.0 4.1 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.
  5. ↑ 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.
  6. ↑ 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.
  7. ↑ 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.
  8. ↑ 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.
  9. ↑ 9.0 9.1 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.
  10. ↑ 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.
  11. ↑ 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.
  12. ↑ 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.
  13. ↑ 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.
  14. ↑ 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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