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Identification
HMDB Protein ID HMDBP08363
Secondary Accession Numbers
  • 14075
Name Dynamin-1
Synonyms Not Available
Gene Name DNM1
Protein Type Unknown
Biological Properties
General Function Involved in GTP binding
Specific Function Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Most probably involved in vesicular trafficking processes. Involved in receptor-mediated endocytosis.
Pathways
  • Bacterial invasion of epithelial cells
  • Endocrine and other factor-regulated calcium reabsorption
  • Endocytosis
  • Fc gamma R-mediated phagocytosis
  • Synaptic vesicle cycle
Reactions
Guanosine triphosphate + Water → Guanosine diphosphate + Phosphate details
GO Classification
Biological Process
endosome organization
receptor-mediated endocytosis
Cellular Component
membrane coat
microtubule
Function
purine nucleotide binding
binding
nucleotide binding
catalytic activity
hydrolase activity
guanyl nucleotide binding
guanyl ribonucleotide binding
gtp binding
gtpase activity
nucleoside-triphosphatase activity
hydrolase activity, acting on acid anhydrides
hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
pyrophosphatase activity
Molecular Function
GTPase activity
phospholipid binding
GTP binding
Cellular Location
  1. Cytoplasm
  2. Cytoplasm
  3. cytoskeleton
Gene Properties
Chromosome Location 9
Locus 9q34
SNPs DNM1
Gene Sequence
>2595 bp
ATGGGCAACCGCGGCATGGAAGATCTCATCCCGCTGGTCAACCGGCTGCAAGACGCCTTC
TCTGCCATCGGCCAGAACGCGGACCTCGACCTGCCGCAGATCGCTGTGGTGGGCGGCCAG
AGCGCCGGCAAGAGCTCGGTGCTCGAGAATTTCGTAGGCAGGGACTTCTTGCCTCGAGGA
TCTGGCATTGTCACCCGACGTCCCCTGGTCTTGCAGCTGGTCAATGCAACCACAGAATAT
GCCGAGTTCCTGCACTGCAAGGGAAAGAAATTCACCGACTTCGAGGAGGTGCGCCTTGAG
ATCGAGGCCGAGACCGACAGGGTCACCGGCACCAACAAGGGCATCTCGCCGGTGCCTATC
AACCTCCGCGTCTACTCGCCGCACGTGCTGAACCTGACCCTGGTGGACCTGCCCGGAATG
ACCAAGGTCCCGGTGGGGGACCAACCTCCCGACATCGAGTTCCAGATCCGAGACATGCTT
ATGCAGTTTGTCACCAAGGAGAACTGCCTCATCCTGGCCGTGTCCCCCGCCAACTCTGAC
CTGGCCAATTCTGACGCCCTCAAGGTCGCCAAGGAGGTGGACCCCCAGGGCCAGCGCACC
ATCGGGGTCATCACCAAGCTGGACCTGATGGACGAGGGCACAGATGCCCGTGATGTGCTG
GAGAACAAGCTGCTCCCCCTGCGCAGAGGCTACATTGGAGTGGTGAACCGGAGCCAGAAG
GACATTGATGGCAAGAAGGACATTACCGCCGCCTTGGCTGCTGAACGAAAGTTCTTCCTC
TCCCATCCATCTTATCGCCACTTGGCTGACCGTATGGGCACGCCCTACCTGCAGAAGGTC
CTCAATCAGCAACTGACGAACCACATCCGGGACACACTGCCGGGGCTGCGGAACAAGCTG
CAGAGCCAGCTACTGTCCATTGAGAAGGAGGTGGAGGAATACAAGAACTTCCGCCCTGAT
GACCCAGCTCGCAAGACCAAGGCCCTGCTGCAGATGGTCCAGCAGTTCGCCGTAGACTTT
GAGAAGCGCATTGAGGGCTCAGGAGATCAGATCGACACCTACGAACTGTCAGGGGGAGCC
CGCATTAACCGAATCTTCCACGAGCGCTTCCCTTTCGAGCTGGTCAAGATGGAGTTTGAT
GAGAAGGAACTCCGAAGGGAGATCAGCTATGCTATCAAGAATATCCATGGCATTAGAACG
GGGCTGTTTACCCCAGACATGGCCTTTGAGACCATTGTGAAAAAGCAGGTGAAGAAGATC
CGAGAACCGTGTCTCAAGTGTGTGGACATGGTTATCTCGGAGCTAATCAGCACCGTTAGA
CAGTGCACCAAGAAGCTCCAGCAGTACCCGCGGCTACGGGAGGAGATGGAGCGCATCGTG
ACCACCCACATCCGGGAGCGCGAGGGCCGCACTAAGGAGCAGGTCATGCTTCTCATCGAT
ATCGAGCTGGCTTACATGAACACCAACCATGAGGACTTCATAGGCTTTGCCAATGCTCAG
CAGAGGAGCAACCAGATGAACAAGAAGAAGACTTCAGGGAACCAGGATGAGATTCTGGTC
ATCCGCAAGGGCTGGCTGACTATCAATAATATTGGCATCATGAAAGGGGGCTCCAAGGAG
TACTGGTTTGTGCTGACTGCTGAGAATCTGTCCTGGTACAAGGATGATGAGGAGAAAGAG
AAGAAATACATGCTGTCTGTGGACAACCTCAAGCTGCGGGACGTGGAGAAGGGCTTTATG
TCGAGCAAGCATATCTTTGCCCTCTTTAACACGGAGCAGAGGAATGTCTACAAGGATTAT
CGGCAGCTGGAGCTAGCCTGTGAGACACAGGAGGAGGTGGACAGCTGGAAGGCCTCCTTC
CTGAGGGCTGGCGTGTACCCTGAGCGTGTTGGGGACAAAGAGAAAGCCAGCGAGACCGAG
GAGAATGGCTCCGACAGCTTCATGCATTCCATGGACCCACAGCTGGAACGGCAAGTGGAG
ACCATCCGGAATCTTGTGGACTCATACATGGCCATTGTCAACAAGACCGTGAGGGACCTC
ATGCCCAAGACCATCATGCACCTCATGATTAACAATACCAAGGAGTTCATCTTCTCGGAG
CTGCTGGCCAACCTGTACTCGTGTGGGGACCAGAACACGCTGATGGAGGAGTCGGCGGAG
CAGGCACAGCGGCGCGACGAGATGCTGCGCATGTACCACGCACTGAAGGAGGCGCTCAGC
ATCATCGGCGACATCAACACGACCACCGTCAGCACGCCCATGCCCCCGCCCGTGGACGAC
TCCTGGCTGCAGGTGCAGAGCGTACCGGCCGGACGCAGGTCGCCCACGTCCAGCCCCACG
CCGCAGCGCCGAGCCCCCGCCGTGCCCCCAGCCCGGCCCGGGTCGCGGGGCCCTGCTCCT
GGGCCTCCGCCTGCTGGGTCCGCCCTGGGGGGGGCGCCCCCCGTGCCCTCCAGGCCGGGG
GCTTCCCCTGACCCTTTCGGCCCTCCCCCTCAGGTGCCCTCGCGCCCCAACCGCGCCCCG
CCCGGGGTCCCCAGCCGATCGGGTCAGGCAAGTCCATCCCGTCCTGAGAGCCCCAGGCCC
CCCTTCGACCTCTAA
Protein Properties
Number of Residues 864
Molecular Weight 96040.03
Theoretical pI 7.005
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Dynamin-1
MGNRGMEDLIPLVNRLQDAFSAIGQNADLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRG
SGIVTRRPLVLQLVNATTEYAEFLHCKGKKFTDFEEVRLEIEAETDRVTGTNKGISPVPI
NLRVYSPHVLNLTLVDLPGMTKVPVGDQPPDIEFQIRDMLMQFVTKENCLILAVSPANSD
LANSDALKVAKEVDPQGQRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQK
DIDGKKDITAALAAERKFFLSHPSYRHLADRMGTPYLQKVLNQQLTNHIRDTLPGLRNKL
QSQLLSIEKEVEEYKNFRPDDPARKTKALLQMVQQFAVDFEKRIEGSGDQIDTYELSGGA
RINRIFHERFPFELVKMEFDEKELRREISYAIKNIHGIRTGLFTPDMAFETIVKKQVKKI
REPCLKCVDMVISELISTVRQCTKKLQQYPRLREEMERIVTTHIREREGRTKEQVMLLID
IELAYMNTNHEDFIGFANAQQRSNQMNKKKTSGNQDEILVIRKGWLTINNIGIMKGGSKE
YWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKGFMSSKHIFALFNTEQRNVYKDY
RQLELACETQEEVDSWKASFLRAGVYPERVGDKEKASETEENGSDSFMHSMDPQLERQVE
TIRNLVDSYMAIVNKTVRDLMPKTIMHLMINNTKEFIFSELLANLYSCGDQNTLMEESAE
QAQRRDEMLRMYHALKEALSIIGDINTTTVSTPMPPPVDDSWLQVQSVPAGRRSPTSSPT
PQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQVPSRPNRAP
PGVPSRSGQASPSRPESPRPPFDL
GenBank ID Protein 55961114
UniProtKB/Swiss-Prot ID Q05193
UniProtKB/Swiss-Prot Entry Name DYN1_HUMAN
PDB IDs
GenBank Gene ID AL590708
GeneCard ID DNM1
GenAtlas ID DNM1
HGNC ID HGNC:2972
References
General References
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  2. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed:15592455 ]
  3. Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed:18088087 ]
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  5. van der Bliek AM, Redelmeier TE, Damke H, Tisdale EJ, Meyerowitz EM, Schmid SL: Mutations in human dynamin block an intermediate stage in coated vesicle formation. J Cell Biol. 1993 Aug;122(3):553-63. [PubMed:8101525 ]
  6. Downing AK, Driscoll PC, Gout I, Salim K, Zvelebil MJ, Waterfield MD: Three-dimensional solution structure of the pleckstrin homology domain from dynamin. Curr Biol. 1994 Oct 1;4(10):884-91. [PubMed:7850421 ]
  7. Ferguson KM, Lemmon MA, Schlessinger J, Sigler PB: Crystal structure at 2.2 A resolution of the pleckstrin homology domain from human dynamin. Cell. 1994 Oct 21;79(2):199-209. [PubMed:7954789 ]
  8. Timm D, Salim K, Gout I, Guruprasad L, Waterfield M, Blundell T: Crystal structure of the pleckstrin homology domain from dynamin. Nat Struct Biol. 1994 Nov;1(11):782-8. [PubMed:7634088 ]