Dynamin-2 (DNM2)
The protein contains 870 amino acids for an estimated molecular weight of 98064 Da.
Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Plays a role in the regulation of neuron morphology, axon growth and formation of neuronal growth cones (By similarity). Plays an important role in vesicular trafficking processes, in particular endocytosis (PubMed:33713620). Involved in cytokinesis (PubMed:12498685). Regulates maturation of apoptotic cell corpse-containing phagosomes by recruiting PIK3C3 to the phagosome membrane (By similarity). (updated: June 2, 2021)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
This protein is annotated as membranous in Gene Ontology, is annotated as membranous in UniProt.
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Biological Process
Antigen processing and presentation of exogenous peptide antigen via MHC class II
Aorta development
Cellular response to carbon monoxide
Cellular response to dopamine
Cellular response to nitric oxide
Cellular response to X-ray
Coronary vasculature development
Dynamin family protein polymerization involved in mitochondrial fission
Endocytosis
G protein-coupled receptor internalization
G2/M transition of mitotic cell cycle
Golgi to plasma membrane transport
Macropinocytosis
Membrane fusion
Membrane organization
Mitochondrial fission
Negative regulation of membrane tubulation
Negative regulation of non-motile cilium assembly
Negative regulation of transforming growth factor beta receptor signaling pathway
Neuron projection morphogenesis
Nitric oxide metabolic process
Organelle fission
Phagocytosis
Positive regulation of apoptotic process
Positive regulation of clathrin-dependent endocytosis
Positive regulation of lamellipodium assembly
Positive regulation of nitric oxide biosynthetic process
Positive regulation of P-type sodium:potassium-exchanging transporter activity
Positive regulation of phagocytosis
Positive regulation of substrate adhesion-dependent cell spreading
Positive regulation of transcription, DNA-templated
Post-Golgi vesicle-mediated transport
Postsynaptic neurotransmitter receptor internalization
Receptor internalization
Receptor-mediated endocytosis
Regulation of axon extension
Regulation of Golgi organization
Regulation of nitric-oxide synthase activity
Regulation of Rac protein signal transduction
Regulation of synapse structure or activity
Regulation of transcription, DNA-templated
Response to cocaine
Response to light stimulus
Signal transduction
Small molecule metabolic process
Spermatogenesis
Synaptic vesicle budding from presynaptic endocytic zone membrane
Synaptic vesicle transport
Transferrin transport
Ventricular septum development
Cellular Component
Axon
Centrosome
Clathrin-coated endocytic vesicle
Clathrin-coated pit
Cytoplasm
Cytoplasmic vesicle
Cytosol
Dendritic spine
Dendritic spine head
Endocytic vesicle membrane
Endosome
Extracellular exosome
Focal adhesion
Glutamatergic synapse
Golgi apparatus
Golgi membrane
Growth cone
Lamellipodium
Membrane
Microtubule
Microtubule cytoskeleton
Midbody
Mitochondrial membrane
Nucleus
Obsolete cell
Perinuclear region of cytoplasm
Phagocytic cup
Phagocytic vesicle membrane
Photoreceptor inner segment
Plasma membrane
Postsynaptic density
Postsynaptic density, intracellular component
Postsynaptic endocytic zone membrane
Postsynaptic membrane
Presynapse
Protein complex
Protein-containing complex
Ruffle membrane
Synapse
Trans-Golgi network
Molecular Function
D2 dopamine receptor binding
Enzyme binding
GTP binding
GTPase activity
Microtubule binding
Nitric-oxide synthase binding
Phosphatidylinositol 3-kinase regulatory subunit binding
Protein complex binding
Protein kinase binding
Protein-containing complex binding
SH3 domain binding
WW domain binding
The reference OMIM entry for this protein is 160150
Myopathy, centronuclear, 1; cnm1
Myopathy, centronuclear, autosomal dominant
Myotubular myopathy, autosomal dominant
A number sign (#) is used with this entry because autosomal dominant centronuclear myopathy-1 (CNM1) is caused by heterozygous mutation in the gene encoding dynamin-2 (DNM2; 602378) on chromosome 19p13.
DESCRIPTION
Autosomal dominant centronuclear myopathy is a congenital myopathy characterized by slowly progressive muscular weakness and wasting (Bitoun et al., 2005). The disorder involves mainly limb girdle, trunk, and neck muscles but may also affect distal muscles. Weakness may be present during childhood or adolescence or may not become evident until the third decade of life, and some affected individuals become wheelchair-bound in their fifties. Ptosis and limitation of eye movements occur frequently. The most prominent histopathologic features include high frequency of centrally located nuclei in a large number of extrafusal muscle fibers (which is the basis of the name of the disorder), radial arrangement of sarcoplasmic strands around the central nuclei, and predominance and hypotrophy of type 1 fibers. - Genetic Heterogeneity of Centronuclear Myopathy Centronuclear myopathy is a genetically heterogeneous disorder. See also X-linked CNM (CNMX; 310400), caused by mutation in the MTM1 gene (300415) on chromosome Xq28; CNM2 (255200), caused by mutation in the BIN1 gene (601248) on chromosome 2q14; CNM3 (614408), caused by mutation in the MYF6 gene (159991) on chromosome 12q21; CNM4 (614807), caused by mutation in the CCDC78 gene (614666) on chromosome 16p13; and CNM5 (615959), caused by mutation in the SPEG gene (615950) on chromosome 2q36. In addition, some patients with mutation in the RYR1 gene (180901) have findings of centronuclear myopathy on skeletal muscle biopsy (see 255320).CLINICAL FEATURES
Spiro et al. (1966) reported an isolated case of what the authors referred to as 'myotubular myopathy.' There was slowly progressive muscle weakness; muscle biopsy showed centrally located nuclei. In the development of skeletal muscle a 'myotubular' stage with centrally located nuclei occurs in utero at about 10 weeks of age. Spiro et al. (1966) thought this disease may represent persistence of fetal muscle. McLeod et al. (1972) reported a family that displayed autosomal dominant inheritance. Slowly progressive muscle weakness began between the first and third decades. It was primarily proximal in distribution but sometimes involved the facial musculature. External ophthalmoplegia and pharyngeal weakness were not features. Sixteen members of the family were affected. Karpati et al. (1970) reported affected mother and daughter. Skeletal muscle pathology showed atrophy predominantly of type 1 muscle fibers, with central nuclei and pale central zones with variably staining granules. These changes were indistinguishable from those in the other genetic varieties of centronuclear myopathy. Mortier et al. (1975) described centronuclear myopathy in teenaged brother and sister whose father may have been affected. Symptoms began in the children at 4 or 5 years of age with a 'sleepy facial expression,' clumsy gait, and easy fatigability. The disease progressed in a few years to generalized muscle weakness and atrophy, ptosis, ophthalmoplegia externa, and areflexia. Distal muscles in the lower limbs were severely affected. The father of the children had ptosis from at least age 20 years and generalized muscle atrophy had been noted at age 25. Wallgren-Pettersson et al. (1995) reviewed the differential diagnosis of the X-lin ... More on the omim web site
July 1, 2021: Protein entry updated
Automatic update: Entry updated from uniprot information.
May 12, 2019: Protein entry updated
Automatic update: model status changed
Nov. 17, 2018: Protein entry updated
Automatic update: model status changed
Feb. 10, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
Oct. 27, 2017: Protein entry updated
Automatic update: model status changed
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 160150 was added.
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed