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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P50570: Variant p.Lys562Glu

Dynamin-2
Gene: DNM2
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Variant information Variant position: help 562 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LP/P [Disclaimer] The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance
Residue change: help From Lysine (K) to Glutamate (E) at position 562 (K562E, p.Lys562Glu). Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties: help Change from large size and basic (K) to medium size and acidic (E) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 1 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page
Variant description: help In CMTDIB and CNM1; with neutropenia; COS7 cells show a reduced uptake of transferrin and low-density lipoprotein complex; impairs PHD domain binding to vesicles composed of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate; does not affect GTP- and salt-induced disassembly; does not induce the formation of high-order oligomers; does not affect phosphorylation. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 562 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 870 The length of the canonical sequence.
Location on the sequence: help WFVLTAESLSWYKDEEEKEK K YMLPLDNLKIRDVEKGFMSN The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         WFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSN

Mouse                         WFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSN

Rat                           WFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSN

Bovine                        WFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSN
Sequence annotation in neighborhood: help The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
  • Type: the type of sequence feature.
  • Positions: endpoints of the sequence feature.
  • Description: contains additional information about the feature.
TypePositionsDescription
Chain 1 – 870 Dynamin-2
Domain 519 – 625 PH
Beta strand 560 – 565



Literature citations
Mutations in the pleckstrin homology domain of dynamin 2 cause dominant intermediate Charcot-Marie-Tooth disease.
Zuechner S.; Noureddine M.; Kennerson M.; Verhoeven K.; Claeys K.; De Jonghe P.; Merory J.; Oliveira S.A.; Speer M.C.; Stenger J.E.; Walizada G.; Zhu D.; Pericak-Vance M.A.; Nicholson G.; Timmerman V.; Vance J.M.;
Nat. Genet. 37:289-294(2005)
Cited for: VARIANTS CMTDIB 555-ASP--GLU-557 DEL; LYS-562 DEL AND GLU-562; CHARACTERIZATION OF VARIANT CMTDIB 555-ASP--GLU-557 DEL; SUBCELLULAR LOCATION; FUNCTION; Dynamin 2 mutations associated with human diseases impair clathrin-mediated receptor endocytosis.
Bitoun M.; Durieux A.-C.; Prudhon B.; Bevilacqua J.A.; Herledan A.; Sakanyan V.; Urtizberea A.; Cartier L.; Romero N.B.; Guicheney P.;
Hum. Mutat. 30:1419-1427(2009)
Cited for: VARIANT CNM1 LYS-650; CHARACTERIZATION OF VARIANTS CNM1 TRP-465; VAL-625 DEL AND LYS-650; CHARACTERIZATION OF VARIANT CMTDIB GLU-562; PATHOPHYSIOLOGICAL PATHWAY IN THE AUTOSOMAL FORMS OF CNM AND DNM2-CMT NEUROPATHY; FUNCTION; TISSUE SPECIFICITY; MUTAGENESIS OF LYS-44; Gain-of-Function Properties of a Dynamin 2 Mutant Implicated in Charcot-Marie-Tooth Disease.
Tassin T.C.; Barylko B.; Hedde P.N.; Chen Y.; Binns D.D.; James N.G.; Mueller J.D.; Jameson D.M.; Taussig R.; Albanesi J.P.;
Front. Cell. Neurosci. 15:745940-745940(2021)
Cited for: VARIANTS CNM1 555-ASP--GLU-557 DEL; GLU-562 AND THR-618; CHARACTERIZATION OF VARIANTS CNM1 555-ASP--GLU-557 DEL; GLU-562 AND THR-618; FUNCTION; CATALYTIC ACTIVITY; SUBUNIT; DOMAIN; PHOSPHORYLATION AT TYR-231 AND TYR-597; MUTAGENESIS OF TYR-231 AND TYR-597;
Disclaimer: Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.