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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P35579: Variant p.Glu1841Lys

Myosin-9
Gene: MYH9
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Variant information Variant position: help 1841 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 Glutamate (E) to Lysine (K) at position 1841 (E1841K, p.Glu1841Lys). 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 medium size and acidic (E) to large size and basic (K) 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 MATINS. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 1841 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 1960 The length of the canonical sequence.
Location on the sequence: help EQLDNETKERQAACKQVRRT E KKLKDVLLQVDDERRNAEQY 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                         EQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQY

                              EQLDNETKERQAACKQVRRAEKKLKDVLLQVDDERRNAEQF

Mouse                         EQLDNETKERQAASKQVRRTEKKLKDVLLQVEDERRNAEQF

Rat                           EQLDNETKERQAASKQVRRAEKKLKDVLLQVEDERRNAEQF

Chicken                       EQLDMETKERQAASKQVRRAEKKLKDILLQVDDERRNAEQF
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 2 – 1960 Myosin-9
Coiled coil 837 – 1926
Modified residue 1845 – 1845 N6-acetyllysine



Literature citations
Mutations in MYH9 result in the May-Hegglin anomaly, and Fechtner and Sebastian syndromes.
Seri M.; Cusano M.; Gangarossa S.; Caridi G.; Bordo D.; Lo Nigro C.; Ghiggeri G.M.; Ravazzolo R.; Savino M.; Del Vecchio M.; d'Apolito M.; Iolascon A.; Zelante L.L.; Savoia A.; Balduini C.L.; Noris P.; Magrini U.; Belletti S.; Heath K.E.; Babcock M.; Glucksman M.J.; Aliprandis E.; Bizzaro N.; Desnick R.J.; Martignetti J.A.;
Nat. Genet. 26:103-105(2000)
Cited for: VARIANTS MATINS LYS-93; CYS-702; CYS-1165; HIS-1424 AND LYS-1841; Mutation of MYH9, encoding non-muscle myosin heavy chain A, in May-Hegglin anomaly.
Kelley M.J.; Jawien W.; Ortel T.L.; Korczak J.F.;
Nat. Genet. 26:106-108(2000)
Cited for: VARIANTS MATINS ILE-1155 AND LYS-1841; Nonmuscle myosin heavy chain IIA mutations define a spectrum of autosomal dominant macrothrombocytopenias: May-Hegglin anomaly and Fechtner, Sebastian, Epstein, and Alport-like syndromes.
Heath K.E.; Campos-Barros A.; Toren A.; Rozenfeld-Granot G.; Carlsson L.E.; Savige J.; Denison J.C.; Gregory M.C.; White J.G.; Barker D.F.; Greinacher A.; Epstein C.J.; Glucksman M.J.; Martignetti J.A.;
Am. J. Hum. Genet. 69:1033-1045(2001)
Cited for: VARIANTS MATINS ASN-373; CYS-702; HIS-702; PRO-1114; ASN-1424; HIS-1424 AND LYS-1841; Identification of six novel MYH9 mutations and genotype-phenotype relationships in autosomal dominant macrothrombocytopenia with leukocyte inclusions.
Kunishima S.; Matsushita T.; Kojima T.; Amemiya N.; Choi Y.M.; Hosaka N.; Inoue M.; Jung Y.; Mamiya S.; Matsumoto K.; Miyajima Y.; Zhang G.; Ruan C.; Saito K.; Song K.S.; Yoon H.-J.; Kamiya T.; Saito H.;
J. Hum. Genet. 46:722-729(2001)
Cited for: VARIANTS MATINS THR-95; CYS-1165; LEU-1165; 1205-LEU--GLN-1207 DEL; HIS-1424; ASN-1424; TYR-1424 AND LYS-1841; VARIANT VAL-1626; Expression of the nonmuscle myosin heavy chain IIA in the human kidney and screening for MYH9 mutations in Epstein and Fechtner syndromes.
Arrondel C.; Vodovar N.; Knebelmann B.; Gruenfeld J.-P.; Gubler M.-C.; Antignac C.; Heidet L.;
J. Am. Soc. Nephrol. 13:65-74(2002)
Cited for: VARIANTS MATINS LEU-96; LEU-1165; TRP-1400; ASN-1424 AND LYS-1841; TISSUE SPECIFICITY; Immunofluorescence analysis of neutrophil nonmuscle myosin heavy chain-A in MYH9 disorders: association of subcellular localization with MYH9 mutations.
Kunishima S.; Matsushita T.; Kojima T.; Sako M.; Kimura F.; Jo E.-K.; Inoue C.; Kamiya T.; Saito H.;
Lab. Invest. 83:115-122(2003)
Cited for: VARIANTS MATINS CYS-1165; LEU-1165; 1205-LEU--GLN-1207 DEL; HIS-1424; ASN-1424; TYR-1424; VAL-1816 AND LYS-1841;
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.