UniProtKB/Swiss-Prot P35579: Variant p.Asp1424Asn

Myosin-9
Gene: MYH9
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Variant information Variant position:

1424 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

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:

From Aspartate (D) to Asparagine (N) at position 1424 (D1424N, p.Asp1424Asn). 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:

Change from medium size and acidic (D) to medium size and polar (N) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

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:

In MATINS; results in reduced protein levels. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs80338831 [ dbSNP | Ensembl ]

Sequence information Variant position:

1424 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:

1960 The length of the canonical sequence.
Location on the sequence:

KVAAYDKLEKTKTRLQQELD D LLVDLDHQRQSACNLEKKQK 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:

The multiple alignment of the region surrounding the variant against various orthologous sequences.

Human                         KVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQK

                              KVAAYDKLEKTKTRLQQELDDLLVDLDHQRRTASNLEKKQK

Mouse                         KVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQK

Rat                           KVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSVSNLEKKQK

Chicken                       KIAAYDKLEKTKTRLQQELDDIAVDLDHQRQTVSNLEKKQK

Sequence annotation in neighborhood:

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.

Type	Positions	Description
Chain	2 – 1960	Myosin-9
Coiled coil	837 – 1926
Modified residue	1404 – 1404	N6-acetyllysine
Modified residue	1410 – 1410	N6-acetyllysine

Literature citations
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; Asp1424Asn MYH9 mutation results in an unstable protein responsible for the phenotypes in May-Hegglin anomaly/Fechtner syndrome.
Deutsch S.; Rideau A.; Bochaton-Piallat M.-L.; Merla G.; Geinoz A.; Gabbiani G.; Schwede T.; Matthes T.; Antonarakis S.E.; Beris P.;
Blood 102:529-534(2003)
Cited for: CHARACTERIZATION OF VARIANT MATINS ASN-1424; 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; MYH9-related disease: may-Hegglin anomaly, Sebastian syndrome, Fechtner syndrome, and Epstein syndrome are not distinct entities but represent a variable expression of a single illness.
Seri M.; Pecci A.; Di Bari F.; Cusano R.; Savino M.; Panza E.; Nigro A.; Noris P.; Gangarossa S.; Rocca B.; Gresele P.; Bizzaro N.; Malatesta P.; Koivisto P.A.; Longo I.; Musso R.; Pecoraro C.; Iolascon A.; Magrini U.; Rodriguez Soriano J.; Renieri A.; Ghiggeri G.M.; Ravazzolo R.; Balduini C.L.; Savoia A.;
Medicine (Baltimore) 82:203-215(2003)
Cited for: VARIANTS MATINS CYS-702; HIS-702; GLN-910; 1066-GLU--ALA-1072 DEL; ILE-1155; ASN-1424 AND HIS-1424; Macrothrombocytopenia and progressive deafness is due to a mutation in MYH9.
Mhatre A.N.; Kim Y.; Brodie H.A.; Lalwani A.K.;
Otol. Neurotol. 24:205-209(2003)
Cited for: VARIANT MATINS ASN-1424;

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.