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UniProtKB/Swiss-Prot Q9Y223: Variant p.Val572Leu

Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
Gene: GNE
Variant information

Variant position:  572
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 Valine (V) to Leucine (L) at position 572 (V572L, p.Val572Leu).
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:  Similar physico-chemical property. Both residues are medium size and hydrophobic.
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 NM.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  572
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  722
The length of the canonical sequence.

Location on the sequence:   HQHELIHGSSFCAAELGHLV  V SLDGPDCSCGSHGCIEAYAS
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                         HQHELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYAS

Mouse                         HQHELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYAS

Rat                           HQHELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYAS

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.

TypePositionsDescription
Chain 1 – 722 Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
Region 406 – 722 N-acetylmannosamine kinase
Metal binding 569 – 569 Zinc
Metal binding 579 – 579 Zinc
Metal binding 581 – 581 Zinc
Metal binding 586 – 586 Zinc
Binding site 566 – 566 Substrate
Binding site 569 – 569 Substrate
Binding site 588 – 588 Substrate
Beta strand 571 – 574


Literature citations

A novel mutation in the GNE gene and a linkage disequilibrium in Japanese pedigrees.
Arai A.; Tanaka K.; Ikeuchi T.; Igarashi S.; Kobayashi H.; Asaka T.; Date H.; Saito M.; Tanaka H.; Kawasaki S.; Uyama E.; Mizusawa H.; Fukuhara N.; Tsuji S.;
Ann. Neurol. 52:516-519(2002)
Cited for: VARIANT NM LEU-572;

Nonaka myopathy is caused by mutations in the UDP-N-acetylglucosamine-2-epimerase/N-acetylmannosamine kinase gene (GNE).
Kayashima T.; Matsuo H.; Satoh A.; Ohta T.; Yoshiura K.; Matsumoto N.; Nakane Y.; Niikawa N.; Kishino T.;
J. Hum. Genet. 47:77-79(2002)
Cited for: VARIANTS NM VAL-460 AND LEU-572;

Four novel mutations associated with autosomal recessive inclusion body myopathy (MIM: 600737).
Darvish D.; Vahedifar P.; Huo Y.;
Mol. Genet. Metab. 77:252-256(2002)
Cited for: VARIANTS NM ASN-225; GLN-246; TRP-246; VAL-460; VAL-524; LEU-572; GLU-576; THR-631; HIS-675; MET-696 AND THR-712;

Distal myopathy with rimmed vacuoles: novel mutations in the GNE gene.
Tomimitsu H.; Ishikawa K.; Shimizu J.; Ohkoshi N.; Kanazawa I.; Mizusawa H.;
Neurology 59:451-454(2002)
Cited for: VARIANTS NM LEU-572 AND VAL-631;

Distal myopathy with rimmed vacuoles is allelic to hereditary inclusion body myopathy.
Nishino I.; Noguchi S.; Murayama K.; Driss A.; Sugie K.; Oya Y.; Nagata T.; Chida K.; Takahashi T.; Takusa Y.; Ohi T.; Nishimiya J.; Sunohara N.; Ciafaloni E.; Kawai M.; Aoki M.; Nonaka I.;
Neurology 59:1689-1693(2002)
Cited for: VARIANTS NM GLN-132; VAL-176; CYS-177; GLN-306; ALA-331; TYR-378; THR-472; LEU-572; THR-630 AND VAL-631;

Mutations spectrum of GNE in hereditary inclusion body myopathy sparing the quadriceps.
Eisenberg I.; Grabov-Nardini G.; Hochner H.; Korner M.; Sadeh M.; Bertorini T.; Bushby K.; Castellan C.; Felice K.; Mendell J.; Merlini L.; Shilling C.; Wirguin I.; Argov Z.; Mitrani-Rosenbaum S.;
Hum. Mutat. 21:99-99(2003)
Cited for: VARIANTS NM LEU-36; PHE-200; ASN-225; GLN-246; VAL-303; TYR-378; VAL-460; CYS-528; THR-557; LEU-572; GLU-576; THR-587; THR-631; VAL-631; MET-696 AND THR-712;

GNE mutations causing distal myopathy with rimmed vacuoles with inflammation.
Yabe I.; Higashi T.; Kikuchi S.; Sasaki H.; Fukazawa T.; Yoshida K.; Tashiro K.;
Neurology 61:384-386(2003)
Cited for: VARIANTS NM THR-472 AND LEU-572;

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.