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UniProtKB/Swiss-Prot P35670: Variant p.Gly85Val

Copper-transporting ATPase 2
Gene: ATP7B
Variant information

Variant position:  85
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 Glycine (G) to Valine (V) at position 85 (G85V, p.Gly85Val).
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 glycine (G) to medium size and hydrophobic (V)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -3
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 WD; decreased copper transport activity; decreased ATPase activity; increased interaction with COMMD1; decreased localization to trans-Golgi network; increased degradation.
Any additional useful information about the variant.

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



Sequence information

Variant position:  85
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  1465
The length of the canonical sequence.

Location on the sequence:   LGMTCQSCVKSIEDRISNLK  G IISMKVSLEQGSATVKYVPS
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                         LGMTCQSCVKSIEDRISNLKGIISMKVSLEQGSATVKYVPS

Mouse                         LGMTCHSCVKSIEDRISSLKGIVNIKVSLEQGSATVRYVPS

Rat                           LGMTCHSCVKSIEDRISSLKGIVSIKVSLEQGSATVKYVPS

Sheep                         VGMTCQSCVKSIEGRVSSLKGIVSIKVSLEQSSAEVRYVPS

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 – 1465 Copper-transporting ATPase 2
Topological domain 1 – 653 Cytoplasmic
Domain 59 – 125 HMA 1
Metal binding 69 – 69 Copper 1
Metal binding 72 – 72 Copper 1


Literature citations

Distinct Wilson's disease mutations in ATP7B are associated with enhanced binding to COMMD1 and reduced stability of ATP7B.
de Bie P.; van de Sluis B.; Burstein E.; van de Berghe P.V.; Muller P.; Berger R.; Gitlin J.D.; Wijmenga C.; Klomp L.W.;
Gastroenterology 133:1316-1326(2007)
Cited for: SUBCELLULAR LOCATION; INTERACTION WITH COMMD1 AND ATOX1; CHARACTERIZATION OF VARIANTS WD SER-41; VAL-85; SER-486; SER-492; HIS-532; LYS-541; ASP-591; PRO-604; GLN-616; TRP-616; ALA-626; SER-641; HIS-642 AND ARG-645;

Diverse functional properties of Wilson disease ATP7B variants.
Huster D.; Kuehne A.; Bhattacharjee A.; Raines L.; Jantsch V.; Noe J.; Schirrmeister W.; Sommerer I.; Sabri O.; Berr F.; Moessner J.; Stieger B.; Caca K.; Lutsenko S.;
Gastroenterology 142:947-956(2012)
Cited for: CHARACTERIZATION OF VARIANTS WD VAL-85; SER-492; TRP-616; ALA-626; ARG-645; SER-710; LEU-760; ASN-765; VAL-769; LEU-840; THR-857; VAL-874; GLN-969; LEU-992; LEU-1052; LYS-1064; GLN-1069; PHE-1083; VAL-1213; VAL-1222; ARG-1266; SER-1270 AND LEU-1273; CHARACTERIZATION OF VARIANTS ALA-406; LEU-456 AND ARG-832; MUTAGENESIS OF ASP-1027 AND THR-1031; FUNCTION; CATALYTIC ACTIVITY; SUBCELLULAR LOCATION;

Further delineation of the molecular pathology of Wilson disease in the Mediterranean population.
Loudianos G.; Dessi V.; Lovicu M.; Angius A.; Nurchi A.; Sturniolo G.C.; Marcellini M.; Zancan L.; Bragetti P.; Akar N.; Yagci R.; Vegnente A.; Cao A.; Pirastu M.;
Hum. Mutat. 12:89-94(1998)
Cited for: VARIANTS WD VAL-85; SER-492; 608-PHE-ASP-609 DELINS TYR; HIS-642; ARG-645; ILE-665; ARG-691; PHE-747; TRP-778; LEU-840; ASN-918; TRP-919; ASN-921; PRO-933; LEU-992; THR-1003; VAL-1018; TRP-1041; VAL-1089; MET-1146; GLY-1183; THR-1183; MET-1216; ASP-1341 AND SER-1358;

Mutation spectrum and polymorphisms in ATP7B identified on direct sequencing of all exons in Chinese Han and Hui ethnic patients with Wilson's disease.
Gu Y.-H.; Kodama H.; Du S.-L.; Gu Q.-J.; Sun H.-J.; Ushijima H.;
Clin. Genet. 64:479-484(2003)
Cited for: VARIANTS WD VAL-85; GLY-765; LEU-778; MET-890; GLY-919; MET-935; TYR-975; LEU-992; ARG-1098; THR-1148; LYS-1173 AND ASN-1248; VARIANTS ASP-14; ALA-406; LEU-456; ARG-832; ALA-1140; ASN-1143 AND SER-1245;

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.