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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P08034: Variant p.Gln80Arg

Gap junction beta-1 protein
Gene: GJB1
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Variant information Variant position: help 80 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 Glutamine (Q) to Arginine (R) at position 80 (Q80R, p.Gln80Arg). 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 polar (Q) to large size and basic (R) 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 CMTX1. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 80 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 283 The length of the canonical sequence.
Location on the sequence: help CNSVCYDQFFPISHVRLWSL Q LILVSTPALLVAMHVAHQQH 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                         CNSVCYDQFFPISHVRLWSLQLILVSTPALLVAMHVAHQQH

Mouse                         CNSVCYDHFFPISHVRLWSLQLILVSTPALLVAMHVAHQQH

Rat                           CNSVCYDHFFPISHVRLWSLQLILVSTPALLVAMHVAHQQH

Bovine                        CNSVCYDHFFPISHVRLWSLQLILVSTPALLVAMHVAHQQH

Horse                         CNSVCYDHFFPISHVRLWSLQLILVSTPALLVAMHVAHQQH

Xenopus laevis                CNSVCYDHFFPISHIRLWALQLIIVSTPALLVAMHVAHLQH
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 – 283 Gap junction beta-1 protein
Transmembrane 76 – 95 Helical
Helix 73 – 102



Literature citations
Correlation between connexin 32 gene mutations and clinical phenotype in X-linked dominant Charcot-Marie-Tooth neuropathy.
Ionasescu V.; Ionasescu R.; Searby C.;
Am. J. Med. Genet. 63:486-491(1996)
Cited for: VARIANTS CMTX1 SER-3; GLN-22; SER-77; ARG-80; GLY-102; TRP-142 AND TRP-164; Connexin32 and X-linked Charcot-Marie-Tooth disease.
Bone L.J.; Deschenes S.M.; Balice-Gordon R.J.; Fischbeck K.H.; Scherer S.S.;
Neurobiol. Dis. 4:221-230(1997)
Cited for: VARIANTS CMTX1 ARG-3; SER-3; CYS-7; SER-12; LEU-13; MET-13; LYS-14; GLN-15; TRP-15; PRO-16; SER-20; ASP-21; GLN-22; PRO-22; GLY-22; ALA-23; PHE-25; LEU-26; ASN-28; THR-28; LEU-29; ASN-30; THR-34; VAL-34; MET-35; MET-38; VAL-40; LYS-41; LEU-44; TYR-49; SER-53; PHE-56; PHE-60; ILE-63; SER-64; CYS-65; GLN-75; PRO-75; TRP-75; SER-77; ARG-80; CYS-85; PHE-85; ALA-86; ASN-86; SER-86; ALA-87; LEU-87; SER-87; PRO-89; HIS-90; VAL-93; GLN-94; TYR-94; MET-95; TYR-100; GLY-102; GLU-103; TRP-107; 111-HIS--HIS-116 DEL; ASN-124; PRO-128; ARG-133; MET-139; TRP-142; GLU-142; LEU-143 DEL; ARG-156; PHE-156; CYS-157; ALA-158; ARG-158; HIS-160; PRO-161; TRP-164; GLN-164; SER-172; LEU-172; TYR-178; ARG-179; LEU-180; MET-181; THR-182; CYS-183; SER-183; HIS-183; THR-185 DEL; LYS-186; GLU-187; GLY-189; ILE-189; 191-THR--PHE-193 DEL; CYS-193; PHE-198; ARG-199; ARG-201; VAL-204; SER-205; LYS-208; TRP-215; CYS-219; HIS-219; GLY-220; CYS-230; LEU-230; CYS-235 AND HIS-238; X-linked Charcot-Marie-Tooth disease and connexin32.
Ionasescu V.V.;
Cell Biol. Int. 22:807-813(1998)
Cited for: VARIANTS CMTX1 SER-3; GLN-22; ALA-70; SER-77; ARG-80; MET-95; GLY-102; TRP-142; TRP-164 AND SER-180; Screening for mutations in the peripheral myelin genes PMP22, MPZ and Cx32 (GJB1) in Russian Charcot-Marie-Tooth neuropathy patients.
Mersiyanova I.V.; Ismailov S.M.; Polyakov A.V.; Dadali E.L.; Fedotov V.P.; Nelis E.; Loefgren A.; Timmerman V.; Van Broeckhoven C.; Evgrafov O.V.;
Hum. Mutat. 15:340-347(2000)
Cited for: VARIANTS CMTX1 20-ILE-GLY-21 DELINS ASN-SER; LYS-34; ARG-80; VAL-90; VAL-93; TRP-107; TRP-142; GLN-164; HIS-183; LYS-186; LEU-193 AND LYS-208;
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.