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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P08034: Variant p.Arg238His

Gap junction beta-1 protein
Gene: GJB1
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Variant information Variant position: help 238 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 Arginine (R) to Histidine (H) at position 238 (R238H, p.Arg238His). 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 large size and basic (R) to medium size and polar (H) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 0 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; localized mainly on the cell membrane forming gap junction-like plaques. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 238 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 ARRAQRRSNPPSRKGSGFGH R LSPEYKQNEINKLLSEQDGS 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                         ARRAQRRSNPPSRKGS-GFGHRLSPEYKQNEINKLLSEQDGS

Mouse                         ARRAQRRSNPPSRKGS-GFGHRLSPEYKQNEINKLLSEQDG

Rat                           ARRAQRRSNPPSRKGS-GFGHRLSPEYKQNEINKLLSEQDG

Bovine                        ARRAQRRSNPPSRKGSGGFGHRLSPEYKQNEINKLLSEQDG

Horse                         ARRAQRRSNPPSRKGS-GFGHRLSPEYKQNEINKLLSEQDG

Xenopus laevis                TRRARRHRDS----GS------ISKEHQQNEMNLLITG--G
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
Topological domain 215 – 283 Cytoplasmic
Modified residue 233 – 233 Phosphoserine
Modified residue 258 – 258 Phosphoserine



Literature citations
Mutation analysis of the connexin 32 (Cx32) gene in Charcot-Marie-Tooth neuropathy type 1: identification of five new mutations.
Nelis E.; Simokovic S.; Timmerman V.; Loefgren A.; Backhovens H.; de Jonghe P.; Martin J.-J.; Van Broeckhoven C.;
Hum. Mutat. 9:47-52(1997)
Cited for: VARIANTS CMTX1 PHE-25; LEU-26; ALA-87 AND HIS-238; 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; Altered formation of hemichannels and gap junction channels caused by C-terminal connexin-32 mutations.
Castro C.; Gomez-Hernandez J.M.; Silander K.; Barrio L.C.;
J. Neurosci. 19:3752-3760(1999)
Cited for: CHARACTERIZATION OF VARIANTS CMTX1 LYS-208; GLN-215; TRP-215; HIS-238 AND GLY-280; Diverse trafficking abnormalities of connexin32 mutants causing CMTX.
Yum S.W.; Kleopa K.A.; Shumas S.; Scherer S.S.;
Neurobiol. Dis. 11:43-52(2002)
Cited for: CHARACTERIZATION OF VARIANTS CMTX ILE-34; LYS-34; THR-34; VAL-34; MET-35; MET-37; MET-38; VAL-40; GLN-75; PRO-75; TRP-75; ILE-205; VAL-213; CYS-219; HIS-219; GLY-220; CYS-230; LEU-230; HIS-238 AND ILE-239;
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.