Variant position: 120 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 175 The length of the canonical sequence.
Location on the sequence:
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 VHGKHEERQDEHGFISREFH RKYRIPADVDPLTITSSLSSD
Mouse VHGKHEERQDEHGFISREFH RKYRIPADVDPLTITSSLSSD
Rat VHGKHEERQDEHGFISREFH RKYRIPADVDPLTITSSLSSD
Pig VHGKHEERQDEHGFISREFH RKYRIPADVDPLTITSSLSSD
Bovine VHGKHEERQDEHGFISREFH RKYRIPADVDPLAITSSLSSD
Rabbit VHGKHEERQDEHGFISREFH RKYRIPADVDPLTITSSLSSD
Sheep VHGKHEERQDEHGFISREFH RKYRIPADVDPLTITSSLSSD
Chicken IHGKHEERQDEHGFIAREFS RKYRIPADVDPLTITSSLSLD
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.
The novel alphaB-crystallin (CRYAB) mutation p.D109G causes restrictive cardiomyopathy.
Brodehl A.; Gaertner-Rommel A.; Klauke B.; Grewe S.A.; Schirmer I.; Peterschroeder A.; Faber L.; Vorgerd M.; Gummert J.; Anselmetti D.; Schulz U.; Paluszkiewicz L.; Milting H.;
Hum. Mutat. 38:947-952(2017)
Cited for: SUBCELLULAR LOCATION; TISSUE SPECIFICITY; INVOLVEMENT IN RESTRICTIVE CARDIOMYOPATHY; VARIANT GLY-109; CHARACTERIZATION OF VARIANT GLY-109 AND GLY-120;
A missense mutation in the alphaB-crystallin chaperone gene causes a desmin-related myopathy.
Vicart P.; Caron A.; Guicheney P.; Li Z.; Prevost M.-C.; Faure A.; Chateau D.; Chapon F.; Tome F.; Dupret J.-M.; Paulin D.; Fardeau M.;
Nat. Genet. 20:92-95(1998)
Cited for: VARIANT MFM2 GLY-120;
Alteration of protein-protein interactions of congenital cataract crystallin mutants.
Fu L.; Liang J.J.-N.;
Invest. Ophthalmol. Vis. Sci. 44:1155-1159(2003)
Cited for: CHARACTERIZATION OF VARIANTS MFM2 GLY-120;
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.