Sequence information
Variant position: 231 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 240 The length of the canonical sequence.
Location on the sequence:
GVCGPGLWERQAREHSERKK
R RRESECKAA
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 GVCGPGLWERQAREHSERKKR RRESECKAA------------------
Mouse GTSSSAAWESQTKE---RKKR RRESECKTT
Rat GTSNSEAWESQTKE---RKKR RRESECKTT
Rabbit GASGPAPWARQAQEHAERKKR RRESECKAA
Caenorhabditis elegans GTVEERILETTTASLPPVTQS QPIGSSSYY
Drosophila GIK------------------ ---------
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.
Type Positions Description
Chain
19 – 240
Extracellular superoxide dismutase [Cu-Zn]
Site
238 – 238
Not glycated
Glycosylation
229 – 229
N-linked (Glc) (glycation) lysine; in vitro
Glycosylation
230 – 230
N-linked (Glc) (glycation) lysine; in vitro
Literature citations
Submission
NIEHS SNPs program;
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]; VARIANTS THR-58; THR-91 AND GLY-231;
10-fold increase in human plasma extracellular superoxide dismutase content caused by a mutation in heparin-binding domain.
Sandstrom J.; Nilsson P.; Karlsson K.; Marklund S.L.;
J. Biol. Chem. 269:19163-19166(1994)
Cited for: VARIANT GLY-231;
Molecular analysis of extracellular-superoxide dismutase gene associated with high level in serum.
Yamada H.; Yamada Y.; Adachi T.; Goto H.; Ogasawara N.; Futenma A.; Kitano M.; Hirano K.; Kato K.;
Jpn. J. Hum. Genet. 40:177-184(1995)
Cited for: VARIANT GLY-231;
Substitution of glycine for arginine-213 in extracellular-superoxide dismutase impairs affinity for heparin and endothelial cell surface.
Adachi T.; Yamada H.; Yamada Y.; Morihara N.; Yamazaki N.; Murakami T.; Futenma A.; Kato K.; Hirano K.;
Biochem. J. 313:235-239(1996)
Cited for: VARIANT GLY-231;
An arginine-213 to glycine mutation in human extracellular-superoxide dismutase reduces susceptibility to trypsin-like proteinases.
Adachi T.; Morihara N.; Yamazaki N.; Yamada H.; Futenma A.; Kato K.; Hirano K.;
J. Biochem. 120:184-188(1996)
Cited for: VARIANT GLY-231;
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.