Variant position: 156 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 195 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 PKPRERPQIGGTIKQPPSNP PPRPPAEARKKPSEEEAAVAA
Mouse PKPKERPQVGGTIKQPPTNP PPRPPAEVRKKPSE---GEEE
Rat PKPKERPQVGGTIKQPPTNP PPRPPAEVRKKPSE---AEEE
Pig PKPKERPQVGGTIKQPPSNP PPRPPPEARKKPGE---EAVA
Bovine PKPKERPQIGGTIKQPPSNP PPRPPAEARKKPSE----EAA
Rabbit PRPKERPQVGGTIKQPPSNP PPRPPVEARKKPGEED-ATPA
Slime mold KQD----------------- ---------------------
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
2 – 195 Cytochrome b-245 light chain
133 – 189 Pro-rich
147 – 147 Phosphothreonine
168 – 168 Phosphoserine
157 – 157 P -> Q. Loss of interaction with NOXO1.
Point mutation in the cytoplasmic domain of the neutrophil p22-phox cytochrome b subunit is associated with a nonfunctional NADPH oxidase and chronic granulomatous disease.
Dinauer M.C.; Pierce E.A.; Erickson R.W.; Muhlebach T.J.; Messner H.; Orkin S.H.; Seger R.A.; Curnutte J.T.;
Proc. Natl. Acad. Sci. U.S.A. 88:11231-11235(1991)
Cited for: VARIANT ARCGD GLN-156;
156Pro-->Gln substitution in the light chain of cytochrome b558 of the human NADPH oxidase (p22-phox) leads to defective translocation of the cytosolic proteins p47-phox and p67-phox.
Leusen J.H.; Bolscher B.G.; Hilarius P.M.; Weening R.S.; Kaulfersch W.; Seger R.A.; Roos D.; Verhoeven A.J.;
J. Exp. Med. 180:2329-2334(1994)
Cited for: CHARACTERIZATION OF VARIANT ARCGD GLN-156;
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.