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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P13498: Variant p.Pro156Gln

Cytochrome b-245 light chain
Gene: CYBA
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Variant information Variant position: help 156 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 Proline (P) to Glutamine (Q) at position 156 (P156Q, p.Pro156Gln). 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 hydrophobic (P) to medium size and polar (Q) 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 CGD4. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 156 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 195 The length of the canonical sequence.
Location on the sequence: help PKPRERPQIGGTIKQPPSNP P PRPPAEARKKPSEEEAAVAA 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                         PKPRERPQIGGTIKQPPSNPPPRPPAEARKKPSEEEAAVAA

Mouse                         PKPKERPQVGGTIKQPPTNPPPRPPAEVRKKPSEGEEEAAS

Rat                           PKPKERPQVGGTIKQPPTNPPPRPPAEVRKKPSEAEEEAAS

Pig                           PKPKERPQVGGTIKQPPSNPPPRPPPEARKKPGEE---AVA

Bovine                        PKPKERPQIGGTIKQPPSNPPPRPPAEARKKPSEE----AA

Rabbit                        PRPKERPQVGGTIKQPPSNPPPRPPVEARKKPGEEDA-TPA

Slime mold                    KQD--------------------------------------

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 2 – 195 Cytochrome b-245 light chain
Region 134 – 195 Disordered
Modified residue 147 – 147 Phosphothreonine
Modified residue 168 – 168 Phosphoserine
Cross 149 – 149 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Mutagenesis 157 – 157 P -> Q. Loss of interaction with NOXO1.



Literature citations
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 CGD4 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 CGD4 GLN-156;
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.