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UniProtKB/Swiss-Prot Q9GZV9: Variant p.Arg179Gln

Fibroblast growth factor 23
Gene: FGF23
Variant information

Variant position:  179
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  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:  From Arginine (R) to Glutamine (Q) at position 179 (R179Q, p.Arg179Gln).
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:  Change from large size and basic (R) to medium size and polar (Q)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  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:  In ADHR; C-terminal processing is abolished; reduced proteolysis by PHEX; resistant to cleavage by furin.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  179
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  251
The length of the canonical sequence.

Location on the sequence:   SRRNEIPLIHFNTPIPRRHT  R SAEDDSERDPLNVLKPRARM
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                         SRRNEIPLIHFNTPIPRRHTRSAEDDSERDPLNVLKPRARM

Mouse                         ARRNEVPLLHFYTVRPRRHTRSAEDPPERDPLNVLKPRPRA

Rat                           ARRNEVPLLHFYTARPRRHTRSAEDPPERDPLNVLKPRPRA

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.

TypePositionsDescription
Chain 25 – 251 Fibroblast growth factor 23
Chain 25 – 179 Fibroblast growth factor 23 N-terminal peptide
Site 179 – 180 Cleavage; by proprotein convertases
Glycosylation 178 – 178 O-linked (GalNAc) threonine


Literature citations

Autosomal dominant hypophosphataemic rickets is associated with mutations in FGF23.
White K.E.; Evans W.E.; O'Riordan J.L.H.; Speer M.C.; Econs M.J.; Lorenz-Depiereux B.; Grabowski M.; Meitinger T.; Strom T.M.;
Nat. Genet. 26:345-348(2000)
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; FUNCTION; VARIANTS ADHR GLN-176; GLN-179 AND TRP-179; VARIANT MET-239;

FGF-23 inhibits renal tubular phosphate transport and is a PHEX substrate.
Bowe A.E.; Finnegan R.; Jan de Beur S.M.; Cho J.; Levine M.A.; Kumar R.; Schiavi S.C.;
Biochem. Biophys. Res. Commun. 284:977-981(2001)
Cited for: FUNCTION; CHARACTERIZATION OF VARIANT ADHR GLN-179;

Polypeptide GalNAc-transferase T3 and familial tumoral calcinosis. Secretion of fibroblast growth factor 23 requires O-glycosylation.
Kato K.; Jeanneau C.; Tarp M.A.; Benet-Pages A.; Lorenz-Depiereux B.; Bennett E.P.; Mandel U.; Strom T.M.; Clausen H.;
J. Biol. Chem. 281:18370-18377(2006)
Cited for: SUBCELLULAR LOCATION; GLYCOSYLATION AT THR-178; CHARACTERIZATION OF VARIANTS ADHR GLN-176 AND GLN-179; IDENTIFICATION BY MASS SPECTROMETRY;

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.