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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P23945: Variant p.Asp224Val

Follicle-stimulating hormone receptor
Gene: FSHR
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Variant information Variant position: help 224 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 Aspartate (D) to Valine (V) at position 224 (D224V, p.Asp224Val). 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 acidic (D) to medium size and hydrophobic (V) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -3 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 ODG1; FSH binding is barely detectable; impaired targeting to the cell membrane; adenylate cyclase stimulation by FSH is 4 +-2% residual activity. Any additional useful information about the variant.


Sequence information Variant position: help 224 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 695 The length of the canonical sequence.
Location on the sequence: help NNLEELPNDVFHGASGPVIL D ISRTRIHSLPSYGLENLKKL 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                         NNLEELPNDVFHGASGPVILDISRTRIHSLPSYGLENLKKL

Mouse                         NNLEELPDDVFQGASGPVVLDISRTKVYSLPNHGLENLKKL

Rat                           NNLEELPNDVFQGASGPVILDISRTKVHSLPNHGLENLKKL

Pig                           DNLEELPNDVFQGASGPVILDISRTRIHSLPSYGLENLKKL

Bovine                        SNLEELPNDVFQGASGPVILDISRTRIRSLPSYGLENLKKL

Sheep                         SNLEELPNDVFQGASGPVILDISRTRIRSLPSYGLENLKKL

Cat                           INLEELPNDVFQGASGPVILDISRTRIHSLPSYGLENIKKL

Horse                         NNLEELPNDVFQGASGPVILDISGTRIHSLPNYGLENLKKL

Chicken                       YNLEKLPEKVFQGAIGPVVLDISRTRISFLPSHGLEFIKKL
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 18 – 695 Follicle-stimulating hormone receptor
Topological domain 18 – 366 Extracellular
Repeat 217 – 240 LRR 8
Alternative sequence 223 – 223 L -> LNRRTRTPTEPNVLLAKYPSGQGVLEEPESLSSSI. In isoform 4.
Alternative sequence 224 – 285 Missing. In isoform Short.
Beta strand 221 – 224



Literature citations
New natural inactivating mutations of the follicle-stimulating hormone receptor: correlations between receptor function and phenotype.
Touraine P.; Beau I.; Gougeon A.; Meduri G.; Desroches A.; Pichard C.; Detoeuf M.; Paniel B.; Prieur M.; Zorn J.-R.; Milgrom E.; Kuttenn F.; Misrahi M.;
Mol. Endocrinol. 13:1844-1854(1999)
Cited for: VARIANTS ODG1 VAL-224 AND VAL-601; CHARACTERIZATION OF VARIANTS ODG1 VAL-224; CYS-573 AND VAL-601;
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.