Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P16473: Variant p.Asn432Asp

Thyrotropin receptor
Gene: TSHR
Feedback?
Variant information Variant position: help 432 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 Asparagine (N) to Aspartate (D) at position 432 (N432D, p.Asn432Asp). 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 polar (N) to medium size and acidic (D) 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 CHNG1; abolishes cell membrane location; abolishes adenylate cyclase-activating G-protein coupled receptor signaling pathway; abolishes phospholipase C-activating G-protein coupled receptor signaling pathway. Any additional useful information about the variant.


Sequence information Variant position: help 432 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 764 The length of the canonical sequence.
Location on the sequence: help MGYKFLRIVVWFVSLLALLG N VFVLLILLTSHYKLNVPRFL 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                         MGYKFLRIVVWFVSLLALLGNVFVLLILLTSHYKLNVPRFL

                              MGYKFLRIVVWFVSLLALLGNVFVLIVLLTSHYKLTVPRFL

Mouse                         MGYRFLRIVVWFVSLLALLGNIFVLLILLTSHYKLTVPRFL

Rat                           MGYKFLRIVVWFVSPMALLGNVFVLFVLLTSHYKLTVPRFL

Pig                           MGYRFLRIVVWFVSLLALLGNVFVLVILLTSHYKLTVPRFL

Bovine                        MGYKFLRIVVWFVSLLALLGNVFVLVILLTSHYKLTVPRFL

Sheep                         MGYKFLRIVVWFVSLLALLGNVFVLVILLTSHYKLTVPRFL

Cat                           MGYKFLRIVVWFVSLLALLGNVFVLIILLTSHYKLTVPRFL
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 21 – 764 Thyrotropin receptor
Transmembrane 414 – 441 Helical; Name=1
Alternative sequence 254 – 764 Missing. In isoform Short.
Alternative sequence 275 – 764 Missing. In isoform 3.
Helix 432 – 441



Literature citations
Loss-of-function variants in a Hungarian cohort reveal structural insights on TSH receptor maturation and signaling.
Labadi A.; Grassi E.S.; Gellen B.; Kleinau G.; Biebermann H.; Ruzsa B.; Gelmini G.; Rideg O.; Miseta A.; Kovacs G.L.; Patocs A.; Felszeghy E.; Nagy E.V.; Mezosi E.; Persani L.;
J. Clin. Endocrinol. Metab. 100:E1039-E1045(2015)
Cited for: VARIANTS CHNG1 ALA-162; ASP-432 AND LEU-449; CHARACTERIZATION OF VARIANTS CHNG1 ASP-432 AND LEU-449;
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.