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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P30556: Variant p.Thr282Met

Type-1 angiotensin II receptor
Gene: AGTR1
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Variant information Variant position: help 282 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 Threonine (T) to Methionine (M) at position 282 (T282M, p.Thr282Met). 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 (T) to medium size and hydrophobic (M) 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 RTD. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 282 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 359 The length of the canonical sequence.
Location on the sequence: help LDVLIQLGIIRDCRIADIVD T AMPITICIAYFNNCLNPLFY 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                         LDVLIQLGIIRDCRIADIVDTAMPITICIAYFNNCLNPLFY

                              LDVLIQLGIIHDCKIADIVDTAMPITICIAYFNNCLNPLFY

Chimpanzee                    LDVLIQLGIIRDCRIADIVDTAMPITICIAYFNNCLNPLFY

Pig                           LDVLIQLGIIHDCKIADIVDTAMPITICLAYFNNCLNPLFY

Bovine                        MDVLIQLGLIRDCKIEDIVDTAMPITICLAYFNNCLNPLFY

Rabbit                        LDVLIQLGVIHDCRIADIVDTAMPITICIAYFNNCLNPLFY

Sheep                         MDVLIQLGLIRDCKIEDIVDTAMPITICLAYFNNCLNPPFY

Chicken                       LDVLIQLHVITDCKITDIVDTAMPFTICIAYFNNCLNPFFY
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 1 – 359 Type-1 angiotensin II receptor
Transmembrane 279 – 304 Helical; Name=7
Mutagenesis 284 – 284 M -> A. Slightly affects binding to eprosartan inhibitor.
Mutagenesis 285 – 285 P -> A. Decreased binding to eprosartan inhibitor.
Mutagenesis 288 – 288 I -> A. Decreased binding to eprosartan inhibitor.
Mutagenesis 292 – 292 Y -> A. Mimics the disordered side chain induced by angiotensin II-binding; increased affinity for G-protein subunit alpha proteins. Decreased affinity for telmisartan.
Helix 274 – 295



Literature citations
Mutations in genes in the renin-angiotensin system are associated with autosomal recessive renal tubular dysgenesis.
Gribouval O.; Gonzales M.; Neuhaus T.; Aziza J.; Bieth E.; Laurent N.; Bouton J.M.; Feuillet F.; Makni S.; Ben Amar H.; Laube G.; Delezoide A.-L.; Bouvier R.; Dijoud F.; Ollagnon-Roman E.; Roume J.; Joubert M.; Antignac C.; Gubler M.-C.;
Nat. Genet. 37:964-968(2005)
Cited for: VARIANT RTD MET-282;
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.