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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P10275: Variant p.Met896Thr

Androgen receptor
Gene: AR
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Variant information Variant position: help 896 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 Methionine (M) to Threonine (T) at position 896 (M896T, p.Met896Thr). 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 (M) to medium size and polar (T) 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 AIS; low androgen binding and transactivation. Any additional useful information about the variant.


Sequence information Variant position: help 896 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 920 The length of the canonical sequence.
Location on the sequence: help QFTFDLLIKSHMVSVDFPEM M AEIISVQVPKILSGKVKPIY 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                         QFTFDLLIKSHMVSVDFPEMMAEIISVQVPKILSGKVKPIY

                              QFTFDLLIKSHMVSVDFPEMMAEIISVQVPKILSGKVKPIY

Rhesus macaque                QFTFDLLIKSHMVSVDFPEMMAEIISVQVPKILSGKVKPIY

Chimpanzee                    QFTFDLLIKSHMVSVDFPEMMAEIISVQVPKILSGKVKPIY

Mouse                         QFTFDLLIKSHMVSVDFPEMMAEIISVQVPKILSGKVKPIY

Rat                           QFTFDLLIKSHMVSVDFPEMMAEIISVQVPKILSGKVKPIY

Pig                           QFTFDLLIKSHMVSVDFPEMMAEIISVQVPKILSGKVKPIY
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 – 920 Androgen receptor
Domain 669 – 900 NR LBD
Region 552 – 919 Interaction with LPXN
Region 592 – 919 Interaction with CCAR1
Region 625 – 919 Interaction with KAT7
Binding site 878 – 878
Site 898 – 898 Interaction with coactivator FXXLF and FXXFY motifs
Modified residue 916 – 916 Phosphotyrosine; by CSK
Alternative sequence 645 – 920 Missing. In isoform 3.
Alternative sequence 649 – 920 Missing. In isoform 4.
Mutagenesis 898 – 898 E -> AQ. Reduced transcription activation in the presence of androgen.
Mutagenesis 898 – 898 E -> KR. Loss of transcription activation in the presence of androgen.
Mutagenesis 916 – 916 Y -> F. Decrease in CSK-induced phosphorylation.
Helix 894 – 902



Literature citations
Structural basis for accommodation of nonsteroidal ligands in the androgen receptor.
Bohl C.E.; Miller D.D.; Chen J.; Bell C.E.; Dalton J.T.;
J. Biol. Chem. 280:37747-37754(2005)
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 665-920 IN COMPLEXES WITH NONSTEROIDAL LIGANDS; MUTAGENESIS OF TRP-742; CHARACTERIZATION OF VARIANT PROSTATE CANCER ALA-878; CHARACTERIZATION OF VARIANT AIS THR-896; Functional characterisation of mutations in the ligand-binding domain of the androgen receptor gene in patients with androgen insensitivity syndrome.
Lundberg Giwercman Y.; Nikoshkov A.; Lindsten K.; Bystroem B.; Pousette A.; Chibalin A.V.; Arvidsson S.; Tiulpakov A.; Semitcheva T.V.; Peterkova V.; Hagenfeldt K.; Ritzen E.M.; Wedell A.;
Hum. Genet. 103:529-531(1998)
Cited for: VARIANTS AIS THR-766; TYR-785 AND THR-896; VARIANT PAIS GLY-841;
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.