Variant position: 896 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 920 The length of the canonical sequence.
Location on the sequence:
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 QFTFDLLIKSHMVSVDFPEM MAEIISVQVPKILSGKVKPIY
Rhesus macaque QFTFDLLIKSHMVSVDFPEM MAEIISVQVPKILSGKVKPIY
Chimpanzee QFTFDLLIKSHMVSVDFPEM MAEIISVQVPKILSGKVKPIY
Mouse QFTFDLLIKSHMVSVDFPEM MAEIISVQVPKILSGKVKPIY
Rat QFTFDLLIKSHMVSVDFPEM MAEIISVQVPKILSGKVKPIY
Pig QFTFDLLIKSHMVSVDFPEM MAEIISVQVPKILSGKVKPIY
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.
Type Positions Description
1 – 920 Androgen receptor
669 – 900 NR LBD
552 – 919 Interaction with LPXN
592 – 919 Interaction with CCAR1
625 – 919 Interaction with KAT7
878 – 878 Androgen
898 – 898 Interaction with coactivator FXXLF and FXXFY motifs
916 – 916 Phosphotyrosine; by CSK
645 – 920 Missing. In isoform 3.
649 – 920 Missing. In isoform 4.
898 – 898 E -> AQ. Reduced transcription activation in the presence of androgen.
898 – 898 E -> KR. Loss of transcription activation in the presence of androgen.
916 – 916 Y -> F. Decrease in CSK-induced phosphorylation.
894 – 902
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;
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.