Sequence information
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: 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: The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human QFTFDLLIKSHMVSVDFPEMM AEIISVQVPKILSGKVKPIY
QFTFDLLIKSHMVSVDFPEMM AEIISVQVPKILSGKVKPIY
Rhesus macaque QFTFDLLIKSHMVSVDFPEMM AEIISVQVPKILSGKVKPIY
Chimpanzee QFTFDLLIKSHMVSVDFPEMM AEIISVQVPKILSGKVKPIY
Mouse QFTFDLLIKSHMVSVDFPEMM AEIISVQVPKILSGKVKPIY
Rat QFTFDLLIKSHMVSVDFPEMM AEIISVQVPKILSGKVKPIY
Pig QFTFDLLIKSHMVSVDFPEMM AEIISVQVPKILSGKVKPIY
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
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 Androgen
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.