UniProtKB/SwissProt variant VAR

Variant information

Variant position:

908

The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:

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:

From Leucine (L) to Phenylalanine (F) at position 908 (L908F, p.Leu908Phe).

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:

Change from medium size and hydrophobic (L) to large size and aromatic (F)

The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:

0

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:

In AIS; almost complete loss of transcription activation.

Any additional useful information about the variant.

Sequence information

Variant position:

908

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:

VSVDFPEMMAEIISVQVPKI L SGKVKPIYFHTQ

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                         VSVDFPEMMAEIISVQVPKILSGKVKPIYFHTQ

                              VSVDFPEMMAEIISVQVPKILSGKVKPIYFHTQ

Rhesus macaque                VSVDFPEMMAEIISVQVPKILSGKVKPIYFHTQ

Chimpanzee                    VSVDFPEMMAEIISVQVPKILSGKVKPIYFHTQ

Mouse                         VSVDFPEMMAEIISVQVPKILSGKVKPIYFHTQ

Rat                           VSVDFPEMMAEIISVQVPKILSGKVKPIYFHTQ

Pig                           VSVDFPEMMAEIISVQVPKILSGKVKPIYFHTQ

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
Region	552 – 919	Interaction with LPXN
Region	592 – 919	Interaction with CCAR1
Region	625 – 919	Interaction with KAT7
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	904 – 908

Literature citations

Wide variation in androgen receptor dysfunction in complete androgen insensitivity syndrome.
Bevan C.L.; Hughes I.A.; Patterson M.N.;
J. Steroid Biochem. Mol. Biol. 61:19-26(1997)
Cited for: VARIANTS AIS ASP-751; PHE-763; THR-766; ASN-865 AND PHE-908;

Human androgen receptor gene ligand-binding-domain mutations leading to disrupted interaction between the N- and C-terminal domains.
Jaeaeskelaeinen J.; Deeb A.; Schwabe J.W.; Mongan N.P.; Martin H.; Hughes I.A.;
J. Mol. Endocrinol. 36:361-368(2006)
Cited for: CHARACTERIZATION OF VARIANTS AIS ASN-696; CYS-764; HIS-775; GLU-799; HIS-856 AND PHE-908;

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P10275: Variant p.Leu908Phe