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UniProtKB/Swiss-Prot P48436: Variant p.Pro170Arg

Transcription factor SOX-9
Gene: SOX9
Variant information

Variant position:  170
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 Proline (P) to Arginine (R) at position 170 (P170R, p.Pro170Arg).
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 (P) to large size and basic (R)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -2
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 CMD1.
Any additional useful information about the variant.



Sequence information

Variant position:  170
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  509
The length of the canonical sequence.

Location on the sequence:   EKRPFVEEAERLRVQHKKDH  P DYKYQPRRRKSVKNGQAEAE
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                         EKRPFVEEAERLRVQHKKDHPDYKYQPRRRKSVKNGQAEAE

                              EKRPFVEEAERLRVQHKKDHPDYKYQPRRRKSVKNGQAEAE

Rhesus macaque                EKRPFVEEAERLRVQHKKDHPDYKYQPRRRKSVKNGQAEAE

Chimpanzee                    EKRPFVEEAERLRVQHKKDHPDYKYQPRRRKSVKNGQAEAE

Mouse                         EKRPFVEEAERLRVQHKKDHPDYKYQPRRRKSVKNGQAEAE

Rat                           EKRPFVEEAERLRVQHKKDHPDYKYQPRRRKSVKNGQAEAE

Pig                           EKRPFVEEAERLRVQHKKDHPDYKYQPRRRKSVKNGQAEAE

Chicken                       EKRPFVEEAERLRVQHKKDHPDYKYQPRRRKSVKNGQSEQE

Xenopus tropicalis            EKRPFVEEAERLRIQHKKDHPDYKYQPRRRKSVKNGQSEQE

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.

TypePositionsDescription
Chain 1 – 509 Transcription factor SOX-9
DNA binding 105 – 173 HMG box
Region 160 – 273 Disordered
Compositional bias 160 – 187 Basic and acidic residues


Literature citations

Mutational analysis of the SOX9 gene in campomelic dysplasia and autosomal sex reversal: lack of genotype/phenotype correlations.
Meyer J.; Suedbeck P.; Held M.; Wagner T.; Schmitz M.L.; Bricarelli F.D.; Eggermont E.; Friedrich U.; Haas O.A.; Kobelt A.; Leroy J.G.; van Maldergem L.; Michel E.; Mitulla B.; Pfeiffer R.A.; Schinzel A.; Schmidt H.; Scherer G.;
Hum. Mol. Genet. 6:91-98(1997)
Cited for: VARIANTS CMD1 LEU-108; ARG-143; PRO-152 AND ARG-170;

Functional and structural studies of wild type SOX9 and mutations causing campomelic dysplasia.
McDowall S.; Argentaro A.; Ranganathan S.; Weller P.; Mertin S.; Mansour S.; Tolmie J.; Harley V.;
J. Biol. Chem. 274:24023-24030(1999)
Cited for: VARIANTS CMD1 LEU-112; VAL-119; TYR-165 AND ARG-170; 3D-STRUCTURE MODELING;

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.