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:
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 EKRPFVEEAERLRVQHKKDH PDYKYQPRRRKSVKNGQAEAE
Rhesus macaque EKRPFVEEAERLRVQHKKDH PDYKYQPRRRKSVKNGQAEAE
Chimpanzee EKRPFVEEAERLRVQHKKDH PDYKYQPRRRKSVKNGQAEAE
Mouse EKRPFVEEAERLRVQHKKDH PDYKYQPRRRKSVKNGQAEAE
Rat EKRPFVEEAERLRVQHKKDH PDYKYQPRRRKSVKNGQAEAE
Pig EKRPFVEEAERLRVQHKKDH PDYKYQPRRRKSVKNGQAEAE
Chicken EKRPFVEEAERLRVQHKKDH PDYKYQPRRRKSVKNGQSEQE
Xenopus tropicalis EKRPFVEEAERLRIQHKKDH PDYKYQPRRRKSVKNGQSEQE
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 – 509 Transcription factor SOX-9
105 – 173 HMG box
160 – 273 Disordered
160 – 187 Basic and acidic residues
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;
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.