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UniProtKB/Swiss-Prot Q9Y210: Variant p.Gly109Ser

Short transient receptor potential channel 6
Gene: TRPC6
Variant information

Variant position:  109
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 Glycine (G) to Serine (S) at position 109 (G109S, p.Gly109Ser).
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 glycine (G) to small size and polar (S)
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 FSGS2; increases calcium ion transport.
Any additional useful information about the variant.



Sequence information

Variant position:  109
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  931
The length of the canonical sequence.

Location on the sequence:   SDRSTSLSIEEERFLDAAEY  G NIPVVRKMLEECHSLNVNCV
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                         SDRSTSLSIEEERFLDAAEYGNIPVVRKMLEECHSLNVNCV

Mouse                         NDHSTSLSIEEERFLDAAEYGNIPVVRKMLEECHSLNVNCV

Bovine                        NDHSTSLSIEEERFLDAAEYGNIPVVRKMLEECLSLNVNCV

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 – 931 Short transient receptor potential channel 6
Topological domain 1 – 438 Cytoplasmic
Repeat 97 – 126 ANK 1
Mutagenesis 110 – 110 N -> H. Increases calcium ion transport.
Mutagenesis 125 – 125 N -> A. No effect on RNF24-binding; when associated with A-127; A-128 and A-130.
Mutagenesis 127 – 127 N -> A. No effect on RNF24-binding; when associated with A-125; A-128 and A-130.
Mutagenesis 128 – 128 C -> A. No effect on RNF24-binding; when associated with A-125; A-127 and A-130.


Literature citations

TRPC6 mutational analysis in a large cohort of patients with focal segmental glomerulosclerosis.
Santin S.; Ars E.; Rossetti S.; Salido E.; Silva I.; Garcia-Maset R.; Gimenez I.; Ruiz P.; Mendizabal S.; Luciano Nieto J.; Pena A.; Camacho J.A.; Fraga G.; Cobo M.A.; Bernis C.; Ortiz A.; de Pablos A.L.; Sanchez-Moreno A.; Pintos G.; Mirapeix E.; Fernandez-Llama P.; Ballarin J.; Torra R.; Zamora I.; Lopez-Hellin J.; Madrid A.; Ventura C.; Vilalta R.; Espinosa L.; Garcia C.; Melgosa M.; Navarro M.; Gimenez A.; Cots J.V.; Alexandra S.; Caramelo C.; Egido J.; San Jose M.D.; de la Cerda F.; Sala P.; Raspall F.; Vila A.; Daza A.M.; Vazquez M.; Ecija J.L.; Espinosa M.; Justa M.L.; Poveda R.; Aparicio C.; Rosell J.; Muley R.; Montenegro J.; Gonzalez D.; Hidalgo E.; de Frutos D.B.; Trillo E.; Gracia S.; de los Rios F.J.;
Nephrol. Dial. Transplant. 24:3089-3096(2009)
Cited for: VARIANTS FSGS2 SER-109; SER-125 AND PRO-780;

TRPC6 G757D Loss-of-Function Mutation Associates with FSGS.
Riehle M.; Buescher A.K.; Gohlke B.O.; Kassmann M.; Kolatsi-Joannou M.; Braesen J.H.; Nagel M.; Becker J.U.; Winyard P.; Hoyer P.F.; Preissner R.; Krautwurst D.; Gollasch M.; Weber S.; Harteneck C.;
J. Am. Soc. Nephrol. 27:2771-2783(2016)
Cited for: MUTAGENESIS OF ASN-110; MET-132; 755-GLU--GLY-757; 755-GLU-GLU-756; 826-LYS-LYS-827 AND GLN-889; VARIANTS FSGS2 SER-109; GLN-112; SER-125; SER-143; GLN-175; LEU-218; ALA-395; ASP-757; PRO-780; CYS-895; LEU-895 AND LYS-897; CHARACTERIZATION OF VARIANTS FSGS2 SER-109; GLN-112; SER-125; SER-143; GLN-175; LEU-218; ALA-395; ASP-757; PRO-780; CYS-895; LEU-895 AND LYS-897; VARIANT VAL-404; CHARACTERIZATION OF VARIANT VAL-404; FUNCTION; SUBCELLULAR LOCATION; SUBUNIT;

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.