Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q14973: Variant p.Arg252His

Hepatic sodium/bile acid cotransporter
Gene: SLC10A1
Feedback?
Variant information Variant position: help 252 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help 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: help From Arginine (R) to Histidine (H) at position 252 (R252H, p.Arg252His). 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: help Change from large size and basic (R) to medium size and polar (H) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 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: help In FHCA2; loss of function in taurocholate transport; loss of localization to the cell membrane due to intracellular retention. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 252 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 349 The length of the canonical sequence.
Location on the sequence: help IGFLLGYVLSALFCLNGRCR R TVSMETGCQNVQLCSTILNV 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         IGFLLGYVLSALFCLNGRCRRTVSMETGCQNVQLCSTILNV

Mouse                         TGFLMGYILSALFRLNPSCRRTISMETGFQNVQLCSTILNV

Rat                           SGFLMGYILSALFQLNPSCRRTISMETGFQNIQLCSTILNV
Sequence annotation in neighborhood: help 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 – 349 Hepatic sodium/bile acid cotransporter
Transmembrane 248 – 273 Discontinuously helical; Name=8
Mutagenesis 261 – 261 Q -> A. Abolishes interaction with HBV myristoylated pre-S1 peptide.
Mutagenesis 263 – 263 V -> W. Disrupts interaction with HBV myristoylated pre-S1 peptide.
Mutagenesis 264 – 264 Q -> AW. Disrupts interaction with HBV myristoylated pre-S1 peptide, reduces bile acid transport and reduces HBV infection.
Mutagenesis 268 – 268 T -> W. Disrupts interaction with HBV myristoylated pre-S1 peptide, reduces bile acid transport and reduces HBV infection.
Mutagenesis 272 – 272 V -> W. Disrupts interaction with HBV myristoylated pre-S1 peptide, reduces bile acid transport and reduces HBV infection.
Helix 248 – 259



Literature citations
Sodium taurocholate cotransporting polypeptide (SLC10A1) deficiency: conjugated hypercholanemia without a clear clinical phenotype.
Vaz F.M.; Paulusma C.C.; Huidekoper H.; de Ru M.; Lim C.; Koster J.; Ho-Mok K.; Bootsma A.H.; Groen A.K.; Schaap F.G.; Oude Elferink R.P.; Waterham H.R.; Wanders R.J.;
Hepatology 61:260-267(2015)
Cited for: FUNCTION; SUBCELLULAR LOCATION; VARIANT FHCA2 HIS-252; CHARACTERIZATION OF VARIANT FHCA2 HIS-252; TRANSPORT ACTIVITY; BIOPHYSICOCHEMICAL PROPERTIES;
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.