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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O94956: Variant p.Glu77Lys

Solute carrier organic anion transporter family member 2B1
Gene: SLCO2B1
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Variant information Variant position: help 77 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help US 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 Glutamate (E) to Lysine (K) at position 77 (E77K, p.Glu77Lys). 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 medium size and acidic (E) to large size and basic (K) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 1 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 a breast cancer sample; somatic mutation. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 77 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 709 The length of the canonical sequence.
Location on the sequence: help LLQLAQLMISGYLKSSISTV E KRFGLSSQTSGLLASFNEVG 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                         LLQLAQLMISGYLKSSISTVEKRFGLSSQTSGLLASFNEVG

Mouse                         LLQLTQLMISGYLKSSISTVEKRFGLSSQISGLLAAFNEVG

Rat                           ILQLAQLMISGYLKSSISTVEKRFGLSSQTSGLLAAFNEVG

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 – 709 Solute carrier organic anion transporter family member 2B1
Topological domain 70 – 88 Extracellular
Alternative sequence 1 – 116 Missing. In isoform 2.
Alternative sequence 6 – 149 Missing. In isoform 4.
Mutagenesis 57 – 57 L -> A. Decreased E1S transport.
Mutagenesis 58 – 58 L -> A. Decreased E1S transport, no change in cell surface expression; increased Km value and decreased Vmax value for E1S transport activity. Decreased taurocholate transport.
Mutagenesis 58 – 58 L -> I. Decreased E1S transport.
Mutagenesis 59 – 59 Q -> A. Decreased E1S transport, no change in cell surface expression; no change in Km value and decreased Vmax value for E1S transport activity. Decreased taurocholate transport.
Mutagenesis 59 – 59 Q -> N. Decreased E1S transport.
Mutagenesis 60 – 60 L -> A. No change in E1S transport.
Mutagenesis 61 – 61 A -> V. Decreased E1S transport, no change in cell surface expression, increased Km value and decreased Vmax value for E1S transport activity. Decreased taurocholate transport.
Mutagenesis 62 – 62 Q -> A. Decreased E1S transport, no change in cell surface expression; no change in Km value and decreased Vmax value for E1S transport activity. Decreased taurocholate transport.
Mutagenesis 62 – 62 Q -> N. Decreased E1S transport; no change in cell surface expression.
Mutagenesis 63 – 63 L -> A. Decreased E1S transport.
Mutagenesis 64 – 64 M -> A. No change in E1S transport.
Mutagenesis 65 – 65 I -> A. Decreased E1S transport, no change in cell surface expression.
Mutagenesis 66 – 66 S -> A. Decreased E1S transport, no change in cell surface expression, increased Km value and decreased Vmax value for E1S transport activity. Decreased taurocholate transport.
Mutagenesis 66 – 66 S -> T. Decreased E1S transport.
Mutagenesis 67 – 67 G -> A. Decreased E1S transport.
Mutagenesis 68 – 68 Y -> A. No change in E1S transport.
Mutagenesis 69 – 69 L -> A. Decreased E1S transport, no change in cell surface expression; no change in Km value and decreased Vmax value for E1S transport activity. Decreased taurocholate transport.
Mutagenesis 69 – 69 L -> I. Decreased E1S transport.



Literature citations
The consensus coding sequences of human breast and colorectal cancers.
Sjoeblom T.; Jones S.; Wood L.D.; Parsons D.W.; Lin J.; Barber T.D.; Mandelker D.; Leary R.J.; Ptak J.; Silliman N.; Szabo S.; Buckhaults P.; Farrell C.; Meeh P.; Markowitz S.D.; Willis J.; Dawson D.; Willson J.K.V.; Gazdar A.F.; Hartigan J.; Wu L.; Liu C.; Parmigiani G.; Park B.H.; Bachman K.E.; Papadopoulos N.; Vogelstein B.; Kinzler K.W.; Velculescu V.E.;
Science 314:268-274(2006)
Cited for: VARIANT [LARGE SCALE ANALYSIS] LYS-77;
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.