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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P98161: Variant p.Glu2771Lys

Polycystin-1
Gene: PKD1
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Variant information Variant position: help 2771 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 Glutamate (E) to Lysine (K) at position 2771 (E2771K, p.Glu2771Lys). 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 PKD1; does not undergo autoproteolytic cleavage. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 2771 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 4303 The length of the canonical sequence.
Location on the sequence: help QAYNLTSALMRILMRSRVLN E EPLTLAGEEIVAQGKRSDPR 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                         QAYNLTSALMRILMRSRVLNEEPLTLAGEEIVAQGKRSDPR

Mouse                         KAYNLSSALMRILMRSRVLNEEPLTLAGEEIVALGKRSDPL

Caenorhabditis elegans        KTQNCEEWAFKLPSPASTLNTAEIT---------DKTLIQV

Slime mold                    EKHK-------------------------------------
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 24 – 4303 Polycystin-1
Topological domain 24 – 3074 Extracellular
Domain 2146 – 2833 REJ
Glycosylation 2754 – 2754 N-linked (GlcNAc...) asparagine



Literature citations
Cleavage of polycystin-1 requires the receptor for egg jelly domain and is disrupted by human autosomal-dominant polycystic kidney disease 1-associated mutations.
Qian F.; Boletta A.; Bhunia A.K.; Xu H.; Liu L.; Ahrabi A.K.; Watnick T.J.; Zhou F.; Germino G.G.;
Proc. Natl. Acad. Sci. U.S.A. 99:16981-16986(2002)
Cited for: FUNCTION IN RENAL TUBULOGENESIS; AUTOCATALYTIC CLEAVAGE AT LEU-3048; CHARACTERIZATION OF VARIANTS PKD1 LYS-2771; PRO-2921; PRO-2993 AND ARG-3016; CHARACTERIZATION OF VARIANT GLN-2791; Mutation analysis of the entire PKD1 gene: genetic and diagnostic implications.
Rossetti S.; Strmecki L.; Gamble V.; Burton S.; Sneddon V.; Peral B.; Roy S.; Bakkaloglu A.; Komel R.; Winearls C.G.; Harris P.C.;
Am. J. Hum. Genet. 68:46-63(2001)
Cited for: VARIANTS PKD1 GLN-13; PHE-75; CYS-139; 1992-PHE-THR-1993 DELINS LEU; 2220-ARG--PRO-2224 DEL; ASP-2336; ASP-2752; ILE-LEU-MET-ARG-2765 INS; MET-2768; LYS-2771; PRO-2816; SER-2858; 3012-THR--TYR-3017 DEL AND 3748-LEU--ARG-3752 DEL; VARIANTS SER-2674; MET-2708; THR-2734; LEU-2735; CYS-2765; MET-2782; ARG-2814; GLY-2888; ILE-2905; ASP-2966 AND LEU-3066; Association of mutation position in polycystic kidney disease 1 (PKD1) gene and development of a vascular phenotype.
Rossetti S.; Chauveau D.; Kubly V.; Slezak J.M.; Saggar-Malik A.K.; Pei Y.; Ong A.C.M.; Stewart F.; Watson M.L.; Bergstralh E.J.; Winearls C.G.; Torres V.E.; Harris P.C.;
Lancet 361:2196-2201(2003)
Cited for: VARIANTS PKD1 ARG-164; GLY-210; ARG-508; ASP-690; ASN-1240 DEL; PRO-1667; LYS-1811; CYS-2092; CYS-2200; ILE-2260 DEL; ARG-2370; TYR-2373; LYS-2771; LEU-2802; ASN-3188 DEL; LEU-3355; PRO-3682 AND ARG-3751; Autosomal dominant polycystic kidney disease: Comprehensive mutation analysis of PKD1 and PKD2 in 700 unrelated patients.
Audrezet M.P.; Gall E.C.; Chen J.M.; Redon S.; Quere I.; Creff J.; Benech C.; Maestri S.; Meur Y.L.; Ferec C.;
Hum. Mutat. 33:1239-1250(2012)
Cited for: VARIANTS PKD1 CYS-325; TRP-611; ASP-698; PRO-727; GLY-1206; CYS-2379; CYS-2767; LYS-2771; ARG-2995; SER-3651; GLN-3750; TRP-3753; CYS-4150 AND TRP-4276;
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.