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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q13563: Variant p.Asp511Val

Polycystin-2
Gene: PKD2
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Variant information Variant position: help 511 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 Aspartate (D) to Valine (V) at position 511 (D511V, p.Asp511Val). 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 (D) to medium size and hydrophobic (V) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -3 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 PKD2; loss of function in the release of Ca(2+) stores from the endoplasmic reticulum; no effect on location at the endoplasmic reticulum; affects channel activity as it is able to abolish channel currents induced by the gain-of-function artificial mutant P-604. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 511 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 968 The length of the canonical sequence.
Location on the sequence: help EILEIRIHKLHYFRSFWNCL D VVIVVLSVVAIGINIYRTSN 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                         EILEIRIHKLHYFRSFWNCLDVVIVVLSVVAIGINIYRTSN

Mouse                         EILEIRIHRLSYFRSFWNCLDVVIVVLSVVAMVINIYRMSN

Bovine                        EILEIRIHKLHYFRSFWNCLDVVIIVLSVVAIGINIYRTSN

Zebrafish                     EALEIRLHRLRYFKSLWNCLDVLIVALSVPAIIMNICRTSA

Caenorhabditis elegans        ELFAIGRHRLHYLTQFWNLVDVVLLGFSVATIILSVNRTKT

Fission yeast                 EIYTRDSSALAFL-SMYVIVDMAVLLCYAFVRTIQIIRKTG
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 – 968 Polycystin-2
Transmembrane 506 – 526 Helical; Name=S3
Alternative sequence 484 – 968 Missing. In isoform 2.
Helix 507 – 527



Literature citations
Polycystin-2 is an intracellular calcium release channel.
Koulen P.; Cai Y.; Geng L.; Maeda Y.; Nishimura S.; Witzgall R.; Ehrlich B.E.; Somlo S.;
Nat. Cell Biol. 4:191-197(2002)
Cited for: FUNCTION; SUBCELLULAR LOCATION; CHARACTERIZATION OF VARIANT PKD2 VAL-511; The polycystin complex mediates Wnt/Ca(2+) signalling.
Kim S.; Nie H.; Nesin V.; Tran U.; Outeda P.; Bai C.X.; Keeling J.; Maskey D.; Watnick T.; Wessely O.; Tsiokas L.;
Nat. Cell Biol. 18:752-764(2016)
Cited for: FUNCTION; INTERACTION WITH PKD1; SUBCELLULAR LOCATION; CHARACTERIZATION OF VARIANT PKD2 VAL-511; Function and regulation of TRPP2 ion channel revealed by a gain-of-function mutant.
Arif Pavel M.; Lv C.; Ng C.; Yang L.; Kashyap P.; Lam C.; Valentino V.; Fung H.Y.; Campbell T.; Moeller S.G.; Zenisek D.; Holtzman N.G.; Yu Y.;
Proc. Natl. Acad. Sci. U.S.A. 113:E2363-E2372(2016)
Cited for: FUNCTION; SUBCELLULAR LOCATION; MUTAGENESIS OF PHE-604; PHE-605 AND 736-LEU-ASN-737; CHARACTERIZATION OF VARIANTS PKD2 GLY-414; GLY-420 AND VAL-511; Hydrophobic pore gates regulate ion permeation in polycystic kidney disease 2 and 2L1 channels.
Zheng W.; Yang X.; Hu R.; Cai R.; Hofmann L.; Wang Z.; Hu Q.; Liu X.; Bulkey D.; Yu Y.; Tang J.; Flockerzi V.; Cao Y.; Cao E.; Chen X.Z.;
Nat. Commun. 9:2302-2302(2018)
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.54 ANGSTROMS) OF 53-792 OF MUTANT PRO-604; FUNCTION; SUBUNIT; SUBCELLULAR LOCATION; TOPOLOGY; MUTAGENESIS OF TRP-201; PHE-604; LEU-677; TYR-684 AND LYS-688; CHARACTERIZATION OF VARIANT PKD2 VAL-511 AND TYR-684 DEL; DISULFIDE BONDS; Aberrant splicing in the PKD2 gene as a cause of polycystic kidney disease.
Reynolds D.M.; Hayashi T.; Cai Y.; Veldhuisen B.; Watnick T.J.; Lens X.M.; Mochizuki T.; Qian F.; Maeda Y.; Li L.; Fossdal R.; Coto E.; Wu G.; Breuning M.H.; Germino G.G.; Peters D.J.M.; Somlo S.;
J. Am. Soc. Nephrol. 10:2342-2351(1999)
Cited for: VARIANT PKD2 VAL-511;
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.