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UniProtKB - Q13563 (PKD2_HUMAN)

Protein

Polycystin-2

Gene

PKD2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Component of a heteromeric calcium-permeable ion channel formed by PKD1 and PKD2 that is activated by interaction between PKD1 and a Wnt family member, such as WNT3A and WNT9B (PubMed:27214281). Can also form a functional, homotetrameric ion channel (PubMed:29899465). Functions as a cation channel involved in fluid-flow mechanosensation by the primary cilium in renal epithelium (PubMed:18695040). Functions as outward-rectifying K+ channel, but is also permeable to Ca2+, and to a much lesser degree also to Na+ (PubMed:11854751, PubMed:15692563, PubMed:27071085, PubMed:27991905). May contribute to the release of Ca2+ stores from the endoplasmic reticulum (PubMed:11854751, PubMed:20881056). Together with TRPV4, forms mechano- and thermosensitive channels in cilium (PubMed:18695040). PKD1 and PKD2 may function through a common signaling pathway that is necessary to maintain the normal, differentiated state of renal tubule cells. Acts as a regulator of cilium length, together with PKD1. The dynamic control of cilium length is essential in the regulation of mechanotransductive signaling. The cilium length response creates a negative feedback loop whereby fluid shear-mediated deflection of the primary cilium, which decreases intracellular cAMP, leads to cilium shortening and thus decreases flow-induced signaling. Also involved in left-right axis specification via its role in sensing nodal flow; forms a complex with PKD1L1 in cilia to facilitate flow detection in left-right patterning. Detection of asymmetric nodal flow gives rise to a Ca2+ signal that is required for normal, asymmetric expression of genes involved in the specification of body left-right laterality (By similarity).By similarityCurated8 Publications

Miscellaneous

The mechanisms that govern channel opening are complex and still under debate; heterologous expression of PKD2 by itself or together with PKD1 gives rise to very low or undetectable spontaneous ion channel activity, in spite of its presence at the cell membrane.2 Publications

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Channnel activity is regulated by phosphorylation (PubMed:16551655, PubMed:20881056, PubMed:26269590). Channnel activity is regulated by intracellular Ca2+ (PubMed:11854751).4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi763CalciumCombined sources1 Publication1
Metal bindingi765CalciumCombined sources1 Publication1
Metal bindingi767CalciumCombined sources1 Publication1
Metal bindingi769Calcium; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi774CalciumCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section specifies the position(s) of the calcium-binding region(s) within the protein. One common calcium-binding motif is the EF-hand, but other calcium-binding motifs also exist.<p><a href='/help/ca_bind' target='_top'>More...</a></p>Calcium bindingi763 – 774PROSITE-ProRule annotationCombined sources2 PublicationsAdd BLAST12

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionCalcium channel, Ion channel, Potassium channel, Voltage-gated channel
Biological processCalcium transport, Ion transport, Potassium transport, Transport, Wnt signaling pathway
LigandCalcium, Metal-binding, Potassium

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-5620916 VxPx cargo-targeting to cilium

SIGNOR Signaling Network Open Resource

More...SIGNORi		Q13563

Protein family/group databases

Transport Classification Database

More...TCDBi		1.A.5.2.1 the polycystin cation channel (pcc) family

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Polycystin-2Curated
Short name:
PC21 Publication
Alternative name(s):
Autosomal dominant polycystic kidney disease type II protein
Polycystic kidney disease 2 protein
Polycystwin1 Publication
R48321
Transient receptor potential cation channel subfamily P member 21 PublicationImported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:PKD2Imported
Synonyms:TRPP21 PublicationImported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 4

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000118762.7

Human Gene Nomenclature Database

More...HGNCi		HGNC:9009 PKD2

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		173910 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q13563

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 219Cytoplasmic3 PublicationsAdd BLAST219
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei220 – 241Helical; Name=S13 PublicationsAdd BLAST22
Topological domaini242 – 468Extracellular3 PublicationsAdd BLAST227
Transmembranei469 – 489Helical; Name=S23 PublicationsAdd BLAST21
Topological domaini490 – 505Cytoplasmic3 PublicationsAdd BLAST16
Transmembranei506 – 526Helical; Name=S33 PublicationsAdd BLAST21
Topological domaini527 – 552Extracellular3 PublicationsAdd BLAST26
Transmembranei553 – 573Helical; Name=S43 PublicationsAdd BLAST21
Topological domaini574 – 597Cytoplasmic3 PublicationsAdd BLAST24
Transmembranei598 – 619Helical; Name=53 PublicationsAdd BLAST22
Topological domaini620 – 631Extracellular3 PublicationsAdd BLAST12
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a region that is buried within a membrane, but does not cross it.<p><a href='/help/intramem' target='_top'>More...</a></p>Intramembranei632 – 646Pore-forming3 PublicationsAdd BLAST15
Topological domaini647 – 654Extracellular3 Publications8
Transmembranei655 – 675Helical; Name=S63 PublicationsAdd BLAST21
Topological domaini676 – 968Cytoplasmic3 PublicationsAdd BLAST293

Keywords - Cellular componenti

Cell membrane, Cell projection, Cilium, Cytoplasmic vesicle, Endoplasmic reticulum, Golgi apparatus, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Polycystic kidney disease 2 with or without polycystic liver disease (PKD2)13 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant disorder characterized by progressive formation and enlargement of cysts in both kidneys, typically leading to end-stage renal disease in adult life. Cysts also occurs in the liver and other organs. It represents approximately 15% of the cases of autosomal dominant polycystic kidney disease. PKD2 is clinically milder than PKD1 but it has a deleterious impact on overall life expectancy.
See also OMIM:613095
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_058822306R → Q in PKD2. 1 PublicationCorresponds to variant dbSNP:rs990932947Ensembl.1
Natural variantiVAR_058823322R → Q in PKD2. 1 PublicationCorresponds to variant dbSNP:rs145877597Ensembl.1
Natural variantiVAR_058824322R → W in PKD2. 1 Publication1
Natural variantiVAR_011073356A → P in PKD2. 2 Publications1
Natural variantiVAR_064394384A → P in PKD2. 1 Publication1
Natural variantiVAR_009195414W → G in PKD2; affects channel activity as it is able to abolish channel currents induced by the gain-of-function artificial mutant P-604. 3 Publications1
Natural variantiVAR_058825420R → G in PKD2; affects channel activity as it is able to abolish channel currents induced by the gain-of-function artificial mutant P-604. 2 Publications1
Natural variantiVAR_011074479Missing in PKD2; somatic mutation. 1 Publication1
Natural variantiVAR_011075504 – 512Missing in PKD2; somatic mutation. 1 Publication9
Natural variantiVAR_058827511D → V 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. 5 PublicationsCorresponds to variant dbSNP:rs121918043EnsemblClinVar.1
Natural variantiVAR_058828632C → R in PKD2. 1 Publication1
Natural variantiVAR_011076684Missing in PKD2; somatic mutation; abolishes channel currents induced by the gain-of-function artificial mutant P-604. 1 Publication1
Natural variantiVAR_058830807R → Q in PKD2. 1 PublicationCorresponds to variant dbSNP:rs147654263EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi76S → A: Abolishes phosphorylation of the N-terminal domain. Abolishes the ability to complement a pkd2-deficient zebrafish mutant; when associated with A-80. 1 Publication1
Mutagenesisi80S → A: Decreases phosphorylation of the N-terminal domain. Abolishes the ability to complement a pkd2-deficient zebrafish mutant; when associated with A-76. 1 Publication1
Mutagenesisi201W → A: Abolishes increased channel activity due to a gain of function mutation; when associated with P-604. 1 Publication1
Mutagenesisi604F → A or I: No effect on channel activation. 1 Publication1
Mutagenesisi604F → P: Gain-of-function mutation resulting in increased channel activity. Absence of gain of function; when associated with F-605 DEL; when associated with A-201; when associated with V-511; when associated with G-414; when associated with G-420; when associated with Y-684 DEL; when associated with A-684. Increased channel activity; when associated with 736-L-N-737 DEL. 2 Publications1
Mutagenesisi605Missing : Abolishes increased channel activity due to a gain of function mutation; when associated with P-604. 1 Publication1
Mutagenesisi677L → N: Gain of function mutation. 1 Publication1
Mutagenesisi684Y → A: Abolishes increased channel activity due to a gain of function mutation; when associated with P-604. 1 Publication1
Mutagenesisi688K → A: Abolishes increased channel activity due to a gain of function mutation; when associated with P-604. 1 Publication1
Mutagenesisi721T → A: Decreases phosphorylation; when associated with A-801; A-812; A-831 and A-943. 1 Publication1
Mutagenesisi736 – 737Missing : Increased channel activity; when associated with P-604. 1 Publication2
Mutagenesisi768Q → G: Strongly increases calcium binding affinity. 1 Publication1
Mutagenesisi771T → A: Loss of calcium-binding site; when associated with A-774. 1 Publication1
Mutagenesisi774E → A: Loss of calcium-binding site; when associated with A-771. 1 Publication1
Mutagenesisi774E → Q: Abolishes calcium binding via the EF-hand. 1 Publication1
Mutagenesisi801S → A: Decreases phosphorylation; when associated with A-721; A-812; A-831 and A-943. 1 Publication1
Mutagenesisi801S → D: Phosphomimetic mutant. No effect on release of Ca(2+) stores from the endoplasmic reticulum. 1 Publication1
Mutagenesisi801S → G: Loss of phosphorylation at this site. Impairs release of Ca(2+) stores from the endoplasmic reticulum. 1 Publication1
Mutagenesisi804S → N: Loss of phosphorylation at Ser-801. 1 Publication1
Mutagenesisi812S → A: Decreases interaction with PACS1 and enhances expression at the cell membrane. Decreases phosphorylation; when associated with A-721; A-801; A-831 and A-943. 2 Publications1
Mutagenesisi812S → D: No effect on interaction with PACS1. 1 Publication1
Mutagenesisi815 – 817DDD → AAA: Strongly decreases interaction with PACS1 and enhances expression at the cell membrane. 1 Publication3
Mutagenesisi829S → A: Abolishes increased channel opening in response to cAMP and phosphorylation by PKA. 1 Publication1
Mutagenesisi831S → A: Decreases phosphorylation; when associated with A-721; A-801; A-812 and A-943. 1 Publication1
Mutagenesisi842L → A: Abolishes oligomerization and interaction with PKD1; when associated with A-846; A-849; A-860; A-863 and A-867. 1 Publication1
Mutagenesisi842L → P: Loss of protein solubility. 1 Publication1
Mutagenesisi846V → A: Abolishes oligomerization and interaction with PKD1; when associated with A-842; A-849; A-860; A-863 and A-867. 1 Publication1
Mutagenesisi846V → E: Loss of protein solubility. 1 Publication1
Mutagenesisi849M → A: Abolishes oligomerization and interaction with PKD1; when associated with A-842; A-846; A-860; A-863 and A-867. 1 Publication1
Mutagenesisi849M → K: Loss of protein solubility. 1 Publication1
Mutagenesisi853I → P: Loss of protein solubility. 1 Publication1
Mutagenesisi856I → K: Loss of protein solubility. 1 Publication1
Mutagenesisi860I → A: Abolishes oligomerization and interaction with PKD1; when associated with A-842; A-846; A-849; A-863 and A-867. 1 Publication1
Mutagenesisi863V → A: Abolishes oligomerization and interaction with PKD1; when associated with A-842; A-846; A-849; A-860 and A-867. 1 Publication1
Mutagenesisi863V → E: Loss of protein solubility; when associated with K-849. 1 Publication1
Mutagenesisi867L → A: Abolishes oligomerization and interaction with PKD1; when associated with A-842; A-846; A-849; A-860 and A-863. 1 Publication1
Mutagenesisi943S → A: Decreases phosphorylation; when associated with A-721; A-801; A-812 and A-831. 1 Publication1

Keywords - Diseasei

Ciliopathy, Disease mutation

Organism-specific databases

DisGeNET

More...DisGeNETi		5311

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

More...GeneReviewsi		PKD2

MalaCards human disease database

More...MalaCardsi		PKD2
MIMi613095 phenotype

Open Targets

More...OpenTargetsi		ENSG00000118762

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		730 Autosomal dominant polycystic kidney disease

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA33343

Chemistry databases

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		504

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		PKD2

Domain mapping of disease mutations (DMDM)

More...DMDMi		116242717

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001643561 – 968Polycystin-2Add BLAST968

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei76Phosphoserine1 Publication1
Modified residuei80Phosphoserine1 Publication1
Modified residuei137Omega-N-methylarginineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi299N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi305N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi328N-linked (GlcNAc...) (complex) asparagine4 Publications1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi331 ↔ 344Combined sources2 Publications
Glycosylationi362N-linked (GlcNAc...) asparagine3 Publications1
Glycosylationi375N-linked (GlcNAc...) asparagine3 Publications1
Modified residuei801Phosphoserine1 Publication1 Publication1
Modified residuei808PhosphoserineBy similarity1
Modified residuei812PhosphoserineCombined sources2 Publications1
Modified residuei829Phosphoserine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated. Phosphorylation is important for protein function; a mutant that lacks the N-terminal phosphorylation sites cannot complement a zebrafish pkd2-deficient mutant (PubMed:16551655). PKD-mediated phosphorylation at the C-terminus regulates its function in the release of Ca2+ stores from the endoplasmic reticulum (PubMed:20881056). PKA-mediated phosphorylation at a C-terminal site strongly increases the open probability of the channel, but does not increase single channel conductance (PubMed:26269590).3 Publications
N-glycosylated. The four subunits in a tetramer probably differ in the extent of glycosylation; simultaneous glycosylation of all experimentally validated sites would probably create steric hindrance. Thus, glycosylation at Asn-305 is not compatible with glycosylation at Asn-328; only one of these two residues is glycosylated at a given time.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Methylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q13563

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q13563

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q13563

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		Q13563

PeptideAtlas

More...PeptideAtlasi		Q13563

PRoteomics IDEntifications database

More...PRIDEi		Q13563

ProteomicsDB human proteome resource

More...ProteomicsDBi		59562
59563 [Q13563-2]
59564 [Q13563-3]
59565 [Q13563-4]
59566 [Q13563-5]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q13563

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		Q13563

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Detected in fetal and adult kidney (PubMed:10770959). Detected at the thick ascending limb of the loop of Henle, at distal tubules, including the distal convoluted tubule and cortical collecting tubules, with weak staining of the collecting duct (PubMed:10770959). Detected on placenta syncytiotrophoblasts (at protein level) (PubMed:26269590). Strongly expressed in ovary, fetal and adult kidney, testis, and small intestine. Not detected in peripheral leukocytes.3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000118762 Expressed in 235 organ(s), highest expression level in thoracic aorta

CleanEx database of gene expression profiles

More...CleanExi		HS_PKD2

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q13563 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q13563 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB004544
HPA015794

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotetramer (PubMed:20881056, PubMed:27768895, PubMed:27991905, PubMed:28092368, PubMed:29899465). Heterotetramer with PKD1, giving rise to a complex formed by one PKD1 chain and three PKD2 chains (PubMed:20881056, PubMed:19556541, PubMed:27214281, PubMed:30093605). Interaction with PKD1 is required for ciliary localization (By similarity) Isoform 1 interacts with PKD1 while isoform 3 does not (By similarity). Interacts with PKD1L1. Interacts with CD2AP (PubMed:10913159). Interacts with HAX1 (PubMed:10760273). Interacts with NEK8 (By similarity). Part of a complex containing AKAP5, ADCY5, ADCY6 and PDE4C (By similarity). Interacts (via C-terminus) with TRPV4 (via C-terminus) (PubMed:18695040). Interacts (via C-terminal acidic region) with PACS1 and PACS2; these interactions retain the protein in the endoplasmic reticulum and prevent trafficking to the cell membrane (PubMed:15692563).By similarity9 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		111328, 46 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q13563

Database of interacting proteins

More...DIPi		DIP-47455N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		Q13563

Protein interaction database and analysis system

More...IntActi		Q13563, 25 interactors

Molecular INTeraction database

More...MINTi		Q13563

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000237596

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q13563

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1968
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KLDNMR-A680-796[»]
2KLENMR-A680-796[»]
2KQ6NMR-A720-797[»]
2Y4QNMR-A717-792[»]
3HRNX-ray1.90A833-895[»]
3HROX-ray1.90A833-872[»]
5K47electron microscopy4.20A/B/C/D185-723[»]
5MKEelectron microscopy4.30A/B/C/D1-968[»]
5MKFelectron microscopy4.20A/B/C/D1-968[»]
5T4Delectron microscopy3.00A/B/C/D198-702[»]
6A70electron microscopy3.60A/F/G185-723[»]
6D1Welectron microscopy3.54A/B/C/D53-792[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		Q13563

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q13563

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q13563

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini750 – 785EF-handPROSITE-ProRule annotation2 PublicationsAdd BLAST36

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni803 – 822Linker1 PublicationAdd BLAST20
Regioni810 – 821Important for interaction with PACS1 and PACS21 PublicationAdd BLAST12

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili833 – 8721 Publication1 PublicationAdd BLAST40

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi641 – 643Selectivity filter1 Publication3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi95 – 107Poly-GluAdd BLAST13
Compositional biasi153 – 157Poly-Arg5

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The C-terminal coiled-coil domain is involved in oligomerization and the interaction with PKD1 (PubMed:18694932, PubMed:19556541). The isolated coiled-coil domain forms a homotrimer in vitro; the homotrimer interacts with a single PKD1 chain (PubMed:19556541). The coiled-coil domain binds calcium and undergoes a calcium-induced conformation change (in vitro) (PubMed:18694932).2 Publications

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the polycystin family.Curated

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3599 Eukaryota
ENOG410XTGE LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000159025

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000230858

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG014945

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q13563

KEGG Orthology (KO)

More...KOi		K04986

Identification of Orthologs from Complete Genome Data

More...OMAi		GVIPSWQ

Database of Orthologous Groups

More...OrthoDBi		426073at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q13563

TreeFam database of animal gene trees

More...TreeFami		TF316484

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.20.120.350, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR011992 EF-hand-dom_pair
IPR002048 EF_hand_dom
IPR013122 PKD1_2_channel
IPR003915 PKD_2
IPR027359 Volt_channel_dom_sf

Pfam protein domain database

More...Pfami		View protein in Pfam
PF08016 PKD_channel, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR01433 POLYCYSTIN2

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF47473 SSF47473, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50222 EF_HAND_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (5+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 5 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 5 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: Q13563-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MVNSSRVQPQ QPGDAKRPPA PRAPDPGRLM AGCAAVGASL AAPGGLCEQR 
        60         70         80         90        100
GLEIEMQRIR QAAARDPPAG AAASPSPPLS SCSRQAWSRD NPGFEAEEEE 
       110        120        130        140        150
EEVEGEEGGM VVEMDVEWRP GSRRSAASSA VSSVGARSRG LGGYHGAGHP 
       160        170        180        190        200
SGRRRRREDQ GPPCPSPVGG GDPLHRHLPL EGQPPRVAWA ERLVRGLRGL 
       210        220        230        240        250
WGTRLMEESS TNREKYLKSV LRELVTYLLF LIVLCILTYG MMSSNVYYYT 
       260        270        280        290        300
RMMSQLFLDT PVSKTEKTNF KTLSSMEDFW KFTEGSLLDG LYWKMQPSNQ 
       310        320        330        340        350
TEADNRSFIF YENLLLGVPR IRQLRVRNGS CSIPQDLRDE IKECYDVYSV 
       360        370        380        390        400
SSEDRAPFGP RNGTAWIYTS EKDLNGSSHW GIIATYSGAG YYLDLSRTRE 
       410        420        430        440        450
ETAAQVASLK KNVWLDRGTR ATFIDFSVYN ANINLFCVVR LLVEFPATGG 
       460        470        480        490        500
VIPSWQFQPL KLIRYVTTFD FFLAACEIIF CFFIFYYVVE EILEIRIHKL 
       510        520        530        540        550
HYFRSFWNCL DVVIVVLSVV AIGINIYRTS NVEVLLQFLE DQNTFPNFEH 
       560        570        580        590        600
LAYWQIQFNN IAAVTVFFVW IKLFKFINFN RTMSQLSTTM SRCAKDLFGF 
       610        620        630        640        650
AIMFFIIFLA YAQLAYLVFG TQVDDFSTFQ ECIFTQFRII LGDINFAEIE 
       660        670        680        690        700
EANRVLGPIY FTTFVFFMFF ILLNMFLAII NDTYSEVKSD LAQQKAEMEL 
       710        720        730        740        750
SDLIRKGYHK ALVKLKLKKN TVDDISESLR QGGGKLNFDE LRQDLKGKGH 
       760        770        780        790        800
TDAEIEAIFT KYDQDGDQEL TEHEHQQMRD DLEKEREDLD LDHSSLPRPM 
       810        820        830        840        850
SSRSFPRSLD DSEEDDDEDS GHSSRRRGSI SSGVSYEEFQ VLVRRVDRME 
       860        870        880        890        900
HSIGSIVSKI DAVIVKLEIM ERAKLKRREV LGRLLDGVAE DERLGRDSEI 
       910        920        930        940        950
HREQMERLVR EELERWESDD AASQISHGLG TPVGLNGQPR PRSSRPSSSQ 
       960 
STEGMEGAGG NGSSNVHV
Length:968
Mass (Da):109,691
Last modified:October 17, 2006 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iF8D2E760EBEA8B47
GO
Isoform 2 (identifier: Q13563-2) [UniParc]FASTAAdd to basket
Also known as: delta6

The sequence of this isoform differs from the canonical sequence as follows:
     476-483: CEIIFCFF → FICSSYGD
     484-968: Missing.

Show »
Length:483
Mass (Da):53,686
Checksum:i6F4CC2DD18EEF56F
GO
Isoform 3 (identifier: Q13563-3) [UniParc]FASTAAdd to basket
Also known as: delta7

The sequence of this isoform differs from the canonical sequence as follows:
     517-572: Missing.

Show »
Length:912
Mass (Da):103,134
Checksum:iEDD0DB1BD7750772
GO
Isoform 4 (identifier: Q13563-4) [UniParc]FASTAAdd to basket
Also known as: delta9

The sequence of this isoform differs from the canonical sequence as follows:
     633-646: IFTQFRIILGDINF → IICSWRSSMIRTLK
     647-968: Missing.

Show »
Length:646
Mass (Da):73,171
Checksum:iC3773DAF9FFDB249
GO
Isoform 5 (identifier: Q13563-5) [UniParc]FASTAAdd to basket
Also known as: delta12/13

The sequence of this isoform differs from the canonical sequence as follows:
     748-841: Missing.

Note: Minor isoform.
Show »
Length:874
Mass (Da):98,838
Checksum:i887260C960F987BE
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
B4DFN3B4DFN3_HUMAN
cDNA FLJ50473, highly similar to Po...
PKD2
386Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti45G → R in AAC16004 (PubMed:9286709).Curated1
Sequence conflicti449G → V in AAC50933 (PubMed:8954772).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05882024P → L1 PublicationCorresponds to variant dbSNP:rs1004860210Ensembl.1
Natural variantiVAR_01107228R → P Common polymorphism. 5 PublicationsCorresponds to variant dbSNP:rs1805044EnsemblClinVar.1
Natural variantiVAR_058821190A → T1 PublicationCorresponds to variant dbSNP:rs117078377EnsemblClinVar.1
Natural variantiVAR_058822306R → Q in PKD2. 1 PublicationCorresponds to variant dbSNP:rs990932947Ensembl.1
Natural variantiVAR_058823322R → Q in PKD2. 1 PublicationCorresponds to variant dbSNP:rs145877597Ensembl.1
Natural variantiVAR_058824322R → W in PKD2. 1 Publication1
Natural variantiVAR_011073356A → P in PKD2. 2 Publications1
Natural variantiVAR_064394384A → P in PKD2. 1 Publication1
Natural variantiVAR_009195414W → G in PKD2; affects channel activity as it is able to abolish channel currents induced by the gain-of-function artificial mutant P-604. 3 Publications1
Natural variantiVAR_058825420R → G in PKD2; affects channel activity as it is able to abolish channel currents induced by the gain-of-function artificial mutant P-604. 2 Publications1
Natural variantiVAR_014919452I → V. Corresponds to variant dbSNP:rs1801612EnsemblClinVar.1
Natural variantiVAR_011074479Missing in PKD2; somatic mutation. 1 Publication1
Natural variantiVAR_058826482F → C1 PublicationCorresponds to variant dbSNP:rs75762896EnsemblClinVar.1
Natural variantiVAR_011075504 – 512Missing in PKD2; somatic mutation. 1 Publication9
Natural variantiVAR_058827511D → V 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. 5 PublicationsCorresponds to variant dbSNP:rs121918043EnsemblClinVar.1
Natural variantiVAR_058828632C → R in PKD2. 1 Publication1
Natural variantiVAR_011076684Missing in PKD2; somatic mutation; abolishes channel currents induced by the gain-of-function artificial mutant P-604. 1 Publication1
Natural variantiVAR_058829800M → L1 PublicationCorresponds to variant dbSNP:rs2234917EnsemblClinVar.1
Natural variantiVAR_058830807R → Q in PKD2. 1 PublicationCorresponds to variant dbSNP:rs147654263EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_042479476 – 483CEIIFCFF → FICSSYGD in isoform 2. Curated8
Alternative sequenceiVSP_042480484 – 968Missing in isoform 2. CuratedAdd BLAST485
Alternative sequenceiVSP_042481517 – 572Missing in isoform 3. CuratedAdd BLAST56
Alternative sequenceiVSP_042482633 – 646IFTQF…GDINF → IICSWRSSMIRTLK in isoform 4. CuratedAdd BLAST14
Alternative sequenceiVSP_042483647 – 968Missing in isoform 4. CuratedAdd BLAST322
Alternative sequenceiVSP_042484748 – 841Missing in isoform 5. CuratedAdd BLAST94

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
U50928 mRNA Translation: AAC50520.1
AF004873
, AF004859, AF004860, AF004861, AF004862, AF004863, AF004864, AF004865, AF004866, AF004867, AF004868, AF004869, AF004870, AF004871, AF004872 Genomic DNA Translation: AAC16004.1
BC112261 mRNA Translation: AAI12262.1
BC112263 mRNA Translation: AAI12264.1
U56813 mRNA Translation: AAC50933.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS3627.1 [Q13563-1]

Protein sequence database of the Protein Information Resource

More...PIRi		G02640

NCBI Reference Sequences

More...RefSeqi		NP_000288.1, NM_000297.3 [Q13563-1]

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.181272

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000237596; ENSP00000237596; ENSG00000118762 [Q13563-1]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		5311

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:5311

UCSC genome browser

More...UCSCi		uc003hre.4 human [Q13563-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Functional Glycomics Gateway - Glycan Binding

Polycystin 2 - Not a C-type lectin

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U50928 mRNA Translation: AAC50520.1
AF004873
, AF004859, AF004860, AF004861, AF004862, AF004863, AF004864, AF004865, AF004866, AF004867, AF004868, AF004869, AF004870, AF004871, AF004872 Genomic DNA Translation: AAC16004.1
BC112261 mRNA Translation: AAI12262.1
BC112263 mRNA Translation: AAI12264.1
U56813 mRNA Translation: AAC50933.1
CCDSiCCDS3627.1 [Q13563-1]
PIRiG02640
RefSeqiNP_000288.1, NM_000297.3 [Q13563-1]
UniGeneiHs.181272

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KLDNMR-A680-796[»]
2KLENMR-A680-796[»]
2KQ6NMR-A720-797[»]
2Y4QNMR-A717-792[»]
3HRNX-ray1.90A833-895[»]
3HROX-ray1.90A833-872[»]
5K47electron microscopy4.20A/B/C/D185-723[»]
5MKEelectron microscopy4.30A/B/C/D1-968[»]
5MKFelectron microscopy4.20A/B/C/D1-968[»]
5T4Delectron microscopy3.00A/B/C/D198-702[»]
6A70electron microscopy3.60A/F/G185-723[»]
6D1Welectron microscopy3.54A/B/C/D53-792[»]
ProteinModelPortaliQ13563
SMRiQ13563
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111328, 46 interactors
CORUMiQ13563
DIPiDIP-47455N
ELMiQ13563
IntActiQ13563, 25 interactors
MINTiQ13563
STRINGi9606.ENSP00000237596

Chemistry databases

BindingDBiQ13563
GuidetoPHARMACOLOGYi504

Protein family/group databases

TCDBi1.A.5.2.1 the polycystin cation channel (pcc) family

PTM databases

iPTMnetiQ13563
PhosphoSitePlusiQ13563

Polymorphism and mutation databases

BioMutaiPKD2
DMDMi116242717

Proteomic databases

EPDiQ13563
jPOSTiQ13563
MaxQBiQ13563
PaxDbiQ13563
PeptideAtlasiQ13563
PRIDEiQ13563
ProteomicsDBi59562
59563 [Q13563-2]
59564 [Q13563-3]
59565 [Q13563-4]
59566 [Q13563-5]

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		5311
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000237596; ENSP00000237596; ENSG00000118762 [Q13563-1]
GeneIDi5311
KEGGihsa:5311
UCSCiuc003hre.4 human [Q13563-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5311
DisGeNETi5311
EuPathDBiHostDB:ENSG00000118762.7

GeneCards: human genes, protein and diseases

More...GeneCardsi		PKD2
GeneReviewsiPKD2
HGNCiHGNC:9009 PKD2
HPAiCAB004544
HPA015794
MalaCardsiPKD2
MIMi173910 gene
613095 phenotype
neXtProtiNX_Q13563
OpenTargetsiENSG00000118762
Orphaneti730 Autosomal dominant polycystic kidney disease
PharmGKBiPA33343

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG3599 Eukaryota
ENOG410XTGE LUCA
GeneTreeiENSGT00940000159025
HOGENOMiHOG000230858
HOVERGENiHBG014945
InParanoidiQ13563
KOiK04986
OMAiGVIPSWQ
OrthoDBi426073at2759
PhylomeDBiQ13563
TreeFamiTF316484

Enzyme and pathway databases

ReactomeiR-HSA-5620916 VxPx cargo-targeting to cilium
SIGNORiQ13563

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		PKD2 human
EvolutionaryTraceiQ13563

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Polycystic_kidney_disease_2

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		5311

Protein Ontology

More...PROi		PR:Q13563

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000118762 Expressed in 235 organ(s), highest expression level in thoracic aorta
CleanExiHS_PKD2
ExpressionAtlasiQ13563 baseline and differential
GenevisibleiQ13563 HS

Family and domain databases

Gene3Di1.20.120.350, 1 hit
InterProiView protein in InterPro
IPR011992 EF-hand-dom_pair
IPR002048 EF_hand_dom
IPR013122 PKD1_2_channel
IPR003915 PKD_2
IPR027359 Volt_channel_dom_sf
PfamiView protein in Pfam
PF08016 PKD_channel, 1 hit
PRINTSiPR01433 POLYCYSTIN2
SUPFAMiSSF47473 SSF47473, 1 hit
PROSITEiView protein in PROSITE
PS50222 EF_HAND_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPKD2_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q13563
Secondary accession number(s): O60441
, Q15764, Q2M1Q3, Q2M1Q5
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: October 17, 2006
Last modified: January 16, 2019
This is version 195 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
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