UniProtKB - Q13563 (PKD2_HUMAN)
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- BLAST>sp|Q13563|PKD2_HUMAN Polycystin-2 OS=Homo sapiens OX=9606 GN=PKD2 PE=1 SV=3 MVNSSRVQPQQPGDAKRPPAPRAPDPGRLMAGCAAVGASLAAPGGLCEQRGLEIEMQRIR QAAARDPPAGAAASPSPPLSSCSRQAWSRDNPGFEAEEEEEEVEGEEGGMVVEMDVEWRP GSRRSAASSAVSSVGARSRGLGGYHGAGHPSGRRRRREDQGPPCPSPVGGGDPLHRHLPL EGQPPRVAWAERLVRGLRGLWGTRLMEESSTNREKYLKSVLRELVTYLLFLIVLCILTYG MMSSNVYYYTRMMSQLFLDTPVSKTEKTNFKTLSSMEDFWKFTEGSLLDGLYWKMQPSNQ TEADNRSFIFYENLLLGVPRIRQLRVRNGSCSIPQDLRDEIKECYDVYSVSSEDRAPFGP RNGTAWIYTSEKDLNGSSHWGIIATYSGAGYYLDLSRTREETAAQVASLKKNVWLDRGTR ATFIDFSVYNANINLFCVVRLLVEFPATGGVIPSWQFQPLKLIRYVTTFDFFLAACEIIF CFFIFYYVVEEILEIRIHKLHYFRSFWNCLDVVIVVLSVVAIGINIYRTSNVEVLLQFLE DQNTFPNFEHLAYWQIQFNNIAAVTVFFVWIKLFKFINFNRTMSQLSTTMSRCAKDLFGF AIMFFIIFLAYAQLAYLVFGTQVDDFSTFQECIFTQFRIILGDINFAEIEEANRVLGPIY FTTFVFFMFFILLNMFLAIINDTYSEVKSDLAQQKAEMELSDLIRKGYHKALVKLKLKKN TVDDISESLRQGGGKLNFDELRQDLKGKGHTDAEIEAIFTKYDQDGDQELTEHEHQQMRD DLEKEREDLDLDHSSLPRPMSSRSFPRSLDDSEEDDDEDSGHSSRRRGSISSGVSYEEFQ VLVRRVDRMEHSIGSIVSKIDAVIVKLEIMERAKLKRREVLGRLLDGVAEDERLGRDSEI HREQMERLVREELERWESDDAASQISHGLGTPVGLNGQPRPRSSRPSSSQSTEGMEGAGG NGSSNVHV
- Align
Polycystin-2
PKD2
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>Select a section on the left to see content.
<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
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
Curated6 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.9"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) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT PKD2 VAL-511. - Ref.11"Trafficking of TRPP2 by PACS proteins represents a novel mechanism of ion channel regulation."
Koettgen M., Benzing T., Simmen T., Tauber R., Buchholz B., Feliciangeli S., Huber T.B., Schermer B., Kramer-Zucker A., Hoepker K., Simmen K.C., Tschucke C.C., Sandford R., Kim E., Thomas G., Walz G.
EMBO J. 24:705-716(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH PACS1 AND PACS2, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-812, MUTAGENESIS OF SER-812 AND 815-ASP--ASP-817. - Ref.12"Identification of an N-terminal glycogen synthase kinase 3 phosphorylation site which regulates the functional localization of polycystin-2 in vivo and in vitro."
Streets A.J., Moon D.J., Kane M.E., Obara T., Ong A.C.
Hum. Mol. Genet. 15:1465-1473(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT SER-76; SER-80 AND SER-812, MUTAGENESIS OF SER-76; SER-80; THR-721; SER-801; SER-812; SER-831 AND SER-943. - Ref.13"TRPP2 and TRPV4 form a polymodal sensory channel complex."
Kottgen M., Buchholz B., Garcia-Gonzalez M.A., Kotsis F., Fu X., Doerken M., Boehlke C., Steffl D., Tauber R., Wegierski T., Nitschke R., Suzuki M., Kramer-Zucker A., Germino G.G., Watnick T., Prenen J., Nilius B., Kuehn E.W., Walz G.
J. Cell Biol. 182:437-447(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH TRPV4, SUBCELLULAR LOCATION. - Ref.15"Protein kinase D-mediated phosphorylation of polycystin-2 (TRPP2) is essential for its effects on cell growth and calcium channel activity."
Streets A.J., Needham A.J., Gill S.K., Ong A.C.
Mol. Biol. Cell 21:3853-3865(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT SER-801, MUTAGENESIS OF SER-801 AND SER-804, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH PKD1. - Ref.26"Structure of the polycystic kidney disease TRP channel polycystin-2 (PC2)."
Grieben M., Pike A.C., Shintre C.A., Venturi E., El-Ajouz S., Tessitore A., Shrestha L., Mukhopadhyay S., Mahajan P., Chalk R., Burgess-Brown N.A., Sitsapesan R., Huiskonen J.T., Carpenter E.P.
Nat. Struct. Mol. Biol. 24:114-122(2017) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (4.20 ANGSTROMS) OF 185-723, FUNCTION, SUBUNIT, TOPOLOGY, GLYCOSYLATION AT ASN-328; ASN-362 AND ASN-375.
Miscellaneous
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.22"Structural and molecular basis of the assembly of the TRPP2/PKD1 complex."
Yu Y., Ulbrich M.H., Li M.H., Buraei Z., Chen X.Z., Ong A.C., Tong L., Isacoff E.Y., Yang J.
Proc. Natl. Acad. Sci. U.S.A. 106:11558-11563(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 833-872, COILED COIL, SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF LEU-842; VAL-846; MET-849; ILE-860; VAL-863 AND LEU-867. - Ref.25"The structure of the polycystic kidney disease channel PKD2 in lipid nanodiscs."
Shen P.S., Yang X., DeCaen P.G., Liu X., Bulkley D., Clapham D.E., Cao E.
Cell 167:763-773(2016) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.00 ANGSTROMS) OF 198-702, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, GLYCOSYLATION AT ASN-328; ASN-362 AND ASN-375, DISULFIDE BONDS.
<p>This subsection of the ‘Function’ section describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.9"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) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT PKD2 VAL-511. - Ref.12"Identification of an N-terminal glycogen synthase kinase 3 phosphorylation site which regulates the functional localization of polycystin-2 in vivo and in vitro."
Streets A.J., Moon D.J., Kane M.E., Obara T., Ong A.C.
Hum. Mol. Genet. 15:1465-1473(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT SER-76; SER-80 AND SER-812, MUTAGENESIS OF SER-76; SER-80; THR-721; SER-801; SER-812; SER-831 AND SER-943. - Ref.15"Protein kinase D-mediated phosphorylation of polycystin-2 (TRPP2) is essential for its effects on cell growth and calcium channel activity."
Streets A.J., Needham A.J., Gill S.K., Ong A.C.
Mol. Biol. Cell 21:3853-3865(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT SER-801, MUTAGENESIS OF SER-801 AND SER-804, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH PKD1. - Ref.18"The cAMP Signaling Pathway and Direct Protein Kinase A Phosphorylation Regulate Polycystin-2 (TRPP2) Channel Function."
del Rocio Cantero M., Velazquez I.F., Streets A.J., Ong A.C.M., Cantiello H.F.
J. Biol. Chem. 290:23888-23896(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-829, TISSUE SPECIFICITY, MUTAGENESIS OF SER-829.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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 bindingi | 763 | CalciumCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 1 Publication<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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 bindingi | 765 | CalciumCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 1 Publication<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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 bindingi | 767 | CalciumCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 1 Publication<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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 bindingi | 769 | Calcium; via carbonyl oxygenCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 1 Publication<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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 bindingi | 774 | CalciumCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 1 Publication<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
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Regions
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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 bindingi | 763 – 774 | PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Combined sources<p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 2 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 12 |
<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
- actinin binding Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- ATPase binding Source: BHF-UCL
- calcium-induced calcium release activity Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- calcium ion binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- cytoskeletal protein binding Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- HLH domain binding Source: BHF-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- identical protein binding Source: IntAct <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- ion channel binding Source: BHF-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- muscle alpha-actinin binding Source: Ensembl
- outward rectifier potassium channel activity Source: UniProtKB
- phosphoprotein binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- potassium channel activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- protein homodimerization activity Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- signaling receptor binding Source: BHF-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- voltage-gated calcium channel activity Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- voltage-gated cation channel activity Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- voltage-gated ion channel activity Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- voltage-gated potassium channel activity Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- voltage-gated sodium channel activity Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<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 - Biological processi
- aorta development Source: UniProtKB <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patterni
- branching involved in ureteric bud morphogenesis Source: UniProtKB <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patterni
- calcium ion transmembrane transport Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- calcium ion transport Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- cell cycle arrest Source: BHF-UCL
- cellular response to calcium ion Source: UniProtKB
- cellular response to cAMP Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- cellular response to fluid shear stress Source: BHF-UCL <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- cellular response to hydrostatic pressure Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- cellular response to osmotic stress Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- cellular response to reactive oxygen species Source: BHF-UCL <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
- centrosome duplication Source: BHF-UCL <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
- cytoplasmic sequestering of transcription factor Source: BHF-UCL <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- detection of mechanical stimulus Source: BHF-UCL
- detection of nodal flow Source: BHF-UCL
- determination of left/right symmetry Source: BHF-UCL
- determination of liver left/right asymmetry Source: BHF-UCL <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- embryonic placenta development Source: BHF-UCL
- heart development Source: UniProtKB <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patterni
- heart looping Source: BHF-UCL <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- JAK-STAT cascade Source: BHF-UCL
- liver development Source: UniProtKB <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patterni
- mesonephric duct development Source: UniProtKB <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patterni
- mesonephric tubule development Source: UniProtKB <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patterni
- metanephric ascending thin limb development Source: UniProtKB <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patterni
- metanephric cortex development Source: UniProtKB <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patterni
- metanephric cortical collecting duct development Source: UniProtKB <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patterni
- metanephric distal tubule development Source: UniProtKB <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patterni
- metanephric mesenchyme development Source: UniProtKB <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patterni
- metanephric part of ureteric bud development Source: UniProtKB <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patterni
- metanephric smooth muscle tissue development Source: UniProtKB <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patterni
- metanephric S-shaped body morphogenesis Source: UniProtKB <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patterni
- negative regulation of cell proliferation Source: BHF-UCL <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
- negative regulation of G1/S transition of mitotic cell cycle Source: BHF-UCL <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- negative regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
- neural tube development Source: UniProtKB <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patterni
- placenta blood vessel development Source: BHF-UCL
- positive regulation of cell cycle arrest Source: BHF-UCL <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- positive regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity Source: BHF-UCL <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of nitric oxide biosynthetic process Source: BHF-UCL <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of transcription by RNA polymerase II Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- potassium ion transmembrane transport Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- protein homotetramerization Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- regulation of calcium ion import Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- regulation of cAMP metabolic process Source: Ensembl
- regulation of cell proliferation Source: BHF-UCL <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- release of sequestered calcium ion into cytosol Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- renal artery morphogenesis Source: UniProtKB <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patterni
- renal tubule morphogenesis Source: BHF-UCL
- sodium ion transmembrane transport Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- spinal cord development Source: UniProtKB <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patterni
<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 function | Calcium channel, Ion channel, Potassium channel, Voltage-gated channel |
| Biological process | Calcium transport, Ion transport, Potassium transport, Transport |
| Ligand | Calcium, 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-2Short name: PC21 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
Alternative name(s): Autosomal dominant polycystic kidney disease type II protein Polycystic kidney disease 2 protein Polycystwin1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
R48321 Transient receptor potential cation channel subfamily P member 21 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
<p>Manually validated information which has been imported from another database.</p> <p><a href="/manual/evidences#ECO:0000312">More...</a></p> Manual assertion inferred from database entriesi |
| <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 <p>Manually validated information which has been imported from another database.</p> <p><a href="/manual/evidences#ECO:0000312">More...</a></p> Manual assertion inferred from database entriesi Synonyms:TRPP21 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
<p>Manually validated information which has been imported from another database.</p> <p><a href="/manual/evidences#ECO:0000312">More...</a></p> Manual assertion inferred from database entriesi |
| <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>Organismi | Homo 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 identifieri | 9606 [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 lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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 |
|
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
Plasma membrane
- cilium membrane 3 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.13"TRPP2 and TRPV4 form a polymodal sensory channel complex."
Kottgen M., Buchholz B., Garcia-Gonzalez M.A., Kotsis F., Fu X., Doerken M., Boehlke C., Steffl D., Tauber R., Wegierski T., Nitschke R., Suzuki M., Kramer-Zucker A., Germino G.G., Watnick T., Prenen J., Nilius B., Kuehn E.W., Walz G.
J. Cell Biol. 182:437-447(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH TRPV4, SUBCELLULAR LOCATION. - Ref.15"Protein kinase D-mediated phosphorylation of polycystin-2 (TRPP2) is essential for its effects on cell growth and calcium channel activity."
Streets A.J., Needham A.J., Gill S.K., Ong A.C.
Mol. Biol. Cell 21:3853-3865(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT SER-801, MUTAGENESIS OF SER-801 AND SER-804, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH PKD1. - Ref.19"Mutations in GANAB, encoding the glucosidase IIalpha subunit, cause autosomal-dominant polycystic kidney and liver disease."
Genkyst Study Group, HALT Progression of Polycystic Kidney Disease Group, Consortium for Radiologic Imaging Studies of Polycystic Kidney Disease
Porath B., Gainullin V.G., Cornec-Le Gall E., Dillinger E.K., Heyer C.M., Hopp K., Edwards M.E., Madsen C.D., Mauritz S.R., Banks C.J., Baheti S., Reddy B., Herrero J.I., Banales J.M., Hogan M.C., Tasic V., Watnick T.J., Chapman A.B. , Vigneau C., Lavainne F., Audrezet M.P., Ferec C., Le Meur Y., Torres V.E., Harris P.C.
Am. J. Hum. Genet. 98:1193-1207(2016) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.25"The structure of the polycystic kidney disease channel PKD2 in lipid nanodiscs."
Shen P.S., Yang X., DeCaen P.G., Liu X., Bulkley D., Clapham D.E., Cao E.
Cell 167:763-773(2016) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.00 ANGSTROMS) OF 198-702, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, GLYCOSYLATION AT ASN-328; ASN-362 AND ASN-375, DISULFIDE BONDS. - Ref.26"Structure of the polycystic kidney disease TRP channel polycystin-2 (PC2)."
Grieben M., Pike A.C., Shintre C.A., Venturi E., El-Ajouz S., Tessitore A., Shrestha L., Mukhopadhyay S., Mahajan P., Chalk R., Burgess-Brown N.A., Sitsapesan R., Huiskonen J.T., Carpenter E.P.
Nat. Struct. Mol. Biol. 24:114-122(2017) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (4.20 ANGSTROMS) OF 185-723, FUNCTION, SUBUNIT, TOPOLOGY, GLYCOSYLATION AT ASN-328; ASN-362 AND ASN-375. - Ref.27"Molecular insights into lipid-assisted Ca2+ regulation of the TRP channel polycystin-2."
Wilkes M., Madej M.G., Kreuter L., Rhinow D., Heinz V., De Sanctis S., Ruppel S., Richter R.M., Joos F., Grieben M., Pike A.C., Huiskonen J.T., Carpenter E.P., Kuhlbrandt W., Witzgall R., Ziegler C.
Nat. Struct. Mol. Biol. 24:123-130(2017) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (4.20 ANGSTROMS) IN COMPLEX WITH CALCIUM AND LIPIDS, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, GLYCOSYLATION AT ASN-299; ASN-305; ASN-328; ASN-362 AND ASN-375, DISULFIDE BONDS.
- Cell membrane 6 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.11"Trafficking of TRPP2 by PACS proteins represents a novel mechanism of ion channel regulation."
Koettgen M., Benzing T., Simmen T., Tauber R., Buchholz B., Feliciangeli S., Huber T.B., Schermer B., Kramer-Zucker A., Hoepker K., Simmen K.C., Tschucke C.C., Sandford R., Kim E., Thomas G., Walz G.
EMBO J. 24:705-716(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH PACS1 AND PACS2, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-812, MUTAGENESIS OF SER-812 AND 815-ASP--ASP-817. - Ref.18"The cAMP Signaling Pathway and Direct Protein Kinase A Phosphorylation Regulate Polycystin-2 (TRPP2) Channel Function."
del Rocio Cantero M., Velazquez I.F., Streets A.J., Ong A.C.M., Cantiello H.F.
J. Biol. Chem. 290:23888-23896(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-829, TISSUE SPECIFICITY, MUTAGENESIS OF SER-829. - Ref.19"Mutations in GANAB, encoding the glucosidase IIalpha subunit, cause autosomal-dominant polycystic kidney and liver disease."
Genkyst Study Group, HALT Progression of Polycystic Kidney Disease Group, Consortium for Radiologic Imaging Studies of Polycystic Kidney Disease
Porath B., Gainullin V.G., Cornec-Le Gall E., Dillinger E.K., Heyer C.M., Hopp K., Edwards M.E., Madsen C.D., Mauritz S.R., Banks C.J., Baheti S., Reddy B., Herrero J.I., Banales J.M., Hogan M.C., Tasic V., Watnick T.J., Chapman A.B. , Vigneau C., Lavainne F., Audrezet M.P., Ferec C., Le Meur Y., Torres V.E., Harris P.C.
Am. J. Hum. Genet. 98:1193-1207(2016) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION. - Ref.20"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) [PubMed] [Europe PMC] [Abstract]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. - Ref.22"Structural and molecular basis of the assembly of the TRPP2/PKD1 complex."
Yu Y., Ulbrich M.H., Li M.H., Buraei Z., Chen X.Z., Ong A.C., Tong L., Isacoff E.Y., Yang J.
Proc. Natl. Acad. Sci. U.S.A. 106:11558-11563(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 833-872, COILED COIL, SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF LEU-842; VAL-846; MET-849; ILE-860; VAL-863 AND LEU-867. - Ref.27"Molecular insights into lipid-assisted Ca2+ regulation of the TRP channel polycystin-2."
Wilkes M., Madej M.G., Kreuter L., Rhinow D., Heinz V., De Sanctis S., Ruppel S., Richter R.M., Joos F., Grieben M., Pike A.C., Huiskonen J.T., Carpenter E.P., Kuhlbrandt W., Witzgall R., Ziegler C.
Nat. Struct. Mol. Biol. 24:123-130(2017) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (4.20 ANGSTROMS) IN COMPLEX WITH CALCIUM AND LIPIDS, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, GLYCOSYLATION AT ASN-299; ASN-305; ASN-328; ASN-362 AND ASN-375, DISULFIDE BONDS.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.25"The structure of the polycystic kidney disease channel PKD2 in lipid nanodiscs."
Shen P.S., Yang X., DeCaen P.G., Liu X., Bulkley D., Clapham D.E., Cao E.
Cell 167:763-773(2016) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.00 ANGSTROMS) OF 198-702, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, GLYCOSYLATION AT ASN-328; ASN-362 AND ASN-375, DISULFIDE BONDS. - Ref.26"Structure of the polycystic kidney disease TRP channel polycystin-2 (PC2)."
Grieben M., Pike A.C., Shintre C.A., Venturi E., El-Ajouz S., Tessitore A., Shrestha L., Mukhopadhyay S., Mahajan P., Chalk R., Burgess-Brown N.A., Sitsapesan R., Huiskonen J.T., Carpenter E.P.
Nat. Struct. Mol. Biol. 24:114-122(2017) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (4.20 ANGSTROMS) OF 185-723, FUNCTION, SUBUNIT, TOPOLOGY, GLYCOSYLATION AT ASN-328; ASN-362 AND ASN-375. - Ref.27"Molecular insights into lipid-assisted Ca2+ regulation of the TRP channel polycystin-2."
Wilkes M., Madej M.G., Kreuter L., Rhinow D., Heinz V., De Sanctis S., Ruppel S., Richter R.M., Joos F., Grieben M., Pike A.C., Huiskonen J.T., Carpenter E.P., Kuhlbrandt W., Witzgall R., Ziegler C.
Nat. Struct. Mol. Biol. 24:123-130(2017) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (4.20 ANGSTROMS) IN COMPLEX WITH CALCIUM AND LIPIDS, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, GLYCOSYLATION AT ASN-299; ASN-305; ASN-328; ASN-362 AND ASN-375, DISULFIDE BONDS.
- Basolateral cell membrane 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.5"Cellular and subcellular distribution of polycystin-2, the protein product of the PKD2 gene."
Foggensteiner L., Bevan A.P., Thomas R., Coleman N., Boulter C., Bradley J., Ibraghimov-Beskrovnaya O., Klinger K., Sandford R.
J. Am. Soc. Nephrol. 11:814-827(2000) [PubMed] [Europe PMC] [Abstract]Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
- cilium membrane 3 Publications
Endoplasmic reticulum
- Endoplasmic reticulum membrane 1 Publication
<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
- Ref.6"In vivo interaction of the adapter protein CD2-associated protein with the type 2 polycystic kidney disease protein, polycystin-2."
Lehtonen S., Ora A., Olkkonen V.M., Geng L., Zerial M., Somlo S., Lehtonen E.
J. Biol. Chem. 275:32888-32893(2000) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CD2AP, SUBCELLULAR LOCATION.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.7"The polycystic kidney disease protein PKD2 interacts with Hax-1, a protein associated with the actin cytoskeleton."
Gallagher A.R., Cedzich A., Gretz N., Somlo S., Witzgall R.
Proc. Natl. Acad. Sci. U.S.A. 97:4017-4022(2000) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH HAX1, SUBCELLULAR LOCATION. - Ref.9"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) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT PKD2 VAL-511. - Ref.11"Trafficking of TRPP2 by PACS proteins represents a novel mechanism of ion channel regulation."
Koettgen M., Benzing T., Simmen T., Tauber R., Buchholz B., Feliciangeli S., Huber T.B., Schermer B., Kramer-Zucker A., Hoepker K., Simmen K.C., Tschucke C.C., Sandford R., Kim E., Thomas G., Walz G.
EMBO J. 24:705-716(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH PACS1 AND PACS2, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-812, MUTAGENESIS OF SER-812 AND 815-ASP--ASP-817. - Ref.15"Protein kinase D-mediated phosphorylation of polycystin-2 (TRPP2) is essential for its effects on cell growth and calcium channel activity."
Streets A.J., Needham A.J., Gill S.K., Ong A.C.
Mol. Biol. Cell 21:3853-3865(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT SER-801, MUTAGENESIS OF SER-801 AND SER-804, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH PKD1. - Ref.27"Molecular insights into lipid-assisted Ca2+ regulation of the TRP channel polycystin-2."
Wilkes M., Madej M.G., Kreuter L., Rhinow D., Heinz V., De Sanctis S., Ruppel S., Richter R.M., Joos F., Grieben M., Pike A.C., Huiskonen J.T., Carpenter E.P., Kuhlbrandt W., Witzgall R., Ziegler C.
Nat. Struct. Mol. Biol. 24:123-130(2017) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (4.20 ANGSTROMS) IN COMPLEX WITH CALCIUM AND LIPIDS, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, GLYCOSYLATION AT ASN-299; ASN-305; ASN-328; ASN-362 AND ASN-375, DISULFIDE BONDS.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.25"The structure of the polycystic kidney disease channel PKD2 in lipid nanodiscs."
Shen P.S., Yang X., DeCaen P.G., Liu X., Bulkley D., Clapham D.E., Cao E.
Cell 167:763-773(2016) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.00 ANGSTROMS) OF 198-702, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, GLYCOSYLATION AT ASN-328; ASN-362 AND ASN-375, DISULFIDE BONDS. - Ref.26"Structure of the polycystic kidney disease TRP channel polycystin-2 (PC2)."
Grieben M., Pike A.C., Shintre C.A., Venturi E., El-Ajouz S., Tessitore A., Shrestha L., Mukhopadhyay S., Mahajan P., Chalk R., Burgess-Brown N.A., Sitsapesan R., Huiskonen J.T., Carpenter E.P.
Nat. Struct. Mol. Biol. 24:114-122(2017) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (4.20 ANGSTROMS) OF 185-723, FUNCTION, SUBUNIT, TOPOLOGY, GLYCOSYLATION AT ASN-328; ASN-362 AND ASN-375. - Ref.27"Molecular insights into lipid-assisted Ca2+ regulation of the TRP channel polycystin-2."
Wilkes M., Madej M.G., Kreuter L., Rhinow D., Heinz V., De Sanctis S., Ruppel S., Richter R.M., Joos F., Grieben M., Pike A.C., Huiskonen J.T., Carpenter E.P., Kuhlbrandt W., Witzgall R., Ziegler C.
Nat. Struct. Mol. Biol. 24:123-130(2017) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (4.20 ANGSTROMS) IN COMPLEX WITH CALCIUM AND LIPIDS, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, GLYCOSYLATION AT ASN-299; ASN-305; ASN-328; ASN-362 AND ASN-375, DISULFIDE BONDS.
- Endoplasmic reticulum membrane 1 Publication
Other locations
- Cytoplasmic vesicle membrane 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.5"Cellular and subcellular distribution of polycystin-2, the protein product of the PKD2 gene."
Foggensteiner L., Bevan A.P., Thomas R., Coleman N., Boulter C., Bradley J., Ibraghimov-Beskrovnaya O., Klinger K., Sandford R.
J. Am. Soc. Nephrol. 11:814-827(2000) [PubMed] [Europe PMC] [Abstract]Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
Note: Retained in the endoplasmic reticulum by interaction with PACS1 and PACS2 (PubMed:15692563). Detected on kidney tubule basolateral membranes and basal cytoplasmic vesicles (PubMed:10770959). Cell surface and cilium localization requires GANAB (PubMed:27259053).2 Publications- Cytoplasmic vesicle membrane 1 Publication
- Ref.11"Trafficking of TRPP2 by PACS proteins represents a novel mechanism of ion channel regulation."
Koettgen M., Benzing T., Simmen T., Tauber R., Buchholz B., Feliciangeli S., Huber T.B., Schermer B., Kramer-Zucker A., Hoepker K., Simmen K.C., Tschucke C.C., Sandford R., Kim E., Thomas G., Walz G.
EMBO J. 24:705-716(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH PACS1 AND PACS2, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-812, MUTAGENESIS OF SER-812 AND 815-ASP--ASP-817. - Ref.19"Mutations in GANAB, encoding the glucosidase IIalpha subunit, cause autosomal-dominant polycystic kidney and liver disease."
Genkyst Study Group, HALT Progression of Polycystic Kidney Disease Group, Consortium for Radiologic Imaging Studies of Polycystic Kidney Disease
Porath B., Gainullin V.G., Cornec-Le Gall E., Dillinger E.K., Heyer C.M., Hopp K., Edwards M.E., Madsen C.D., Mauritz S.R., Banks C.J., Baheti S., Reddy B., Herrero J.I., Banales J.M., Hogan M.C., Tasic V., Watnick T.J., Chapman A.B. , Vigneau C., Lavainne F., Audrezet M.P., Ferec C., Le Meur Y., Torres V.E., Harris P.C.
Am. J. Hum. Genet. 98:1193-1207(2016) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
Cytoskeleton
- ciliary basal body Source: MGI <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- mitotic spindle Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Endoplasmic reticulum
- endoplasmic reticulum Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- endoplasmic reticulum membrane Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- integral component of cytoplasmic side of endoplasmic reticulum membrane Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- integral component of lumenal side of endoplasmic reticulum membrane Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Extracellular region or secreted
- extracellular exosome Source: UniProtKBInferred from high throughput direct assayi
Plasma Membrane
- basal plasma membrane Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- ciliary membrane Source: UniProtKB-SubCell
- integral component of plasma membrane Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- plasma membrane Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Other locations
- basal cortex Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- cell-cell junction Source: Ensembl
- cilium Source: BHF-UCL
- cytoplasm Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- cytoplasmic vesicle membrane Source: UniProtKB-SubCell
- lamellipodium Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- motile cilium Source: BHF-UCL
- non-motile cilium Source: BHF-UCL
- polycystin complex Source: BHF-UCL
Topology
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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 domaini | 1 – 219 | Cytoplasmic3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 219 | |
| <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>Transmembranei | 220 – 241 | Helical; Name=S13 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 22 | |
| <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 domaini | 242 – 468 | Extracellular3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 227 | |
| <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>Transmembranei | 469 – 489 | Helical; Name=S23 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 21 | |
| <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 domaini | 490 – 505 | Cytoplasmic3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 16 | |
| <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>Transmembranei | 506 – 526 | Helical; Name=S33 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 21 | |
| <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 domaini | 527 – 552 | Extracellular3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 26 | |
| <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>Transmembranei | 553 – 573 | Helical; Name=S43 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 21 | |
| <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 domaini | 574 – 597 | Cytoplasmic3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 24 | |
| <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>Transmembranei | 598 – 619 | Helical; Name=53 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 22 | |
| <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 domaini | 620 – 631 | Extracellular3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 12 | |
| <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>Intramembranei | 632 – 646 | Pore-forming3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 15 | |
| <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 domaini | 647 – 654 | Extracellular3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 8 | |
| <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>Transmembranei | 655 – 675 | Helical; Name=S63 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 21 | |
| <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 domaini | 676 – 968 | Cytoplasmic3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 293 |
<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>Keywords - Cellular componenti
Cell membrane, Cell projection, Cilium, Cytoplasmic vesicle, Endoplasmic reticulum, 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 (PKD2)11 Publications
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More...</a></p>
Manual assertion based on experiment ini
- Ref.9"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) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT PKD2 VAL-511. - Ref.20"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) [PubMed] [Europe PMC] [Abstract]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. - Ref.28"A spectrum of mutations in the second gene for autosomal dominant polycystic kidney disease (PKD2)."
Veldhuisen B., Saris J.J., de Haij S., Hayashi T., Reynolds D.M., Mochizuki T., Elles R., Fossdal R., Bogdanova N., van Dijk M.A., Coto E., Ravine D., Noerby S., Verellen-Dumoulin C., Breuning M.H., Somlo S., Peters D.J.M.
Am. J. Hum. Genet. 61:547-555(1997) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT PKD2 GLY-414. - Ref.29"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) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT PKD2 VAL-511. - Ref.30"Seven novel mutations of the PKD2 gene in families with autosomal dominant polycystic kidney disease."
Torra R., Viribay M., Telleria D., Badenas C., Watson M., Harris P.C., Darnell A., San Millan J.L.
Kidney Int. 56:28-33(1999) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT PKD2 PRO-356, VARIANT PRO-28. - Ref.31"Mutations of PKD1 in ADPKD2 cysts suggest a pathogenic effect of trans-heterozygous mutations."
Watnick T.J., He N., Wang K., Liang Y., Parfrey P., Hefferton D., St George-Hyslop P.H., Germino G.G., Pei Y.
Nat. Genet. 25:143-144(2000) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS PKD2 ILE-479 DEL; 504-ARG--VAL-512 DEL AND TYR-684 DEL. - Ref.32"Four novel mutations of the PKD2 gene in Czech families with autosomal dominant polycystic kidney disease."
Reiterova J., Stekrova J., Peters D.J.M., Kapras J., Kohoutova M., Merta M., Zidovska J.
Hum. Mutat. 19:573-573(2002) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT PKD2 TRP-322, VARIANTS LEU-24; PRO-28 AND LEU-800. - Ref.33"Genotype-renal function correlation in type 2 autosomal dominant polycystic kidney disease."
Magistroni R., He N., Wang K., Andrew R., Johnson A., Gabow P., Dicks E., Parfrey P., Torra R., San-Millan J.L., Coto E., Van Dijk M., Breuning M., Peters D., Bogdanova N., Ligabue G., Albertazzi A., Hateboer N. , Demetriou K., Pierides A., Deltas C., St George-Hyslop P., Ravine D., Pei Y.
J. Am. Soc. Nephrol. 14:1164-1174(2003) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS PKD2 PRO-356; GLY-414; ARG-632 AND GLN-807. - Ref.34"PKD2 mutations in a Czech population with autosomal dominant polycystic kidney disease."
Stekrova J., Reiterova J., Merta M., Damborsky J., Zidovska J., Kebrdlova V., Kohoutova M.
Nephrol. Dial. Transplant. 19:1116-1122(2004) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS PKD2 GLN-306 AND GLY-420, VARIANT PRO-28. - Ref.35"Genetics and phenotypic characteristics of autosomal dominant polycystic kidney disease in Finns."
Peltola P., Lumiaho A., Miettinen R., Pihlajamaeki J., Sandford R., Laakso M.
J. Mol. Med. 83:638-646(2005) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT PKD2 GLN-322. - Ref.37"Novel PKD1 and PKD2 mutations in autosomal dominant polycystic kidney disease (ADPKD)."
Hoefele J., Mayer K., Scholz M., Klein H.G.
Nephrol. Dial. Transplant. 26:2181-2188(2011) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT PKD2 PRO-384.
Koulen P., Cai Y., Geng L., Maeda Y., Nishimura S., Witzgall R., Ehrlich B.E., Somlo S.
Nat. Cell Biol. 4:191-197(2002) [PubMed] [Europe PMC] [Abstract]
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) [PubMed] [Europe PMC] [Abstract]
Veldhuisen B., Saris J.J., de Haij S., Hayashi T., Reynolds D.M., Mochizuki T., Elles R., Fossdal R., Bogdanova N., van Dijk M.A., Coto E., Ravine D., Noerby S., Verellen-Dumoulin C., Breuning M.H., Somlo S., Peters D.J.M.
Am. J. Hum. Genet. 61:547-555(1997) [PubMed] [Europe PMC] [Abstract]
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) [PubMed] [Europe PMC] [Abstract]
Torra R., Viribay M., Telleria D., Badenas C., Watson M., Harris P.C., Darnell A., San Millan J.L.
Kidney Int. 56:28-33(1999) [PubMed] [Europe PMC] [Abstract]
Watnick T.J., He N., Wang K., Liang Y., Parfrey P., Hefferton D., St George-Hyslop P.H., Germino G.G., Pei Y.
Nat. Genet. 25:143-144(2000) [PubMed] [Europe PMC] [Abstract]
Reiterova J., Stekrova J., Peters D.J.M., Kapras J., Kohoutova M., Merta M., Zidovska J.
Hum. Mutat. 19:573-573(2002) [PubMed] [Europe PMC] [Abstract]
Magistroni R., He N., Wang K., Andrew R., Johnson A., Gabow P., Dicks E., Parfrey P., Torra R., San-Millan J.L., Coto E., Van Dijk M., Breuning M., Peters D., Bogdanova N., Ligabue G., Albertazzi A., Hateboer N. , Demetriou K., Pierides A., Deltas C., St George-Hyslop P., Ravine D., Pei Y.
J. Am. Soc. Nephrol. 14:1164-1174(2003) [PubMed] [Europe PMC] [Abstract]
Stekrova J., Reiterova J., Merta M., Damborsky J., Zidovska J., Kebrdlova V., Kohoutova M.
Nephrol. Dial. Transplant. 19:1116-1122(2004) [PubMed] [Europe PMC] [Abstract]
Peltola P., Lumiaho A., Miettinen R., Pihlajamaeki J., Sandford R., Laakso M.
J. Mol. Med. 83:638-646(2005) [PubMed] [Europe PMC] [Abstract]
Hoefele J., Mayer K., Scholz M., Klein H.G.
Nephrol. Dial. Transplant. 26:2181-2188(2011) [PubMed] [Europe PMC] [Abstract]
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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_058822 | 306 | R → Q in PKD2. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_058823 | 322 | R → Q in PKD2. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_058824 | 322 | R → W in PKD2. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_011073 | 356 | A → P in PKD2. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_064394 | 384 | A → P in PKD2. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_009195 | 414 | W → 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 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_058825 | 420 | R → 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 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_011074 | 479 | Missing in PKD2; somatic mutation. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_011075 | 504 – 512 | Missing in PKD2; somatic mutation. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 9 | |
| <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_058827 | 511 | D → 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. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_058828 | 632 | C → R in PKD2. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_011076 | 684 | Missing in PKD2; somatic mutation. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_058830 | 807 | R → Q in PKD2. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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>Mutagenesisi | 76 | S → A: Abolishes phosphorylation of the N-terminal domain. Abolishes the ability to complement a pkd2-deficient zebrafish mutant; when associated with A-80. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 80 | S → A: Decreases phosphorylation of the N-terminal domain. Abolishes the ability to complement a pkd2-deficient zebrafish mutant; when associated with A-76. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 604 | F → A or I: No effect on channel activation. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 604 | F → P: Gain-of-function mutation resulting in increased channel activity. Absence of gain of function; when associated with F-605 DEL; when associated with V-511; when associated with G-414; when associated with G-420. Increased channel activity; when associated with 736-L-N-737 DEL. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 605 | Missing : Abolishes increased channel activity due to a gain of function mutation; when associated with P-604. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 721 | T → A: Decreases phosphorylation; when associated with A-801; A-812; A-831 and A-943. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 736 – 737 | Missing : Increased channel activity; when associated with P-604. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 2 | |
| <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>Mutagenesisi | 768 | Q → G: Strongly increases calcium binding affinity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 771 | T → A: Loss of calcium-binding site; when associated with A-774. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 774 | E → A: Loss of calcium-binding site; when associated with A-771. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 774 | E → Q: Abolishes calcium binding via the EF-hand. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 801 | S → A: Decreases phosphorylation; when associated with A-721; A-812; A-831 and A-943. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 801 | S → D: Phosphomimetic mutant. No effect on release of Ca(2+) stores from the endoplasmic reticulum. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 801 | S → G: Loss of phosphorylation at this site. Impairs release of Ca(2+) stores from the endoplasmic reticulum. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 804 | S → N: Loss of phosphorylation at Ser-801. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 812 | S → 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 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 812 | S → D: No effect on interaction with PACS1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 815 – 817 | DDD → AAA: Strongly decreases interaction with PACS1 and enhances expression at the cell membrane. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 3 | |
| <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>Mutagenesisi | 829 | S → A: Abolishes increased channel opening in response to cAMP and phosphorylation by PKA. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 831 | S → A: Decreases phosphorylation; when associated with A-721; A-801; A-812 and A-943. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 842 | L → A: Abolishes oligomerization and interaction with PKD1; when associated with A-846; A-849; A-860; A-863 and A-867. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 842 | L → P: Loss of protein solubility. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 846 | V → A: Abolishes oligomerization and interaction with PKD1; when associated with A-842; A-849; A-860; A-863 and A-867. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 846 | V → E: Loss of protein solubility. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 849 | M → A: Abolishes oligomerization and interaction with PKD1; when associated with A-842; A-846; A-860; A-863 and A-867. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 849 | M → K: Loss of protein solubility. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 853 | I → P: Loss of protein solubility. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 856 | I → K: Loss of protein solubility. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 860 | I → A: Abolishes oligomerization and interaction with PKD1; when associated with A-842; A-846; A-849; A-863 and A-867. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 863 | V → A: Abolishes oligomerization and interaction with PKD1; when associated with A-842; A-846; A-849; A-860 and A-867. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 863 | V → E: Loss of protein solubility; when associated with K-849. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 867 | L → A: Abolishes oligomerization and interaction with PKD1; when associated with A-842; A-846; A-849; A-860 and A-863. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 943 | S → A: Decreases phosphorylation; when associated with A-721; A-801; A-812 and A-831. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
<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>Keywords - Diseasei
Ciliopathy, Disease mutationOrganism-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 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 613095 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 key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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_0000164356 | 1 – 968 | Polycystin-2Add BLAST | 968 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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 residuei | 76 | Phosphoserine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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 residuei | 80 | Phosphoserine1 Publication <p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
| 1 | |
| <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 residuei | 137 | Omega-N-methylarginineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <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>Glycosylationi | 299 | N-linked (GlcNAc...) asparagine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Glycosylationi | 305 | N-linked (GlcNAc...) asparagine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Glycosylationi | 328 | N-linked (GlcNAc...) (complex) asparagine4 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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 bondi | 331 ↔ 344 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 2 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| ||
| <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>Glycosylationi | 362 | N-linked (GlcNAc...) asparagine3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Glycosylationi | 375 | N-linked (GlcNAc...) asparagine3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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 residuei | 801 | Phosphoserine1 Publication <p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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 residuei | 808 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <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 residuei | 812 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
| 1 | |
| <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 residuei | 829 | Phosphoserine1 Publication <p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
| 1 |
<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
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.12"Identification of an N-terminal glycogen synthase kinase 3 phosphorylation site which regulates the functional localization of polycystin-2 in vivo and in vitro."
Streets A.J., Moon D.J., Kane M.E., Obara T., Ong A.C.
Hum. Mol. Genet. 15:1465-1473(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT SER-76; SER-80 AND SER-812, MUTAGENESIS OF SER-76; SER-80; THR-721; SER-801; SER-812; SER-831 AND SER-943. - Ref.15"Protein kinase D-mediated phosphorylation of polycystin-2 (TRPP2) is essential for its effects on cell growth and calcium channel activity."
Streets A.J., Needham A.J., Gill S.K., Ong A.C.
Mol. Biol. Cell 21:3853-3865(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT SER-801, MUTAGENESIS OF SER-801 AND SER-804, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH PKD1. - Ref.18"The cAMP Signaling Pathway and Direct Protein Kinase A Phosphorylation Regulate Polycystin-2 (TRPP2) Channel Function."
del Rocio Cantero M., Velazquez I.F., Streets A.J., Ong A.C.M., Cantiello H.F.
J. Biol. Chem. 290:23888-23896(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-829, TISSUE SPECIFICITY, MUTAGENESIS OF SER-829.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.27"Molecular insights into lipid-assisted Ca2+ regulation of the TRP channel polycystin-2."
Wilkes M., Madej M.G., Kreuter L., Rhinow D., Heinz V., De Sanctis S., Ruppel S., Richter R.M., Joos F., Grieben M., Pike A.C., Huiskonen J.T., Carpenter E.P., Kuhlbrandt W., Witzgall R., Ziegler C.
Nat. Struct. Mol. Biol. 24:123-130(2017) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (4.20 ANGSTROMS) IN COMPLEX WITH CALCIUM AND LIPIDS, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, GLYCOSYLATION AT ASN-299; ASN-305; ASN-328; ASN-362 AND ASN-375, DISULFIDE BONDS.
<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>Keywords - PTMi
Disulfide bond, Glycoprotein, Methylation, PhosphoproteinProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | 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
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"PKD2, a gene for polycystic kidney disease that encodes an integral membrane protein."
Mochizuki T., Wu G., Hayashi T., Xenophontos S.L., Veldhuisen B., Saris J.J., Reynolds D.M., Cai Y., Gabow P.A., Pierides A., Kimberling W.J., Breuning M.H., Deltas C.C., Peters D.J.M., Somlo S.
Science 272:1339-1342(1996) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY. - Ref.5"Cellular and subcellular distribution of polycystin-2, the protein product of the PKD2 gene."
Foggensteiner L., Bevan A.P., Thomas R., Coleman N., Boulter C., Bradley J., Ibraghimov-Beskrovnaya O., Klinger K., Sandford R.
J. Am. Soc. Nephrol. 11:814-827(2000) [PubMed] [Europe PMC] [Abstract]Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION. - Ref.18"The cAMP Signaling Pathway and Direct Protein Kinase A Phosphorylation Regulate Polycystin-2 (TRPP2) Channel Function."
del Rocio Cantero M., Velazquez I.F., Streets A.J., Ong A.C.M., Cantiello H.F.
J. Biol. Chem. 290:23888-23896(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-829, TISSUE SPECIFICITY, MUTAGENESIS OF SER-829.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000118762 |
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
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
9 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.6"In vivo interaction of the adapter protein CD2-associated protein with the type 2 polycystic kidney disease protein, polycystin-2."
Lehtonen S., Ora A., Olkkonen V.M., Geng L., Zerial M., Somlo S., Lehtonen E.
J. Biol. Chem. 275:32888-32893(2000) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CD2AP, SUBCELLULAR LOCATION. - Ref.7"The polycystic kidney disease protein PKD2 interacts with Hax-1, a protein associated with the actin cytoskeleton."
Gallagher A.R., Cedzich A., Gretz N., Somlo S., Witzgall R.
Proc. Natl. Acad. Sci. U.S.A. 97:4017-4022(2000) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH HAX1, SUBCELLULAR LOCATION. - Ref.11"Trafficking of TRPP2 by PACS proteins represents a novel mechanism of ion channel regulation."
Koettgen M., Benzing T., Simmen T., Tauber R., Buchholz B., Feliciangeli S., Huber T.B., Schermer B., Kramer-Zucker A., Hoepker K., Simmen K.C., Tschucke C.C., Sandford R., Kim E., Thomas G., Walz G.
EMBO J. 24:705-716(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH PACS1 AND PACS2, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-812, MUTAGENESIS OF SER-812 AND 815-ASP--ASP-817. - Ref.13"TRPP2 and TRPV4 form a polymodal sensory channel complex."
Kottgen M., Buchholz B., Garcia-Gonzalez M.A., Kotsis F., Fu X., Doerken M., Boehlke C., Steffl D., Tauber R., Wegierski T., Nitschke R., Suzuki M., Kramer-Zucker A., Germino G.G., Watnick T., Prenen J., Nilius B., Kuehn E.W., Walz G.
J. Cell Biol. 182:437-447(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH TRPV4, SUBCELLULAR LOCATION. - Ref.15"Protein kinase D-mediated phosphorylation of polycystin-2 (TRPP2) is essential for its effects on cell growth and calcium channel activity."
Streets A.J., Needham A.J., Gill S.K., Ong A.C.
Mol. Biol. Cell 21:3853-3865(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT SER-801, MUTAGENESIS OF SER-801 AND SER-804, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH PKD1. - Ref.22"Structural and molecular basis of the assembly of the TRPP2/PKD1 complex."
Yu Y., Ulbrich M.H., Li M.H., Buraei Z., Chen X.Z., Ong A.C., Tong L., Isacoff E.Y., Yang J.
Proc. Natl. Acad. Sci. U.S.A. 106:11558-11563(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 833-872, COILED COIL, SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF LEU-842; VAL-846; MET-849; ILE-860; VAL-863 AND LEU-867. - Ref.25"The structure of the polycystic kidney disease channel PKD2 in lipid nanodiscs."
Shen P.S., Yang X., DeCaen P.G., Liu X., Bulkley D., Clapham D.E., Cao E.
Cell 167:763-773(2016) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.00 ANGSTROMS) OF 198-702, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, GLYCOSYLATION AT ASN-328; ASN-362 AND ASN-375, DISULFIDE BONDS. - Ref.26"Structure of the polycystic kidney disease TRP channel polycystin-2 (PC2)."
Grieben M., Pike A.C., Shintre C.A., Venturi E., El-Ajouz S., Tessitore A., Shrestha L., Mukhopadhyay S., Mahajan P., Chalk R., Burgess-Brown N.A., Sitsapesan R., Huiskonen J.T., Carpenter E.P.
Nat. Struct. Mol. Biol. 24:114-122(2017) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (4.20 ANGSTROMS) OF 185-723, FUNCTION, SUBUNIT, TOPOLOGY, GLYCOSYLATION AT ASN-328; ASN-362 AND ASN-375. - Ref.27"Molecular insights into lipid-assisted Ca2+ regulation of the TRP channel polycystin-2."
Wilkes M., Madej M.G., Kreuter L., Rhinow D., Heinz V., De Sanctis S., Ruppel S., Richter R.M., Joos F., Grieben M., Pike A.C., Huiskonen J.T., Carpenter E.P., Kuhlbrandt W., Witzgall R., Ziegler C.
Nat. Struct. Mol. Biol. 24:123-130(2017) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (4.20 ANGSTROMS) IN COMPLEX WITH CALCIUM AND LIPIDS, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, GLYCOSYLATION AT ASN-299; ASN-305; ASN-328; ASN-362 AND ASN-375, DISULFIDE BONDS.
<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
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| itself | 8 | EBI-7813714,EBI-7813714 | ||
| Hax1 | O35387 | 3 | EBI-7813714,EBI-642449 | From Mus musculus. |
| ID2 | Q02363 | 7 | EBI-7813714,EBI-713450 | |
| itpr1 | Q91908 | 2 | EBI-7813714,EBI-9633447 | From Xenopus laevis. |
| KRT40 | Q6A162 | 3 | EBI-7813714,EBI-10171697 | |
| KRTAP10-8 | P60410 | 3 | EBI-7813714,EBI-10171774 | |
| MAGEA8 | P43361 | 3 | EBI-7813714,EBI-10182930 | |
| PKD1 | P98161 | 8 | EBI-7813714,EBI-1752013 | |
| PKD1 | P98161-3 | 4 | EBI-9837017,EBI-15930070 | |
| Pkd1 | O08852 | 2 | EBI-9837017,EBI-6666305 | From Mus musculus. |
| PLSCR1 | O15162 | 3 | EBI-7813714,EBI-740019 | |
| RYR2 | J9P3Y7 | 2 | EBI-9837017,EBI-15630134 | From Canis lupus familiaris. |
| TRPC1 | P48995 | 3 | EBI-7813714,EBI-929665 | |
| TRPC1 | P48995-2 | 4 | EBI-7813714,EBI-9830970 |
<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
- actinin binding Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- ATPase binding Source: BHF-UCL
- cytoskeletal protein binding Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- HLH domain binding Source: BHF-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- identical protein binding Source: IntAct <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- ion channel binding Source: BHF-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- muscle alpha-actinin binding Source: Ensembl
- phosphoprotein binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- protein homodimerization activity Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- signaling receptor binding Source: BHF-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
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, 26 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
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 217 – 241 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 25 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 246 – 257 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 276 – 283 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 286 – 291 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 304 – 306 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 310 – 312 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 313 – 326 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 328 – 330 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 335 – 337 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 338 – 340 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 350 – 352 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 364 – 366 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 371 – 373 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 390 – 394 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 399 – 411 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 419 – 430 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 431 – 434 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 435 – 444 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 452 – 460 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 468 – 491 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 24 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 506 – 527 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 22 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 528 – 530 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 533 – 540 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 549 – 571 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 23 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 572 – 579 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 581 – 618 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 38 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 619 – 622 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 624 – 626 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 629 – 641 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 647 – 652 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 656 – 669 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 670 – 672 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 673 – 692 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 20 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 730 – 734 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 738 – 744 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 745 – 747 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 752 – 762 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 763 – 766 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 767 – 771 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 773 – 777 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 781 – 783 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 793 – 795 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 836 – 894 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 59 |
3D structure databases
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 key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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>Domaini | 750 – 785 | EF-handPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi 2 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 36 |
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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>Regioni | 803 – 822 | Linker1 Publication <p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
| 20 | |
| <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>Regioni | 810 – 821 | Important for interaction with PACS1 and PACS21 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 12 |
Coiled coil
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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 coili | 833 – 872 | 1 Publication <p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 40 |
Motif
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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>Motifi | 641 – 643 | Selectivity filter1 Publication <p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
| 3 |
Compositional bias
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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 biasi | 95 – 107 | Poly-GluAdd BLAST | 13 | |
| <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 biasi | 153 – 157 | Poly-Arg | 5 |
<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
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.21"Domain mapping of the polycystin-2 C-terminal tail using de novo molecular modeling and biophysical analysis."
Celic A., Petri E.T., Demeler B., Ehrlich B.E., Boggon T.J.
J. Biol. Chem. 283:28305-28312(2008) [PubMed] [Europe PMC] [Abstract] - Ref.22"Structural and molecular basis of the assembly of the TRPP2/PKD1 complex."
Yu Y., Ulbrich M.H., Li M.H., Buraei Z., Chen X.Z., Ong A.C., Tong L., Isacoff E.Y., Yang J.
Proc. Natl. Acad. Sci. U.S.A. 106:11558-11563(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 833-872, COILED COIL, SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF LEU-842; VAL-846; MET-849; ILE-860; VAL-863 AND LEU-867.
<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
<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>Keywords - Domaini
Coiled coil, Transmembrane, Transmembrane helixPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG3599 Eukaryota ENOG410XTGE LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00700000104221 |
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 | QAWSRDN |
Database of Orthologous Groups More...OrthoDBi | EOG091G034F |
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 basketAdded 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.
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
The sequence of this isoform differs from the canonical sequence as follows:
476-483: CEIIFCFF → FICSSYGD
484-968: Missing.
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
VIPSWQFQPL KLIRYVTTFD FFLAAFICSS YGD
The sequence of this isoform differs from the canonical sequence as follows:
517-572: Missing.
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 DVVIVVLFKF INFNRTMSQL STTMSRCAKD LFGFAIMFFI
560 570 580 590 600
IFLAYAQLAY LVFGTQVDDF STFQECIFTQ FRIILGDINF AEIEEANRVL
610 620 630 640 650
GPIYFTTFVF FMFFILLNMF LAIINDTYSE VKSDLAQQKA EMELSDLIRK
660 670 680 690 700
GYHKALVKLK LKKNTVDDIS ESLRQGGGKL NFDELRQDLK GKGHTDAEIE
710 720 730 740 750
AIFTKYDQDG DQELTEHEHQ QMRDDLEKER EDLDLDHSSL PRPMSSRSFP
760 770 780 790 800
RSLDDSEEDD DEDSGHSSRR RGSISSGVSY EEFQVLVRRV DRMEHSIGSI
810 820 830 840 850
VSKIDAVIVK LEIMERAKLK RREVLGRLLD GVAEDERLGR DSEIHREQME
860 870 880 890 900
RLVREELERW ESDDAASQIS HGLGTPVGLN GQPRPRSSRP SSSQSTEGME
910
GAGGNGSSNV HV
The sequence of this isoform differs from the canonical sequence as follows:
633-646: IFTQFRIILGDINF → IICSWRSSMIRTLK
647-968: Missing.
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
AIMFFIIFLA YAQLAYLVFG TQVDDFSTFQ ECIICSWRSS MIRTLK
The sequence of this isoform differs from the canonical sequence as follows:
748-841: Missing.
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 LRQDLKGLVR
760 770 780 790 800
RVDRMEHSIG SIVSKIDAVI VKLEIMERAK LKRREVLGRL LDGVAEDERL
810 820 830 840 850
GRDSEIHREQ MERLVREELE RWESDDAASQ ISHGLGTPVG LNGQPRPRSS
860 870
RPSSSQSTEG MEGAGGNGSS NVHV
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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 conflicti | 45 | G → R in AAC16004 (PubMed:9286709).Curated | 1 | |
| <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 conflicti | 449 | G → V in AAC50933 (PubMed:8954772).Curated | 1 |
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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_058820 | 24 | P → L1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_011072 | 28 | R → P Common polymorphism. 5 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_058821 | 190 | A → T1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_058822 | 306 | R → Q in PKD2. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_058823 | 322 | R → Q in PKD2. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_058824 | 322 | R → W in PKD2. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_011073 | 356 | A → P in PKD2. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_064394 | 384 | A → P in PKD2. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_009195 | 414 | W → 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 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_058825 | 420 | R → 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 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_014919 | 452 | I → V. Corresponds to variant dbSNP:rs1801612EnsemblClinVar. | 1 | |
| <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_011074 | 479 | Missing in PKD2; somatic mutation. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_058826 | 482 | F → C1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_011075 | 504 – 512 | Missing in PKD2; somatic mutation. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 9 | |
| <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_058827 | 511 | D → 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. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_058828 | 632 | C → R in PKD2. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_011076 | 684 | Missing in PKD2; somatic mutation. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_058829 | 800 | M → L1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_058830 | 807 | R → Q in PKD2. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Alternative sequence
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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_042479 | 476 – 483 | CEIIFCFF → FICSSYGD in isoform 2. Curated | 8 | |
| <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_042480 | 484 – 968 | Missing in isoform 2. CuratedAdd BLAST | 485 | |
| <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_042481 | 517 – 572 | Missing in isoform 3. CuratedAdd BLAST | 56 | |
| <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_042482 | 633 – 646 | IFTQF…GDINF → IICSWRSSMIRTLK in isoform 4. CuratedAdd BLAST | 14 | |
| <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_042483 | 647 – 968 | Missing in isoform 4. CuratedAdd BLAST | 322 | |
| <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_042484 | 748 – 841 | Missing in isoform 5. CuratedAdd BLAST | 94 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks 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] |
<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>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
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q13563 | UPI000387D684 | 728 | |||
| PC-2 (Fragment) | 71 |
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q13563 | UPI000387D684 | 728 | |||
| Polycystin 2, transient receptor potential cation channel | 973 | ||||
| UPI000905940F | 970 | ||||
| UPI0007661F44 | 763 | ||||
| Polycystin 2, transient receptor potential cation channel |