UniProtKB - Q13563 (PKD2_HUMAN)
(max 400 entries)
Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the 'basket' to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>
Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)
>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 NGSSNVHVCommunity curation ()Add a publicationFeedback
Protein
Polycystin-2
Gene
PKD2
Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>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
Component of a heteromeric calcium-permeable ion channel formed by PKD1 and PKD2 that is activated by interaction between PKD1 and a Wnt family member, such as WNT3A and WNT9B (PubMed:27214281). Can also form a functional, homotetrameric ion channel (PubMed:29899465). Functions as a cation channel involved in fluid-flow mechanosensation by the primary cilium in renal epithelium (PubMed:18695040). Functions as outward-rectifying K+ channel, but is also permeable to Ca2+, and to a much lesser degree also to Na+ (PubMed:11854751, PubMed:15692563, PubMed:27071085, PubMed:27991905). May contribute to the release of Ca2+ stores from the endoplasmic reticulum (PubMed:11854751, PubMed:20881056). Together with TRPV4, forms mechano- and thermosensitive channels in cilium (PubMed:18695040). PKD1 and PKD2 may function through a common signaling pathway that is necessary to maintain the normal, differentiated state of renal tubule cells. Acts as a regulator of cilium length, together with PKD1. The dynamic control of cilium length is essential in the regulation of mechanotransductive signaling. The cilium length response creates a negative feedback loop whereby fluid shear-mediated deflection of the primary cilium, which decreases intracellular cAMP, leads to cilium shortening and thus decreases flow-induced signaling. Also involved in left-right axis specification via its role in sensing nodal flow; forms a complex with PKD1L1 in cilia to facilitate flow detection in left-right patterning. Detection of asymmetric nodal flow gives rise to a Ca2+ signal that is required for normal, asymmetric expression of genes involved in the specification of body left-right laterality (By similarity).By 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
Curated8 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, ACTIVITY 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, ACTIVITY REGULATION, PHOSPHORYLATION AT SER-801, MUTAGENESIS OF SER-801 AND SER-804, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH PKD1. - Ref.20"The polycystin complex mediates Wnt/Ca(2+) signalling."
Kim S., Nie H., Nesin V., Tran U., Outeda P., Bai C.X., Keeling J., Maskey D., Watnick T., Wessely O., Tsiokas L.
Nat. Cell Biol. 18:752-764(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH PKD1, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT PKD2 VAL-511. - Ref.27"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.29"Hydrophobic pore gates regulate ion permeation in polycystic kidney disease 2 and 2L1 channels."
Zheng W., Yang X., Hu R., Cai R., Hofmann L., Wang Z., Hu Q., Liu X., Bulkey D., Yu Y., Tang J., Flockerzi V., Cao Y., Cao E., Chen X.Z.
Nat. Commun. 9:2302-2302(2018) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.54 ANGSTROMS) OF 53-792 OF MUTANT PRO-604, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF TRP-201; PHE-604; LEU-677; TYR-684 AND LYS-688, CHARACTERIZATION OF VARIANT PKD2 VAL-511 AND TYR-684 DEL, DISULFIDE BONDS.
Miscellaneous
The mechanisms that govern channel opening are complex and still under debate; heterologous expression of PKD2 by itself or together with PKD1 gives rise to very low or undetectable spontaneous ion channel activity, in spite of its presence at the cell membrane.2 Publications
Manual assertion based on experiment ini
- Ref.23"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.26"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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi
Channel activity is regulated by phosphorylation (PubMed:16551655, PubMed:20881056, PubMed:26269590). Channel activity is regulated by intracellular Ca2+ (PubMed:11854751).4 Publications
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, ACTIVITY 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, ACTIVITY 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, ACTIVITY 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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 PublicationManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 765 | CalciumCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 767 | CalciumCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 769 | Calcium; via carbonyl oxygenCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 774 | CalciumCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 |
Regions
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sourcesManual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual 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%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p>
Inferred from direct assayi
- "Alpha-actinin associates with polycystin-2 and regulates its channel activity."
Li Q., Montalbetti N., Shen P.Y., Dai X.Q., Cheeseman C.I., Karpinski E., Wu G., Cantiello H.F., Chen X.Z.
Hum Mol Genet 14:1587-1603(2005) [PubMed] [Europe PMC] [Abstract]
- ATPase binding Source: BHF-UCL
- calcium-induced calcium release activity Source: BHF-UCLInferred from direct assayi
- 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.
- calcium ion binding Source: UniProtKBInferred from direct assayi
- Ref.25"A high-resolution structure of the EF-hand domain of human polycystin-2."
Allen M.D., Qamar S., Vadivelu M.K., Sandford R.N., Bycroft M.
Protein Sci. 23:1301-1308(2014) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY NMR OF 717-792 IN COMPLEX WITH CALCIUM, DOMAIN, MUTAGENESIS OF GLN-768 AND GLU-774.
- cation 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%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p>
Inferred from mutant phenotypei
- Ref.29"Hydrophobic pore gates regulate ion permeation in polycystic kidney disease 2 and 2L1 channels."
Zheng W., Yang X., Hu R., Cai R., Hofmann L., Wang Z., Hu Q., Liu X., Bulkey D., Yu Y., Tang J., Flockerzi V., Cao Y., Cao E., Chen X.Z.
Nat. Commun. 9:2302-2302(2018) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.54 ANGSTROMS) OF 53-792 OF MUTANT PRO-604, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF TRP-201; PHE-604; LEU-677; TYR-684 AND LYS-688, CHARACTERIZATION OF VARIANT PKD2 VAL-511 AND TYR-684 DEL, DISULFIDE BONDS.
- cytoskeletal protein binding Source: BHF-UCLInferred from direct assayi
- 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.
- 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%2Dgo%2Devidence%2Dcodes#ipi">GO evidence code guide</a></p>
Inferred from physical interactioni
- "Polycystin-1 and polycystin-2 regulate the cell cycle through the helix-loop-helix inhibitor Id2."
Li X., Luo Y., Starremans P.G., McNamara C.A., Pei Y., Zhou J.
Nat Cell Biol 7:1202-1212(2005) [PubMed] [Europe PMC] [Abstract]
- identical protein binding Source: IntActInferred from physical interactioni
- "A polycystin-2 (TRPP2) dimerization domain essential for the function of heteromeric polycystin complexes."
Giamarchi A., Feng S., Rodat-Despoix L., Xu Y., Bubenshchikova E., Newby L.J., Hao J., Gaudioso C., Crest M., Lupas A.N., Honore E., Williamson M.P., Obara T., Ong A.C., Delmas P.
EMBO J 29:1176-1191(2010) [PubMed] [Europe PMC] [Abstract] - Ref.28"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. - Ref.23"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. - "Macromolecular assembly of polycystin-2 intracytosolic C-terminal domain."
Ferreira F.M., Oliveira L.C., Germino G.G., Onuchic J.N., Onuchic L.F.
Proc Natl Acad Sci U S A 108:9833-9838(2011) [PubMed] [Europe PMC] [Abstract] - Ref.27"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.
- ion channel binding Source: BHF-UCLInferred from physical interactioni
- "Specific association of the gene product of PKD2 with the TRPC1 channel."
Tsiokas L., Arnould T., Zhu C., Kim E., Walz G., Sukhatme V.P.
Proc Natl Acad Sci U S A 96:3934-3939(1999) [PubMed] [Europe PMC] [Abstract]
- muscle alpha-actinin binding Source: GO_Central
<p>Inferred from Biological aspect of Ancestor</p>
<p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iba">GO evidence code guide</a></p>
Inferred from biological aspect of ancestori
- "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
- outward rectifier potassium channel activity Source: UniProtKB
- phosphoprotein binding Source: UniProtKBInferred from physical interactioni
- "PRKCSH/80K-H, the protein mutated in polycystic liver disease, protects polycystin-2/TRPP2 against HERP-mediated degradation."
Gao H., Wang Y., Wegierski T., Skouloudaki K., Putz M., Fu X., Engel C., Boehlke C., Peng H., Kuehn E.W., Kim E., Kramer-Zucker A., Walz G.
Hum Mol Genet 19:16-24(2010) [PubMed] [Europe PMC] [Abstract]
- potassium channel activity Source: UniProtKBInferred from direct assayi
- 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, ACTIVITY REGULATION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-829, TISSUE SPECIFICITY, MUTAGENESIS OF SER-829.
- protein homodimerization activity Source: BHF-UCLInferred from direct assayi
- "Homo- and heterodimeric interactions between the gene products of PKD1 and PKD2."
Tsiokas L., Kim E., Arnould T., Sukhatme V.P., Walz G.
Proc Natl Acad Sci U S A 94:6965-6970(1997) [PubMed] [Europe PMC] [Abstract]
- signaling receptor binding Source: BHF-UCLInferred from physical interactioni
- "Polycystin 2 interacts with type I inositol 1,4,5-trisphosphate receptor to modulate intracellular Ca2+ signaling."
Li Y., Wright J.M., Qian F., Germino G.G., Guggino W.B.
J Biol Chem 280:41298-41306(2005) [PubMed] [Europe PMC] [Abstract]
- voltage-gated calcium channel activity Source: BHF-UCLInferred from direct assayi
- "Polycystin-2, the protein mutated in autosomal dominant polycystic kidney disease (ADPKD), is a Ca2+-permeable nonselective cation channel."
Gonzalez-Perrett S., Kim K., Ibarra C., Damiano A.E., Zotta E., Batelli M., Harris P.C., Reisin I.L., Arnaout M.A., Cantiello H.F.
Proc Natl Acad Sci U S A 98:1182-1187(2001) [PubMed] [Europe PMC] [Abstract] - 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.
- voltage-gated cation channel activity Source: BHF-UCLInferred from direct assayi
- "Polycystin-2, the protein mutated in autosomal dominant polycystic kidney disease (ADPKD), is a Ca2+-permeable nonselective cation channel."
Gonzalez-Perrett S., Kim K., Ibarra C., Damiano A.E., Zotta E., Batelli M., Harris P.C., Reisin I.L., Arnaout M.A., Cantiello H.F.
Proc Natl Acad Sci U S A 98:1182-1187(2001) [PubMed] [Europe PMC] [Abstract]
- voltage-gated ion channel activity Source: BHF-UCLInferred from direct assayi
- 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.
- voltage-gated potassium channel activity Source: UniProtKBInferred from mutant phenotypei
- Ref.21"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.
- voltage-gated sodium channel activity Source: BHF-UCLInferred from direct assayi
- "Polycystin-2, the protein mutated in autosomal dominant polycystic kidney disease (ADPKD), is a Ca2+-permeable nonselective cation channel."
Gonzalez-Perrett S., Kim K., Ibarra C., Damiano A.E., Zotta E., Batelli M., Harris P.C., Reisin I.L., Arnaout M.A., Cantiello H.F.
Proc Natl Acad Sci U S A 98:1182-1187(2001) [PubMed] [Europe PMC] [Abstract]
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%2Dgo%2Devidence%2Dcodes#iep">GO evidence code guide</a></p>
Inferred from expression patterni
- "Expression of PKD1 and PKD2 transcripts and proteins in human embryo and during normal kidney development."
Chauvet V., Qian F., Boute N., Cai Y., Phakdeekitacharoen B., Onuchic L.F., Attie-Bitach T., Guicharnaud L., Devuyst O., Germino G.G., Gubler M.C.
Am J Pathol 160:973-983(2002) [PubMed] [Europe PMC] [Abstract]
- branching involved in ureteric bud morphogenesis Source: UniProtKBInferred from expression patterni
- "Expression of PKD1 and PKD2 transcripts and proteins in human embryo and during normal kidney development."
Chauvet V., Qian F., Boute N., Cai Y., Phakdeekitacharoen B., Onuchic L.F., Attie-Bitach T., Guicharnaud L., Devuyst O., Germino G.G., Gubler M.C.
Am J Pathol 160:973-983(2002) [PubMed] [Europe PMC] [Abstract]
- calcium ion transmembrane transport Source: BHF-UCLInferred from direct assayi
- 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.
- calcium ion transport Source: BHF-UCLInferred from direct assayi
- "Polycystin-2, the protein mutated in autosomal dominant polycystic kidney disease (ADPKD), is a Ca2+-permeable nonselective cation channel."
Gonzalez-Perrett S., Kim K., Ibarra C., Damiano A.E., Zotta E., Batelli M., Harris P.C., Reisin I.L., Arnaout M.A., Cantiello H.F.
Proc Natl Acad Sci U S A 98:1182-1187(2001) [PubMed] [Europe PMC] [Abstract]
- cell-cell signaling by wnt Source: UniProtKBInferred from direct assayi
- Ref.20"The polycystin complex mediates Wnt/Ca(2+) signalling."
Kim S., Nie H., Nesin V., Tran U., Outeda P., Bai C.X., Keeling J., Maskey D., Watnick T., Wessely O., Tsiokas L.
Nat. Cell Biol. 18:752-764(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH PKD1, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT PKD2 VAL-511.
- cell cycle arrest Source: BHF-UCL
- cellular response to calcium ion Source: UniProtKB
- cellular response to cAMP Source: UniProtKBInferred from mutant phenotypei
- 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, ACTIVITY REGULATION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-829, TISSUE SPECIFICITY, MUTAGENESIS OF SER-829.
- cellular response to fluid shear stress Source: BHF-UCLInferred from mutant phenotypei
- "Ciliary polycystin-2 is a mechanosensitive calcium channel involved in nitric oxide signaling cascades."
AbouAlaiwi W.A., Takahashi M., Mell B.R., Jones T.J., Ratnam S., Kolb R.J., Nauli S.M.
Circ Res 104:860-869(2009) [PubMed] [Europe PMC] [Abstract]
- cellular response to hydrostatic pressure Source: BHF-UCLInferred from direct assayi
- "Effect of hydro-osmotic pressure on polycystin-2 channel function in the human syncytiotrophoblast."
Montalbetti N., Li Q., Gonzalez-Perrett S., Semprine J., Chen X.Z., Cantiello H.F.
Pflugers Arch 451:294-303(2005) [PubMed] [Europe PMC] [Abstract]
- cellular response to osmotic stress Source: BHF-UCLInferred from direct assayi
- "Effect of hydro-osmotic pressure on polycystin-2 channel function in the human syncytiotrophoblast."
Montalbetti N., Li Q., Gonzalez-Perrett S., Semprine J., Chen X.Z., Cantiello H.F.
Pflugers Arch 451:294-303(2005) [PubMed] [Europe PMC] [Abstract]
- 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%2Dgo%2Devidence%2Dcodes#nas">GO evidence code guide</a></p>
Non-traceable author statementi
- "Reactive oxygen species inhibit polycystin-2 (TRPP2) cation channel activity in term human syncytiotrophoblast."
Montalbetti N., Cantero M.R., Dalghi M.G., Cantiello H.F.
Placenta 29:510-518(2008) [PubMed] [Europe PMC] [Abstract]
- centrosome duplication Source: BHF-UCLNon-traceable author statementi
- "Centrosome overduplication and mitotic instability in PKD2 transgenic lines."
Burtey S., Riera M., Ribe E., Pennenkamp P., Rance R., Luciani J., Dworniczak B., Mattei M.G., Fontes M.
Cell Biol Int 32:1193-1198(2008) [PubMed] [Europe PMC] [Abstract]
- cilium organization Source: MGIInferred from mutant phenotypei
- "Tubby family proteins are adapters for ciliary trafficking of integral membrane proteins."
Badgandi H.B., Hwang S.H., Shimada I.S., Loriot E., Mukhopadhyay S.
J. Cell Biol. 216:743-760(2017) [PubMed] [Europe PMC] [Abstract]
- cytoplasmic sequestering of transcription factor Source: BHF-UCLInferred from mutant phenotypei
- "Polycystin-1 and polycystin-2 regulate the cell cycle through the helix-loop-helix inhibitor Id2."
Li X., Luo Y., Starremans P.G., McNamara C.A., Pei Y., Zhou J.
Nat Cell Biol 7:1202-1212(2005) [PubMed] [Europe PMC] [Abstract]
- 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-UCLInferred from mutant phenotypei
- "Association of PKD2 (polycystin 2) mutations with left-right laterality defects."
Bataille S., Demoulin N., Devuyst O., Audrezet M.P., Dahan K., Godin M., Fontes M., Pirson Y., Burtey S.
Am J Kidney Dis 58:456-460(2011) [PubMed] [Europe PMC] [Abstract]
- embryonic placenta development Source: BHF-UCL
- heart development Source: UniProtKBInferred from expression patterni
- "Expression of PKD1 and PKD2 transcripts and proteins in human embryo and during normal kidney development."
Chauvet V., Qian F., Boute N., Cai Y., Phakdeekitacharoen B., Onuchic L.F., Attie-Bitach T., Guicharnaud L., Devuyst O., Germino G.G., Gubler M.C.
Am J Pathol 160:973-983(2002) [PubMed] [Europe PMC] [Abstract]
- heart looping Source: BHF-UCLInferred from mutant phenotypei
- "Association of PKD2 (polycystin 2) mutations with left-right laterality defects."
Bataille S., Demoulin N., Devuyst O., Audrezet M.P., Dahan K., Godin M., Fontes M., Pirson Y., Burtey S.
Am J Kidney Dis 58:456-460(2011) [PubMed] [Europe PMC] [Abstract]
- inorganic cation transmembrane transport Source: UniProtKBInferred from mutant phenotypei
- Ref.29"Hydrophobic pore gates regulate ion permeation in polycystic kidney disease 2 and 2L1 channels."
Zheng W., Yang X., Hu R., Cai R., Hofmann L., Wang Z., Hu Q., Liu X., Bulkey D., Yu Y., Tang J., Flockerzi V., Cao Y., Cao E., Chen X.Z.
Nat. Commun. 9:2302-2302(2018) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.54 ANGSTROMS) OF 53-792 OF MUTANT PRO-604, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF TRP-201; PHE-604; LEU-677; TYR-684 AND LYS-688, CHARACTERIZATION OF VARIANT PKD2 VAL-511 AND TYR-684 DEL, DISULFIDE BONDS.
- liver development Source: UniProtKBInferred from expression patterni
- "Expression of PKD1 and PKD2 transcripts and proteins in human embryo and during normal kidney development."
Chauvet V., Qian F., Boute N., Cai Y., Phakdeekitacharoen B., Onuchic L.F., Attie-Bitach T., Guicharnaud L., Devuyst O., Germino G.G., Gubler M.C.
Am J Pathol 160:973-983(2002) [PubMed] [Europe PMC] [Abstract]
- mesonephric duct development Source: UniProtKBInferred from expression patterni
- "Expression of PKD1 and PKD2 transcripts and proteins in human embryo and during normal kidney development."
Chauvet V., Qian F., Boute N., Cai Y., Phakdeekitacharoen B., Onuchic L.F., Attie-Bitach T., Guicharnaud L., Devuyst O., Germino G.G., Gubler M.C.
Am J Pathol 160:973-983(2002) [PubMed] [Europe PMC] [Abstract]
- mesonephric tubule development Source: UniProtKBInferred from expression patterni
- "Expression of PKD1 and PKD2 transcripts and proteins in human embryo and during normal kidney development."
Chauvet V., Qian F., Boute N., Cai Y., Phakdeekitacharoen B., Onuchic L.F., Attie-Bitach T., Guicharnaud L., Devuyst O., Germino G.G., Gubler M.C.
Am J Pathol 160:973-983(2002) [PubMed] [Europe PMC] [Abstract]
- metanephric ascending thin limb development Source: UniProtKBInferred from expression patterni
- "Expression of PKD1 and PKD2 transcripts and proteins in human embryo and during normal kidney development."
Chauvet V., Qian F., Boute N., Cai Y., Phakdeekitacharoen B., Onuchic L.F., Attie-Bitach T., Guicharnaud L., Devuyst O., Germino G.G., Gubler M.C.
Am J Pathol 160:973-983(2002) [PubMed] [Europe PMC] [Abstract]
- metanephric cortex development Source: UniProtKBInferred from expression patterni
- "Expression of PKD1 and PKD2 transcripts and proteins in human embryo and during normal kidney development."
Chauvet V., Qian F., Boute N., Cai Y., Phakdeekitacharoen B., Onuchic L.F., Attie-Bitach T., Guicharnaud L., Devuyst O., Germino G.G., Gubler M.C.
Am J Pathol 160:973-983(2002) [PubMed] [Europe PMC] [Abstract]
- metanephric cortical collecting duct development Source: UniProtKBInferred from expression patterni
- "Expression of PKD1 and PKD2 transcripts and proteins in human embryo and during normal kidney development."
Chauvet V., Qian F., Boute N., Cai Y., Phakdeekitacharoen B., Onuchic L.F., Attie-Bitach T., Guicharnaud L., Devuyst O., Germino G.G., Gubler M.C.
Am J Pathol 160:973-983(2002) [PubMed] [Europe PMC] [Abstract]
- metanephric distal tubule development Source: UniProtKBInferred from expression patterni
- "Expression of PKD1 and PKD2 transcripts and proteins in human embryo and during normal kidney development."
Chauvet V., Qian F., Boute N., Cai Y., Phakdeekitacharoen B., Onuchic L.F., Attie-Bitach T., Guicharnaud L., Devuyst O., Germino G.G., Gubler M.C.
Am J Pathol 160:973-983(2002) [PubMed] [Europe PMC] [Abstract]
- metanephric mesenchyme development Source: UniProtKBInferred from expression patterni
- "Expression of PKD1 and PKD2 transcripts and proteins in human embryo and during normal kidney development."
Chauvet V., Qian F., Boute N., Cai Y., Phakdeekitacharoen B., Onuchic L.F., Attie-Bitach T., Guicharnaud L., Devuyst O., Germino G.G., Gubler M.C.
Am J Pathol 160:973-983(2002) [PubMed] [Europe PMC] [Abstract]
- metanephric part of ureteric bud development Source: UniProtKBInferred from expression patterni
- "Expression of PKD1 and PKD2 transcripts and proteins in human embryo and during normal kidney development."
Chauvet V., Qian F., Boute N., Cai Y., Phakdeekitacharoen B., Onuchic L.F., Attie-Bitach T., Guicharnaud L., Devuyst O., Germino G.G., Gubler M.C.
Am J Pathol 160:973-983(2002) [PubMed] [Europe PMC] [Abstract]
- metanephric smooth muscle tissue development Source: UniProtKBInferred from expression patterni
- "Expression of PKD1 and PKD2 transcripts and proteins in human embryo and during normal kidney development."
Chauvet V., Qian F., Boute N., Cai Y., Phakdeekitacharoen B., Onuchic L.F., Attie-Bitach T., Guicharnaud L., Devuyst O., Germino G.G., Gubler M.C.
Am J Pathol 160:973-983(2002) [PubMed] [Europe PMC] [Abstract]
- metanephric S-shaped body morphogenesis Source: UniProtKBInferred from expression patterni
- "Expression of PKD1 and PKD2 transcripts and proteins in human embryo and during normal kidney development."
Chauvet V., Qian F., Boute N., Cai Y., Phakdeekitacharoen B., Onuchic L.F., Attie-Bitach T., Guicharnaud L., Devuyst O., Germino G.G., Gubler M.C.
Am J Pathol 160:973-983(2002) [PubMed] [Europe PMC] [Abstract]
- negative regulation of cell population proliferation Source: BHF-UCLNon-traceable author statementi
- "Polycystin-2 down-regulates cell proliferation via promoting PERK-dependent phosphorylation of eIF2alpha."
Liang G., Yang J., Wang Z., Li Q., Tang Y., Chen X.Z.
Hum Mol Genet 17:3254-3262(2008) [PubMed] [Europe PMC] [Abstract]
- negative regulation of G1/S transition of mitotic cell cycle Source: BHF-UCLInferred from mutant phenotypei
- "Polycystin-1 and polycystin-2 regulate the cell cycle through the helix-loop-helix inhibitor Id2."
Li X., Luo Y., Starremans P.G., McNamara C.A., Pei Y., Zhou J.
Nat Cell Biol 7:1202-1212(2005) [PubMed] [Europe PMC] [Abstract]
- negative regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
- neural tube development Source: UniProtKBInferred from expression patterni
- "Expression of PKD1 and PKD2 transcripts and proteins in human embryo and during normal kidney development."
Chauvet V., Qian F., Boute N., Cai Y., Phakdeekitacharoen B., Onuchic L.F., Attie-Bitach T., Guicharnaud L., Devuyst O., Germino G.G., Gubler M.C.
Am J Pathol 160:973-983(2002) [PubMed] [Europe PMC] [Abstract]
- placenta blood vessel development Source: BHF-UCL
- positive regulation of cell cycle arrest Source: BHF-UCLInferred from mutant phenotypei
- "Polycystin-1 and polycystin-2 regulate the cell cycle through the helix-loop-helix inhibitor Id2."
Li X., Luo Y., Starremans P.G., McNamara C.A., Pei Y., Zhou J.
Nat Cell Biol 7:1202-1212(2005) [PubMed] [Europe PMC] [Abstract]
- positive regulation of cyclin-dependent protein serine/threonine kinase activity Source: BHF-UCLInferred from mutant phenotypei
- "Polycystin-1 and polycystin-2 regulate the cell cycle through the helix-loop-helix inhibitor Id2."
Li X., Luo Y., Starremans P.G., McNamara C.A., Pei Y., Zhou J.
Nat Cell Biol 7:1202-1212(2005) [PubMed] [Europe PMC] [Abstract]
- positive regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity Source: BHF-UCLInferred from mutant phenotypei
- "Polycystin 2 interacts with type I inositol 1,4,5-trisphosphate receptor to modulate intracellular Ca2+ signaling."
Li Y., Wright J.M., Qian F., Germino G.G., Guggino W.B.
J Biol Chem 280:41298-41306(2005) [PubMed] [Europe PMC] [Abstract]
- positive regulation of nitric oxide biosynthetic process Source: BHF-UCLInferred from mutant phenotypei
- "Ciliary polycystin-2 is a mechanosensitive calcium channel involved in nitric oxide signaling cascades."
AbouAlaiwi W.A., Takahashi M., Mell B.R., Jones T.J., Ratnam S., Kolb R.J., Nauli S.M.
Circ Res 104:860-869(2009) [PubMed] [Europe PMC] [Abstract]
- positive regulation of transcription by RNA polymerase II Source: BHF-UCLInferred from direct assayi
- "Polycystin-1 and polycystin-2 regulate the cell cycle through the helix-loop-helix inhibitor Id2."
Li X., Luo Y., Starremans P.G., McNamara C.A., Pei Y., Zhou J.
Nat Cell Biol 7:1202-1212(2005) [PubMed] [Europe PMC] [Abstract]
- potassium ion transmembrane transport Source: UniProtKBInferred from direct assayi
- 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, ACTIVITY REGULATION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-829, TISSUE SPECIFICITY, MUTAGENESIS OF SER-829.
- protein heterotetramerization Source: UniProtKBInferred from direct assayi
- Ref.30
- protein homotetramerization Source: UniProtKBInferred from direct assayi
- Ref.28"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.
- protein tetramerization Source: UniProtKBInferred from direct assayi
- Ref.29"Hydrophobic pore gates regulate ion permeation in polycystic kidney disease 2 and 2L1 channels."
Zheng W., Yang X., Hu R., Cai R., Hofmann L., Wang Z., Hu Q., Liu X., Bulkey D., Yu Y., Tang J., Flockerzi V., Cao Y., Cao E., Chen X.Z.
Nat. Commun. 9:2302-2302(2018) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.54 ANGSTROMS) OF 53-792 OF MUTANT PRO-604, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF TRP-201; PHE-604; LEU-677; TYR-684 AND LYS-688, CHARACTERIZATION OF VARIANT PKD2 VAL-511 AND TYR-684 DEL, DISULFIDE BONDS.
- receptor signaling pathway via JAK-STAT Source: BHF-UCL
- regulation of calcium ion import Source: BHF-UCLInferred from direct assayi
- 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.
- regulation of cell population proliferation Source: BHF-UCLInferred from mutant phenotypei
- "Deficiency of polycystin-2 reduces Ca2+ channel activity and cell proliferation in ADPKD lymphoblastoid cells."
Aguiari G., Banzi M., Gessi S., Cai Y., Zeggio E., Manzati E., Piva R., Lambertini E., Ferrari L., Peters D.J., Lanza F., Harris P.C., Borea P.A., Somlo S., Del Senno L.
FASEB J 18:884-886(2004) [PubMed] [Europe PMC] [Abstract]
- release of sequestered calcium ion into cytosol Source: BHF-UCLInferred from direct assayi
- 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.
- renal artery morphogenesis Source: UniProtKBInferred from expression patterni
- "Expression of PKD1 and PKD2 transcripts and proteins in human embryo and during normal kidney development."
Chauvet V., Qian F., Boute N., Cai Y., Phakdeekitacharoen B., Onuchic L.F., Attie-Bitach T., Guicharnaud L., Devuyst O., Germino G.G., Gubler M.C.
Am J Pathol 160:973-983(2002) [PubMed] [Europe PMC] [Abstract]
- renal tubule morphogenesis Source: BHF-UCL
- sodium ion transmembrane transport Source: BHF-UCLInferred from direct assayi
- "Polycystin-2, the protein mutated in autosomal dominant polycystic kidney disease (ADPKD), is a Ca2+-permeable nonselective cation channel."
Gonzalez-Perrett S., Kim K., Ibarra C., Damiano A.E., Zotta E., Batelli M., Harris P.C., Reisin I.L., Arnaout M.A., Cantiello H.F.
Proc Natl Acad Sci U S A 98:1182-1187(2001) [PubMed] [Europe PMC] [Abstract]
- spinal cord development Source: UniProtKBInferred from expression patterni
- "Expression of PKD1 and PKD2 transcripts and proteins in human embryo and during normal kidney development."
Chauvet V., Qian F., Boute N., Cai Y., Phakdeekitacharoen B., Onuchic L.F., Attie-Bitach T., Guicharnaud L., Devuyst O., Germino G.G., Gubler M.C.
Am J Pathol 160:973-983(2002) [PubMed] [Europe PMC] [Abstract]
- Wnt signaling pathway Source: UniProtKB-KW
<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, Wnt signaling pathway |
| Ligand | Calcium, Metal-binding, Potassium |
Enzyme and pathway databases
Pathway Commons web resource for biological pathway data More...PathwayCommonsi | Q13563 |
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%5Fand%5Ftaxonomy%5Fsection">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-2CuratedShort 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 Manual assertion based on opinion ini
R48321 Transient receptor potential cation channel subfamily P member 21 Publication 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%5Fand%5Ftaxonomy%5Fsection">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 Manual assertion inferred from database entriesi Synonyms:TRPP21 Publication Manual assertion based on opinion ini
Manual assertion inferred from database entriesi |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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
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 |
Eukaryotic Pathogen, Vector and Host Database Resources More...VEuPathDBi | HostDB:ENSG00000118762.7 |
<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
Golgi apparatus
- Golgi apparatus By similarity
Manual assertion inferred from sequence similarity toi
- Golgi apparatus By similarity
Plasma membrane
- cilium membrane 3 Publications
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, ACTIVITY 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.
Manual assertion based on experiment ini
- Ref.26"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.27"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.28"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. - Ref.29"Hydrophobic pore gates regulate ion permeation in polycystic kidney disease 2 and 2L1 channels."
Zheng W., Yang X., Hu R., Cai R., Hofmann L., Wang Z., Hu Q., Liu X., Bulkey D., Yu Y., Tang J., Flockerzi V., Cao Y., Cao E., Chen X.Z.
Nat. Commun. 9:2302-2302(2018) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.54 ANGSTROMS) OF 53-792 OF MUTANT PRO-604, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF TRP-201; PHE-604; LEU-677; TYR-684 AND LYS-688, CHARACTERIZATION OF VARIANT PKD2 VAL-511 AND TYR-684 DEL, DISULFIDE BONDS. - Ref.30
- Cell membrane 9 Publications
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, ACTIVITY 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"The polycystin complex mediates Wnt/Ca(2+) signalling."
Kim S., Nie H., Nesin V., Tran U., Outeda P., Bai C.X., Keeling J., Maskey D., Watnick T., Wessely O., Tsiokas L.
Nat. Cell Biol. 18:752-764(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH PKD1, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT PKD2 VAL-511. - Ref.21"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.23"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.28"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. - Ref.29"Hydrophobic pore gates regulate ion permeation in polycystic kidney disease 2 and 2L1 channels."
Zheng W., Yang X., Hu R., Cai R., Hofmann L., Wang Z., Hu Q., Liu X., Bulkey D., Yu Y., Tang J., Flockerzi V., Cao Y., Cao E., Chen X.Z.
Nat. Commun. 9:2302-2302(2018) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.54 ANGSTROMS) OF 53-792 OF MUTANT PRO-604, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF TRP-201; PHE-604; LEU-677; TYR-684 AND LYS-688, CHARACTERIZATION OF VARIANT PKD2 VAL-511 AND TYR-684 DEL, DISULFIDE BONDS. - Ref.30
Manual assertion based on experiment ini
- Ref.26"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.27"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.28"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. - Ref.29"Hydrophobic pore gates regulate ion permeation in polycystic kidney disease 2 and 2L1 channels."
Zheng W., Yang X., Hu R., Cai R., Hofmann L., Wang Z., Hu Q., Liu X., Bulkey D., Yu Y., Tang J., Flockerzi V., Cao Y., Cao E., Chen X.Z.
Nat. Commun. 9:2302-2302(2018) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.54 ANGSTROMS) OF 53-792 OF MUTANT PRO-604, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF TRP-201; PHE-604; LEU-677; TYR-684 AND LYS-688, CHARACTERIZATION OF VARIANT PKD2 VAL-511 AND TYR-684 DEL, DISULFIDE BONDS. - Ref.30
- Basolateral cell membrane 1 Publication
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.
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, ACTIVITY REGULATION, PHOSPHORYLATION AT SER-801, MUTAGENESIS OF SER-801 AND SER-804, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH PKD1. - Ref.28"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.
Manual assertion based on experiment ini
- Ref.26"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.27"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.28"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. - Ref.29"Hydrophobic pore gates regulate ion permeation in polycystic kidney disease 2 and 2L1 channels."
Zheng W., Yang X., Hu R., Cai R., Hofmann L., Wang Z., Hu Q., Liu X., Bulkey D., Yu Y., Tang J., Flockerzi V., Cao Y., Cao E., Chen X.Z.
Nat. Commun. 9:2302-2302(2018) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.54 ANGSTROMS) OF 53-792 OF MUTANT PRO-604, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF TRP-201; PHE-604; LEU-677; TYR-684 AND LYS-688, CHARACTERIZATION OF VARIANT PKD2 VAL-511 AND TYR-684 DEL, DISULFIDE BONDS. - Ref.30
- Endoplasmic reticulum membrane 1 Publication
Other locations
- Cytoplasmic vesicle membrane 1 Publication
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: PKD2 localization to the plasma and ciliary membranes requires PKD1. PKD1:PKD2 interaction is required to reach the Golgi apparatus form endoplasmic reticulum and then traffic to the cilia (By similarity). 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).By similarity- 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.
Manual assertion inferred from sequence similarity toi
2 PublicationsManual assertion based on experiment ini
Cytoskeleton
- ciliary basal body Source: MGIInferred from direct assayi
- "Pericentrin forms a complex with intraflagellar transport proteins and polycystin-2 and is required for primary cilia assembly."
Jurczyk A., Gromley A., Redick S., San Agustin J., Witman G., Pazour G.J., Peters D.J.M., Doxsey S.
J. Cell Biol. 166:637-643(2004) [PubMed] [Europe PMC] [Abstract]
- mitotic spindle Source: BHF-UCLInferred from direct assayi
- "PKD2 interacts and co-localizes with mDia1 to mitotic spindles of dividing cells: role of mDia1 IN PKD2 localization to mitotic spindles."
Rundle D.R., Gorbsky G., Tsiokas L.
J Biol Chem 279:29728-29739(2004) [PubMed] [Europe PMC] [Abstract]
- ciliary basal body Source: MGIInferred from direct assayi
Endoplasmic reticulum
- endoplasmic reticulum Source: UniProtKBInferred from direct assayi
- "PRKCSH/80K-H, the protein mutated in polycystic liver disease, protects polycystin-2/TRPP2 against HERP-mediated degradation."
Gao H., Wang Y., Wegierski T., Skouloudaki K., Putz M., Fu X., Engel C., Boehlke C., Peng H., Kuehn E.W., Kim E., Kramer-Zucker A., Walz G.
Hum Mol Genet 19:16-24(2010) [PubMed] [Europe PMC] [Abstract]
- endoplasmic reticulum membrane Source: BHF-UCLInferred from direct assayi
- 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. - "Deficiency of polycystin-2 reduces Ca2+ channel activity and cell proliferation in ADPKD lymphoblastoid cells."
Aguiari G., Banzi M., Gessi S., Cai Y., Zeggio E., Manzati E., Piva R., Lambertini E., Ferrari L., Peters D.J., Lanza F., Harris P.C., Borea P.A., Somlo S., Del Senno L.
FASEB J 18:884-886(2004) [PubMed] [Europe PMC] [Abstract]
- integral component of cytoplasmic side of endoplasmic reticulum membrane Source: BHF-UCLInferred from direct assayi
- "The human polycystin-2 protein represents an integral membrane protein with six membrane-spanning domains and intracellular N- and C-termini."
Hoffmeister H., Gallagher A.R., Rascle A., Witzgall R.
Biochem J 433:285-294(2011) [PubMed] [Europe PMC] [Abstract]
- integral component of lumenal side of endoplasmic reticulum membrane Source: BHF-UCLInferred from direct assayi
- "The human polycystin-2 protein represents an integral membrane protein with six membrane-spanning domains and intracellular N- and C-termini."
Hoffmeister H., Gallagher A.R., Rascle A., Witzgall R.
Biochem J 433:285-294(2011) [PubMed] [Europe PMC] [Abstract]
- endoplasmic reticulum Source: UniProtKBInferred from direct assayi
Extracellular region or secreted
- extracellular exosome Source: UniProtKBInferred from high throughput direct assayi
- "Large-scale proteomics and phosphoproteomics of urinary exosomes."
Gonzales P.A., Pisitkun T., Hoffert J.D., Tchapyjnikov D., Star R.A., Kleta R., Wang N.S., Knepper M.A.
J Am Soc Nephrol 20:363-379(2009) [PubMed] [Europe PMC] [Abstract]
- extracellular exosome Source: UniProtKBInferred from high throughput direct assayi
Golgi apparatus
- Golgi apparatus Source: UniProtKB
Plasma Membrane
- basal plasma membrane Source: BHF-UCLInferred from direct assayi
- 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.
- ciliary membrane Source: UniProtKB-SubCell
- integral component of plasma membrane Source: UniProtKBInferred from direct assayi
- 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, ACTIVITY REGULATION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-829, TISSUE SPECIFICITY, MUTAGENESIS OF SER-829. - Ref.28"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. - Ref.29"Hydrophobic pore gates regulate ion permeation in polycystic kidney disease 2 and 2L1 channels."
Zheng W., Yang X., Hu R., Cai R., Hofmann L., Wang Z., Hu Q., Liu X., Bulkey D., Yu Y., Tang J., Flockerzi V., Cao Y., Cao E., Chen X.Z.
Nat. Commun. 9:2302-2302(2018) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.54 ANGSTROMS) OF 53-792 OF MUTANT PRO-604, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF TRP-201; PHE-604; LEU-677; TYR-684 AND LYS-688, CHARACTERIZATION OF VARIANT PKD2 VAL-511 AND TYR-684 DEL, DISULFIDE BONDS. - Ref.30
- plasma membrane Source: BHF-UCLInferred from direct assayi
- 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. - "Effect of hydro-osmotic pressure on polycystin-2 channel function in the human syncytiotrophoblast."
Montalbetti N., Li Q., Gonzalez-Perrett S., Semprine J., Chen X.Z., Cantiello H.F.
Pflugers Arch 451:294-303(2005) [PubMed] [Europe PMC] [Abstract]
- basal plasma membrane Source: BHF-UCLInferred from direct assayi
Other locations
- basal cortex Source: BHF-UCLInferred from direct assayi
- 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.
- cation channel complex Source: UniProtKBInferred from direct assayi
- Ref.30
- cell-cell junction Source: Ensembl
- cilium Source: MGIInferred from direct assayi
- "Tubby family proteins are adapters for ciliary trafficking of integral membrane proteins."
Badgandi H.B., Hwang S.H., Shimada I.S., Loriot E., Mukhopadhyay S.
J. Cell Biol. 216:743-760(2017) [PubMed] [Europe PMC] [Abstract]
- cytoplasm Source: BHF-UCLInferred from direct assayi
- 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.
- cytoplasmic vesicle membrane Source: UniProtKB-SubCell
- lamellipodium Source: BHF-UCLInferred from direct assayi
- 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.
- membrane Source: GO_CentralInferred from biological aspect of ancestori
- "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
- motile cilium Source: BHF-UCL
- non-motile cilium Source: BHF-UCL
- polycystin complex Source: BHF-UCL
- basal cortex Source: BHF-UCLInferred from direct assayi
Topology
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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 Manual assertion based on experiment ini
| 219 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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 Manual assertion based on experiment ini
| 22 | |
| Topological domaini | 242 – 468 | Extracellular3 Publications Manual assertion based on experiment ini
| 227 | |
| Transmembranei | 469 – 489 | Helical; Name=S23 Publications Manual assertion based on experiment ini
| 21 | |
| Topological domaini | 490 – 505 | Cytoplasmic3 Publications Manual assertion based on experiment ini
| 16 | |
| Transmembranei | 506 – 526 | Helical; Name=S33 Publications Manual assertion based on experiment ini
| 21 | |
| Topological domaini | 527 – 552 | Extracellular3 Publications Manual assertion based on experiment ini
| 26 | |
| Transmembranei | 553 – 573 | Helical; Name=S43 Publications Manual assertion based on experiment ini
| 21 | |
| Topological domaini | 574 – 597 | Cytoplasmic3 Publications Manual assertion based on experiment ini
| 24 | |
| Transmembranei | 598 – 619 | Helical; Name=53 Publications Manual assertion based on experiment ini
| 22 | |
| Topological domaini | 620 – 631 | Extracellular3 Publications Manual assertion based on experiment ini
| 12 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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 Manual assertion based on experiment ini
| 15 | |
| Topological domaini | 647 – 654 | Extracellular3 Publications Manual assertion based on experiment ini
| 8 | |
| Transmembranei | 655 – 675 | Helical; Name=S63 Publications Manual assertion based on experiment ini
| 21 | |
| Topological domaini | 676 – 968 | Cytoplasmic3 Publications Manual assertion based on experiment ini
| 293 |
Keywords - Cellular componenti
Cell membrane, Cell projection, Cilium, Cytoplasmic vesicle, Endoplasmic reticulum, Golgi apparatus, Membrane<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei
Polycystic kidney disease 2 with or without polycystic liver disease (PKD2)13 PublicationsManual 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"The polycystin complex mediates Wnt/Ca(2+) signalling."
Kim S., Nie H., Nesin V., Tran U., Outeda P., Bai C.X., Keeling J., Maskey D., Watnick T., Wessely O., Tsiokas L.
Nat. Cell Biol. 18:752-764(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH PKD1, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT PKD2 VAL-511. - Ref.21"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.29"Hydrophobic pore gates regulate ion permeation in polycystic kidney disease 2 and 2L1 channels."
Zheng W., Yang X., Hu R., Cai R., Hofmann L., Wang Z., Hu Q., Liu X., Bulkey D., Yu Y., Tang J., Flockerzi V., Cao Y., Cao E., Chen X.Z.
Nat. Commun. 9:2302-2302(2018) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.54 ANGSTROMS) OF 53-792 OF MUTANT PRO-604, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF TRP-201; PHE-604; LEU-677; TYR-684 AND LYS-688, CHARACTERIZATION OF VARIANT PKD2 VAL-511 AND TYR-684 DEL, DISULFIDE BONDS. - Ref.31"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.32"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.33"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.34"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.35"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.36"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.37"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.38"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.40"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.
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]
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
"The polycystin complex mediates Wnt/Ca(2+) signalling."
Kim S., Nie H., Nesin V., Tran U., Outeda P., Bai C.X., Keeling J., Maskey D., Watnick T., Wessely O., Tsiokas L.
Nat. Cell Biol. 18:752-764(2016) [PubMed] [Europe PMC] [Abstract]
Kim S., Nie H., Nesin V., Tran U., Outeda P., Bai C.X., Keeling J., Maskey D., Watnick T., Wessely O., Tsiokas L.
Nat. Cell Biol. 18:752-764(2016) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PKD1, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT PKD2 VAL-511.
Ref.21
"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]
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.29
"Hydrophobic pore gates regulate ion permeation in polycystic kidney disease 2 and 2L1 channels."
Zheng W., Yang X., Hu R., Cai R., Hofmann L., Wang Z., Hu Q., Liu X., Bulkey D., Yu Y., Tang J., Flockerzi V., Cao Y., Cao E., Chen X.Z.
Nat. Commun. 9:2302-2302(2018) [PubMed] [Europe PMC] [Abstract]
Zheng W., Yang X., Hu R., Cai R., Hofmann L., Wang Z., Hu Q., Liu X., Bulkey D., Yu Y., Tang J., Flockerzi V., Cao Y., Cao E., Chen X.Z.
Nat. Commun. 9:2302-2302(2018) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.54 ANGSTROMS) OF 53-792 OF MUTANT PRO-604, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF TRP-201; PHE-604; LEU-677; TYR-684 AND LYS-688, CHARACTERIZATION OF VARIANT PKD2 VAL-511 AND TYR-684 DEL, DISULFIDE BONDS.
Ref.31
"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]
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.32
"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]
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.33
"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]
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.34
"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]
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.35
"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]
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.36
"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]
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.37
"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]
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.38
"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]
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.40
"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]
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.
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant disorder characterized by progressive formation and enlargement of cysts in both kidneys, typically leading to end-stage renal disease in adult life. Cysts also occurs in the liver and other organs. It represents approximately 15% of the cases of autosomal dominant polycystic kidney disease. PKD2 is clinically milder than PKD1 but it has a deleterious impact on overall life expectancy.
Related information in OMIM| 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 Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_058823 | 322 | R → Q in PKD2. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_058824 | 322 | R → W in PKD2. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_011073 | 356 | A → P in PKD2. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_064394 | 384 | A → P in PKD2. 1 Publication Manual assertion based on experiment ini
| 1 | |
| 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 Manual assertion based on experiment ini
| 1 | |
| 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 Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_011074 | 479 | Missing in PKD2; somatic mutation. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_011075 | 504 – 512 | Missing in PKD2; somatic mutation. 1 Publication Manual assertion based on experiment ini
| 9 | |
| 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. 5 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_058828 | 632 | C → R in PKD2. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_011076 | 684 | Missing in PKD2; somatic mutation; abolishes channel currents induced by the gain-of-function artificial mutant P-604. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_058830 | 807 | R → Q in PKD2. 1 Publication 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%5Fand%5Fbiotech%5Fsection">'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 Manual assertion based on experiment ini
| 1 | |
| 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 Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 201 | W → A: Abolishes increased channel activity due to a gain of function mutation; when associated with P-604. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 604 | F → A or I: No effect on channel activation. 1 Publication Manual assertion based on experiment ini
| 1 | |
| 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 A-201; when associated with V-511; when associated with G-414; when associated with G-420; when associated with Y-684 DEL; when associated with A-684. Increased channel activity; when associated with 736-L-N-737 DEL. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 605 | Missing : Abolishes increased channel activity due to a gain of function mutation; when associated with P-604. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 677 | L → N: Gain of function mutation. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 684 | Y → A: Abolishes increased channel activity due to a gain of function mutation; when associated with P-604. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 688 | K → A: Abolishes increased channel activity due to a gain of function mutation; when associated with P-604. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 721 | T → A: Decreases phosphorylation; when associated with A-801; A-812; A-831 and A-943. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 736 – 737 | Missing : Increased channel activity; when associated with P-604. 1 Publication Manual assertion based on experiment ini
| 2 | |
| Mutagenesisi | 768 | Q → G: Strongly increases calcium binding affinity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 771 | T → A: Loss of calcium-binding site; when associated with A-774. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 774 | E → A: Loss of calcium-binding site; when associated with A-771. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 774 | E → Q: Abolishes calcium binding via the EF-hand. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 801 | S → A: Decreases phosphorylation; when associated with A-721; A-812; A-831 and A-943. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 801 | S → D: Phosphomimetic mutant. No effect on release of Ca(2+) stores from the endoplasmic reticulum. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 801 | S → G: Loss of phosphorylation at this site. Impairs release of Ca(2+) stores from the endoplasmic reticulum. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 804 | S → N: Loss of phosphorylation at Ser-801. 1 Publication Manual assertion based on experiment ini
| 1 | |
| 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 Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 812 | S → D: No effect on interaction with PACS1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 815 – 817 | DDD → AAA: Strongly decreases interaction with PACS1 and enhances expression at the cell membrane. 1 Publication Manual assertion based on experiment ini
| 3 | |
| Mutagenesisi | 829 | S → A: Abolishes increased channel opening in response to cAMP and phosphorylation by PKA. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 831 | S → A: Decreases phosphorylation; when associated with A-721; A-801; A-812 and A-943. 1 Publication Manual assertion based on experiment ini
| 1 | |
| 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 Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 842 | L → P: Loss of protein solubility. 1 Publication Manual assertion based on experiment ini
| 1 | |
| 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 Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 846 | V → E: Loss of protein solubility. 1 Publication Manual assertion based on experiment ini
| 1 | |
| 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 Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 849 | M → K: Loss of protein solubility. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 853 | I → P: Loss of protein solubility. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 856 | I → K: Loss of protein solubility. 1 Publication Manual assertion based on experiment ini
| 1 | |
| 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 Manual assertion based on experiment ini
| 1 | |
| 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 Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 863 | V → E: Loss of protein solubility; when associated with K-849. 1 Publication Manual assertion based on experiment ini
| 1 | |
| 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 Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 943 | S → A: Decreases phosphorylation; when associated with A-721; A-801; A-812 and A-831. 1 Publication Manual assertion based on experiment ini
| 1 |
Keywords - Diseasei
Ciliopathy, Disease variantOrganism-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 |
| 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 |
Miscellaneous databases
Pharos NIH Druggable Genome Knowledgebase More...Pharosi | Q13563, Tchem |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL5465 |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 504 |
Genetic variation 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 or proteolytic cleavage.<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 Manual assertion based on experiment ini
| 1 | |
| Modified residuei | 80 | Phosphoserine1 Publication Manual assertion inferred by curator fromi
| 1 | |
| Modified residuei | 137 | Omega-N-methylarginineBy similarity Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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 Manual assertion based on experiment ini
| 1 | |
| Glycosylationi | 305 | N-linked (GlcNAc...) asparagine1 Publication Manual assertion based on experiment ini
| 1 | |
| Glycosylationi | 328 | N-linked (GlcNAc...) (complex) asparagine4 Publications 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 Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion based on experiment ini
| ||
| Glycosylationi | 362 | N-linked (GlcNAc...) asparagine3 Publications Manual assertion based on experiment ini
| 1 | |
| Glycosylationi | 375 | N-linked (GlcNAc...) asparagine3 Publications Manual assertion based on experiment ini
| 1 | |
| Modified residuei | 801 | Phosphoserine1 Publication Manual assertion inferred by curator fromi
Manual assertion based on experiment ini
| 1 | |
| Modified residuei | 808 | PhosphoserineBy similarity Manual assertion inferred from sequence similarity toi | 1 | |
| Modified residuei | 812 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
Manual assertion inferred by curator fromi
| 1 | |
| Modified residuei | 829 | Phosphoserine1 Publication Manual assertion inferred by curator fromi
| 1 |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
Phosphorylated. Phosphorylation is important for protein function; a mutant that lacks the N-terminal phosphorylation sites cannot complement a zebrafish pkd2-deficient mutant (PubMed:16551655). PKD-mediated phosphorylation at the C-terminus regulates its function in the release of Ca2+ stores from the endoplasmic reticulum (PubMed:20881056). PKA-mediated phosphorylation at a C-terminal site strongly increases the open probability of the channel, but does not increase single channel conductance (PubMed:26269590).3 Publications
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, ACTIVITY 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, ACTIVITY 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, ACTIVITY REGULATION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-829, TISSUE SPECIFICITY, MUTAGENESIS OF SER-829.
N-glycosylated. The four subunits in a tetramer probably differ in the extent of glycosylation; simultaneous glycosylation of all experimentally validated sites would probably create steric hindrance. Thus, glycosylation at Asn-305 is not compatible with glycosylation at Asn-328; only one of these two residues is glycosylated at a given time.1 Publication
Manual assertion based on experiment ini
- Ref.28"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.
Keywords - PTMi
Disulfide bond, Glycoprotein, Methylation, PhosphoproteinProteomic databases
jPOST - Japan Proteome Standard Repository/Database More...jPOSTi | Q13563 |
MassIVE - Mass Spectrometry Interactive Virtual Environment More...MassIVEi | 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: a multi-organism proteome resource More...ProteomicsDBi | 59562 [Q13563-1] 59563 [Q13563-2] 59564 [Q13563-3] 59565 [Q13563-4] 59566 [Q13563-5] |
PTM databases
GlyGen: Computational and Informatics Resources for Glycoscience More...GlyGeni | Q13563, 5 sites |
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q13563 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q13563 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
Detected in fetal and adult kidney (PubMed:10770959). Detected at the thick ascending limb of the loop of Henle, at distal tubules, including the distal convoluted tubule and cortical collecting tubules, with weak staining of the collecting duct (PubMed:10770959). Detected on placenta syncytiotrophoblasts (at protein level) (PubMed:26269590). Strongly expressed in ovary, fetal and adult kidney, testis, and small intestine. Not detected in peripheral leukocytes.3 Publications
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, ACTIVITY 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, Expressed in thoracic aorta and 244 other tissues |
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 | ENSG00000118762, Low tissue specificity |
<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Homotetramer (PubMed:20881056, PubMed:27768895, PubMed:27991905, PubMed:28092368, PubMed:29899465). Heterotetramer with PKD1, giving rise to a complex formed by one PKD1 chain and three PKD2 chains (PubMed:20881056, PubMed:19556541, PubMed:27214281, PubMed:30093605). Interaction with PKD1 is required for ciliary localization (By similarity)
Isoform 1 interacts with PKD1 while isoform 3 does not (By similarity).
Interacts with PKD1L1.
Interacts with CD2AP (PubMed:10913159).
Interacts with HAX1 (PubMed:10760273).
Interacts with NEK8 (By similarity).
Part of a complex containing AKAP5, ADCY5, ADCY6 and PDE4C (By similarity).
Interacts (via C-terminus) with TRPV4 (via C-terminus) (PubMed:18695040).
Interacts (via C-terminal acidic region) with PACS1 and PACS2; these interactions retain the protein in the endoplasmic reticulum and prevent trafficking to the cell membrane (PubMed:15692563).
By similarityManual assertion inferred from sequence similarity toi
9 PublicationsManual 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, ACTIVITY REGULATION, PHOSPHORYLATION AT SER-801, MUTAGENESIS OF SER-801 AND SER-804, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH PKD1. - Ref.23"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.26"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.27"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.28"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%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
Show more detailsHide detailsQ13563
PKD2 - isoform 1 [Q13563-1]
| With | #Exp. | IntAct |
|---|---|---|
| PKD1 [P98161] | 5 | EBI-9837017,EBI-1752013 |
| PKD1 - isoform 3 [P98161-3] | 4 | EBI-9837017,EBI-15930070 |
| itself | 12 | EBI-9837017,EBI-9837017 |
| Pkd1 [O08852] from Mus musculus. | 2 | EBI-9837017,EBI-6666305 |
GO - Molecular functioni
- actinin binding Source: BHF-UCLInferred from direct assayi
- "Alpha-actinin associates with polycystin-2 and regulates its channel activity."
Li Q., Montalbetti N., Shen P.Y., Dai X.Q., Cheeseman C.I., Karpinski E., Wu G., Cantiello H.F., Chen X.Z.
Hum Mol Genet 14:1587-1603(2005) [PubMed] [Europe PMC] [Abstract]
- ATPase binding Source: BHF-UCL
- cytoskeletal protein binding Source: BHF-UCLInferred from direct assayi
- 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.
- HLH domain binding Source: BHF-UCLInferred from physical interactioni
- "Polycystin-1 and polycystin-2 regulate the cell cycle through the helix-loop-helix inhibitor Id2."
Li X., Luo Y., Starremans P.G., McNamara C.A., Pei Y., Zhou J.
Nat Cell Biol 7:1202-1212(2005) [PubMed] [Europe PMC] [Abstract]
- identical protein binding Source: IntActInferred from physical interactioni
- "A polycystin-2 (TRPP2) dimerization domain essential for the function of heteromeric polycystin complexes."
Giamarchi A., Feng S., Rodat-Despoix L., Xu Y., Bubenshchikova E., Newby L.J., Hao J., Gaudioso C., Crest M., Lupas A.N., Honore E., Williamson M.P., Obara T., Ong A.C., Delmas P.
EMBO J 29:1176-1191(2010) [PubMed] [Europe PMC] [Abstract] - Ref.28"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. - Ref.23"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. - "Macromolecular assembly of polycystin-2 intracytosolic C-terminal domain."
Ferreira F.M., Oliveira L.C., Germino G.G., Onuchic J.N., Onuchic L.F.
Proc Natl Acad Sci U S A 108:9833-9838(2011) [PubMed] [Europe PMC] [Abstract] - Ref.27"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.
- ion channel binding Source: BHF-UCLInferred from physical interactioni
- "Specific association of the gene product of PKD2 with the TRPC1 channel."
Tsiokas L., Arnould T., Zhu C., Kim E., Walz G., Sukhatme V.P.
Proc Natl Acad Sci U S A 96:3934-3939(1999) [PubMed] [Europe PMC] [Abstract]
- muscle alpha-actinin binding Source: GO_CentralInferred from biological aspect of ancestori
- "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
- phosphoprotein binding Source: UniProtKBInferred from physical interactioni
- "PRKCSH/80K-H, the protein mutated in polycystic liver disease, protects polycystin-2/TRPP2 against HERP-mediated degradation."
Gao H., Wang Y., Wegierski T., Skouloudaki K., Putz M., Fu X., Engel C., Boehlke C., Peng H., Kuehn E.W., Kim E., Kramer-Zucker A., Walz G.
Hum Mol Genet 19:16-24(2010) [PubMed] [Europe PMC] [Abstract]
- protein homodimerization activity Source: BHF-UCLInferred from direct assayi
- "Homo- and heterodimeric interactions between the gene products of PKD1 and PKD2."
Tsiokas L., Kim E., Arnould T., Sukhatme V.P., Walz G.
Proc Natl Acad Sci U S A 94:6965-6970(1997) [PubMed] [Europe PMC] [Abstract]
- signaling receptor binding Source: BHF-UCLInferred from physical interactioni
- "Polycystin 2 interacts with type I inositol 1,4,5-trisphosphate receptor to modulate intracellular Ca2+ signaling."
Li Y., Wright J.M., Qian F., Germino G.G., Guggino W.B.
J Biol Chem 280:41298-41306(2005) [PubMed] [Europe PMC] [Abstract]
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGRID) More...BioGRIDi | 111328, 59 interactors |
ComplexPortal: manually curated resource of macromolecular complexes More...ComplexPortali | CPX-4001, PKD1-PKD2 Polycystin complex |
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, 41 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 |
Miscellaneous databases
RNAct, Protein-RNA interaction predictions for model organisms. More...RNActi | Q13563, protein |
<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
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> 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 | 214 – 241 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 28 | |
| Helixi | 247 – 257 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| Helixi | 270 – 272 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 276 – 284 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| Helixi | 286 – 291 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> 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 Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> 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 Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 313 – 315 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 320 – 326 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| Helixi | 328 – 330 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 335 – 337 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Turni | 338 – 340 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Turni | 350 – 352 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 363 – 367 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Turni | 371 – 375 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 382 – 386 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 390 – 394 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 399 – 411 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| Beta strandi | 419 – 430 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| Turni | 431 – 434 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 435 – 444 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| Beta strandi | 452 – 460 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| Helixi | 468 – 495 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 28 | |
| Turni | 500 – 503 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 504 – 506 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 507 – 527 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 21 | |
| Turni | 528 – 530 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 533 – 538 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Helixi | 549 – 572 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 24 | |
| Helixi | 573 – 575 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 581 – 619 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 39 | |
| Turni | 620 – 622 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 624 – 626 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 629 – 641 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| Helixi | 646 – 652 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| Helixi | 656 – 667 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| Helixi | 668 – 672 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 673 – 697 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 25 | |
| Turni | 730 – 734 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 738 – 744 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| Turni | 745 – 747 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 752 – 762 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| Beta strandi | 763 – 766 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 767 – 771 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 773 – 777 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Turni | 781 – 783 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 793 – 795 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 836 – 894 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 59 |
3D structure databases
Biological Magnetic Resonance Data Bank More...BMRBi | Q13563 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q13563 |
Database of comparative protein structure models More...ModBasei | Search... |
Protein Data Bank in Europe - Knowledge Base More...PDBe-KBi | 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%5Fand%5Fdomains%5Fsection">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 Manual assertion according to rulesi 2 PublicationsManual 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 Manual assertion inferred by curator fromi
| 20 | |
| Regioni | 810 – 821 | Important for interaction with PACS1 and PACS21 Publication 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 Manual assertion inferred by curator fromi
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 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 | |
| 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
The C-terminal coiled-coil domain is involved in oligomerization and the interaction with PKD1 (PubMed:18694932, PubMed:19556541). The isolated coiled-coil domain forms a homotrimer in vitro; the homotrimer interacts with a single PKD1 chain (PubMed:19556541). The coiled-coil domain binds calcium and undergoes a calcium-induced conformation change (in vitro) (PubMed:18694932).2 Publications
Manual assertion based on experiment ini
- Ref.22"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.23"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
Belongs to the polycystin family.Curated
Keywords - Domaini
Coiled coil, Transmembrane, Transmembrane helixPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG3599, Eukaryota |
Ensembl GeneTree More...GeneTreei | ENSGT00940000159025 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | CLU_012097_0_0_1 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q13563 |
Identification of Orthologs from Complete Genome Data More...OMAi | YHGAGHP |
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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basketAdded to basketThis entry has 5 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All
Isoform 1 (identifier: Q13563-1) [UniParc]FASTAAdd to basketAdded to basket
This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
« Hide
Show »10 20 30 40 50
MVNSSRVQPQ QPGDAKRPPA PRAPDPGRLM AGCAAVGASL AAPGGLCEQR
60 70 80 90 100
GLEIEMQRIR QAAARDPPAG AAASPSPPLS SCSRQAWSRD NPGFEAEEEE
110 120 130 140 150
EEVEGEEGGM VVEMDVEWRP GSRRSAASSA VSSVGARSRG LGGYHGAGHP
160 170 180 190 200
SGRRRRREDQ GPPCPSPVGG GDPLHRHLPL EGQPPRVAWA ERLVRGLRGL
210 220 230 240 250
WGTRLMEESS TNREKYLKSV LRELVTYLLF LIVLCILTYG MMSSNVYYYT
260 270 280 290 300
RMMSQLFLDT PVSKTEKTNF KTLSSMEDFW KFTEGSLLDG LYWKMQPSNQ
310 320 330 340 350
TEADNRSFIF YENLLLGVPR IRQLRVRNGS CSIPQDLRDE IKECYDVYSV
360 370 380 390 400
SSEDRAPFGP RNGTAWIYTS EKDLNGSSHW GIIATYSGAG YYLDLSRTRE
410 420 430 440 450
ETAAQVASLK KNVWLDRGTR ATFIDFSVYN ANINLFCVVR LLVEFPATGG
460 470 480 490 500
VIPSWQFQPL KLIRYVTTFD FFLAACEIIF CFFIFYYVVE EILEIRIHKL
510 520 530 540 550
HYFRSFWNCL DVVIVVLSVV AIGINIYRTS NVEVLLQFLE DQNTFPNFEH
560 570 580 590 600
LAYWQIQFNN IAAVTVFFVW IKLFKFINFN RTMSQLSTTM SRCAKDLFGF
610 620 630 640 650
AIMFFIIFLA YAQLAYLVFG TQVDDFSTFQ ECIFTQFRII LGDINFAEIE
660 670 680 690 700
EANRVLGPIY FTTFVFFMFF ILLNMFLAII NDTYSEVKSD LAQQKAEMEL
710 720 730 740 750
SDLIRKGYHK ALVKLKLKKN TVDDISESLR QGGGKLNFDE LRQDLKGKGH
760 770 780 790 800
TDAEIEAIFT KYDQDGDQEL TEHEHQQMRD DLEKEREDLD LDHSSLPRPM
810 820 830 840 850
SSRSFPRSLD DSEEDDDEDS GHSSRRRGSI SSGVSYEEFQ VLVRRVDRME
860 870 880 890 900
HSIGSIVSKI DAVIVKLEIM ERAKLKRREV LGRLLDGVAE DERLGRDSEI
910 920 930 940 950
HREQMERLVR EELERWESDD AASQISHGLG TPVGLNGQPR PRSSRPSSSQ
960
STEGMEGAGG NGSSNVHV
Length:968
Mass (Da):109,691
Last modified:October 17, 2006 - v3
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:iF8D2E760EBEA8B47
Isoform 2 (identifier: Q13563-2) [UniParc]FASTAAdd to basketAdded to basket
Also known as: delta6
The sequence of this isoform differs from the canonical sequence as follows:
476-483: CEIIFCFF → FICSSYGD
484-968: Missing.
« Hide
Show »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
Isoform 3 (identifier: Q13563-3) [UniParc]FASTAAdd to basketAdded to basket
Also known as: delta7
The sequence of this isoform differs from the canonical sequence as follows:
517-572: Missing.
« Hide
10 20 30 40 50
MVNSSRVQPQ QPGDAKRPPA PRAPDPGRLM AGCAAVGASL AAPGGLCEQR
60 70 80