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Q13563 (PKD2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Polycystin-2
Alternative name(s):
Autosomal dominant polycystic kidney disease type II protein
Polycystic kidney disease 2 protein
Polycystwin
R48321
Gene names
Name:PKD2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length968 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Functions as a calcium permeable cation channel involved in fluid-flow mechanosensation by the primary cilium in renal epithelium. PKD1 and PKD2 may function through a common signaling pathway that is necessary for normal tubulogenesis. 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 downstream of nodal flow: forms a complex with PKD2 in cilia to facilitate flow detection in left/right patterning By similarity.

Subunit structure

Forms homooligomers. Isoform 1 interacts with PKD1 while isoform 3 does not By similarity. Interacts with PKD1L1. PKD1 requires the presence of PKD2 for stable expression. Interacts with CD2AP. Interacts with HAX1. Interacts with NEK8 By similarity. Part of a complex containing AKAP5, ADCY5, ADCY6 and PDE4C By similarity. Ref.5 Ref.6 Ref.11

Subcellular location

Cell projectioncilium membrane; Multi-pass membrane protein By similarity. Endoplasmic reticulum By similarity Ref.6.

Tissue specificity

Strongly expressed in ovary, fetal and adult kidney, testis, and small intestine. Not detected in peripheral leukocytes. Ref.1

Domain

The C-terminal coiled-coil domain binds calcium and undergoes a calcium-induced conformation change. It is implicated in oligomerization and the interaction with PKD1. Ref.11

Involvement in disease

Polycystic kidney disease 2 (PKD2) [MIM:613095]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21

Sequence similarities

Belongs to the polycystin family.

Contains 1 EF-hand domain.

Ontologies

Keywords
   Biological processIon transport
Transport
   Cellular componentCell membrane
Cell projection
Cilium
Endoplasmic reticulum
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseCiliopathy
Disease mutation
   DomainCoiled coil
Transmembrane
Transmembrane helix
   LigandCalcium
Metal-binding
   Molecular functionIon channel
   PTMGlycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processJAK-STAT cascade

Inferred from sequence or structural similarity. Source: BHF-UCL

aorta development

Inferred from expression pattern PubMed 11891195. Source: UniProtKB

branching involved in ureteric bud morphogenesis

Inferred from expression pattern PubMed 11891195. Source: UniProtKB

calcium ion transmembrane transport

Inferred from direct assay PubMed 11854751. Source: BHF-UCL

calcium ion transport

Inferred from direct assay PubMed 11252306. Source: BHF-UCL

cell cycle arrest

Inferred from sequence or structural similarity. Source: BHF-UCL

cellular response to fluid shear stress

Inferred from mutant phenotype PubMed 19265036. Source: BHF-UCL

cellular response to hydrostatic pressure

Inferred from direct assay PubMed 16025301. Source: BHF-UCL

cellular response to osmotic stress

Inferred from direct assay PubMed 16025301. Source: BHF-UCL

cellular response to reactive oxygen species

Non-traceable author statement PubMed 18417208. Source: BHF-UCL

centrosome duplication

Non-traceable author statement PubMed 18725310. Source: BHF-UCL

cytoplasmic sequestering of transcription factor

Inferred from mutant phenotype PubMed 16311606. Source: BHF-UCL

detection of mechanical stimulus

Inferred from sequence or structural similarity. Source: BHF-UCL

detection of nodal flow

Inferred from sequence or structural similarity. Source: BHF-UCL

determination of left/right symmetry

Inferred from sequence or structural similarity. Source: BHF-UCL

determination of liver left/right asymmetry

Inferred from mutant phenotype PubMed 21719175. Source: BHF-UCL

embryonic placenta development

Inferred from sequence or structural similarity. Source: BHF-UCL

heart development

Inferred from expression pattern PubMed 11891195. Source: UniProtKB

heart looping

Inferred from mutant phenotype PubMed 21719175. Source: BHF-UCL

liver development

Inferred from expression pattern PubMed 11891195. Source: UniProtKB

mesonephric duct development

Inferred from expression pattern PubMed 11891195. Source: UniProtKB

mesonephric tubule development

Inferred from expression pattern PubMed 11891195. Source: UniProtKB

metanephric S-shaped body morphogenesis

Inferred from expression pattern PubMed 11891195. Source: UniProtKB

metanephric ascending thin limb development

Inferred from expression pattern PubMed 11891195. Source: UniProtKB

metanephric cortex development

Inferred from expression pattern PubMed 11891195. Source: UniProtKB

metanephric cortical collecting duct development

Inferred from expression pattern PubMed 11891195. Source: UniProtKB

metanephric distal tubule development

Inferred from expression pattern PubMed 11891195. Source: UniProtKB

metanephric mesenchyme development

Inferred from expression pattern PubMed 11891195. Source: UniProtKB

metanephric part of ureteric bud development

Inferred from expression pattern PubMed 11891195. Source: UniProtKB

metanephric smooth muscle tissue development

Inferred from expression pattern PubMed 11891195. Source: UniProtKB

negative regulation of G1/S transition of mitotic cell cycle

Inferred from mutant phenotype PubMed 16311606. Source: BHF-UCL

negative regulation of cell proliferation

Non-traceable author statement PubMed 18664456. Source: BHF-UCL

negative regulation of ryanodine-sensitive calcium-release channel activity

Inferred from sequence or structural similarity. Source: BHF-UCL

neural tube development

Inferred from expression pattern PubMed 11891195. Source: UniProtKB

placenta blood vessel development

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of cell cycle arrest

Inferred from mutant phenotype PubMed 16311606. Source: BHF-UCL

positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle

Inferred from direct assay PubMed 16311606. Source: BHF-UCL

positive regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity

Inferred from mutant phenotype PubMed 16223735. Source: BHF-UCL

positive regulation of nitric oxide biosynthetic process

Inferred from mutant phenotype PubMed 19265036. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 16311606. Source: BHF-UCL

regulation of cAMP metabolic process

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of calcium ion import

Inferred from direct assay PubMed 11854751. Source: BHF-UCL

regulation of cell proliferation

Inferred from mutant phenotype PubMed 15001556. Source: BHF-UCL

release of sequestered calcium ion into cytosol

Inferred from direct assay PubMed 11854751. Source: BHF-UCL

renal artery morphogenesis

Inferred from expression pattern PubMed 11891195. Source: UniProtKB

renal tubule morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

sodium ion transmembrane transport

Inferred from direct assay PubMed 11252306. Source: BHF-UCL

spinal cord development

Inferred from expression pattern PubMed 11891195. Source: UniProtKB

   Cellular_componentbasal cortex

Inferred from direct assay PubMed 10770959. Source: BHF-UCL

basal plasma membrane

Inferred from direct assay PubMed 10770959. Source: BHF-UCL

cell-cell junction

Inferred from electronic annotation. Source: Ensembl

ciliary basal body

Inferred from direct assay PubMed 15337773. Source: MGI

ciliary membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cilium

Inferred from sequence or structural similarity. Source: BHF-UCL

cytoplasm

Inferred from direct assay PubMed 10770959. Source: BHF-UCL

endoplasmic reticulum

Inferred from direct assay Ref.6PubMed 15123714PubMed 15692563. Source: BHF-UCL

endoplasmic reticulum membrane

Inferred from direct assay PubMed 11854751PubMed 15001556. Source: BHF-UCL

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

integral component of cytoplasmic side of endoplasmic reticulum membrane

Inferred from direct assay PubMed 21044049. Source: BHF-UCL

integral component of lumenal side of endoplasmic reticulum membrane

Inferred from direct assay PubMed 21044049. Source: BHF-UCL

integral component of plasma membrane

Inferred from direct assay PubMed 21044049. Source: BHF-UCL

lamellipodium

Inferred from direct assay Ref.6. Source: BHF-UCL

mitotic spindle

Inferred from direct assay PubMed 15123714. Source: BHF-UCL

motile primary cilium

Inferred from sequence or structural similarity. Source: BHF-UCL

nonmotile primary cilium

Inferred from sequence or structural similarity. Source: BHF-UCL

plasma membrane

Inferred from direct assay PubMed 15692563PubMed 16025301. Source: BHF-UCL

polycystin complex

Inferred from sequence or structural similarity. Source: BHF-UCL

   Molecular_functionATPase binding

Inferred from sequence or structural similarity. Source: BHF-UCL

HLH domain binding

Inferred from physical interaction PubMed 16311606. Source: BHF-UCL

actinin binding

Inferred from direct assay PubMed 15843396. Source: BHF-UCL

calcium ion binding

Inferred from sequence or structural similarity. Source: BHF-UCL

calcium-induced calcium release activity

Inferred from direct assay PubMed 11854751. Source: BHF-UCL

cytoskeletal protein binding

Inferred from direct assay Ref.6. Source: BHF-UCL

identical protein binding

Inferred from physical interaction PubMed 20168298. Source: IntAct

ion channel binding

Inferred from physical interaction PubMed 10097141. Source: BHF-UCL

phosphoprotein binding

Inferred from physical interaction PubMed 19801576. Source: UniProt

potassium channel activity

Inferred from sequence or structural similarity. Source: BHF-UCL

protein homodimerization activity

Inferred from direct assay PubMed 9192675. Source: BHF-UCL

receptor binding

Inferred from physical interaction PubMed 16223735. Source: BHF-UCL

voltage-gated calcium channel activity

Inferred from direct assay PubMed 11252306PubMed 15692563. Source: BHF-UCL

voltage-gated cation channel activity

Inferred from direct assay PubMed 11252306. Source: BHF-UCL

voltage-gated ion channel activity

Inferred from direct assay PubMed 11854751. Source: BHF-UCL

voltage-gated sodium channel activity

Inferred from direct assay PubMed 11252306. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself8EBI-7813714,EBI-7813714
PKD1P981617EBI-7813714,EBI-1752013

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13563-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q13563-2)

Also known as: delta6;

The sequence of this isoform differs from the canonical sequence as follows:
     476-483: CEIIFCFF → FICSSYGD
     484-968: Missing.
Isoform 3 (identifier: Q13563-3)

Also known as: delta7;

The sequence of this isoform differs from the canonical sequence as follows:
     517-572: Missing.
Isoform 4 (identifier: Q13563-4)

Also known as: delta9;

The sequence of this isoform differs from the canonical sequence as follows:
     633-646: IFTQFRIILGDINF → IICSWRSSMIRTLK
     647-968: Missing.
Isoform 5 (identifier: Q13563-5)

Also known as: delta12/13;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 968968Polycystin-2
PRO_0000164356

Regions

Topological domain1 – 223223Cytoplasmic Potential
Transmembrane224 – 24421Helical; Potential
Topological domain245 – 468224Extracellular Potential
Transmembrane469 – 48921Helical; Potential
Topological domain490 – 50516Cytoplasmic Potential
Transmembrane506 – 52621Helical; Potential
Topological domain527 – 55024Extracellular Potential
Transmembrane551 – 57121Helical; Potential
Topological domain572 – 59827Cytoplasmic Potential
Transmembrane599 – 61921Helical; Potential
Topological domain620 – 65839Extracellular Potential
Transmembrane659 – 67921Helical; Potential
Topological domain680 – 968289Cytoplasmic Potential
Domain750 – 78536EF-hand
Calcium binding763 – 77412 Ref.11
Region704 – 79491EF-hand domain
Region803 – 82220Linker
Region828 – 968141C-terminal coiled coil domain
Coiled coil838 – 92689 Potential
Motif316 – 32813Polycystin motif
Compositional bias95 – 10713Poly-Glu
Compositional bias153 – 1575Poly-Arg

Amino acid modifications

Modified residue8121Phosphoserine Ref.10
Glycosylation2991N-linked (GlcNAc...) Potential
Glycosylation3051N-linked (GlcNAc...) Potential
Glycosylation3281N-linked (GlcNAc...) (complex) Ref.9
Glycosylation3621N-linked (GlcNAc...) Potential
Glycosylation3751N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence476 – 4838CEIIFCFF → FICSSYGD in isoform 2.
VSP_042479
Alternative sequence484 – 968485Missing in isoform 2.
VSP_042480
Alternative sequence517 – 57256Missing in isoform 3.
VSP_042481
Alternative sequence633 – 64614IFTQF…GDINF → IICSWRSSMIRTLK in isoform 4.
VSP_042482
Alternative sequence647 – 968322Missing in isoform 4.
VSP_042483
Alternative sequence748 – 84194Missing in isoform 5.
VSP_042484
Natural variant241P → L. Ref.16
VAR_058820
Natural variant281R → P Common polymorphism; possibly damaging. Ref.3 Ref.14 Ref.16 Ref.18 Ref.20
Corresponds to variant rs1805044 [ dbSNP | Ensembl ].
VAR_011072
Natural variant1901A → T. Ref.20
Corresponds to variant rs117078377 [ dbSNP | Ensembl ].
VAR_058821
Natural variant3061R → Q in PKD2. Ref.18
VAR_058822
Natural variant3221R → Q in PKD2. Ref.19
VAR_058823
Natural variant3221R → W in PKD2. Ref.16
VAR_058824
Natural variant3561A → P in PKD2. Ref.14 Ref.17
VAR_011073
Natural variant3841A → P in PKD2. Ref.21
VAR_064394
Natural variant4141W → G in PKD2. Ref.12 Ref.17
VAR_009195
Natural variant4201R → G in PKD2. Ref.18
VAR_058825
Natural variant4521I → V.
Corresponds to variant rs1801612 [ dbSNP | Ensembl ].
VAR_014919
Natural variant4791Missing in PKD2; somatic mutation. Ref.15
VAR_011074
Natural variant4821F → C. Ref.20
Corresponds to variant rs75762896 [ dbSNP | Ensembl ].
VAR_058826
Natural variant504 – 5129Missing in PKD2; somatic mutation.
VAR_011075
Natural variant5111D → V in PKD2. Ref.13
VAR_058827
Natural variant6321C → R in PKD2. Ref.17
VAR_058828
Natural variant6841Missing in PKD2; somatic mutation. Ref.15
VAR_011076
Natural variant8001M → L. Ref.16
Corresponds to variant rs2234917 [ dbSNP | Ensembl ].
VAR_058829
Natural variant8071R → Q in PKD2. Ref.17
Corresponds to variant rs147654263 [ dbSNP | Ensembl ].
VAR_058830

Experimental info

Mutagenesis7711T → A: Loss of calcium-binding site; when associated with A-774. Ref.11
Mutagenesis7741E → A: Loss of calcium-binding site; when associated with A-771. Ref.11
Mutagenesis8421L → P: Loss of protein solubility. Ref.11
Mutagenesis8461V → E: Loss of protein solubility. Ref.11
Mutagenesis8491M → K: Loss of protein solubility. Ref.11
Mutagenesis8531I → P: Loss of protein solubility. Ref.11
Mutagenesis8561I → K: Loss of protein solubility. Ref.11
Mutagenesis8631V → E: Loss of protein solubility; when associated with K-849. Ref.11
Sequence conflict451G → R in AAC16004. Ref.2
Sequence conflict4491G → V in AAC50933. Ref.4

Secondary structure

.................. 968
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 17, 2006. Version 3.
Checksum: F8D2E760EBEA8B47

FASTA968109,691
        10         20         30         40         50         60 
MVNSSRVQPQ QPGDAKRPPA PRAPDPGRLM AGCAAVGASL AAPGGLCEQR GLEIEMQRIR 

        70         80         90        100        110        120 
QAAARDPPAG AAASPSPPLS SCSRQAWSRD NPGFEAEEEE EEVEGEEGGM VVEMDVEWRP 

       130        140        150        160        170        180 
GSRRSAASSA VSSVGARSRG LGGYHGAGHP SGRRRRREDQ GPPCPSPVGG GDPLHRHLPL 

       190        200        210        220        230        240 
EGQPPRVAWA ERLVRGLRGL WGTRLMEESS TNREKYLKSV LRELVTYLLF LIVLCILTYG 

       250        260        270        280        290        300 
MMSSNVYYYT RMMSQLFLDT PVSKTEKTNF KTLSSMEDFW KFTEGSLLDG LYWKMQPSNQ 

       310        320        330        340        350        360 
TEADNRSFIF YENLLLGVPR IRQLRVRNGS CSIPQDLRDE IKECYDVYSV SSEDRAPFGP 

       370        380        390        400        410        420 
RNGTAWIYTS EKDLNGSSHW GIIATYSGAG YYLDLSRTRE ETAAQVASLK KNVWLDRGTR 

       430        440        450        460        470        480 
ATFIDFSVYN ANINLFCVVR LLVEFPATGG VIPSWQFQPL KLIRYVTTFD FFLAACEIIF 

       490        500        510        520        530        540 
CFFIFYYVVE EILEIRIHKL HYFRSFWNCL DVVIVVLSVV AIGINIYRTS NVEVLLQFLE 

       550        560        570        580        590        600 
DQNTFPNFEH LAYWQIQFNN IAAVTVFFVW IKLFKFINFN RTMSQLSTTM SRCAKDLFGF 

       610        620        630        640        650        660 
AIMFFIIFLA YAQLAYLVFG TQVDDFSTFQ ECIFTQFRII LGDINFAEIE EANRVLGPIY 

       670        680        690        700        710        720 
FTTFVFFMFF ILLNMFLAII NDTYSEVKSD LAQQKAEMEL SDLIRKGYHK ALVKLKLKKN 

       730        740        750        760        770        780 
TVDDISESLR QGGGKLNFDE LRQDLKGKGH TDAEIEAIFT KYDQDGDQEL TEHEHQQMRD 

       790        800        810        820        830        840 
DLEKEREDLD LDHSSLPRPM SSRSFPRSLD DSEEDDDEDS GHSSRRRGSI SSGVSYEEFQ 

       850        860        870        880        890        900 
VLVRRVDRME HSIGSIVSKI DAVIVKLEIM ERAKLKRREV LGRLLDGVAE DERLGRDSEI 

       910        920        930        940        950        960 
HREQMERLVR EELERWESDD AASQISHGLG TPVGLNGQPR PRSSRPSSSQ STEGMEGAGG 


NGSSNVHV 

« Hide

Isoform 2 (delta6) [UniParc].

Checksum: 6F4CC2DD18EEF56F
Show »

FASTA48353,686
Isoform 3 (delta7) [UniParc].

Checksum: EDD0DB1BD7750772
Show »

FASTA912103,134
Isoform 4 (delta9) [UniParc].

Checksum: C3773DAF9FFDB249
Show »

FASTA64673,171
Isoform 5 (delta12/13) [UniParc].

Checksum: 887260C960F987BE
Show »

FASTA87498,838

References

« Hide 'large scale' references
[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.
[2]"Characterization of the exon structure of the polycystic kidney disease 2 gene (PKD2)."
Hayashi T., Mochizuki T., Reynolds D.M., Wu G., Cai Y., Somlo S.
Genomics 44:131-136(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT PRO-28.
[4]"A gene similar to PKD1 maps to chromosome 4q22: a candidate gene for PKD2."
Schneider M.C., Rodriguez A., Nomura H., Zhou J., Morton C.C., Reeders S.T., Weremowicz S.
Genomics 38:1-4(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 361-968 (ISOFORM 1).
Tissue: Mammary gland.
[5]"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.
[6]"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.
[7]"Polycystin channels and kidney disease."
Stayner C., Zhou J.
Trends Pharmacol. Sci. 22:543-546(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[8]"A splice form of polycystin-2, lacking exon 7, does not interact with polycystin-1."
Hackmann K., Markoff A., Qian F., Bogdanova N., Germino G.G., Pennekamp P., Dworniczak B., Horst J., Gerke V.
Hum. Mol. Genet. 14:3249-3262(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORMS 2; 3; 4 AND 5).
[9]"A strategy for precise and large scale identification of core fucosylated glycoproteins."
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.
Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-328.
[10]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-812, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"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]
Cited for: 3D-STRUCTURE MODELING, PROTEIN SEQUENCE OF 711-715; 720-724; 804-808 AND 823-827, IDENTIFICATION BY MASS SPECTROMETRY, DOMAIN, CALCIUM-BINDING, CIRCULAR DICHROISM, SUBUNIT, MUTAGENESIS OF THR-771; GLU-774; LEU-842; VAL-846; MET-849; ILE-853; ILE-856 AND VAL-863.
[12]"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.
[13]"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.
[14]"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.
[15]"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.
[16]"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.
[17]"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. expand/collapse author list , 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.
[18]"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.
[19]"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.
[20]"Novel method for genomic analysis of PKD1 and PKD2 mutations in autosomal dominant polycystic kidney disease."
Tan Y.-C., Blumenfeld J.D., Anghel R., Donahue S., Belenkaya R., Balina M., Parker T., Levine D., Leonard D.G.B., Rennert H.
Hum. Mutat. 30:264-273(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PRO-28; THR-190 AND CYS-482.
[21]"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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U50928 mRNA. Translation: AAC50520.1.
AF004873 expand/collapse EMBL AC list , AF004859, AF004860, AF004861, AF004862, AF004863, AF004864, AF004865, AF004866, AF004867, AF004868, AF004869, AF004870, AF004871, AF004872 Genomic DNA. Translation: AAC16004.1.
BC112261 mRNA. Translation: AAI12262.1.
BC112263 mRNA. Translation: AAI12264.1.
U56813 mRNA. Translation: AAC50933.1.
PIRG02640.
RefSeqNP_000288.1. NM_000297.3.
UniGeneHs.181272.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KLDNMR-A680-796[»]
2KLENMR-A680-796[»]
2KQ6NMR-A720-797[»]
2Y4QNMR-A717-792[»]
3HRNX-ray1.90A833-895[»]
3HROX-ray1.90A833-872[»]
ProteinModelPortalQ13563.
SMRQ13563. Positions 720-797, 833-895.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111328. 8 interactions.
DIPDIP-47455N.
IntActQ13563. 3 interactions.
MINTMINT-6618167.
STRING9606.ENSP00000237596.

Chemistry

BindingDBQ13563.
ChEMBLCHEMBL5465.
GuidetoPHARMACOLOGY504.

Protein family/group databases

TCDB1.A.5.2.1. the polycystin cation channel (pcc) family.

PTM databases

PhosphoSiteQ13563.

Polymorphism databases

DMDM116242717.

Proteomic databases

PaxDbQ13563.
PeptideAtlasQ13563.
PRIDEQ13563.

Protocols and materials databases

DNASU5311.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000237596; ENSP00000237596; ENSG00000118762. [Q13563-1]
GeneID5311.
KEGGhsa:5311.
UCSCuc003hre.3. human. [Q13563-1]

Organism-specific databases

CTD5311.
GeneCardsGC04P088929.
HGNCHGNC:9009. PKD2.
HPACAB004544.
HPA015794.
HPA055297.
MIM173910. gene.
613095. phenotype.
neXtProtNX_Q13563.
Orphanet730. Autosomal dominant polycystic kidney disease.
PharmGKBPA33343.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG325704.
HOGENOMHOG000230858.
HOVERGENHBG014945.
InParanoidQ13563.
KOK04986.
OMAAWSRDNP.
OrthoDBEOG7N8ZTW.
PhylomeDBQ13563.
TreeFamTF316484.

Gene expression databases

ArrayExpressQ13563.
BgeeQ13563.
CleanExHS_PKD2.
GenevestigatorQ13563.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
1.20.120.350. 1 hit.
InterProIPR027359. Channel_four-helix_dom.
IPR011992. EF-hand-dom_pair.
IPR002048. EF_hand_dom.
IPR013122. PKD1_2_channel.
IPR003915. PKD_2.
[Graphical view]
PfamPF08016. PKD_channel. 1 hit.
[Graphical view]
PRINTSPR01433. POLYCYSTIN2.
PROSITEPS50222. EF_HAND_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPKD2. human.
EvolutionaryTraceQ13563.
GeneWikiPolycystic_kidney_disease_2.
GenomeRNAi5311.
NextBio20536.
PROQ13563.
SOURCESearch...

Entry information

Entry namePKD2_HUMAN
AccessionPrimary (citable) accession number: Q13563
Secondary accession number(s): O60441 expand/collapse secondary AC list , Q15764, Q2M1Q3, Q2M1Q5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: October 17, 2006
Last modified: April 16, 2014
This is version 146 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM