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O35245

- PKD2_MOUSE

UniProt

O35245 - PKD2_MOUSE

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Protein

Polycystin-2

Gene

Pkd2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi761 – 77212PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. ATPase binding Source: MGI
  2. calcium channel activity Source: MGI
  3. calcium-induced calcium release activity Source: Ensembl
  4. calcium ion binding Source: BHF-UCL
  5. channel activity Source: MGI
  6. identical protein binding Source: BHF-UCL
  7. potassium channel activity Source: MGI
  8. receptor binding Source: MGI
  9. voltage-gated calcium channel activity Source: Ensembl
  10. voltage-gated sodium channel activity Source: Ensembl

GO - Biological processi

  1. aorta development Source: Ensembl
  2. branching involved in ureteric bud morphogenesis Source: Ensembl
  3. calcium ion transport Source: MGI
  4. cell cycle arrest Source: MGI
  5. cellular calcium ion homeostasis Source: MGI
  6. cellular response to fluid shear stress Source: BHF-UCL
  7. cellular response to hydrostatic pressure Source: Ensembl
  8. cellular response to osmotic stress Source: Ensembl
  9. cytoplasmic sequestering of transcription factor Source: Ensembl
  10. detection of mechanical stimulus Source: MGI
  11. detection of nodal flow Source: BHF-UCL
  12. determination of left/right symmetry Source: MGI
  13. determination of liver left/right asymmetry Source: Ensembl
  14. embryonic placenta development Source: BHF-UCL
  15. heart development Source: MGI
  16. heart looping Source: Ensembl
  17. JAK-STAT cascade Source: MGI
  18. kidney development Source: MGI
  19. liver development Source: MGI
  20. mesonephric duct development Source: Ensembl
  21. metanephric ascending thin limb development Source: Ensembl
  22. metanephric cortex development Source: Ensembl
  23. metanephric cortical collecting duct development Source: Ensembl
  24. metanephric distal tubule development Source: Ensembl
  25. metanephric mesenchyme development Source: Ensembl
  26. metanephric part of ureteric bud development Source: Ensembl
  27. metanephric smooth muscle tissue development Source: Ensembl
  28. metanephric S-shaped body morphogenesis Source: Ensembl
  29. negative regulation of G1/S transition of mitotic cell cycle Source: Ensembl
  30. negative regulation of ryanodine-sensitive calcium-release channel activity Source: MGI
  31. neural tube development Source: Ensembl
  32. placenta blood vessel development Source: BHF-UCL
  33. positive regulation of cell cycle arrest Source: Ensembl
  34. positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle Source: Ensembl
  35. positive regulation of gene expression Source: UniProtKB
  36. positive regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity Source: Ensembl
  37. positive regulation of nitric oxide biosynthetic process Source: BHF-UCL
  38. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  39. potassium ion transmembrane transport Source: GOC
  40. regulation of calcium ion import Source: Ensembl
  41. regulation of cAMP metabolic process Source: MGI
  42. regulation of cell proliferation Source: Ensembl
  43. release of sequestered calcium ion into cytosol Source: BHF-UCL
  44. renal artery morphogenesis Source: Ensembl
  45. renal system development Source: MGI
  46. renal tubule morphogenesis Source: UniProtKB
  47. spinal cord development Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Ion channel

Keywords - Biological processi

Ion transport, Transport

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Polycystin-2
Alternative name(s):
Polycystic kidney disease 2 protein homolog
Gene namesi
Name:Pkd2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:1099818. Pkd2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 221221CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei222 – 24221HelicalSequence AnalysisAdd
BLAST
Topological domaini243 – 466224ExtracellularSequence AnalysisAdd
BLAST
Transmembranei467 – 48721HelicalSequence AnalysisAdd
BLAST
Topological domaini488 – 50316CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei504 – 52421HelicalSequence AnalysisAdd
BLAST
Topological domaini525 – 54824ExtracellularSequence AnalysisAdd
BLAST
Transmembranei549 – 56921HelicalSequence AnalysisAdd
BLAST
Topological domaini570 – 59627CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei597 – 61721HelicalSequence AnalysisAdd
BLAST
Topological domaini618 – 65639ExtracellularSequence AnalysisAdd
BLAST
Transmembranei657 – 67721HelicalSequence AnalysisAdd
BLAST
Topological domaini678 – 966289CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. basal cortex Source: BHF-UCL
  2. basal plasma membrane Source: Ensembl
  3. ciliary basal body Source: MGI
  4. cilium Source: BHF-UCL
  5. cytoplasm Source: BHF-UCL
  6. endoplasmic reticulum Source: MGI
  7. extracellular vesicular exosome Source: Ensembl
  8. filamentous actin Source: Ensembl
  9. integral component of cytoplasmic side of endoplasmic reticulum membrane Source: Ensembl
  10. integral component of lumenal side of endoplasmic reticulum membrane Source: Ensembl
  11. integral component of plasma membrane Source: Ensembl
  12. lamellipodium Source: Ensembl
  13. mitotic spindle Source: BHF-UCL
  14. motile primary cilium Source: MGI
  15. nonmotile primary cilium Source: MGI
  16. plasma membrane Source: MGI
  17. polycystin complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cilium, Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi442 – 4421E → G in lrm4; mice exhibit gross left-right abnormalities. Embryos do not show defects in kidney development. The nodes appear normal. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 966966Polycystin-2PRO_0000164357Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi297 – 2971N-linked (GlcNAc...)Sequence Analysis
Glycosylationi303 – 3031N-linked (GlcNAc...)Sequence Analysis
Glycosylationi326 – 3261N-linked (GlcNAc...)Sequence Analysis
Glycosylationi360 – 3601N-linked (GlcNAc...)Sequence Analysis
Glycosylationi373 – 3731N-linked (GlcNAc...)Sequence Analysis
Modified residuei810 – 8101PhosphoserineBy similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiO35245.
PaxDbiO35245.
PRIDEiO35245.

PTM databases

PhosphoSiteiO35245.

Expressioni

Tissue specificityi

Expressed in mesenchymally derived structures in the developing embryo at day 12.5. Isoform 1 is predominantly expressed in kidney at all developmental stages with high levels also detected in lung. Isoform 3 shows highest expression in brain with lower expression in kidney and lung, low levels in thymus and is hardly detectable in liver.3 Publications

Gene expression databases

BgeeiO35245.
CleanExiMM_PKD2.
GenevestigatoriO35245.

Interactioni

Subunit structurei

Forms homooligomers. Isoform 1 interacts with PKD1 while isoform 3 does not. PKD1 requires the presence of PKD2 for stable expression. Interacts with CD2AP. Interacts with HAX1 (By similarity). Interacts with NEK8. Part of a complex containing AKAP5, ADCY5, ADCY6 and PDE4C. Isoform 3 does not interact with PKD1. Interacts with PKD1L1.By similarity3 Publications

Protein-protein interaction databases

BioGridi202205. 8 interactions.
DIPiDIP-60904N.
IntActiO35245. 3 interactions.

Structurei

3D structure databases

ProteinModelPortaliO35245.
SMRiO35245. Positions 723-793, 832-868.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini748 – 78336EF-handPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni702 – 79291EF-hand domainBy similarityAdd
BLAST
Regioni801 – 82020LinkerBy similarityAdd
BLAST
Regioni821 – 966146C-terminal coiled coil domainBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili837 – 91781Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi314 – 32613Polycystin motifAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi95 – 995Poly-Asp
Compositional biasi151 – 1544Poly-Arg

Domaini

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 (By similarity).By similarity

Sequence similaritiesi

Belongs to the polycystin family.Curated
Contains 1 EF-hand domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG325704.
GeneTreeiENSGT00700000104221.
HOGENOMiHOG000230858.
HOVERGENiHBG014945.
InParanoidiO35245.
KOiK04986.
OMAiAWSRDNP.
OrthoDBiEOG7N8ZTW.
TreeFamiTF316484.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
1.20.120.350. 1 hit.
InterProiIPR027359. Channel_four-helix_dom.
IPR011992. EF-hand-dom_pair.
IPR002048. EF_hand_dom.
IPR013122. PKD1_2_channel.
IPR003915. PKD_2.
[Graphical view]
PfamiPF08016. PKD_channel. 1 hit.
[Graphical view]
PRINTSiPR01433. POLYCYSTIN2.
PROSITEiPS50222. EF_HAND_2. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O35245-1) [UniParc]FASTAAdd to Basket

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

« Hide

        10         20         30         40         50
MVNSRRVQPQ PPGDAGRSPA PRASGPGRLV AGGAGLAVPG GLGEQRGLEI
60 70 80 90 100
EMERIRQAAA RDPPAGASAS PSPPLSSCSR QAWSRDNPGF EAEEDDDDDE
110 120 130 140 150
VEGEEGGMVV EMDVEWRPGS RRSASSSAVS SVGARGRGLG SYRGAAHLSG
160 170 180 190 200
RRRRLEDQGA QCPSPAGGGD PLHRHLPLEG QPPRVAWAER LVRGLRGLWG
210 220 230 240 250
TRLMEESNAN REKYLKSVLR ELVTYLFFLV VLCILTYGMM SSNVYYYTRT
260 270 280 290 300
LSQLFIDTPV SKTEKTNFKT LSSMEDFWKF TEGSFLDGLY WKAQTSNHTQ
310 320 330 340 350
ADNRSFIFYE NLLLGVPRLR QLRVRNGSCS IPQDLRDEIK ECYDVYSVSS
360 370 380 390 400
EDRAPFGPRN GTAWMYTSEK ELNGSSHWGI IASYSGAGYY LDLSRTREET
410 420 430 440 450
AAQLAGLRRN FWLDRGTRAA FIDFSVYNAN INLFCVVRLL AEFPATGGVV
460 470 480 490 500
PSWQFQPVKL IRYVTAFDFF LAACEIIFCF FIIYYVVEEI LEIRIHRLSY
510 520 530 540 550
FRSFWNCLDV VIVVLSVVAM VINIYRMSNA EGLLQFLEDQ NSFPNFEHVA
560 570 580 590 600
YWQIQFNNIS AVMVFLVWIK LFKFINFNRT MSQLSTTMSR CAKDLFGFTI
610 620 630 640 650
MFSIIFLAYA QLAYLVFGTQ VDDFSTFQEC IFTQFRIILG DINFAEIEEA
660 670 680 690 700
NRVLGPLYFT TFVFFMFFIL LNMFLAIIND SYSEVKSDLA QQKAEMELSD
710 720 730 740 750
LIRKGCQKAL VKLKLKRNTV DAISESLRQG GGKLNFDELR QDLKGKGHTD
760 770 780 790 800
AEIEAIFTKY DQDGDQELTE REHQQMRDDL EKEREDLDLE HSSLPRPMSS
810 820 830 840 850
RSFPRSLDDS EEEDDEDSGH SSRRRGSISS GVSYEEFQVL VRRVDRMEHS
860 870 880 890 900
IGSIVSKIDA VIVKLEIMER AKLKRREVLG RLLDGVAEDA RLGRDSEIHR
910 920 930 940 950
EQMERLVREE LERWESDDAA SQTGHGVSTQ VGLGGQPHPR NPRPPSSQSA
960
EGLEGGGGNG SANVHA
Length:966
Mass (Da):108,982
Last modified:July 27, 2011 - v2
Checksum:i59B96AB3AE5226D3
GO
Isoform 2 (identifier: O35245-2) [UniParc]FASTAAdd to Basket

Also known as: delta6

The sequence of this isoform differs from the canonical sequence as follows:
     474-481: CEIIFCFF → FICSSYGD
     482-966: Missing.

Show »
Length:481
Mass (Da):53,299
Checksum:iFE3F3890EA24ED54
GO
Isoform 3 (identifier: O35245-3) [UniParc]FASTAAdd to Basket

Also known as: delta7

The sequence of this isoform differs from the canonical sequence as follows:
     515-570: Missing.

Show »
Length:910
Mass (Da):102,420
Checksum:i0440C0F721450995
GO
Isoform 4 (identifier: O35245-4) [UniParc]FASTAAdd to Basket

Also known as: delta9

The sequence of this isoform differs from the canonical sequence as follows:
     631-644: IFTQFRIILGDINF → IICSWRSSMIRTLK
     645-966: Missing.

Show »
Length:644
Mass (Da):72,702
Checksum:i10DCCE0B2DD5C4AD
GO
Isoform 5 (identifier: O35245-5) [UniParc]FASTAAdd to Basket

Also known as: delta12/13

The sequence of this isoform differs from the canonical sequence as follows:
     746-839: Missing.

Note: Minor isoform.

Show »
Length:872
Mass (Da):98,082
Checksum:i855914112AD1FEB7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti365 – 3651M → I in AAC53388. (PubMed:9339380)Curated
Sequence conflicti370 – 3701K → R in AAC53388. (PubMed:9339380)Curated
Sequence conflicti560 – 5601S → A in AAC53388. (PubMed:9339380)Curated
Sequence conflicti688 – 6892DL → SV in CAA74551. (PubMed:9716661)Curated
Sequence conflicti746 – 7461K → E in CAA73727. (PubMed:9716661)Curated
Sequence conflicti746 – 7461K → E in CAA74551. (PubMed:9716661)Curated
Sequence conflicti746 – 7461K → E in ACN11624. (PubMed:16192288)Curated
Sequence conflicti800 – 8001S → N in BAC35407. (PubMed:16141072)Curated
Sequence conflicti942 – 9421P → S in AAC53388. (PubMed:9339380)Curated
Sequence conflicti957 – 9571G → S in AAC53388. (PubMed:9339380)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei474 – 4818CEIIFCFF → FICSSYGD in isoform 2. CuratedVSP_042485
Alternative sequencei482 – 966485Missing in isoform 2. CuratedVSP_042486Add
BLAST
Alternative sequencei515 – 57056Missing in isoform 3. 1 PublicationVSP_042487Add
BLAST
Alternative sequencei631 – 64414IFTQF…GDINF → IICSWRSSMIRTLK in isoform 4. CuratedVSP_042488Add
BLAST
Alternative sequencei645 – 966322Missing in isoform 4. CuratedVSP_042489Add
BLAST
Alternative sequencei746 – 83994Missing in isoform 5. CuratedVSP_042490Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF014010 mRNA. Translation: AAC53388.1.
Y13278 mRNA. Translation: CAA73727.1.
Y14105
, Y14106, Y14107, Y14108, Y14109, Y14110, Y14111, Y14112, Y14113, Y14114, Y14115, Y14116, Y14117, Y14118, Y14119 Genomic DNA. Translation: CAA74551.1.
Y14120 mRNA. Translation: CAA74552.1.
FJ609779 mRNA. Translation: ACN11624.1.
AK053502 mRNA. Translation: BAC35407.1.
AC123687 Genomic DNA. No translation available.
AC124106 Genomic DNA. No translation available.
AF242389 Genomic DNA. Translation: AAG13267.1.
CCDSiCCDS19487.1. [O35245-1]
RefSeqiNP_032887.3. NM_008861.3. [O35245-1]
XP_006534878.1. XM_006534815.1. [O35245-3]
UniGeneiMm.483692.
Mm.6442.

Genome annotation databases

EnsembliENSMUST00000086831; ENSMUSP00000084041; ENSMUSG00000034462. [O35245-1]
GeneIDi18764.
KEGGimmu:18764.
UCSCiuc012eab.1. mouse. [O35245-1]
uc012eac.1. mouse. [O35245-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF014010 mRNA. Translation: AAC53388.1 .
Y13278 mRNA. Translation: CAA73727.1 .
Y14105
, Y14106 , Y14107 , Y14108 , Y14109 , Y14110 , Y14111 , Y14112 , Y14113 , Y14114 , Y14115 , Y14116 , Y14117 , Y14118 , Y14119 Genomic DNA. Translation: CAA74551.1 .
Y14120 mRNA. Translation: CAA74552.1 .
FJ609779 mRNA. Translation: ACN11624.1 .
AK053502 mRNA. Translation: BAC35407.1 .
AC123687 Genomic DNA. No translation available.
AC124106 Genomic DNA. No translation available.
AF242389 Genomic DNA. Translation: AAG13267.1 .
CCDSi CCDS19487.1. [O35245-1 ]
RefSeqi NP_032887.3. NM_008861.3. [O35245-1 ]
XP_006534878.1. XM_006534815.1. [O35245-3 ]
UniGenei Mm.483692.
Mm.6442.

3D structure databases

ProteinModelPortali O35245.
SMRi O35245. Positions 723-793, 832-868.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202205. 8 interactions.
DIPi DIP-60904N.
IntActi O35245. 3 interactions.

PTM databases

PhosphoSitei O35245.

Proteomic databases

MaxQBi O35245.
PaxDbi O35245.
PRIDEi O35245.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000086831 ; ENSMUSP00000084041 ; ENSMUSG00000034462 . [O35245-1 ]
GeneIDi 18764.
KEGGi mmu:18764.
UCSCi uc012eab.1. mouse. [O35245-1 ]
uc012eac.1. mouse. [O35245-3 ]

Organism-specific databases

CTDi 5311.
MGIi MGI:1099818. Pkd2.

Phylogenomic databases

eggNOGi NOG325704.
GeneTreei ENSGT00700000104221.
HOGENOMi HOG000230858.
HOVERGENi HBG014945.
InParanoidi O35245.
KOi K04986.
OMAi AWSRDNP.
OrthoDBi EOG7N8ZTW.
TreeFami TF316484.

Miscellaneous databases

ChiTaRSi Pkd2. mouse.
NextBioi 294963.
PROi O35245.
SOURCEi Search...

Gene expression databases

Bgeei O35245.
CleanExi MM_PKD2.
Genevestigatori O35245.

Family and domain databases

Gene3Di 1.10.238.10. 1 hit.
1.20.120.350. 1 hit.
InterProi IPR027359. Channel_four-helix_dom.
IPR011992. EF-hand-dom_pair.
IPR002048. EF_hand_dom.
IPR013122. PKD1_2_channel.
IPR003915. PKD_2.
[Graphical view ]
Pfami PF08016. PKD_channel. 1 hit.
[Graphical view ]
PRINTSi PR01433. POLYCYSTIN2.
PROSITEi PS50222. EF_HAND_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning, cDNA sequence analysis, and chromosomal localization of mouse Pkd2."
    Wu G.Q., Mochizuki T., Le T.C., Cai Y., Hayashi T., Reynolds D.M., Somlo S.
    Genomics 45:220-223(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Characterization of the murine polycystic kidney disease (Pkd2) gene."
    Pennekamp P., Bogdanova N., Wilda M., Markoff A., Hameister H., Horst J., Dworniczak B.
    Mamm. Genome 9:749-752(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
  3. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), ALTERNATIVE SPLICING (ISOFORMS 2; 3; 4 AND 5), LACK OF INTERACTION OF ISOFORM 3 WITH PKD1, TISSUE SPECIFICITY.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Eye.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  6. "Cloning and characterization of the murine pkd2 promoter."
    Park J.H., Li L., Cai Y., Hayashi T., Dong F., Maeda Y., Rubin C., Somlo S., Wu G.
    Genomics 66:305-312(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-95.
    Strain: 129/Ola.
  7. "Polycystins 1 and 2 mediate mechanosensation in the primary cilium of kidney cells."
    Nauli S.M., Alenghat F.J., Luo Y., Williams E., Vassilev P., Li X., Elia A.E., Lu W., Brown E.M., Quinn S.J., Ingber D.E., Zhou J.
    Nat. Genet. 33:129-137(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  8. "Nek8 regulates the expression and localization of polycystin-1 and polycystin-2."
    Sohara E., Luo Y., Zhang J., Manning D.K., Beier D.R., Zhou J.
    J. Am. Soc. Nephrol. 19:469-476(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NEK8.
  9. "Identification of signaling pathways regulating primary cilium length and flow-mediated adaptation."
    Besschetnova T.Y., Kolpakova-Hart E., Guan Y., Zhou J., Olsen B.R., Shah J.V.
    Curr. Biol. 20:182-187(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS REGULATOR OF CILIUM LENGTH.
  10. "Polycystin-2 and phosphodiesterase 4C are components of a ciliary A-kinase anchoring protein complex that is disrupted in cystic kidney diseases."
    Choi Y.H., Suzuki A., Hajarnis S., Ma Z., Chapin H.C., Caplan M.J., Pontoglio M., Somlo S., Igarashi P.
    Proc. Natl. Acad. Sci. U.S.A. 108:10679-10684(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AKAP5; ADCY5; ADCY6 AND PDE4C.
  11. Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PKD1L1, MUTAGENESIS OF GLU-442, TISSUE SPECIFICITY.

Entry informationi

Entry nameiPKD2_MOUSE
AccessioniPrimary (citable) accession number: O35245
Secondary accession number(s): C0KJK2
, E9Q4F6, E9QQA3, Q8BPR6, Q9ES37, Q9QWP0, Q9Z193, Q9Z194
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 27, 2011
Last modified: November 26, 2014
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3