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Protein Page:
polycystin 2 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
polycystin 2 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. Functions as a calcium permeable cation channel. Defects in PKD2 are the cause of polycystic kidney disease autosomal dominant type 2 (ADPKD2). ADPKD2 is 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. ADPKD2 is clinically milder than ADPKD1 but it has a deleterious impact on overall life expectancy. Belongs to the polycystin family. 5 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Channel, cation; Membrane protein, multi-pass; Membrane protein, integral
Cellular Component: endoplasmic reticulum membrane; nonmotile primary cilium; integral to plasma membrane; endoplasmic reticulum; intercellular junction; cilium; filamentous actin; lamellipodium; cytoplasm; basal plasma membrane; plasma membrane; motile primary cilium; basal cortex
Molecular Function: voltage-gated cation channel activity; identical protein binding; actinin binding; protein homodimerization activity; voltage-gated ion channel activity; phosphoprotein binding; calcium ion binding; muscle alpha-actinin binding; ATPase binding; voltage-gated calcium channel activity; calcium-induced calcium release activity; protein binding; potassium channel activity; voltage-gated sodium channel activity; cytoskeletal protein binding; HLH domain binding; receptor binding
Biological Process: neural tube development; cytoplasmic sequestering of transcription factor; positive regulation of inositol-1,4,5-triphosphate receptor activity; embryonic placenta development; positive regulation of nitric oxide biosynthetic process; regulation of cAMP metabolic process; heart development; detection of mechanical stimulus; liver development; JAK-STAT cascade; G1/S-specific positive regulation of cyclin-dependent protein kinase activity; regulation of cell proliferation; negative regulation of cell proliferation; ureteric bud branching; spinal cord development; release of sequestered calcium ion into cytosol; calcium ion transport; positive regulation of transcription from RNA polymerase II promoter; heart looping; determination of left/right symmetry; cell cycle arrest; centrosome duplication
Reference #:  Q13563 (UniProtKB)
Alt. Names/Synonyms: APKD2; Autosomal dominant polycystic kidney disease type II protein; MGC138466; MGC138468; Pc-2; PC2; PKD2; PKD4; polycystic kidney disease 2 (autosomal dominant); Polycystic kidney disease 2 protein; Polycystin-2; Polycystwin; R48321; transient receptor potential cation channel, subfamily P, member 2; TRPP2
Gene Symbols: PKD2
Molecular weight: 109,691 Da
Basal Isoelectric point: 5.49  Predict pI for various phosphorylation states
Select Structure to View Below

polycystin 2

Protein Structure Not Found.


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Sites Implicated In
cell cycle regulation: S801‑p
activity, induced: S801‑p, S812‑p
intracellular localization: S76‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 3 S74-p PPAGAAAsPsPPLsS
1 3 S76-p AGAAAsPsPPLsSCS
1 0 S80-p AsPsPPLsSCSRQAW
0 1 S125 WRPGSRRSAASSAVS
0 1 A127 PGSRRSAASSAVSsV
0 1 S133-p AASSAVSsVGARsRG
0 5 R137 AVSsVGARsRGLGGY
0 1 S138-p VSsVGARsRGLGGYH
0 7 H145 sRGLGGYHGAGHPsG
0 1 S151-p YHGAGHPsGRRRRRE
0 2 S166-p DQGPPCPsPVGGGDP
0 1 S254-p YYYTRMMsQLFLDtP
0 1 T260-p MsQLFLDtPVsKTEK
0 1 S263-p LFLDtPVsKTEKTNF
0 1 S307-p QTEADNRsFIFYENL
0 1 S408-p ETAAQVAsLKKNVWL
0 1 T588-p RTMSQLStTMsRCAK
0 2 S591-p SQLStTMsRCAKDLF
0 1 K695-ub KSDLAQQkAEMELSD
1 0 T721 KLKLKKNTVDDISES
2 0 S801-p SSLPRPMsSRSFPRS
0 1 S808 sSRSFPRSLDDsEED
3 17 S812-p FPRSLDDsEEDDDED
2 2 S829-p HSSRRRGsIssGVSY
0 1 S831-p SRRRGsIssGVSYEE
0 1 S832-p RRRGsIssGVSYEEF
0 1 S835 GsIssGVSYEEFQVL
0 1 S852-p RVDRMEHsIGSIVSK
0 1 T931 QISHGLGTPVGLNGQ
0 1 S943 NGQPRPRSSRPSSsQ
0 1 S944 GQPRPRSSRPSSsQS
0 1 S948 PRSSRPSSsQStEGM
0 2 S949-p RSSRPSSsQStEGME
0 1 S951 SRPSSsQStEGMEGA
0 1 T952-p RPSSsQStEGMEGAG
  mouse

 
S70-p PPAGASAsPsPPLSS
S72-p AGASAsPsPPLSSCS
S76 AsPsPPLSSCSRQAW
S123-p WRPGSRRsAsSSAVS
S125-p PGSRRsAsSSAVSSV
S131 AsSSAVSSVGArGRG
R135-m1 AVSSVGArGRGLGSY
G136 VSSVGArGRGLGSYr
R143-m1 GRGLGSYrGAAHLSG
S149 YrGAAHLSGRRRRLE
S164 DQGAQCPSPAGGGDP
S252 YYYTRTLSQLFIDTP
T258 LSQLFIDTPVSKTEK
S261 LFIDTPVSKTEKTNF
S305 HTQADNRSFIFYENL
G406 ETAAQLAGLRRNFWL
T586 RTMSQLSTTMSRCAK
S589 SQLSTTMSRCAKDLF
K693 KSDLAQQKAEMELSD
T719-p KLKLKRNtVDAISES
S799-p SSLPRPMsSRSFPRs
S806-p sSRSFPRsLDDsEEE
S810-p FPRsLDDsEEEDDED
S827-p HSSRRRGsIssGVsY
S829-p SRRRGsIssGVsYEE
S830-p RRRGsIssGVsYEEF
S833-p GsIssGVsYEEFQVL
S850 RVDRMEHSIGSIVSK
T929 QTGHGVSTQVGLGGQ
N941 GGQPHPRNPRPPssQ
P942 GQPHPRNPRPPssQs
S946-p PRNPRPPssQsAEGL
S947-p RNPRPPssQsAEGLE
S949-p PRPPssQsAEGLEGG
A950 RPPssQsAEGLEGGG
  rat

 
S70 PPAGASASPSPPLSS
S72 AGASASPSPPLSSCS
S76 ASPSPPLSSCSRQAW
P123 WRPGSRRPASSSAVS
S125 PGSRRPASSSAVSSA
S131 ASSSAVSSAGArGRG
R135-m1 AVSSAGArGRGLGSY
G136 VSSAGArGRGLGSYR
R143 GRGLGSYRGAAYPSG
S149 YRGAAYPSGRRRRLE
S164 DQGAPCPSPAGGGDP
S252 YYYTRTLSQLFIDTP
T258 LSQLFIDTPVSKTEK
S261 LFIDTPVSKTEKTNF
S305 HTQADNRSFIFYENL
G406 ETAAQLAGLRRNFWL
T586 RTMSQLSTTMSRCAK
S589 SQLSTTMSRCAKDLF
K693 KSDLAQQKAEMELSD
T719 KLKLKRNTVDAISES
S799 SSLPRPMSSRSFPRS
S806 SSRSFPRSLDDsEEE
S810-p FPRSLDDsEEEDDED
S827 HSSRRRGSISSGVSY
S829 SRRRGSISSGVSYEE
S830 RRRGSISSGVSYEEF
S833 GSISSGVSYEEFQVL
S850 RVDRMEHSIGSIVSK
T929-p QSGHGLGtQVGLGGQ
S941-p GGQSHPRssRPPSSQ
S942-p GQSHPRssRPPSSQS
S946 PRssRPPSSQSAEGL
S947 RssRPPSSQSAEGLE
S949 sRPPSSQSAEGLEGG
A950 RPPSSQSAEGLEGGG
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