PKD2_MOUSE - dbPTM
PKD2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PKD2_MOUSE
UniProt AC O35245
Protein Name Polycystin-2
Gene Name Pkd2 {ECO:0000312|MGI:MGI:1099818}
Organism Mus musculus (Mouse).
Sequence Length 966
Subcellular Localization Cell projection, cilium membrane
Multi-pass membrane protein . Cell membrane
Multi-pass membrane protein . Basolateral cell membrane
Multi-pass membrane protein . Cytoplasmic vesicle membrane . Endoplasmic reticulum membrane . Detected on kidne
Protein Description Functions as a cation channel involved in fluid-flow mechanosensation by the primary cilium in renal epithelium. [PubMed: 12514735]
Protein Sequence MVNSRRVQPQPPGDAGRSPAPRASGPGRLVAGGAGLAVPGGLGEQRGLEIEMERIRQAAARDPPAGASASPSPPLSSCSRQAWSRDNPGFEAEEDDDDDEVEGEEGGMVVEMDVEWRPGSRRSASSSAVSSVGARGRGLGSYRGAAHLSGRRRRLEDQGAQCPSPAGGGDPLHRHLPLEGQPPRVAWAERLVRGLRGLWGTRLMEESNANREKYLKSVLRELVTYLFFLVVLCILTYGMMSSNVYYYTRTLSQLFIDTPVSKTEKTNFKTLSSMEDFWKFTEGSFLDGLYWKAQTSNHTQADNRSFIFYENLLLGVPRLRQLRVRNGSCSIPQDLRDEIKECYDVYSVSSEDRAPFGPRNGTAWMYTSEKELNGSSHWGIIASYSGAGYYLDLSRTREETAAQLAGLRRNFWLDRGTRAAFIDFSVYNANINLFCVVRLLAEFPATGGVVPSWQFQPVKLIRYVTAFDFFLAACEIIFCFFIIYYVVEEILEIRIHRLSYFRSFWNCLDVVIVVLSVVAMVINIYRMSNAEGLLQFLEDQNSFPNFEHVAYWQIQFNNISAVMVFLVWIKLFKFINFNRTMSQLSTTMSRCAKDLFGFTIMFSIIFLAYAQLAYLVFGTQVDDFSTFQECIFTQFRIILGDINFAEIEEANRVLGPLYFTTFVFFMFFILLNMFLAIINDSYSEVKSDLAQQKAEMELSDLIRKGCQKALVKLKLKRNTVDAISESLRQGGGKLNFDELRQDLKGKGHTDAEIEAIFTKYDQDGDQELTEREHQQMRDDLEKEREDLDLEHSSLPRPMSSRSFPRSLDDSEEEDDEDSGHSSRRRGSISSGVSYEEFQVLVRRVDRMEHSIGSIVSKIDAVIVKLEIMERAKLKRREVLGRLLDGVAEDARLGRDSEIHREQMERLVREELERWESDDAASQTGHGVSTQVGLGGQPHPRNPRPPSSQSAEGLEGGGGNGSANVHA
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
18PhosphorylationPPGDAGRSPAPRASG
CCCCCCCCCCCCCCC		25.2126824392
68PhosphorylationRDPPAGASASPSPPL
HCCCCCCCCCCCCCC		28.5028066266
70PhosphorylationPPAGASASPSPPLSS
CCCCCCCCCCCCCHH		24.3426824392
72PhosphorylationAGASASPSPPLSSCS
CCCCCCCCCCCHHHC		36.3326824392
76PhosphorylationASPSPPLSSCSRQAW
CCCCCCCHHHCCCCC		34.7619060867
77PhosphorylationSPSPPLSSCSRQAWS
CCCCCCHHHCCCCCC		24.6428066266
79PhosphorylationSPPLSSCSRQAWSRD
CCCCHHHCCCCCCCC		29.4028066266
123PhosphorylationWRPGSRRSASSSAVS
ECCCCCCCCCCCCCH		31.2429472430
125PhosphorylationPGSRRSASSSAVSSV
CCCCCCCCCCCCHHC		26.5229472430
126PhosphorylationGSRRSASSSAVSSVG
CCCCCCCCCCCHHCC		23.2529472430
127PhosphorylationSRRSASSSAVSSVGA
CCCCCCCCCCHHCCC		30.1427600695
130PhosphorylationSASSSAVSSVGARGR
CCCCCCCHHCCCCCC		21.0127600695
135MethylationAVSSVGARGRGLGSY
CCHHCCCCCCCCCCC		29.4324129315
141PhosphorylationARGRGLGSYRGAAHL
CCCCCCCCCCCHHHH		19.3929514104
143MethylationGRGLGSYRGAAHLSG
CCCCCCCCCHHHHHC		29.9418958335
149PhosphorylationYRGAAHLSGRRRRLE
CCCHHHHHCCCHHHH		22.0127149854
164PhosphorylationDQGAQCPSPAGGGDP
HCCCCCCCCCCCCCC		34.7025619855
250PhosphorylationNVYYYTRTLSQLFID
CHHHHHCCHHHHHCC		23.9824759943
261PhosphorylationLFIDTPVSKTEKTNF
HHCCCCCCCCCCCCC		34.7524759943
263PhosphorylationIDTPVSKTEKTNFKT
CCCCCCCCCCCCCCC		34.9024759943
297N-linked_GlycosylationYWKAQTSNHTQADNR
EEEEECCCCCCCCCC		45.68-
303N-linked_GlycosylationSNHTQADNRSFIFYE
CCCCCCCCCEEEEEC		44.50-
326N-linked_GlycosylationLRQLRVRNGSCSIPQ
HHHHHHCCCCCCCCH		43.82-
360N-linked_GlycosylationRAPFGPRNGTAWMYT
CCCCCCCCCEEEEEE		56.13-
373N-linked_GlycosylationYTSEKELNGSSHWGI
EECCEECCCCCCEEE		49.76-
503PhosphorylationHRLSYFRSFWNCLDV
HHHHHHHHHHHHHHH		25.3925777480
516PhosphorylationDVVIVVLSVVAMVIN
HHHHHHHHHHHHHHH		11.7025777480
525PhosphorylationVAMVINIYRMSNAEG
HHHHHHHHHHCCHHH		8.8625777480
719PhosphorylationKLKLKRNTVDAISES
HHHCCHHHHHHHHHH		24.6427717184
724PhosphorylationRNTVDAISESLRQGG
HHHHHHHHHHHHHCC		23.8925619855
726PhosphorylationTVDAISESLRQGGGK
HHHHHHHHHHHCCCC		23.2825619855
792PhosphorylationEDLDLEHSSLPRPMS
HHHCCCCCCCCCCCC		24.9728066266
793PhosphorylationDLDLEHSSLPRPMSS
HHCCCCCCCCCCCCC		44.2826824392
799PhosphorylationSSLPRPMSSRSFPRS
CCCCCCCCCCCCCCC		25.8630352176
800PhosphorylationSLPRPMSSRSFPRSL
CCCCCCCCCCCCCCC		26.2025338131
802PhosphorylationPRPMSSRSFPRSLDD
CCCCCCCCCCCCCCC		41.3625338131
806PhosphorylationSSRSFPRSLDDSEEE
CCCCCCCCCCCCCCC		36.0727087446
810PhosphorylationFPRSLDDSEEEDDED
CCCCCCCCCCCCCCC		46.7227087446
818PhosphorylationEEEDDEDSGHSSRRR
CCCCCCCCCCCCCCC		36.0425619855
821PhosphorylationDDEDSGHSSRRRGSI
CCCCCCCCCCCCCCC		29.1225619855
822PhosphorylationDEDSGHSSRRRGSIS
CCCCCCCCCCCCCCC		24.9225338131
827PhosphorylationHSSRRRGSISSGVSY
CCCCCCCCCCCCCCH		19.9326824392
829PhosphorylationSRRRGSISSGVSYEE
CCCCCCCCCCCCHHH		23.8021183079
830PhosphorylationRRRGSISSGVSYEEF
CCCCCCCCCCCHHHH		41.3619060867
833PhosphorylationGSISSGVSYEEFQVL
CCCCCCCCHHHHHHH		30.2822817900
834PhosphorylationSISSGVSYEEFQVLV
CCCCCCCHHHHHHHH		19.6425168779
916PhosphorylationEELERWESDDAASQT
HHHHHHHCCCHHHHC		33.5528066266
921PhosphorylationWESDDAASQTGHGVS
HHCCCHHHHCCCCCC		29.9625338131
946PhosphorylationPRNPRPPSSQSAEGL
CCCCCCCCCCCCCCC		43.6322942356
947PhosphorylationRNPRPPSSQSAEGLE
CCCCCCCCCCCCCCC		33.6522942356
949PhosphorylationPRPPSSQSAEGLEGG
CCCCCCCCCCCCCCC		30.1822942356
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
719TPhosphorylationKinasePKG1Q13976
PSP
827SPhosphorylationKinasePKG1Q13976
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PKD2_MOUSE !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of PKD2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TERA_MOUSEVcpphysical
18178578
PSMD7_MOUSEPsmd7physical
18178578
HERP1_MOUSEHerpud1physical
18178578
CD2AP_MOUSECd2apphysical
10913159
WWTR1_MOUSEWwtr1physical
17636028
CUL1_MOUSECul1physical
17636028
FBW1A_MOUSEBtrcphysical
17636028
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PKD2_MOUSE

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-810, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory