CNKR3_HUMAN - dbPTM
CNKR3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CNKR3_HUMAN
UniProt AC Q6P9H4
Protein Name Connector enhancer of kinase suppressor of ras 3
Gene Name CNKSR3
Organism Homo sapiens (Human).
Sequence Length 555
Subcellular Localization Cytoplasm . Apical cell membrane
Peripheral membrane protein .
Protein Description Involved in transepithelial sodium transport. Regulates aldosterone-induced and epithelial sodium channel (ENaC)-mediated sodium transport through regulation of ENaC cell surface expression. Acts as a scaffold protein coordinating the assembly of an ENaC-regulatory complex (ERC)..
Protein Sequence MEPVTKWSPKQVVDWTRGLDDCLQQYVHKFEREKINGEQLLQISHQDLEELGVTRIGHQELVLEAVDLLCALNYGLETDNMKNLVLKLRASSHNLQNYISSRRKSPAYDGNTSRKAPNEFLTSVVELIGAAKALLAWLDRAPFTGITDFSVTKNKIIQLCLDLTTTVQKDCFVAEMEDKVLTVVKVLNGICDKTIRSTTDPVMSQCACLEEVHLPNIKPGEGLGMYIKSTYDGLHVITGTTENSPADRSQKIHAGDEVIQVNQQTVVGWQLKNLVKKLRENPTGVVLLLKKRPTGSFNFTPAPLKNLRWKPPLVQTSPPPATTQSPESTMDTSLKKEKSAILDLYIPPPPAVPYSPRDENGSFVYGGSSKCKQPLPGPKGSESPNSFLDQESRRRRFTIADSDQLPGYSVETNILPTKMREKTPSYGKPRPLSMPADGNWMGIVDPFARPRGHGRKGEDALCRYFSNERIPPIIEESSSPPYRFSRPTTERHLVRGADYIRGSRCYINSDLHSSATIPFQEEGTKKKSGSSATKSSSTEPSLLVSWFTRLKLLTH
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
8PhosphorylationMEPVTKWSPKQVVDW
CCCCCCCCHHHHHHH		24.6324719451
34UbiquitinationVHKFEREKINGEQLL
HHHHHHHHCCHHHHE		47.9329967540
105PhosphorylationYISSRRKSPAYDGNT
HHHHCCCCCCCCCCC		16.98-
113PhosphorylationPAYDGNTSRKAPNEF
CCCCCCCCCCCCHHH		35.47-
225UbiquitinationKPGEGLGMYIKSTYD
CCCCCCCEEEEEECC		3.622189047
244PhosphorylationITGTTENSPADRSQK
EEECCCCCCCCHHHC		18.4221082442
280UbiquitinationNLVKKLRENPTGVVL
HHHHHHHHCCCEEEE		77.3727667366
283PhosphorylationKKLRENPTGVVLLLK
HHHHHCCCEEEEEEE		54.9418491316
290UbiquitinationTGVVLLLKKRPTGSF
CEEEEEEECCCCCCC		46.8627667366
291PhosphorylationGVVLLLKKRPTGSFN
EEEEEEECCCCCCCC		64.6832645325
294PhosphorylationLLLKKRPTGSFNFTP
EEEECCCCCCCCCCC		49.8728857561
295UbiquitinationLLKKRPTGSFNFTPA
EEECCCCCCCCCCCC		32.6821890473
300UbiquitinationPTGSFNFTPAPLKNL
CCCCCCCCCCCCCCC		21.4622817900
300PhosphorylationPTGSFNFTPAPLKNL
CCCCCCCCCCCCCCC		21.4625159151
305UbiquitinationNFTPAPLKNLRWKPP
CCCCCCCCCCCCCCC		53.5322817900
310UbiquitinationPLKNLRWKPPLVQTS
CCCCCCCCCCCEECC		30.2622817900
322PhosphorylationQTSPPPATTQSPEST
ECCCCCCCCCCCCHH		31.0127732954
323PhosphorylationTSPPPATTQSPESTM
CCCCCCCCCCCCHHC		29.2025850435
325PhosphorylationPPPATTQSPESTMDT
CCCCCCCCCCHHCCC		28.6625850435
328PhosphorylationATTQSPESTMDTSLK
CCCCCCCHHCCCCCC		32.2027732954
329PhosphorylationTTQSPESTMDTSLKK
CCCCCCHHCCCCCCH		19.8727732954
332PhosphorylationSPESTMDTSLKKEKS
CCCHHCCCCCCHHHC		25.7428857561
333PhosphorylationPESTMDTSLKKEKSA
CCHHCCCCCCHHHCC		33.6528857561
339PhosphorylationTSLKKEKSAILDLYI
CCCCHHHCCEEEEEC		22.9528348404
355PhosphorylationPPPAVPYSPRDENGS
CCCCCCCCCCCCCCC		13.8519276368
362PhosphorylationSPRDENGSFVYGGSS
CCCCCCCCEEECCCC		24.1128857561
365PhosphorylationDENGSFVYGGSSKCK
CCCCCEEECCCCCCC		17.48-
368PhosphorylationGSFVYGGSSKCKQPL
CCEEECCCCCCCCCC		23.4328857561
381PhosphorylationPLPGPKGSESPNSFL
CCCCCCCCCCCCCCC		40.8123401153
383PhosphorylationPGPKGSESPNSFLDQ
CCCCCCCCCCCCCCH		30.9529255136
386PhosphorylationKGSESPNSFLDQESR
CCCCCCCCCCCHHHH		30.4830266825
392PhosphorylationNSFLDQESRRRRFTI
CCCCCHHHHHCCEEE		26.0023403867
398PhosphorylationESRRRRFTIADSDQL
HHHHCCEEECCCCCC		17.2820736484
408PhosphorylationDSDQLPGYSVETNIL
CCCCCCCCEEECCCC		13.9627642862
425PhosphorylationKMREKTPSYGKPRPL
CCCCCCCCCCCCCCC		52.3124719451
426PhosphorylationMREKTPSYGKPRPLS
CCCCCCCCCCCCCCC		30.30-
433PhosphorylationYGKPRPLSMPADGNW
CCCCCCCCCCCCCCC		25.9622617229
464PhosphorylationGEDALCRYFSNERIP
CHHHHHHHHCCCCCC		15.4628857561
466PhosphorylationDALCRYFSNERIPPI
HHHHHHHCCCCCCCC		28.9327422710
472PhosphorylationFSNERIPPIIEESSS
HCCCCCCCCCCCCCC		37.5132645325
477PhosphorylationIPPIIEESSSPPYRF
CCCCCCCCCCCCCCC		24.2729978859
478PhosphorylationPPIIEESSSPPYRFS
CCCCCCCCCCCCCCC		50.5821815630
479PhosphorylationPIIEESSSPPYRFSR
CCCCCCCCCCCCCCC		38.8925850435
482PhosphorylationEESSSPPYRFSRPTT
CCCCCCCCCCCCCCC		27.8927251275
483MethylationESSSPPYRFSRPTTE
CCCCCCCCCCCCCCC		28.92-
485PhosphorylationSSPPYRFSRPTTERH
CCCCCCCCCCCCCHH		28.4923403867
488PhosphorylationPYRFSRPTTERHLVR
CCCCCCCCCCHHHHC		39.9323403867
489PhosphorylationYRFSRPTTERHLVRG
CCCCCCCCCHHHHCC		33.4323403867
495MethylationTTERHLVRGADYIRG
CCCHHHHCCCCCCCC		40.73-
503PhosphorylationGADYIRGSRCYINSD
CCCCCCCCCEEECCC		14.8827470641
506PhosphorylationYIRGSRCYINSDLHS
CCCCCCEEECCCCCC		11.3028152594
514PhosphorylationINSDLHSSATIPFQE
ECCCCCCCCEECCCC		20.77-
537PhosphorylationSSATKSSSTEPSLLV
CCCCCCCCCCHHHHH		43.8322210691
545PhosphorylationTEPSLLVSWFTRLKL
CCHHHHHHHHHHHHH		19.22-
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

Oops, there are no upstream regulatory protein records of CNKR3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CNKR3_HUMAN !!
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 CNKR3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RHG39_HUMANARHGAP39physical
28514442
VCIP1_HUMANVCPIP1physical
28514442
DIP2B_HUMANDIP2Bphysical
28514442
GT252_HUMANCOLGALT2physical
28514442
NISCH_HUMANNISCHphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CNKR3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383, AND MASSSPECTROMETRY.

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