CNKR3_MOUSE - dbPTM
CNKR3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CNKR3_MOUSE
UniProt AC Q8BMA3
Protein Name Connector enhancer of kinase suppressor of ras 3
Gene Name Cnksr3
Organism Mus musculus (Mouse).
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 MEPVTKWSPKQVVDWTRGLDDCLQPYVHKFEREKIDGEQLLKISHQDLEELGVTRIGHQELVLEAVDLLCALNYGLETDTMKNLVLKLRASSHNLQNYISSRRKSPAYDGNTSRKPPNEFLTSVVELIGAAKALLAWLDRAPFTGITDLSVTKNKIIQLCLDLTTAVQKDCLIAEMEDKVLNVVKVLNGICDKTMRSTTDPVMSQCACLEEVHLPNVRPGEGLGMYIKSTYDGLHVITGTTENSPADRSQKIHAGDEVIQVNRQTVVGWQLKNLVRKLRENPTGVVLLLKKRPTGSFSFTPAPLKNLRWKPPLVQTSPPPTTTQSPESTMDASLKKEKPAILDLYIPPPPAVPYSPRDENVSFGYRGHSKSKQPLPVRKGSESPNSFLDQESQRRRFTIADSDQLPGYSVETNVLPTKMRGKTPSYGKPRPLSMPADGNWMGIVDPFAKPRGNGRKGEDALCRYFSNERITPITEESASPMYRFSRPLTERHLVRGADYIRGSRCYINSDLHSSATIPFQEEGSKKKSASSSAKASSGEPSLLVSWLTRLKLLTH
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
CCCCCCCCHHHHHHC
24.6322817900
34UbiquitinationVHKFEREKIDGEQLL
HHHHHHHCCCHHHHE
52.9322790023
150PhosphorylationFTGITDLSVTKNKII
CCCCCCCCCCHHHHH
30.4720139300
240PhosphorylationGLHVITGTTENSPAD
CEEEEEECCCCCCCC
23.4520415495
241PhosphorylationLHVITGTTENSPADR
EEEEEECCCCCCCCH
34.2229899451
244PhosphorylationITGTTENSPADRSQK
EEECCCCCCCCHHHC
18.4222817900
362PhosphorylationSPRDENVSFGYRGHS
CCCCCCCCCCCCCCC
25.2427742792
381PhosphorylationPLPVRKGSESPNSFL
CCCCCCCCCCCCCCC
37.6326824392
383PhosphorylationPVRKGSESPNSFLDQ
CCCCCCCCCCCCCCH
30.9526824392
386PhosphorylationKGSESPNSFLDQESQ
CCCCCCCCCCCHHHH
30.4825619855
392PhosphorylationNSFLDQESQRRRFTI
CCCCCHHHHHCCEEE
24.2928059163
398PhosphorylationESQRRRFTIADSDQL
HHHHCCEEECCCCCC
17.2824719451
418UbiquitinationETNVLPTKMRGKTPS
ECCCCCCCCCCCCCC
25.3522790023
425PhosphorylationKMRGKTPSYGKPRPL
CCCCCCCCCCCCCCC
52.3124719451
433PhosphorylationYGKPRPLSMPADGNW
CCCCCCCCCCCCCCC
25.9621082442
464PhosphorylationGEDALCRYFSNERIT
CHHHHHHHHCCCCCC
15.4623984901
466PhosphorylationDALCRYFSNERITPI
HHHHHHHCCCCCCCC
28.9323737553
471PhosphorylationYFSNERITPITEESA
HHCCCCCCCCCCCCC
18.1723984901
479PhosphorylationPITEESASPMYRFSR
CCCCCCCCCCCCCCC
21.3429514104
489PhosphorylationYRFSRPLTERHLVRG
CCCCCCCCHHHHHCC
33.3924719451
499PhosphorylationHLVRGADYIRGSRCY
HHHCCCCEECCCCEE
7.6224719451
503PhosphorylationGADYIRGSRCYINSD
CCCEECCCCEEECCC
14.8826824392

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_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CNKR3_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 CNKR3_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of CNKR3_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CNKR3_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381, AND MASSSPECTROMETRY.

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