CNKR2_MOUSE - dbPTM
CNKR2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CNKR2_MOUSE
UniProt AC Q80YA9
Protein Name Connector enhancer of kinase suppressor of ras 2
Gene Name Cnksr2
Organism Mus musculus (Mouse).
Sequence Length 1032
Subcellular Localization Cytoplasm. Membrane
Peripheral membrane protein.
Protein Description May function as an adapter protein or regulator of Ras signaling pathways..
Protein Sequence MALIMEPVSKWSPSQVVDWMKGLDDCLQQYIKNFEREKISGDQLLRITHQELEDLGVSRIGHQELILEAVDLLCALNYGLETENLKTLSHKLNASAKNLQNFITGRRRSGHYDGRTSRKLPNDFLTSVVDLIGAAKSLLAWLDRSPFAAVTDYSVTRNNVIQLCLELTTIVQQDCTVYETENKILHVCKTLSGVCDHIISLSSDPLVSQSAHLEVIQLANIKPSEGLGMYIKSTYDGLHVITGTTENSPADRCKKIHAGDEVIQVNHQTVVGWQLKNLVNALREDPSGVILTLKKRPQSMLTSAPALLKNMRWKPLALQPLIPRSPTSSVATPSSTISTPTKRDSSALQDLYIPPPPAEPYIPRDEKGNLPCEDLRGHMVGKPVHKGSESPNSFLDQEYRKRFNIVEEDTVLYCYEYEKGRSSSQGRRESTPTYGKLRPISMPVEYNWVGDYEDPNKMKRDSRRENSLLRYMSNEKIAQEEYMFQRNSKKDTGKKSKKKGDKSNSPAHYSLLPSLQMDALRQDIMGTPVPETTLYHTFQQSSLQHKSKKKNKGAISGKSKRRISCKDLGRGDCEGWLWKKKDAKSYFSQKWKKYWFVLKDASLYWYINEEDEKAEGFISLPEFKIDRASECRKKYAFKACHPKIKSFYFAAEHLDDMNRWLNRINMLTAGYAERERIKQEQDYWSESDKEEADTPSTPKQDSPPPPYDTYPRPPSMSCASPYVEAKHSRLSSTETSQSQSSHEEFRQEVTGSSAVSPIRKTASQRRSWQDLIETPLTSSGLHYLQTLPLEDSVFSDSAAISPEHRRQSTLPTQKCHLQDHYGPYPLAESERMQVLNGNGGKPRSFTLPRDSGFNHCCLNTPVSACDPQDDIQPPEVEEEEEEEEEEAAGENVGEKNENREEKLGDSLQDLYRALEEASLSPLGEHRISTKMEYKLSFIKRCNDPVMNEKLHRLRILKSTLKAREGEVAIIDKVLDNPDLTSKEFQQWKQMYLDLFLDICQSTTSNDPLSISSEVDVLTSSLTHTHSYIETHV
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
12PhosphorylationMEPVSKWSPSQVVDW
CCCCCCCCHHHHHHH		20.5722817900
38UbiquitinationIKNFEREKISGDQLL
HHHCHHHHCCHHHHH		48.68-
87PhosphorylationLETENLKTLSHKLNA
CCCCCHHHHHHHHCH		36.3428978645
89PhosphorylationTENLKTLSHKLNASA
CCCHHHHHHHHCHHH		24.6528978645
104PhosphorylationKNLQNFITGRRRSGH
HHHHHHHHCCCCCCC		22.0928978645
244PhosphorylationGLHVITGTTENSPAD
CEEEEEECCCCCHHH		23.4520415495
245PhosphorylationLHVITGTTENSPADR
EEEEEECCCCCHHHH		34.2229899451
248PhosphorylationITGTTENSPADRCKK
EEECCCCCHHHHHCC		18.4225521595
276 (in isoform 2)Phosphorylation-32.8929899451
278 (in isoform 2)Phosphorylation-2.7629899451
279 (in isoform 2)Phosphorylation-5.7229899451
286 (in isoform 2)Phosphorylation-28.3829899451
289 (in isoform 2)Phosphorylation-3.6829899451
294UbiquitinationSGVILTLKKRPQSML
CCEEEEECCCCHHHH		41.31-
325PhosphorylationLQPLIPRSPTSSVAT
EECCCCCCCCCCCCC		27.4625521595
327PhosphorylationPLIPRSPTSSVATPS
CCCCCCCCCCCCCCC		34.5830372032
328PhosphorylationLIPRSPTSSVATPSS
CCCCCCCCCCCCCCC		26.6320415495
329O-linked_GlycosylationIPRSPTSSVATPSST
CCCCCCCCCCCCCCC		20.4622645316
329PhosphorylationIPRSPTSSVATPSST
CCCCCCCCCCCCCCC		20.4620415495
335PhosphorylationSSVATPSSTISTPTK
CCCCCCCCCCCCCCC		30.8521082442
336PhosphorylationSVATPSSTISTPTKR
CCCCCCCCCCCCCCC		24.2422817900
338PhosphorylationATPSSTISTPTKRDS
CCCCCCCCCCCCCCC		28.5525521595
339PhosphorylationTPSSTISTPTKRDSS
CCCCCCCCCCCCCCC		31.0025521595
341PhosphorylationSSTISTPTKRDSSAL
CCCCCCCCCCCCCCH		38.5122807455
388PhosphorylationGKPVHKGSESPNSFL
CCCCCCCCCCCCCCC		39.4425521595
390PhosphorylationPVHKGSESPNSFLDQ
CCCCCCCCCCCCCCH		30.9525521595
393PhosphorylationKGSESPNSFLDQEYR
CCCCCCCCCCCHHHH		30.4825521595
399PhosphorylationNSFLDQEYRKRFNIV
CCCCCHHHHHHCCCC		18.7920415495
422PhosphorylationYEYEKGRSSSQGRRE
EEECCCCCCCCCCCC		42.9029899451
430PhosphorylationSSQGRRESTPTYGKL
CCCCCCCCCCCCCCC		37.5629899451
431PhosphorylationSQGRRESTPTYGKLR
CCCCCCCCCCCCCCC		18.2029899451
433PhosphorylationGRRESTPTYGKLRPI
CCCCCCCCCCCCCCC		45.02-
462PhosphorylationPNKMKRDSRRENSLL
CCCCCCCCHHHHHHH		36.9529899451
467PhosphorylationRDSRRENSLLRYMSN
CCCHHHHHHHHHHHH		24.8322324799
473PhosphorylationNSLLRYMSNEKIAQE
HHHHHHHHHHHHHHH		32.66-
476UbiquitinationLRYMSNEKIAQEEYM
HHHHHHHHHHHHHHH		47.82-
488PhosphorylationEYMFQRNSKKDTGKK
HHHHHHCCCCCCCCC		43.1822324799
503PhosphorylationSKKKGDKSNSPAHYS
CCCCCCCCCCHHHHH		47.4824925903
505PhosphorylationKKGDKSNSPAHYSLL
CCCCCCCCHHHHHHH		30.4724925903
509PhosphorylationKSNSPAHYSLLPSLQ
CCCCHHHHHHHHHHC		11.7924925903
510PhosphorylationSNSPAHYSLLPSLQM
CCCHHHHHHHHHHCH		17.3524925903
532PhosphorylationMGTPVPETTLYHTFQ
CCCCCCHHHHHHHHH		18.9422807455
535PhosphorylationPVPETTLYHTFQQSS
CCCHHHHHHHHHHHH		9.2029899451
537PhosphorylationPETTLYHTFQQSSLQ
CHHHHHHHHHHHHHC		15.0229899451
541PhosphorylationLYHTFQQSSLQHKSK
HHHHHHHHHHCCCCC		23.4119060867
542PhosphorylationYHTFQQSSLQHKSKK
HHHHHHHHHCCCCCC		27.9222807455
558AcetylationNKGAISGKSKRRISC
CCCCCCCCCCCCCCH		46.117714105
560AcetylationGAISGKSKRRISCKD
CCCCCCCCCCCCHHH		49.546566931
564PhosphorylationGKSKRRISCKDLGRG
CCCCCCCCHHHCCCC		17.19-
619PhosphorylationEKAEGFISLPEFKID
HCCCCCEECCCCCCC		35.29-
646PhosphorylationACHPKIKSFYFAAEH
HHCHHHHHHHHHHHH		28.7529899451
683PhosphorylationRIKQEQDYWSESDKE
HHHHHHHHCCHHHHC		15.5522817900
685PhosphorylationKQEQDYWSESDKEEA
HHHHHHCCHHHHCCC		22.4625521595
687PhosphorylationEQDYWSESDKEEADT
HHHHCCHHHHCCCCC		48.7622324799
694PhosphorylationSDKEEADTPSTPKQD
HHHCCCCCCCCCCCC		26.6220415495
696PhosphorylationKEEADTPSTPKQDSP
HCCCCCCCCCCCCCC		60.4825521595
697PhosphorylationEEADTPSTPKQDSPP
CCCCCCCCCCCCCCC		35.3920415495
702PhosphorylationPSTPKQDSPPPPYDT
CCCCCCCCCCCCCCC		36.4925521595
707PhosphorylationQDSPPPPYDTYPRPP
CCCCCCCCCCCCCCC		27.0523970565
709PhosphorylationSPPPPYDTYPRPPSM
CCCCCCCCCCCCCCC		29.5823970565
728PhosphorylationPYVEAKHSRLSSTET
CHHHHHHHHCCCCCC		33.9220415495
731PhosphorylationEAKHSRLSSTETSQS
HHHHHHCCCCCCCCC		33.8220415495
732PhosphorylationAKHSRLSSTETSQSQ
HHHHHCCCCCCCCCC		34.5520415495
733PhosphorylationKHSRLSSTETSQSQS
HHHHCCCCCCCCCCC		39.6520415495
735PhosphorylationSRLSSTETSQSQSSH
HHCCCCCCCCCCCHH		31.9620415495
736PhosphorylationRLSSTETSQSQSSHE
HCCCCCCCCCCCHHH		22.9220415495
738PhosphorylationSSTETSQSQSSHEEF
CCCCCCCCCCHHHHH		31.6220415495
740PhosphorylationTETSQSQSSHEEFRQ
CCCCCCCCHHHHHHH		38.6220415495
741PhosphorylationETSQSQSSHEEFRQE
CCCCCCCHHHHHHHH		27.5520415495
750PhosphorylationEEFRQEVTGSSAVSP
HHHHHHHHCCCCCCC		30.5120415495
752PhosphorylationFRQEVTGSSAVSPIR
HHHHHHCCCCCCCHH		13.0329899451
753PhosphorylationRQEVTGSSAVSPIRK
HHHHHCCCCCCCHHH		33.7520415495
756PhosphorylationVTGSSAVSPIRKTAS
HHCCCCCCCHHHCHH		17.8330372032
767PhosphorylationKTASQRRSWQDLIET
HCHHHCCCHHHHHHC		31.1422324799
792PhosphorylationQTLPLEDSVFSDSAA
EECCCCCCCCCCCCC		18.7122324799
795PhosphorylationPLEDSVFSDSAAISP
CCCCCCCCCCCCCCH		28.6222324799
797PhosphorylationEDSVFSDSAAISPEH
CCCCCCCCCCCCHHH		20.5722324799
801PhosphorylationFSDSAAISPEHRRQS
CCCCCCCCHHHHHHC		21.3629899451
808PhosphorylationSPEHRRQSTLPTQKC
CHHHHHHCCCCCCCC		30.0522324799
809PhosphorylationPEHRRQSTLPTQKCH
HHHHHHCCCCCCCCC		28.5522324799
812PhosphorylationRRQSTLPTQKCHLQD
HHHCCCCCCCCCCCC		43.7129899451
846PhosphorylationGGKPRSFTLPRDSGF
CCCCCCEECCCCCCC		36.7822817900
906PhosphorylationREEKLGDSLQDLYRA
HHHHHHHHHHHHHHH		26.5725521595
920PhosphorylationALEEASLSPLGEHRI
HHHHHCCCCCCCCCC		18.6429899451
972UbiquitinationGEVAIIDKVLDNPDL
CCEEEEEECCCCCCC		34.00-
1011PhosphorylationSNDPLSISSEVDVLT
CCCCCCCCCCHHHHH		19.64-
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 CNKR2_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CNKR2_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 CNKR2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RHG39_MOUSEArhgap39physical
28671696
ARHG7_MOUSEArhgef7physical
28671696
KCC2A_MOUSECamk2aphysical
28671696
KCC2B_MOUSECamk2bphysical
28671696
CAPR1_MOUSECaprin1physical
28671696
CSK21_MOUSECsnk2a1physical
28671696
CYH1_MOUSECyth1physical
28671696
CYH2_MOUSECyth2physical
28671696
CYH3_MOUSECyth3physical
28671696
DLG3_MOUSEDlg3physical
28671696
GIT1_MOUSEGit1physical
28671696
GLNA_MOUSEGlulphysical
28671696
GNAO_MOUSEGnao1physical
28671696
GBB1_MOUSEGnb1physical
28671696
GRM4_MOUSEGrm4physical
28671696
AINX_MOUSEInaphysical
28671696
IQEC1_MOUSEIqsec1physical
28671696
LRIG2_MOUSELrig2physical
28671696
MINK1_MOUSEMink1physical
28671696
NFL_MOUSENeflphysical
28671696
PARK7_MOUSEPark7physical
28671696
PARN_MOUSEParnphysical
28671696
PGK1_MOUSEPgk1physical
28671696
KAPCB_MOUSEPrkacbphysical
28671696
KPCG_MOUSEPrkcgphysical
28671696
RHEB_MOUSERhebphysical
28671696
SPTB2_MOUSESptbn1physical
28671696
SYT1_MOUSESyt1physical
28671696
TNIK_MOUSETnikphysical
28671696
TENR_MOUSETnrphysical
28671696
AGAP2_MOUSEAgap2physical
28671696
BAIP2_MOUSEBaiap2physical
28671696
DLG1_MOUSEDlg1physical
28671696
DLG2_MOUSEDlg2physical
28671696
DLG4_MOUSEDlg4physical
28671696
DLGP1_MOUSEDlgap1physical
28671696
LRRC7_MOUSELrrc7physical
28671696
SHAN3_MOUSEShank3physical
28671696
AP180_MOUSESnap91physical
28671696
SYGP1_MOUSESyngap1physical
28671696
ZO1_MOUSETjp1physical
28671696
1433Z_MOUSEYwhazphysical
28671696
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CNKR2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325; THR-846 ANDSER-906, AND MASS SPECTROMETRY.
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248; SER-467 ANDSER-906, AND MASS SPECTROMETRY.
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390, AND MASSSPECTROMETRY.

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