NDRG2_MOUSE - dbPTM
NDRG2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NDRG2_MOUSE
UniProt AC Q9QYG0
Protein Name Protein NDRG2
Gene Name Ndrg2
Organism Mus musculus (Mouse).
Sequence Length 371
Subcellular Localization Cytoplasm . Cytoplasm, perinuclear region. Cell projection, growth cone. In neurons, seems to concentrate at axonal growth cone. Perinuclear in neurons (By similarity)..
Protein Description Contributes to the regulation of the Wnt signaling pathway. Down-regulates CTNNB1-mediated transcriptional activation of target genes, such as CCND1, and may thereby act as tumor suppressor. May be involved in dendritic cell and neuron differentiation (By similarity)..
Protein Sequence MAELQEVQITEEKPLLPGQTPETAKEAELAARILLDQGQTHSVETPYGSVTFTVYGTPKPKRPAIFTYHDVGLNYKSCFQPLFRFGDMQEIIQNFVRVHVDAPGMEEGAPVFPLGYQYPSLDQLADMIPCILQYLNFSTIIGVGVGAGAYILSRYALNHPDTVEGLVLINIDPNAKGWMDWAAHKLTGLTSSIPDMILGHLFSQEELSGNSELIQKYRGIIQHAPNLENIELYWNSYNNRRDLNFERGGETTLKCPVMLVVGDQAPHEDAVVECNSKLDPTQTSFLKMADSGGQPQLTQPGKLTEAFKYFLQGMGYMASSCMTRLSRSRTASLTSAASIDGSRSRSRTLSQSSESGTLPSGPPGHTMEVSC
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
2Acetylation------MAELQEVQI
------CCCCEEEEE		26.63-
10PhosphorylationELQEVQITEEKPLLP
CCEEEEECCCCCCCC		22.4722817900
13AcetylationEVQITEEKPLLPGQT
EEEECCCCCCCCCCC		34.4323954790
20 (in isoform 2)Phosphorylation-29.0727818261
20PhosphorylationKPLLPGQTPETAKEA
CCCCCCCCHHHHHHH		29.0723737553
23PhosphorylationLPGQTPETAKEAELA
CCCCCHHHHHHHHHH		44.2123737553
25AcetylationGQTPETAKEAELAAR
CCCHHHHHHHHHHHH		65.9523954790
25UbiquitinationGQTPETAKEAELAAR
CCCHHHHHHHHHHHH		65.9522790023
26 (in isoform 2)Phosphorylation-44.9325177544
28UbiquitinationPETAKEAELAARILL
HHHHHHHHHHHHHHH		39.7827667366
33 (in isoform 2)Phosphorylation-3.7225177544
42PhosphorylationLDQGQTHSVETPYGS
HHCCCCEEEECCCEE		25.6525367039
45PhosphorylationGQTHSVETPYGSVTF
CCCEEEECCCEEEEE		21.4725367039
47PhosphorylationTHSVETPYGSVTFTV
CEEEECCCEEEEEEE		29.4729899451
49PhosphorylationSVETPYGSVTFTVYG
EEECCCEEEEEEEEC		16.4920415495
51PhosphorylationETPYGSVTFTVYGTP
ECCCEEEEEEEECCC		18.4523984901
53PhosphorylationPYGSVTFTVYGTPKP
CCEEEEEEEECCCCC		11.9426643407
55PhosphorylationGSVTFTVYGTPKPKR
EEEEEEEECCCCCCC		16.5423984901
57PhosphorylationVTFTVYGTPKPKRPA
EEEEEECCCCCCCCE		15.5126643407
61MalonylationVYGTPKPKRPAIFTY
EECCCCCCCCEEEEE		76.7126320211
68NitrationKRPAIFTYHDVGLNY
CCCEEEEECCCCCCH		5.81-
78S-nitrosylationVGLNYKSCFQPLFRF
CCCCHHHHHHHHHHC		3.0021278135
78S-palmitoylationVGLNYKSCFQPLFRF
CCCCHHHHHHHHHHC		3.0028526873
78S-nitrosocysteineVGLNYKSCFQPLFRF
CCCCHHHHHHHHHHC		3.00-
216AcetylationGNSELIQKYRGIIQH
CCHHHHHHHHHHHHH		29.8923954790
287UbiquitinationPTQTSFLKMADSGGQ
CCCCCHHHHHHCCCC		29.9922790023
288UbiquitinationTQTSFLKMADSGGQP
CCCCHHHHHHCCCCC		5.6527667366
291UbiquitinationSFLKMADSGGQPQLT
CHHHHHHCCCCCCCC		34.9727667366
302UbiquitinationPQLTQPGKLTEAFKY
CCCCCCCHHHHHHHH		59.9422790023
305UbiquitinationTQPGKLTEAFKYFLQ
CCCCHHHHHHHHHHH		63.6527667366
316PhosphorylationYFLQGMGYMASSCMT
HHHHHHHHHHHHHHH		4.8024925903
319PhosphorylationQGMGYMASSCMTRLS
HHHHHHHHHHHHHHH		13.9324925903
320PhosphorylationGMGYMASSCMTRLSR
HHHHHHHHHHHHHHH		9.8124925903
321S-nitrosylationMGYMASSCMTRLSRS
HHHHHHHHHHHHHHC		2.7521278135
321S-nitrosocysteineMGYMASSCMTRLSRS
HHHHHHHHHHHHHHC		2.75-
323PhosphorylationYMASSCMTRLSRSRT
HHHHHHHHHHHHCCC		32.5524925903
326PhosphorylationSSCMTRLSRSRTASL
HHHHHHHHHCCCCCC		25.5624925903
328PhosphorylationCMTRLSRSRTASLTS
HHHHHHHCCCCCCCC		30.5225521595
330PhosphorylationTRLSRSRTASLTSAA
HHHHHCCCCCCCCCH		23.1118388127
332PhosphorylationLSRSRTASLTSAASI
HHHCCCCCCCCCHHC		31.4118388127
334PhosphorylationRSRTASLTSAASIDG
HCCCCCCCCCHHCCC		17.5225521595
335PhosphorylationSRTASLTSAASIDGS
CCCCCCCCCHHCCCC		27.4225521595
338PhosphorylationASLTSAASIDGSRSR
CCCCCCHHCCCCCCC		22.4125521595
342PhosphorylationSAASIDGSRSRSRTL
CCHHCCCCCCCCCCC		24.2825521595
344PhosphorylationASIDGSRSRSRTLSQ
HHCCCCCCCCCCCCC		35.9825521595
346PhosphorylationIDGSRSRSRTLSQSS
CCCCCCCCCCCCCCC		30.7525521595
348PhosphorylationGSRSRSRTLSQSSES
CCCCCCCCCCCCCCC		31.8225521595
350PhosphorylationRSRSRTLSQSSESGT
CCCCCCCCCCCCCCC		27.6625521595
352PhosphorylationRSRTLSQSSESGTLP
CCCCCCCCCCCCCCC		32.4725521595
353PhosphorylationSRTLSQSSESGTLPS
CCCCCCCCCCCCCCC		28.3025521595
355PhosphorylationTLSQSSESGTLPSGP
CCCCCCCCCCCCCCC		38.7425521595
357PhosphorylationSQSSESGTLPSGPPG
CCCCCCCCCCCCCCC		44.7825521595
360PhosphorylationSESGTLPSGPPGHTM
CCCCCCCCCCCCCCE		68.0224925903
366PhosphorylationPSGPPGHTMEVSC--
CCCCCCCCEEEEC--		22.4228833060
370PhosphorylationPGHTMEVSC------
CCCCEEEEC------		10.7824925903
371S-nitrosylationGHTMEVSC-------
CCCEEEEC-------		8.5821278135
371S-nitrosocysteineGHTMEVSC-------
CCCEEEEC-------		8.58-
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
330TPhosphorylationKinaseSGK1Q9WVC6
Uniprot
332SPhosphorylationKinasePKCTQ02111
PSP
332SPhosphorylationKinaseSGK1Q9WVC6
Uniprot
332SPhosphorylationKinaseAKT-FAMILY-GPS
348TPhosphorylationKinaseAKT1P31750
Uniprot
348TPhosphorylationKinaseSGK1Q9WVC6
Uniprot
348TPhosphorylationKinaseAKT-FAMILY-GPS
350SPhosphorylationKinaseAKT-FAMILY-GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NDRG2_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 NDRG2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of NDRG2_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NDRG2_MOUSE

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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-332 AND SER-338, ANDMASS SPECTROMETRY.
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis.";
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
J. Proteome Res. 7:3957-3967(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326; SER-328; THR-330;SER-332; SER-346 AND THR-348, AND MASS SPECTROMETRY.
"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-328; THR-330; SER-332;THR-334; SER-335; SER-338; SER-342; SER-344; THR-348; SER-350;SER-352; SER-353; SER-355 AND THR-357, AND MASS SPECTROMETRY.
"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-332 AND SER-352, ANDMASS SPECTROMETRY.
"Akt mediates insulin-stimulated phosphorylation of Ndrg2: evidencefor cross-talk with protein kinase C theta.";
Burchfield J.G., Lennard A.J., Narasimhan S., Hughes W.E.,Wasinger V.C., Corthals G.L., Okuda T., Kondoh H., Biden T.J.,Schmitz-Peiffer C.;
J. Biol. Chem. 279:18623-18632(2004).
Cited for: PHOSPHORYLATION AT SER-332 AND THR-348, AND SUBCELLULAR LOCATION.
"Exploitation of KESTREL to identify NDRG family members asphysiological substrates for SGK1 and GSK3.";
Murray J.T., Campbell D.G., Morrice N., Auld G.C., Shpiro N.,Marquez R., Peggie M., Bain J., Bloomberg G.B., Grahammer F., Lang F.,Wulff P., Kuhl D., Cohen P.;
Biochem. J. 384:477-488(2004).
Cited for: PHOSPHORYLATION AT THR-330; SER-332; THR-348 AND SER-350, AND TISSUESPECIFICITY.

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