NDRG2_HUMAN - dbPTM
NDRG2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NDRG2_HUMAN
UniProt AC Q9UN36
Protein Name Protein NDRG2
Gene Name NDRG2
Organism Homo sapiens (Human).
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..
Protein Sequence MAELQEVQITEEKPLLPGQTPEAAKEAELAARILLDQGQTHSVETPYGSVTFTVYGTPKPKRPAILTYHDVGLNYKSCFQPLFQFEDMQEIIQNFVRVHVDAPGMEEGAPVFPLGYQYPSLDQLADMIPCVLQYLNFSTIIGVGVGAGAYILARYALNHPDTVEGLVLINIDPNAKGWMDWAAHKLTGLTSSIPEMILGHLFSQEELSGNSELIQKYRNIITHAPNLDNIELYWNSYNNRRDLNFERGGDITLRCPVMLVVGDQAPHEDAVVECNSKLDPTQTSFLKMADSGGQPQLTQPGKLTEAFKYFLQGMGYMASSCMTRLSRSRTASLTSAASVDGNRSRSRTLSQSSESGTLSSGPPGHTMEVSC
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		26.6322223895
13UbiquitinationEVQITEEKPLLPGQT
EEEECCCCCCCCCCC		34.4330230243
20PhosphorylationKPLLPGQTPEAAKEA
CCCCCCCCHHHHHHH		29.0727050516
23UbiquitinationLPGQTPEAAKEAELA
CCCCCHHHHHHHHHH		25.6630230243
43PhosphorylationDQGQTHSVETPYGSV
HCCCCEEEECCCEEE		8.0327251275
45PhosphorylationGQTHSVETPYGSVTF
CCCEEEECCCEEEEE		21.4728152594
47PhosphorylationTHSVETPYGSVTFTV
CEEEECCCEEEEEEE		29.4728152594
49PhosphorylationSVETPYGSVTFTVYG
EEECCCEEEEEEEEC		16.4928152594
51PhosphorylationETPYGSVTFTVYGTP
ECCCEEEEEEEECCC		18.4527251275
53PhosphorylationPYGSVTFTVYGTPKP
CCEEEEEEEECCCCC		11.9424260401
55PhosphorylationGSVTFTVYGTPKPKR
EEEEEEEECCCCCCC		16.5424260401
57PhosphorylationVTFTVYGTPKPKRPA
EEEEEECCCCCCCCE		15.5128348404
190PhosphorylationAHKLTGLTSSIPEMI
HHHHHCCCCCHHHHH		23.0522210691
217PhosphorylationNSELIQKYRNIITHA
CHHHHHHHHHHHHHC		7.7822210691
247MethylationRRDLNFERGGDITLR
CCCCCCCCCCCEEEE		50.70115484669
276PhosphorylationDAVVECNSKLDPTQT
CCEEECCCCCCCCCC		46.37-
284PhosphorylationKLDPTQTSFLKMADS
CCCCCCCCHHHHHHC		20.8224719451
292PhosphorylationFLKMADSGGQPQLTQ
HHHHHHCCCCCCCCC		39.0232142685
309PhosphorylationKLTEAFKYFLQGMGY
HHHHHHHHHHHHHHH		11.7626437602
319PhosphorylationQGMGYMASSCMTRLS
HHHHHHHHHHHHHHH		13.9327251275
320PhosphorylationGMGYMASSCMTRLSR
HHHHHHHHHHHHHHH		9.8130576142
322PhosphorylationGYMASSCMTRLSRSR
HHHHHHHHHHHHHCC		2.3632142685
323PhosphorylationYMASSCMTRLSRSRT
HHHHHHHHHHHHCCC		32.5530576142
326PhosphorylationSSCMTRLSRSRTASL
HHHHHHHHHCCCCCC		25.5621712546
327PhosphorylationSCMTRLSRSRTASLT
HHHHHHHHCCCCCCC		34.4532142685
328PhosphorylationCMTRLSRSRTASLTS
HHHHHHHCCCCCCCC		30.5223927012
330PhosphorylationTRLSRSRTASLTSAA
HHHHHCCCCCCCCCC		23.1119664994
332PhosphorylationLSRSRTASLTSAASV
HHHCCCCCCCCCCCC		31.4119664994
334PhosphorylationRSRTASLTSAASVDG
HCCCCCCCCCCCCCC		17.5229255136
335PhosphorylationSRTASLTSAASVDGN
CCCCCCCCCCCCCCC		27.4229255136
338PhosphorylationASLTSAASVDGNRSR
CCCCCCCCCCCCCCC		22.0619664994
341PhosphorylationTSAASVDGNRSRSRT
CCCCCCCCCCCCCEE		29.3332142685
344PhosphorylationASVDGNRSRSRTLSQ
CCCCCCCCCCEECCC		38.3128176443
346PhosphorylationVDGNRSRSRTLSQSS
CCCCCCCCEECCCCC		30.7527273156
348PhosphorylationGNRSRSRTLSQSSES
CCCCCCEECCCCCCC		31.8223927012
350PhosphorylationRSRSRTLSQSSESGT
CCCCEECCCCCCCCC		27.6623927012
352PhosphorylationRSRTLSQSSESGTLS
CCEECCCCCCCCCCC		32.4727273156
353PhosphorylationSRTLSQSSESGTLSS
CEECCCCCCCCCCCC		28.3027273156
355PhosphorylationTLSQSSESGTLSSGP
ECCCCCCCCCCCCCC		38.7430278072
357PhosphorylationSQSSESGTLSSGPPG
CCCCCCCCCCCCCCC		32.5223927012
359PhosphorylationSSESGTLSSGPPGHT
CCCCCCCCCCCCCCC		32.8423927012
360PhosphorylationSESGTLSSGPPGHTM
CCCCCCCCCCCCCCE		59.4323927012
366PhosphorylationSSGPPGHTMEVSC--
CCCCCCCCEEEEC--		22.4223927012
370PhosphorylationPGHTMEVSC------
CCCCEEEEC------		10.7823927012
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
330TPhosphorylationKinaseSGK1O00141
PSP
330TPhosphorylationKinaseSGK-FAMILY-GPS
330TPhosphorylationKinaseSGK_GROUP-PhosphoELM
332SPhosphorylationKinaseAKT1P31749
PSP
332SPhosphorylationKinaseRPS6KA1Q15418
GPS
332SPhosphorylationKinaseRPS6KB1P23443
GPS
332SPhosphorylationKinaseSGK1O00141
PSP
332SPhosphorylationKinaseSGK-FAMILY-GPS
332SPhosphorylationKinaseSGK_GROUP-PhosphoELM
346SPhosphorylationKinaseSGK1O00141
PSP
348TPhosphorylationKinaseAKT1P31749
PSP
348TPhosphorylationKinaseSGK1O00141
PSP
348TPhosphorylationKinaseSGK-FAMILY-GPS
348TPhosphorylationKinaseSGK_GROUP-PhosphoELM
350SPhosphorylationKinaseRPS6KA1Q15418
GPS
350SPhosphorylationKinaseRPS6KB1P23443
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NDRG2_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 NDRG2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AT1B1_HUMANATP1B1physical
21771789
HSP7C_HUMANHSPA8physical
26186194
BAG5_HUMANBAG5physical
26186194
NDRG1_HUMANNDRG1physical
26186194
NDRG1_HUMANNDRG1physical
28514442
HSP7C_HUMANHSPA8physical
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 NDRG2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-328; THR-330; SER-332; SER-338; THR-348;SER-350; SER-352 AND SER-353, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328; SER-332; SER-338AND THR-348, AND MASS SPECTROMETRY.
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-328; THR-330; SER-332; SER-338; THR-348;SER-350; SER-352 AND SER-353, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328; THR-330; SER-338;THR-348; SER-350 AND SER-353, AND MASS SPECTROMETRY.

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