NDRG2_RAT - dbPTM
NDRG2_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NDRG2_RAT
UniProt AC Q8VBU2
Protein Name Protein NDRG2
Gene Name Ndrg2
Organism Rattus norvegicus (Rat).
Sequence Length 371
Subcellular Localization Cytoplasm. Cytoplasm, perinuclear region. Cell projection, growth cone. In neurons, seems to concentrate at axonal growth cone.
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 (By similarity). May be involved in dendritic cell and neuron differentiation..
Protein Sequence MAELQEVQITEEKPLLPGQTPEAAKEAELAARILLDQGQTHSVETPYGSVTFTVYGTPKPKRPAIFTYHDVGLNYKSCFQPLFQFGDMQEIIQNFVRVHVDAPGMEEGAPVFPLGYQYPSQDQLADMIPCILQYLNFSTIIGVGVGAGAYILSRYALNHPDTVEGLVLINIDPNAKGWMDWAAHKLTGLTSSIPEMILGHLFSQEELSGNSELIQKYRSLITHAPNLENIELYWNSYNNRRDLNFERGGEMTLKCPVMLVVGDQAPHEDAVVECNSKLDPTQTSFLKMADSGGQPQLTQPGKLTEAFKYFVQGMGYMASSCMTRLSRSRTASLTSAASIDGSRSRSRTLSQSSESGTLPSGPPGHTMEVSC
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
22.4722673903
13AcetylationEVQITEEKPLLPGQT
EEEECCCCCCCCCCC
34.4322902405
13UbiquitinationEVQITEEKPLLPGQT
EEEECCCCCCCCCCC
34.43-
20PhosphorylationKPLLPGQTPEAAKEA
CCCCCCCCHHHHHHH
29.0722673903
47PhosphorylationTHSVETPYGSVTFTV
CEEEECCCEEEEEEE
29.47-
49PhosphorylationSVETPYGSVTFTVYG
EEECCCEEEEEEEEC
16.49-
55PhosphorylationGSVTFTVYGTPKPKR
EEEEEEEECCCCCCC
16.54-
61AcetylationVYGTPKPKRPAIFTY
EECCCCCCCCEEEEE
76.7122902405
326PhosphorylationSSCMTRLSRSRTASL
HHHHHHHHHCCCCCC
25.5621738781
328PhosphorylationCMTRLSRSRTASLTS
HHHHHHHCCCCCCCC
30.5228825834
330PhosphorylationTRLSRSRTASLTSAA
HHHHHCCCCCCCCCH
23.1128825834
332PhosphorylationLSRSRTASLTSAASI
HHHCCCCCCCCCHHC
31.4119700791
334PhosphorylationRSRTASLTSAASIDG
HCCCCCCCCCHHCCC
17.5228825834
335PhosphorylationSRTASLTSAASIDGS
CCCCCCCCCHHCCCC
27.4228825834
338PhosphorylationASLTSAASIDGSRSR
CCCCCCHHCCCCCCC
22.4128825834
342PhosphorylationSAASIDGSRSRSRTL
CCHHCCCCCCCCCCC
24.2828689409
344PhosphorylationASIDGSRSRSRTLSQ
HHCCCCCCCCCCCCC
35.9829779826
346PhosphorylationIDGSRSRSRTLSQSS
CCCCCCCCCCCCCCC
30.7521738781
348PhosphorylationGSRSRSRTLSQSSES
CCCCCCCCCCCCCCC
31.8228825834
350PhosphorylationRSRSRTLSQSSESGT
CCCCCCCCCCCCCCC
27.6628825834
352PhosphorylationRSRTLSQSSESGTLP
CCCCCCCCCCCCCCC
32.4728825834
353PhosphorylationSRTLSQSSESGTLPS
CCCCCCCCCCCCCCC
28.3028825834
355PhosphorylationTLSQSSESGTLPSGP
CCCCCCCCCCCCCCC
38.7427097102
357PhosphorylationSQSSESGTLPSGPPG
CCCCCCCCCCCCCCC
44.7827097102
360PhosphorylationSESGTLPSGPPGHTM
CCCCCCCCCCCCCCE
68.0227097102
366PhosphorylationPSGPPGHTMEVSC--
CCCCCCCCEEEEC--
22.4227097102
370PhosphorylationPGHTMEVSC------
CCCCEEEEC------
10.7827097102

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
332SPhosphorylationKinasePRKCQQ02111
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NDRG2_RAT !!

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_RAT !!

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

Oops, there are no PPI records of NDRG2_RAT !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NDRG2_RAT

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS.";
Moser K., White F.M.;
J. Proteome Res. 5:98-104(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332 AND SER-338, 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: IDENTIFICATION BY MASS SPECTROMETRY (ISOFORM 1), AND PHOSPHORYLATIONAT SER-332.

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