NDRG3_HUMAN - dbPTM
NDRG3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NDRG3_HUMAN
UniProt AC Q9UGV2
Protein Name Protein NDRG3
Gene Name NDRG3
Organism Homo sapiens (Human).
Sequence Length 375
Subcellular Localization
Protein Description
Protein Sequence MDELQDVQLTEIKPLLNDKNGTRNFQDFDCQEHDIETTHGVVHVTIRGLPKGNRPVILTYHDIGLNHKSCFNAFFNFEDMQEITQHFAVCHVDAPGQQEGAPSFPTGYQYPTMDELAEMLPPVLTHLSLKSIIGIGVGAGAYILSRFALNHPELVEGLVLINVDPCAKGWIDWAASKLSGLTTNVVDIILAHHFGQEELQANLDLIQTYRMHIAQDINQDNLQLFLNSYNGRRDLEIERPILGQNDNKSKTLKCSTLLVVGDNSPAVEAVVECNSRLNPINTTLLKMADCGGLPQVVQPGKLTEAFKYFLQGMGYIPSASMTRLARSRTHSTSSSLGSGESPFSRSVTSNQSDGTQESCESPDVLDRHQTMEVSC
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
1Acetylation-------MDELQDVQ
-------CCCCCCCE		9.0122814378
13 (in isoform 3)Ubiquitination-24.3121890473
13UbiquitinationDVQLTEIKPLLNDKN
CCEEEECHHHHCCCC		24.3121890473
13 (in isoform 2)Ubiquitination-24.3121890473
13 (in isoform 1)Ubiquitination-24.3121890473
13UbiquitinationDVQLTEIKPLLNDKN
CCEEEECHHHHCCCC		24.3121890473
128PhosphorylationPPVLTHLSLKSIIGI
HHHHHHHCHHHHHCC		26.5824719451
286UbiquitinationPINTTLLKMADCGGL
CCCHHHHHHHHCCCC		34.84-
303PhosphorylationVVQPGKLTEAFKYFL
CCCCCHHHHHHHHHH		28.8426552605
308PhosphorylationKLTEAFKYFLQGMGY
HHHHHHHHHHHHCCC		11.7626552605
315PhosphorylationYFLQGMGYIPSASMT
HHHHHCCCCCCHHHH		10.7725850435
318PhosphorylationQGMGYIPSASMTRLA
HHCCCCCCHHHHHHH		24.3425850435
320PhosphorylationMGYIPSASMTRLARS
CCCCCCHHHHHHHHC		25.6425850435
322PhosphorylationYIPSASMTRLARSRT
CCCCHHHHHHHHCCC		21.7525693802
327PhosphorylationSMTRLARSRTHSTSS
HHHHHHHCCCCCCCC		35.6023927012
329PhosphorylationTRLARSRTHSTSSSL
HHHHHCCCCCCCCCC		22.7920201521
331PhosphorylationLARSRTHSTSSSLGS
HHHCCCCCCCCCCCC		29.3920201521
332O-linked_GlycosylationARSRTHSTSSSLGSG
HHCCCCCCCCCCCCC		25.6423301498
332PhosphorylationARSRTHSTSSSLGSG
HHCCCCCCCCCCCCC		25.6420201521
333PhosphorylationRSRTHSTSSSLGSGE
HCCCCCCCCCCCCCC		22.4225159151
334PhosphorylationSRTHSTSSSLGSGES
CCCCCCCCCCCCCCC		29.6623927012
335PhosphorylationRTHSTSSSLGSGESP
CCCCCCCCCCCCCCC		36.2023927012
338PhosphorylationSTSSSLGSGESPFSR
CCCCCCCCCCCCCCC		44.6823927012
341PhosphorylationSSLGSGESPFSRSVT
CCCCCCCCCCCCCCC		34.4723927012
344PhosphorylationGSGESPFSRSVTSNQ
CCCCCCCCCCCCCCC		27.3423927012
346PhosphorylationGESPFSRSVTSNQSD
CCCCCCCCCCCCCCC		28.6625463755
348PhosphorylationSPFSRSVTSNQSDGT
CCCCCCCCCCCCCCC		24.1722167270
349PhosphorylationPFSRSVTSNQSDGTQ
CCCCCCCCCCCCCCH		30.6222167270
352PhosphorylationRSVTSNQSDGTQESC
CCCCCCCCCCCHHCC		42.1122167270
355PhosphorylationTSNQSDGTQESCESP
CCCCCCCCHHCCCCC		33.8730278072
358PhosphorylationQSDGTQESCESPDVL
CCCCCHHCCCCCCCH		17.2323927012
361PhosphorylationGTQESCESPDVLDRH
CCHHCCCCCCCHHHH		30.6325159151
370PhosphorylationDVLDRHQTMEVSC--
CCHHHHHHCEECC--		14.8027273156
374PhosphorylationRHQTMEVSC------
HHHHCEECC------		10.7825159151
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 NDRG3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NDRG3_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 NDRG3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CSTF1_HUMANCSTF1physical
26344197
PEPL1_HUMANNPEPL1physical
26344197
TADBP_HUMANTARDBPphysical
26344197
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 NDRG3_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 MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-352 AND SER-361, 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-331 AND SER-335, ANDMASS 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 MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-352 AND SER-361, 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 THR-322; SER-331; THR-332;SER-334; SER-335; SER-352 AND SER-374, AND MASS SPECTROMETRY.

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