NDRG1_HUMAN - dbPTM
NDRG1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NDRG1_HUMAN
UniProt AC Q92597
Protein Name Protein NDRG1
Gene Name NDRG1
Organism Homo sapiens (Human).
Sequence Length 394
Subcellular Localization Cytoplasm, cytosol. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Nucleus. Cell membrane. Mainly cytoplasmic but differentially localized to other regions. Associates with the plasma membrane in intestinal epithelia and lactatin
Protein Description Stress-responsive protein involved in hormone responses, cell growth, and differentiation. Acts as a tumor suppressor in many cell types. Necessary but not sufficient for p53/TP53-mediated caspase activation and apoptosis. Has a role in cell trafficking, notably of the Schwann cell, and is necessary for the maintenance and development of the peripheral nerve myelin sheath. Required for vesicular recycling of CDH1 and TF. May also function in lipid trafficking. Protects cells from spindle disruption damage. Functions in p53/TP53-dependent mitotic spindle checkpoint. Regulates microtubule dynamics and maintains euploidy..
Protein Sequence MSREMQDVDLAEVKPLVEKGETITGLLQEFDVQEQDIETLHGSVHVTLCGTPKGNRPVILTYHDIGMNHKTCYNPLFNYEDMQEITQHFAVCHVDAPGQQDGAASFPAGYMYPSMDQLAEMLPGVLQQFGLKSIIGMGTGAGAYILTRFALNNPEMVEGLVLINVNPCAEGWMDWAASKISGWTQALPDMVVSHLFGKEEMQSNVEVVHTYRQHIVNDMNPGNLHLFINAYNSRRDLEIERPMPGTHTVTLQCPALLVVGDSSPAVDAVVECNSKLDPTKTTLLKMADCGGLPQISQPAKLAEAFKYFVQGMGYMPSASMTRLMRSRTASGSSVTSLDGTRSRSHTSEGTRSRSHTSEGTRSRSHTSEGAHLDITPNSGAAGNSAGPKSMEVSC
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------MSREMQDVD
------CCCCCCCCC		36.6319413330
2Phosphorylation------MSREMQDVD
------CCCCCCCCC		36.6323401153
5Sulfoxidation---MSREMQDVDLAE
---CCCCCCCCCHHH		3.9121406390
14UbiquitinationDVDLAEVKPLVEKGE
CCCHHHHHHHHHCCC		24.922190698
14SumoylationDVDLAEVKPLVEKGE
CCCHHHHHHHHHCCC		24.92-
14SumoylationDVDLAEVKPLVEKGE
CCCHHHHHHHHHCCC		24.92-
19UbiquitinationEVKPLVEKGETITGL
HHHHHHHCCCCHHHH		55.35-
47PhosphorylationLHGSVHVTLCGTPKG
HCCEEEEEECCCCCC		11.0625627689
51PhosphorylationVHVTLCGTPKGNRPV
EEEEECCCCCCCCCE		22.3425627689
67SulfoxidationLTYHDIGMNHKTCYN
EEEEECCCCCCCCCC		4.9230846556
137SulfoxidationGLKSIIGMGTGAGAY
CCHHHHCCCCCHHHH		2.8228183972
181PhosphorylationDWAASKISGWTQALP
HHHHHHHCCHHHHHH		31.8228348404
201SulfoxidationHLFGKEEMQSNVEVV
HHHCHHHHHHCCEEE		5.7730846556
203PhosphorylationFGKEEMQSNVEVVHT
HCHHHHHHCCEEEEE		41.3428555341
211PhosphorylationNVEVVHTYRQHIVND
CCEEEEEEHHHHHCC		8.0627642862
219SulfoxidationRQHIVNDMNPGNLHL
HHHHHCCCCCCCEEE		5.7130846556
285UbiquitinationPTKTTLLKMADCGGL
CCHHHHHHHHHCCCC		34.84-
289GlutathionylationTLLKMADCGGLPQIS
HHHHHHHCCCCCCCC		3.1922555962
300UbiquitinationPQISQPAKLAEAFKY
CCCCCHHHHHHHHHH		55.71-
306UbiquitinationAKLAEAFKYFVQGMG
HHHHHHHHHHHHCCC		44.84-
307PhosphorylationKLAEAFKYFVQGMGY
HHHHHHHHHHHCCCC		11.5227251275
312SulfoxidationFKYFVQGMGYMPSAS
HHHHHHCCCCCCCHH		1.6230846556
315SulfoxidationFVQGMGYMPSASMTR
HHHCCCCCCCHHHHH		1.4330846556
317PhosphorylationQGMGYMPSASMTRLM
HCCCCCCCHHHHHHH		19.2228857561
319PhosphorylationMGYMPSASMTRLMRS
CCCCCCHHHHHHHHC		25.6428355574
320SulfoxidationGYMPSASMTRLMRSR
CCCCCHHHHHHHHCC		2.2430846556
321PhosphorylationYMPSASMTRLMRSRT
CCCCHHHHHHHHCCC		20.3920201521
326PhosphorylationSMTRLMRSRTASGSS
HHHHHHHCCCCCCCC		21.7322167270
328PhosphorylationTRLMRSRTASGSSVT
HHHHHCCCCCCCCCC		26.8229255136
330PhosphorylationLMRSRTASGSSVTSL
HHHCCCCCCCCCCCC		38.3019664994
331PhosphorylationMRSRTASGSSVTSLD
HHCCCCCCCCCCCCC		22.8317322306
332PhosphorylationRSRTASGSSVTSLDG
HCCCCCCCCCCCCCC		21.0929255136
333PhosphorylationSRTASGSSVTSLDGT
CCCCCCCCCCCCCCC		32.7029255136
335PhosphorylationTASGSSVTSLDGTRS
CCCCCCCCCCCCCCC		26.0629255136
336PhosphorylationASGSSVTSLDGTRSR
CCCCCCCCCCCCCCC		23.4729255136
340PhosphorylationSVTSLDGTRSRSHTS
CCCCCCCCCCCCCCC		25.7427273156
342PhosphorylationTSLDGTRSRSHTSEG
CCCCCCCCCCCCCCC		37.6627273156
344PhosphorylationLDGTRSRSHTSEGTR
CCCCCCCCCCCCCCC		32.1527273156
346PhosphorylationGTRSRSHTSEGTRSR
CCCCCCCCCCCCCCC		29.7127273156
347O-linked_GlycosylationTRSRSHTSEGTRSRS
CCCCCCCCCCCCCCC		28.7130379171
347PhosphorylationTRSRSHTSEGTRSRS
CCCCCCCCCCCCCCC		28.7127273156
350PhosphorylationRSHTSEGTRSRSHTS
CCCCCCCCCCCCCCC		22.7830576142
352PhosphorylationHTSEGTRSRSHTSEG
CCCCCCCCCCCCCCC		37.6627273156
354PhosphorylationSEGTRSRSHTSEGTR
CCCCCCCCCCCCCCC		32.1522322096
356PhosphorylationGTRSRSHTSEGTRSR
CCCCCCCCCCCCCCC		29.7127273156
357O-linked_GlycosylationTRSRSHTSEGTRSRS
CCCCCCCCCCCCCCC		28.7130379171
357PhosphorylationTRSRSHTSEGTRSRS
CCCCCCCCCCCCCCC		28.7127273156
360PhosphorylationRSHTSEGTRSRSHTS
CCCCCCCCCCCCCCC		22.7822322096
362PhosphorylationHTSEGTRSRSHTSEG
CCCCCCCCCCCCCCC		37.6622322096
364PhosphorylationSEGTRSRSHTSEGAH
CCCCCCCCCCCCCCE		32.1522322096
366PhosphorylationGTRSRSHTSEGAHLD
CCCCCCCCCCCCEEE		29.7122322096
367PhosphorylationTRSRSHTSEGAHLDI
CCCCCCCCCCCEEEC		28.7122322096
367O-linked_GlycosylationTRSRSHTSEGAHLDI
CCCCCCCCCCCEEEC		28.71OGP
375PhosphorylationEGAHLDITPNSGAAG
CCCEEECCCCCCCCC		18.9822322096
378PhosphorylationHLDITPNSGAAGNSA
EEECCCCCCCCCCCC		30.8922322096
378O-linked_GlycosylationHLDITPNSGAAGNSA
EEECCCCCCCCCCCC		30.89OGP
384PhosphorylationNSGAAGNSAGPKSME
CCCCCCCCCCCCCCC		33.4122322096
384O-linked_GlycosylationNSGAAGNSAGPKSME
CCCCCCCCCCCCCCC		33.41OGP
389PhosphorylationGNSAGPKSMEVSC--
CCCCCCCCCCCCC--		24.2522322096
393PhosphorylationGPKSMEVSC------
CCCCCCCCC------		10.7822322096
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
328TPhosphorylationKinaseSGK_GROUP-PhosphoELM
328TPhosphorylationKinaseSGK1O00141
Uniprot
328TPhosphorylationKinaseSGK-FAMILY-GPS
330SPhosphorylationKinaseSGK_GROUP-PhosphoELM
330SPhosphorylationKinasePRKACAP17612
GPS
330SPhosphorylationKinaseSGK1O00141
Uniprot
330SPhosphorylationKinaseSGK-FAMILY-GPS
332SPhosphorylationKinaseSGK1O00141
Uniprot
342SPhosphorylationKinaseGSK3AP49840
PSP
346TPhosphorylationKinaseSGK_GROUP-PhosphoELM
346TPhosphorylationKinaseSGK-FAMILY-GPS
346TPhosphorylationKinaseSGK1O00141
Uniprot
352SPhosphorylationKinaseGSK3AP49840
PSP
356TPhosphorylationKinaseSGK-FAMILY-GPS
356TPhosphorylationKinaseSGK1O00141
Uniprot
356TPhosphorylationKinaseSGK_GROUP-PhosphoELM
362SPhosphorylationKinaseGSK3AP49840
PSP
364SPhosphorylationKinaseSGK1O00141
Uniprot
366TPhosphorylationKinaseSGK1O00141
Uniprot
366TPhosphorylationKinasePRKACAP17612
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NDRG1_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 NDRG1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HS90A_HUMANHSP90AA1physical
17220478
GRP78_HUMANHSPA5physical
17220478
TERA_HUMANVCPphysical
17220478
CALX_HUMANCANXphysical
17220478
PRS6A_HUMANPSMC3physical
17220478
PRS7_HUMANPSMC2physical
17220478
PSMD2_HUMANPSMD2physical
17220478
XRCC6_HUMANXRCC6physical
17220478
RUVB2_HUMANRUVBL2physical
17220478
ILF3_HUMANILF3physical
17220478
SC23A_HUMANSEC23Aphysical
17220478
COPB2_HUMANCOPB2physical
17220478
CLH1_HUMANCLTCphysical
17220478
AP2M1_HUMANAP2M1physical
17220478
AP1M2_HUMANAP1M2physical
17220478
NEP_HUMANMMEphysical
17220478
CTNB1_HUMANCTNNB1physical
17220478
ACTG_HUMANACTG1physical
17220478
KINH_HUMANKIF5Bphysical
17220478
2ABA_HUMANPPP2R2Aphysical
17220478
TLE3_HUMANTLE3physical
17220478
DHB4_HUMANHSD17B4physical
17220478
CNDP2_HUMANCNDP2physical
17220478
SYDC_HUMANDARSphysical
17220478
ODO2_HUMANDLSTphysical
17220478
ACSL3_HUMANACSL3physical
17220478
FAS_HUMANFASNphysical
17220478
AOFA_HUMANMAOAphysical
17220478
LDHA_HUMANLDHAphysical
17220478
KPYM_HUMANPKMphysical
17220478
RPN2_HUMANRPN2physical
17220478
SYTC_HUMANTARSphysical
17220478
GLYM_HUMANSHMT2physical
17220478
ADT3_HUMANSLC25A6physical
17220478
AT1A1_HUMANATP1A1physical
17220478
EF2_HUMANEEF2physical
17220478
EF1G_HUMANEEF1Gphysical
17220478
IF2G_HUMANEIF2S3physical
17220478
EIF3E_HUMANEIF3Ephysical
17220478
PABP1_HUMANPABPC1physical
17220478
RS3_HUMANRPS3physical
17220478
RS6_HUMANRPS6physical
17220478
RL24_HUMANRPL24physical
17220478
RL3_HUMANRPL3physical
17220478
RS16_HUMANRPS16physical
17220478
RS8_HUMANRPS8physical
17220478
RS20_HUMANRPS20physical
17220478
RS9_HUMANRPS9physical
17220478
RL4_HUMANRPL4physical
17220478
RS26_HUMANRPS26physical
17220478
NUCL_HUMANNCLphysical
17220478
HNRPF_HUMANHNRNPFphysical
17220478
HNRPU_HUMANHNRNPUphysical
17220478
HNRH1_HUMANHNRNPH1physical
17220478
DDX1_HUMANDDX1physical
17220478
DDX5_HUMANDDX5physical
17220478
RENT1_HUMANUPF1physical
17220478
EWS_HUMANEWSR1physical
17220478
CADH1_HUMANCDH1physical
17220478
BACH_HUMANACOT7physical
22863883
DX39B_HUMANDDX39Bphysical
22863883
GSHR_HUMANGSRphysical
22863883
LDHA_HUMANLDHAphysical
22863883
6PGD_HUMANPGDphysical
22863883
B2L11_HUMANBCL2L11physical
19622774
DHX15_HUMANDHX15physical
26344197
G6PD_HUMANG6PDphysical
26344197
PUR2_HUMANGARTphysical
26344197
HIP1R_HUMANHIP1Rphysical
26344197
NIF3L_HUMANNIF3L1physical
26344197
NTM1A_HUMANNTMT1physical
26344197
TADBP_HUMANTARDBPphysical
26344197
UFM1_HUMANUFM1physical
26344197
Drug and Disease Associations
Kegg Disease
H00264 Charcot-Marie-Tooth disease (CMT); Hereditary motor and sensory neuropathy; Peroneal muscular atroph
OMIM Disease
601455Charcot-Marie-Tooth disease 4D (CMT4D)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NDRG1_HUMAN

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Related Literatures of Post-Translational Modification
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 THR-328; SER-330 ANDSER-333, AND MASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, AND MASSSPECTROMETRY.
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330; SER-332; SER-333;THR-335 AND SER-364, 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-326; THR-328; SER-330;SER-332; SER-333; THR-335; SER-336; SER-364 AND THR-375, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326; THR-328 ANDSER-330, AND MASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319; SER-330 ANDSER-336, AND MASS SPECTROMETRY.
"SGK1 activity in Na+ absorbing airway epithelial cells monitored byassaying NDRG1-Thr346/356/366 phosphorylation.";
Inglis S.K., Gallacher M., Brown S.G., McTavish N., Getty J.,Husband E.M., Murray J.T., Wilson S.M.;
Pflugers Arch. 457:1287-1301(2009).
Cited for: PHOSPHORYLATION AT THR-346; THR-356 AND THR-366.
"Toward a global characterization of the phosphoproteome in prostatecancer cells: identification of phosphoproteins in the LNCaP cellline.";
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
Electrophoresis 28:2027-2034(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-366, AND MASSSPECTROMETRY.

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