dbPTM

NDRG1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NDRG1_MOUSE
UniProt AC	Q62433
Protein Name	Protein NDRG1
Gene Name	Ndrg1
Organism	Mus musculus (Mouse).
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. 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 (By similarity). 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..
Protein Sequence	MSRELHDVDLAEVKPLVEKGESITGLLQEFDVQEQDIETLHGSLHVTLCGTPKGNRPVILTYHDIGMNHKTCYNPLFNSEDMQEITQHFAVCHVDAPGQQDGAPSFPVGYMYPSMDQLAEMLPGVLHQFGLKSVIGMGTGAGAYILTRFALNNPEMVEGLVLMNVNPCAEGWMDWAASKISGWTQALPDMVVSHLFGKEEIHNNVEVVHTYRQHILNDMNPSNLHLFISAYNSRRDLEIERPMPGTHTVTLQCPALLVVGDNSPAVDAVVECNSKLDPTKTTLLKMADCGGLPQISQPAKLAEAFKYFVQGMGYMPSASMTRLMRSRTASGSSVTSLEGTRSRSHTSEGPRSRSHTSEGSRSRSHTSEDARLNITPNSGATGNNAGPKSMEVSC

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSRELHDVD ------CCCCCCCCC	34.17	-
2	Phosphorylation	------MSRELHDVD ------CCCCCCCCC	34.17	26824392
14	Ubiquitination	DVDLAEVKPLVEKGE CCCHHHHHHHHHCCC	24.92	-
144	Phosphorylation	MGTGAGAYILTRFAL CCCCHHHHHHHHHHH	8.78	29899451
147	Phosphorylation	GAGAYILTRFALNNP CHHHHHHHHHHHCCH	17.74	29899451
246	Phosphorylation	IERPMPGTHTVTLQC ECCCCCCCEEEEEEC	14.43	26239621
248	Phosphorylation	RPMPGTHTVTLQCPA CCCCCCEEEEEECCE	18.28	26239621
250	Phosphorylation	MPGTHTVTLQCPALL CCCCEEEEEECCEEE	16.56	26239621
253	Glutathionylation	THTVTLQCPALLVVG CEEEEEECCEEEEEC	2.09	24333276
289	S-nitrosocysteine	TLLKMADCGGLPQIS HHHHHHHCCCCCCCC	3.19	-
289	S-nitrosylation	TLLKMADCGGLPQIS HHHHHHHCCCCCCCC	3.19	21278135
300	Ubiquitination	PQISQPAKLAEAFKY CCCCCHHHHHHHHHH	55.71	-
307	Phosphorylation	KLAEAFKYFVQGMGY HHHHHHHHHHHCCCC	11.52	22817900
314	Phosphorylation	YFVQGMGYMPSASMT HHHHCCCCCCCHHHH	9.28	22817900
317	Phosphorylation	QGMGYMPSASMTRLM HCCCCCCCHHHHHHH	19.22	26239621
319	Phosphorylation	MGYMPSASMTRLMRS CCCCCCHHHHHHHHC	25.64	26239621
321	Phosphorylation	YMPSASMTRLMRSRT CCCCHHHHHHHHCCC	20.39	26239621
326	Phosphorylation	SMTRLMRSRTASGSS HHHHHHHCCCCCCCC	21.73	27087446
328	Phosphorylation	TRLMRSRTASGSSVT HHHHHCCCCCCCCCC	26.82	24925903
330	Phosphorylation	LMRSRTASGSSVTSL HHHCCCCCCCCCCCE	38.30	24925903
332	Phosphorylation	RSRTASGSSVTSLEG HCCCCCCCCCCCEEE	21.09	24925903
333	Phosphorylation	SRTASGSSVTSLEGT CCCCCCCCCCCEEEC	32.70	25521595
335	Phosphorylation	TASGSSVTSLEGTRS CCCCCCCCCEEECCC	29.55	24925903
336	Phosphorylation	ASGSSVTSLEGTRSR CCCCCCCCEEECCCC	23.44	25521595
340	Phosphorylation	SVTSLEGTRSRSHTS CCCCEEECCCCCCCC	18.98	24925903
342	Phosphorylation	TSLEGTRSRSHTSEG CCEEECCCCCCCCCC	37.66	25521595
344	Phosphorylation	LEGTRSRSHTSEGPR EEECCCCCCCCCCCC	32.15	27087446
346	Phosphorylation	GTRSRSHTSEGPRSR ECCCCCCCCCCCCCC	29.71	27087446
347	Phosphorylation	TRSRSHTSEGPRSRS CCCCCCCCCCCCCCC	34.82	25266776
352	Phosphorylation	HTSEGPRSRSHTSEG CCCCCCCCCCCCCCC	41.07	26824392
354	Phosphorylation	SEGPRSRSHTSEGSR CCCCCCCCCCCCCCC	32.15	25266776
356	Phosphorylation	GPRSRSHTSEGSRSR CCCCCCCCCCCCCCC	29.71	18347057
357	Phosphorylation	PRSRSHTSEGSRSRS CCCCCCCCCCCCCCC	34.24	22817900
360	Phosphorylation	RSHTSEGSRSRSHTS CCCCCCCCCCCCCCC	24.03	25266776
362	Phosphorylation	HTSEGSRSRSHTSED CCCCCCCCCCCCCCC	39.57	26824392
364	Phosphorylation	SEGSRSRSHTSEDAR CCCCCCCCCCCCCCC	32.15	25168779
366	Phosphorylation	GSRSRSHTSEDARLN CCCCCCCCCCCCCCC	34.75	26824392
367	Phosphorylation	SRSRSHTSEDARLNI CCCCCCCCCCCCCCC	28.23	25168779
375	Phosphorylation	EDARLNITPNSGATG CCCCCCCCCCCCCCC	18.49	26824392
378	Phosphorylation	RLNITPNSGATGNNA CCCCCCCCCCCCCCC	30.89	20531401
381	Phosphorylation	ITPNSGATGNNAGPK CCCCCCCCCCCCCCC	43.92	25619855
389	Phosphorylation	GNNAGPKSMEVSC-- CCCCCCCCCCCCC--	24.25	25521595
393	Phosphorylation	GPKSMEVSC------ CCCCCCCCC------	10.78	25521595

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
330	S	Phosphorylation	Kinase	SGK1	Q9WVC6	Uniprot
332	S	Phosphorylation	Kinase	SGK1	Q9WVC6	GPS
346	T	Phosphorylation	Kinase	SGK1	Q9WVC6	Uniprot
356	T	Phosphorylation	Kinase	SGK1	Q9WVC6	Uniprot
366	T	Phosphorylation	Kinase	SGK1	Q9WVC6	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of NDRG1_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 NDRG1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of NDRG1_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of NDRG1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-2; THR-346 AND SER-362,AND MASS SPECTROMETRY.	19367708 [Abstract]
"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 THR-328; SER-330; THR-335AND SER-336, AND MASS SPECTROMETRY.	17242355 [Abstract]
"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 SER-330; SER-332 AND THR-346, SUBCELLULAR LOCATION,TISSUE SPECIFICITY, AND MASS SPECTROMETRY.	15461589 [Abstract]