dbPTM

NDE1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NDE1_HUMAN
UniProt AC	Q9NXR1
Protein Name	Nuclear distribution protein nudE homolog 1
Gene Name	NDE1
Organism	Homo sapiens (Human).
Sequence Length	335
Subcellular Localization	Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton, spindle. Cleavage furrow. Localizes to the interphase and S phase centrosome. During mitosis, p
Protein Description	Required for centrosome duplication and formation and function of the mitotic spindle. Essential for the development of the cerebral cortex. May regulate the production of neurons by controlling the orientation of the mitotic spindle during division of cortical neuronal progenitors of the proliferative ventricular zone of the brain. Orientation of the division plane perpendicular to the layers of the cortex gives rise to two proliferative neuronal progenitors whereas parallel orientation of the division plane yields one proliferative neuronal progenitor and a post-mitotic neuron. A premature shift towards a neuronal fate within the progenitor population may result in an overall reduction in the final number of neurons and an increase in the number of neurons in the deeper layers of the cortex..
Protein Sequence	MEDSGKTFSSEEEEANYWKDLAMTYKQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQEKPRTPMPSSVEAERTDTAVQATGSVPSTPIAHRGPSSSLNTPGSFRRGLDDSTGGTPLTPAARISALNIVGDLLRKVGALESKLASCRNLVYDQSPNRTGGPASGRSSKNRDGGERRPSSTSVPLGDKGLDTSCRWLSKSTTRSSSSC

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MEDSGKTFSSE ----CCCCCCCCCCH	28.96	28450419
7	Phosphorylation	-MEDSGKTFSSEEEE -CCCCCCCCCCHHHH	32.07	23663014
9	Phosphorylation	EDSGKTFSSEEEEAN CCCCCCCCCHHHHHH	41.91	25159151
10	Phosphorylation	DSGKTFSSEEEEANY CCCCCCCCHHHHHHH	44.85	25159151
131	Phosphorylation	LERAKRATIMSLEDF HHHHHHHHHCCHHHH	22.65	21677187
133	Sulfoxidation	RAKRATIMSLEDFEQ HHHHHHHCCHHHHHH	3.04	21406390
154	Phosphorylation	ERNAFLESELDEKEN HHHHHHHHHHHHHHH	45.68	-
165	Phosphorylation	EKENLLESVQRLKDE HHHHHHHHHHHHHHH	24.42	25159151
191	Phosphorylation	QKQEKPRTPMPSSVE HHHCCCCCCCCCCCE	32.25	29255136
193	Sulfoxidation	QEKPRTPMPSSVEAE HCCCCCCCCCCCEEC	5.06	21406390
195	Phosphorylation	KPRTPMPSSVEAERT CCCCCCCCCCEECCC	40.54	20068231
196	Phosphorylation	PRTPMPSSVEAERTD CCCCCCCCCEECCCC	20.36	21815630
202	Phosphorylation	SSVEAERTDTAVQAT CCCEECCCCCCCHHC	29.25	25850435
204	Phosphorylation	VEAERTDTAVQATGS CEECCCCCCCHHCCC	28.28	25850435
209	Phosphorylation	TDTAVQATGSVPSTP CCCCCHHCCCCCCCC	16.95	30266825
211 (in isoform 2)	Phosphorylation	-	26.88	18220336
211	Phosphorylation	TAVQATGSVPSTPIA CCCHHCCCCCCCCCC	26.88	30266825
214	Phosphorylation	QATGSVPSTPIAHRG HHCCCCCCCCCCCCC	44.66	30266825
215 (in isoform 2)	Phosphorylation	-	16.79	18220336
215	Phosphorylation	ATGSVPSTPIAHRGP HCCCCCCCCCCCCCC	16.79	25159151
223	Phosphorylation	PIAHRGPSSSLNTPG CCCCCCCCCCCCCCC	35.07	23403867
224	Phosphorylation	IAHRGPSSSLNTPGS CCCCCCCCCCCCCCC	41.81	25159151
225	Phosphorylation	AHRGPSSSLNTPGSF CCCCCCCCCCCCCCC	29.94	23403867
228	Phosphorylation	GPSSSLNTPGSFRRG CCCCCCCCCCCCCCC	34.03	25159151
228 (in isoform 2)	Phosphorylation	-	34.03	18220336
231	Phosphorylation	SSLNTPGSFRRGLDD CCCCCCCCCCCCCCC	19.45	23401153
239	Phosphorylation	FRRGLDDSTGGTPLT CCCCCCCCCCCCCCC	28.72	23401153
240	Phosphorylation	RRGLDDSTGGTPLTP CCCCCCCCCCCCCCH	46.77	30266825
243	Phosphorylation	LDDSTGGTPLTPAAR CCCCCCCCCCCHHHH	19.23	30266825
246	Phosphorylation	STGGTPLTPAARISA CCCCCCCCHHHHHHH	16.46	30266825
252	Phosphorylation	LTPAARISALNIVGD CCHHHHHHHHHHHHH	22.58	28348404
270	Ubiquitination	KVGALESKLASCRNL HHCHHHHHHHHHHHC	38.40	-
273	Phosphorylation	ALESKLASCRNLVYD HHHHHHHHHHHCCCC	24.85	26074081
274	S-palmitoylation	LESKLASCRNLVYDQ HHHHHHHHHHCCCCC	2.51	19927128
279	Phosphorylation	ASCRNLVYDQSPNRT HHHHHCCCCCCCCCC	16.07	21945579
282	Phosphorylation	RNLVYDQSPNRTGGP HHCCCCCCCCCCCCC	22.65	19664994
286	Phosphorylation	YDQSPNRTGGPASGR CCCCCCCCCCCCCCC	53.80	22199227
291	Phosphorylation	NRTGGPASGRSSKNR CCCCCCCCCCCCCCC	37.56	30576142
294	Phosphorylation	GGPASGRSSKNRDGG CCCCCCCCCCCCCCC	49.54	21712546
306	Phosphorylation	DGGERRPSSTSVPLG CCCCCCCCCCCCCCC	44.42	29255136
306 (in isoform 2)	Phosphorylation	-	44.42	25849741
307	Phosphorylation	GGERRPSSTSVPLGD CCCCCCCCCCCCCCC	27.64	27273156
307 (in isoform 2)	Phosphorylation	-	27.64	25159151
308	Phosphorylation	GERRPSSTSVPLGDK CCCCCCCCCCCCCCC	37.77	30266825
308 (in isoform 2)	Phosphorylation	-	37.77	23927012
309	Phosphorylation	ERRPSSTSVPLGDKG CCCCCCCCCCCCCCC	24.56	30266825
309 (in isoform 2)	Phosphorylation	-	24.56	25627689
320 (in isoform 2)	Phosphorylation	-	37.34	25159151
328	Phosphorylation	CRWLSKSTTRSSSSC CHHHCCCCCCCCCCC	40.11	20068231
329 (in isoform 2)	Phosphorylation	-	26.39	24719451
331	Phosphorylation	LSKSTTRSSSSC--- HCCCCCCCCCCC---	23.41	27732954
332	Phosphorylation	SKSTTRSSSSC---- CCCCCCCCCCC----	28.53	25159151
333	Phosphorylation	KSTTRSSSSC----- CCCCCCCCCC-----	24.13	20068231
337	Phosphorylation	RSSSSC--------- CCCCCC---------	40.69	27732954

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
131	T	Phosphorylation	Kinase	PRKACA	P17612	GPS
191	T	Phosphorylation	Kinase	CDK1	P06493	PSP
191	T	Phosphorylation	Kinase	CDK5	Q00535	PSP
215	T	Phosphorylation	Kinase	CDK1	P06493	PSP
228	T	Phosphorylation	Kinase	CDK1	P06493	PSP
228	T	Phosphorylation	Kinase	CDK2	P24941	PSP
243	T	Phosphorylation	Kinase	CDK1	P06493	PSP
246	T	Phosphorylation	Kinase	CDK1	P06493	PSP
282	S	Phosphorylation	Kinase	CDK1	P06493	PSP
306	S	Phosphorylation	Kinase	PRKACA	P17612	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
246	T	Phosphorylation		16682949
Phosphorylation at Thr-246 is essential for the G2/M transition (By similarity).

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 NDE1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LIS1_HUMAN	PAFAH1B1	physical	10931877
NDEL1_HUMAN	NDEL1	physical	24722188
ANDR_HUMAN	AR	physical	24722188
ARNT2_HUMAN	ARNT2	physical	24722188
RIMB1_HUMAN	BZRAP1	physical	24722188
NDE1_HUMAN	NDE1	physical	24722188
FAM9B_HUMAN	FAM9B	physical	24722188
GOGA2_HUMAN	GOLGA2	physical	24722188
HXA2_HUMAN	HOXA2	physical	24722188
LZTS2_HUMAN	LZTS2	physical	24722188
MED4_HUMAN	MED4	physical	24722188
MKRN3_HUMAN	MKRN3	physical	24722188
NDC80_HUMAN	NDC80	physical	24722188
REL_HUMAN	REL	physical	24722188
TFP11_HUMAN	TFIP11	physical	24722188
TRI27_HUMAN	TRIM27	physical	24722188
TTC1_HUMAN	TTC1	physical	24722188
UBQL1_HUMAN	UBQLN1	physical	24722188
USBP1_HUMAN	USHBP1	physical	24722188
WAC_HUMAN	WAC	physical	24722188
ZN398_HUMAN	ZNF398	physical	24722188
DCA13_HUMAN	DCAF13	physical	26496610
MTNB_HUMAN	APIP	physical	26496610
AMZ2_HUMAN	AMZ2	physical	26496610
CLP1L_HUMAN	CLPTM1L	physical	26496610
LIS1_HUMAN	PAFAH1B1	physical	27173435

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614019	Lissencephaly 4 (LIS4)
605013	Microhydranencephaly (MHAC)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of NDE1_HUMAN

Related Literatures of Post-Translational Modification

Palmitoylation
Reference	PubMed
"Ndel1 palmitoylation: a new mean to regulate cytoplasmic dyneinactivity."; Shmueli A., Segal M., Sapir T., Tsutsumi R., Noritake J., Bar A.,Sapoznik S., Fukata Y., Orr I., Fukata M., Reiner O.; EMBO J. 29:107-119(2010). Cited for: PALMITOYLATION AT CYS-274 BY ZDHHC2; ZDHHC3 AND ZDHHC7.	19927128 [Abstract]
Phosphorylation
Reference	PubMed
"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-282, AND MASSSPECTROMETRY.	19690332 [Abstract]
"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-211; THR-215; THR-228;SER-231; SER-239; THR-240; THR-243; THR-246 AND SER-282, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211; THR-215 ANDTHR-228, AND MASS SPECTROMETRY.	18220336 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306 AND SER-307, ANDMASS SPECTROMETRY.	17287340 [Abstract]
"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-282, AND MASSSPECTROMETRY.	16964243 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-279, AND MASSSPECTROMETRY.	15592455 [Abstract]

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