NDE1_MOUSE - dbPTM
NDE1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NDE1_MOUSE
UniProt AC Q9CZA6
Protein Name Nuclear distribution protein nudE homolog 1
Gene Name Nde1
Organism Mus musculus (Mouse).
Sequence Length 344
Subcellular Localization Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. Chromosome, centromere, kinetochore. 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 MEDSGKTFESEEEETNYWRDLAMTYKQRAENTQEELREFQEGSREYEAELEAQLQQIETRNRDLLSENNRLRMELESVKEKFEMQHSEGYRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQDKPRTPMPGSGQAKRTDMAVQATGSVPSTPVAHRGPSSGLNTPGMFRRGLDSSTSGTPLTPAARISALNIVGDLLRKVGALESKLASCRNFMYDQSPSRTSGPASGRGTKNRDGVDRRPGSTSVGDKGSGKRLEFGKPASEPASPALPSAQGVVKLLL
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
7Phosphorylation-MEDSGKTFESEEEE
-CCCCCCCCCCHHHH
35.8426643407
10PhosphorylationDSGKTFESEEEETNY
CCCCCCCCHHHHHHH
46.2326643407
15PhosphorylationFESEEEETNYWRDLA
CCCHHHHHHHHHHHH
36.5730635358
17PhosphorylationSEEEETNYWRDLAMT
CHHHHHHHHHHHHHH
14.8330635358
90PhosphorylationEMQHSEGYRQISALE
HHHHCHHHHHHHHHH
8.69-
211PhosphorylationMAVQATGSVPSTPVA
EEEEECCCCCCCCCC
26.8819060867
214PhosphorylationQATGSVPSTPVAHRG
EECCCCCCCCCCCCC
43.0921183079
215PhosphorylationATGSVPSTPVAHRGP
ECCCCCCCCCCCCCC
18.7319060867
223PhosphorylationPVAHRGPSSGLNTPG
CCCCCCCCCCCCCCC
39.6028066266
224PhosphorylationVAHRGPSSGLNTPGM
CCCCCCCCCCCCCCH
50.8928066266
228PhosphorylationGPSSGLNTPGMFRRG
CCCCCCCCCCHHHCC
26.6826824392
238PhosphorylationMFRRGLDSSTSGTPL
HHHCCCCCCCCCCCC
40.3324759943
239PhosphorylationFRRGLDSSTSGTPLT
HHCCCCCCCCCCCCC
26.6823984901
240PhosphorylationRRGLDSSTSGTPLTP
HCCCCCCCCCCCCCH
34.8223984901
241PhosphorylationRGLDSSTSGTPLTPA
CCCCCCCCCCCCCHH
42.4923984901
243PhosphorylationLDSSTSGTPLTPAAR
CCCCCCCCCCCHHHH
18.2022817900
246PhosphorylationSTSGTPLTPAARISA
CCCCCCCCHHHHHHH
16.4621082442
274S-palmitoylationLESKLASCRNFMYDQ
HHHHHHHCCCCCCCC
3.24-
278OxidationLASCRNFMYDQSPSR
HHHCCCCCCCCCCCC
4.0417242355
279PhosphorylationASCRNFMYDQSPSRT
HHCCCCCCCCCCCCC
13.4929895711
282PhosphorylationRNFMYDQSPSRTSGP
CCCCCCCCCCCCCCC
23.1926824392
284PhosphorylationFMYDQSPSRTSGPAS
CCCCCCCCCCCCCCC
54.1329895711
291PhosphorylationSRTSGPASGRGTKNR
CCCCCCCCCCCCCCC
31.9629514104
293MethylationTSGPASGRGTKNRDG
CCCCCCCCCCCCCCC
47.3058858713
295PhosphorylationGPASGRGTKNRDGVD
CCCCCCCCCCCCCCC
24.6423832136
307PhosphorylationGVDRRPGSTSVGDKG
CCCCCCCCCCCCCCC
21.8620139300
307 (in isoform 3)Phosphorylation-21.8619854140
308PhosphorylationVDRRPGSTSVGDKGS
CCCCCCCCCCCCCCC
33.0920139300
308 (in isoform 3)Phosphorylation-33.0919854140
309PhosphorylationDRRPGSTSVGDKGSG
CCCCCCCCCCCCCCC
26.2920139300
315PhosphorylationTSVGDKGSGKRLEFG
CCCCCCCCCCCCCCC
47.0520139300
315 (in isoform 3)Phosphorylation-47.0519854140
326PhosphorylationLEFGKPASEPASPAL
CCCCCCCCCCCCCCC
53.2726824392
330PhosphorylationKPASEPASPALPSAQ
CCCCCCCCCCCCCCC
22.7826824392
335PhosphorylationPASPALPSAQGVVKL
CCCCCCCCCCCHHHH
33.7928066266

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
90YPhosphorylationKinaseFGFR1P11362
PSP
279YPhosphorylationKinaseFGFR1P11362
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
246TPhosphorylation

21529751

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_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LIS1_HUMANPAFAH1B1physical
11163258
LIS1_MOUSEPafah1b1physical
11163258
LIS1_HUMANPAFAH1B1physical
20360068
DIXC1_HUMANDIXDC1physical
20360068
NDEL1_HUMANNDEL1physical
20360068
SYNE1_HUMANSYNE1physical
20360068
NDE1_HUMANNDE1physical
20360068
CCSE2_HUMANCCSER2physical
20360068
RFA2_HUMANRPA2physical
20360068
DYL1_MOUSEDynll1physical
21911489
DC1I1_MOUSEDync1i1physical
21911489
SMC3_MOUSESmc3physical
25245017
SMC1A_MOUSESmc1aphysical
25245017
RAD21_MOUSERad21physical
25245017
SMCA5_MOUSESmarca5physical
25245017
P53_MOUSETrp53genetic
25245017

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NDE1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Human mutations in NDE1 cause extreme microcephaly withlissencephaly.";
Alkuraya F.S., Cai X., Emery C., Mochida G.H., Al-Dosari M.S.,Felie J.M., Hill R.S., Barry B.J., Partlow J.N., Gascon G.G.,Kentab A., Jan M., Shaheen R., Feng Y., Walsh C.A.;
Am. J. Hum. Genet. 88:536-547(2011).
Cited for: PHOSPHORYLATION AT THR-246.
"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-246, AND MASSSPECTROMETRY.

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