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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
7 | Phosphorylation | -MEDSGKTFESEEEE -CCCCCCCCCCHHHH | 35.84 | 26643407 | |
10 | Phosphorylation | DSGKTFESEEEETNY CCCCCCCCHHHHHHH | 46.23 | 26643407 | |
15 | Phosphorylation | FESEEEETNYWRDLA CCCHHHHHHHHHHHH | 36.57 | 30635358 | |
17 | Phosphorylation | SEEEETNYWRDLAMT CHHHHHHHHHHHHHH | 14.83 | 30635358 | |
90 | Phosphorylation | EMQHSEGYRQISALE HHHHCHHHHHHHHHH | 8.69 | - | |
211 | Phosphorylation | MAVQATGSVPSTPVA EEEEECCCCCCCCCC | 26.88 | 19060867 | |
214 | Phosphorylation | QATGSVPSTPVAHRG EECCCCCCCCCCCCC | 43.09 | 21183079 | |
215 | Phosphorylation | ATGSVPSTPVAHRGP ECCCCCCCCCCCCCC | 18.73 | 19060867 | |
223 | Phosphorylation | PVAHRGPSSGLNTPG CCCCCCCCCCCCCCC | 39.60 | 28066266 | |
224 | Phosphorylation | VAHRGPSSGLNTPGM CCCCCCCCCCCCCCH | 50.89 | 28066266 | |
228 | Phosphorylation | GPSSGLNTPGMFRRG CCCCCCCCCCHHHCC | 26.68 | 26824392 | |
238 | Phosphorylation | MFRRGLDSSTSGTPL HHHCCCCCCCCCCCC | 40.33 | 24759943 | |
239 | Phosphorylation | FRRGLDSSTSGTPLT HHCCCCCCCCCCCCC | 26.68 | 23984901 | |
240 | Phosphorylation | RRGLDSSTSGTPLTP HCCCCCCCCCCCCCH | 34.82 | 23984901 | |
241 | Phosphorylation | RGLDSSTSGTPLTPA CCCCCCCCCCCCCHH | 42.49 | 23984901 | |
243 | Phosphorylation | LDSSTSGTPLTPAAR CCCCCCCCCCCHHHH | 18.20 | 22817900 | |
246 | Phosphorylation | STSGTPLTPAARISA CCCCCCCCHHHHHHH | 16.46 | 21082442 | |
274 | S-palmitoylation | LESKLASCRNFMYDQ HHHHHHHCCCCCCCC | 3.24 | - | |
278 | Oxidation | LASCRNFMYDQSPSR HHHCCCCCCCCCCCC | 4.04 | 17242355 | |
279 | Phosphorylation | ASCRNFMYDQSPSRT HHCCCCCCCCCCCCC | 13.49 | 29895711 | |
282 | Phosphorylation | RNFMYDQSPSRTSGP CCCCCCCCCCCCCCC | 23.19 | 26824392 | |
284 | Phosphorylation | FMYDQSPSRTSGPAS CCCCCCCCCCCCCCC | 54.13 | 29895711 | |
291 | Phosphorylation | SRTSGPASGRGTKNR CCCCCCCCCCCCCCC | 31.96 | 29514104 | |
293 | Methylation | TSGPASGRGTKNRDG CCCCCCCCCCCCCCC | 47.30 | 58858713 | |
295 | Phosphorylation | GPASGRGTKNRDGVD CCCCCCCCCCCCCCC | 24.64 | 23832136 | |
307 | Phosphorylation | GVDRRPGSTSVGDKG CCCCCCCCCCCCCCC | 21.86 | 20139300 | |
307 (in isoform 3) | Phosphorylation | - | 21.86 | 19854140 | |
308 | Phosphorylation | VDRRPGSTSVGDKGS CCCCCCCCCCCCCCC | 33.09 | 20139300 | |
308 (in isoform 3) | Phosphorylation | - | 33.09 | 19854140 | |
309 | Phosphorylation | DRRPGSTSVGDKGSG CCCCCCCCCCCCCCC | 26.29 | 20139300 | |
315 | Phosphorylation | TSVGDKGSGKRLEFG CCCCCCCCCCCCCCC | 47.05 | 20139300 | |
315 (in isoform 3) | Phosphorylation | - | 47.05 | 19854140 | |
326 | Phosphorylation | LEFGKPASEPASPAL CCCCCCCCCCCCCCC | 53.27 | 26824392 | |
330 | Phosphorylation | KPASEPASPALPSAQ CCCCCCCCCCCCCCC | 22.78 | 26824392 | |
335 | Phosphorylation | PASPALPSAQGVVKL CCCCCCCCCCCHHHH | 33.79 | 28066266 |
Modified Location | Modified Residue | Modification | Function | Reference |
---|---|---|---|---|
246 | T | Phosphorylation |
| 21529751 |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
LIS1_HUMAN | PAFAH1B1 | physical | 11163258 | |
LIS1_MOUSE | Pafah1b1 | physical | 11163258 | |
LIS1_HUMAN | PAFAH1B1 | physical | 20360068 | |
DIXC1_HUMAN | DIXDC1 | physical | 20360068 | |
NDEL1_HUMAN | NDEL1 | physical | 20360068 | |
SYNE1_HUMAN | SYNE1 | physical | 20360068 | |
NDE1_HUMAN | NDE1 | physical | 20360068 | |
CCSE2_HUMAN | CCSER2 | physical | 20360068 | |
RFA2_HUMAN | RPA2 | physical | 20360068 | |
DYL1_MOUSE | Dynll1 | physical | 21911489 | |
DC1I1_MOUSE | Dync1i1 | physical | 21911489 | |
SMC3_MOUSE | Smc3 | physical | 25245017 | |
SMC1A_MOUSE | Smc1a | physical | 25245017 | |
RAD21_MOUSE | Rad21 | physical | 25245017 | |
SMCA5_MOUSE | Smarca5 | physical | 25245017 | |
P53_MOUSE | Trp53 | genetic | 25245017 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"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. |