NDEL1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NDEL1_MOUSE
• UniProt AC: Q9ERR1
• Protein Name: Nuclear distribution protein nudE-like 1
• Gene Name: Ndel1
• Organism: Mus musculus (Mouse).
• Sequence Length: 345
• Subcellular Localization: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton, spindle. Localizes to the kinetochore in a CENPF-dependent manner. Colocalizes with DISC1 in th
• Protein Description: Required for organization of the cellular microtubule array and microtubule anchoring at the centrosome. May regulate microtubule organization at least in part by targeting the microtubule severing protein KATNA1 to the centrosome. Also positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus ends. Required for several dynein- and microtubule-dependent processes such as the maintenance of Golgi integrity, the centripetal motion of secretory vesicles and the coupling of the nucleus and centrosome. Also required during brain development for the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. Plays a role, together with DISC1, in the regulation of neurite outgrowth. Required for mitosis in some cell types but appears to be dispensible for mitosis in cortical neuronal progenitors, which instead requires NDE1. Facilitates the polymerization of neurofilaments from the individual subunits NEFH and NEFL. Positively regulates lysosome peripheral distribution and ruffled border formation in osteoclasts. [PubMed: 27777970]
• Protein Sequence: MDGEDIPDFSSLKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRERQQEVTRKSAPSSPTLDCEKMDSAVQASLSLPATPVGKGTENSFPSPKAIPNGFGTSPLTPSARISALNIVGDLLRKVGALESKLAACRNFAKDQASRKSYVPGSVNCGVMNSNGPECPRSGRATFFHKGAVNGFDPAPPPPGLGSSRPSSAPGMLPLSV

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
74	Phosphorylation	ADNQRLKYEVEALKE HHHHHHHHHHHHHHH	29.78	29472430
87	Phosphorylation	KEKLEHQYAQSYKQV HHHHHHHHHHHHHHH	14.44	-
155	Phosphorylation	ERNAFLESELDEKES HHHCCHHHHCCHHHH	45.68	-
162	Phosphorylation	SELDEKESLLVSVQR HHCCHHHHHHHHHHH	37.76	-
166	Phosphorylation	EKESLLVSVQRLKDE HHHHHHHHHHHHHHH	16.71	-
191	Phosphorylation	RERQQEVTRKSAPSS HHHHHHHHHHCCCCC	31.46	22817900
194	Phosphorylation	QQEVTRKSAPSSPTL HHHHHHHCCCCCCCC	41.96	25521595
197	Phosphorylation	VTRKSAPSSPTLDCE HHHHCCCCCCCCCHH	48.98	27087446
198	Phosphorylation	TRKSAPSSPTLDCEK HHHCCCCCCCCCHHH	22.35	25521595
200	Phosphorylation	KSAPSSPTLDCEKMD HCCCCCCCCCHHHHC	36.86	25521595
208	Phosphorylation	LDCEKMDSAVQASLS CCHHHHCHHHHHHHC	27.17	25619855
213	Phosphorylation	MDSAVQASLSLPATP HCHHHHHHHCCCCCC	11.03	25619855
215	Phosphorylation	SAVQASLSLPATPVG HHHHHHHCCCCCCCC	29.79	25521595
219	Phosphorylation	ASLSLPATPVGKGTE HHHCCCCCCCCCCCC	19.30	25521595
228	Phosphorylation	VGKGTENSFPSPKAI CCCCCCCCCCCCCCC	32.10	25777480
231	Phosphorylation	GTENSFPSPKAIPNG CCCCCCCCCCCCCCC	36.70	25521595
241	Phosphorylation	AIPNGFGTSPLTPSA CCCCCCCCCCCCHHH	25.55	24759943
242	Phosphorylation	IPNGFGTSPLTPSAR CCCCCCCCCCCHHHH	20.49	23527152
245	Phosphorylation	GFGTSPLTPSARISA CCCCCCCCHHHHHHH	20.69	22817900
251	Phosphorylation	LTPSARISALNIVGD CCHHHHHHHHHHHHH	22.58	17060449
273	S-palmitoylation	LESKLAACRNFAKDQ HHHHHHHHHHHHCCH	2.80	-
335	Phosphorylation	GLGSSRPSSAPGMLP CCCCCCCCCCCCCCC	37.71	29472430
336	Phosphorylation	LGSSRPSSAPGMLPL CCCCCCCCCCCCCCC	40.96	29472430
344	Phosphorylation	APGMLPLSV------ CCCCCCCCC------	24.68	28066266

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
198	S	Phosphorylation	Kinase	CDK5	P49615	PhosphoELM
198	S	Phosphorylation	Kinase	CDK5	Q00535	PSP
219	T	Phosphorylation	Kinase	MAPK3	Q63844	GPS
219	T	Phosphorylation	Kinase	MAPK1	P63085	GPS
219	T	Phosphorylation	Kinase	CDK5	P49615	PhosphoELM
219	T	Phosphorylation	Kinase	CDK5	Q00535	PSP
231	S	Phosphorylation	Kinase	CDK5	Q00535	PSP
231	S	Phosphorylation	Kinase	CDK5	P49615	PhosphoELM
242	S	Phosphorylation	Kinase	CDK5	P49615	PhosphoELM
242	S	Phosphorylation	Kinase	CDK1	P11440	Uniprot
245	T	Phosphorylation	Kinase	CDK5	P49615	PhosphoELM
245	T	Phosphorylation	Kinase	CDK1	P11440	Uniprot
245	T	Phosphorylation	Kinase	MAPK1	P63085	Uniprot
251	S	Phosphorylation	Kinase	AURKA	O14965	GPS
332	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
336	S	Phosphorylation	Kinase	DYRK2	Q92630	PSP
336	S	Phosphorylation	Kinase	DYRK2	Q5U4C9	PSP
336	S	Phosphorylation	Kinase	HIPK4	Q3V016	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
273	C	Palmitoylation	Palmitoylation at Cys-273 reduces affinity for dynein.	-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of NDEL1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NFL_MOUSE	Nefl	physical	15208636
NFH_MOUSE	Nefh	physical	15208636
LIS1_MOUSE	Pafah1b1	physical	15208636
DYHC1_MOUSE	Dync1h1	physical	15208636
DCTN1_MOUSE	Dctn1	physical	15208636
DC1I1_MOUSE	Dync1i1	physical	18331715
DYHC1_MOUSE	Dync1h1	physical	18331715
RHG01_MOUSE	Arhgap1	physical	18331715
LIS1_MOUSE	Pafah1b1	physical	18331715
1433E_MOUSE	Ywhae	physical	18331715
TBA1A_MOUSE	Tuba1a	physical	18331715
TBB1_MOUSE	Tubb1	physical	18331715
BASI_HUMAN	BSG	physical	26496610
LIS1_HUMAN	PAFAH1B1	physical	26496610
VEZF1_HUMAN	VEZF1	physical	26496610
OGT1_HUMAN	OGT	physical	26496610
TRI29_HUMAN	TRIM29	physical	26496610
S43A3_HUMAN	SLC43A3	physical	26496610
CCSE2_HUMAN	CCSER2	physical	26496610
NDE1_HUMAN	NDE1	physical	26496610
S12A9_HUMAN	SLC12A9	physical	26496610
FAKD5_HUMAN	FASTKD5	physical	26496610
PCGF6_HUMAN	PCGF6	physical	26496610
DIXC1_HUMAN	DIXDC1	physical	26496610
C1QT6_HUMAN	C1QTNF6	physical	26496610
PGM2L_HUMAN	PGM2L1	physical	26496610

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"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 SER-215 AND THR-219, ANDMASS SPECTROMETRY.
PubMed: 17242355