dbPTM

NDEL1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NDEL1_HUMAN
UniProt AC	Q9GZM8
Protein Name	Nuclear distribution protein nudE-like 1
Gene Name	NDEL1
Organism	Homo sapiens (Human).
Sequence Length	345
Subcellular Localization	Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton, spindle. Localizes to the cell body of the motor neurons and colocalizes with assembled neurofi
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 (By similarity)..
Protein Sequence	MDGEDIPDFSSLKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRERQQEVTRKSAPSSPTLDCEKMDSAVQASLSLPATPVGKGTENTFPSPKAIPNGFGTSPLTPSARISALNIVGDLLRKVGALESKLAACRNFAKDQASRKSYISGNVNCGVLNGNGTKFSRSGHTSFFDKGAVNGFDPAPPPPGLGSSRPSSAPGMLPLSV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
10	Phosphorylation	GEDIPDFSSLKEETA CCCCCCHHHHHHHHH	41.98	27251275
11	Phosphorylation	EDIPDFSSLKEETAY CCCCCHHHHHHHHHH	43.38	27251275
44	Phosphorylation	LVEFQEGSRELEAEL HHHHHHHCHHHHHHH	23.10	25159151
74	Phosphorylation	ADNQRLKYEVEALKE HHHHHHHHHHHHHHH	29.78	30266825
87	Phosphorylation	KEKLEHQYAQSYKQV HHHHHHHHHHHHHHH	14.44	-
114	Phosphorylation	IKEQLHKYVRELEQA HHHHHHHHHHHHHHC	8.26	29978859
132	Phosphorylation	LERAKRATIVSLEDF HHHHHHHEEEEHHHH	26.41	21677187
135	Phosphorylation	AKRATIVSLEDFEQR HHHHEEEEHHHHHHH	23.38	-
155	Phosphorylation	ERNAFLESELDEKES HHHCCHHHHCCHHHH	45.68	-
166	Phosphorylation	EKESLLVSVQRLKDE HHHHHHHHHHHHHHH	16.71	28555341
191	Phosphorylation	RERQQEVTRKSAPSS HHHHHHHHHCCCCCC	31.46	26074081
194	Phosphorylation	QQEVTRKSAPSSPTL HHHHHHCCCCCCCCC	41.96	29255136
197	Phosphorylation	VTRKSAPSSPTLDCE HHHCCCCCCCCCCHH	48.98	29255136
198	Phosphorylation	TRKSAPSSPTLDCEK HHCCCCCCCCCCHHH	22.35	29255136
200	Phosphorylation	KSAPSSPTLDCEKMD CCCCCCCCCCHHHHC	36.86	29255136
208	Phosphorylation	LDCEKMDSAVQASLS CCHHHHCHHHHHHHC	27.17	22199227
213	Phosphorylation	MDSAVQASLSLPATP HCHHHHHHHCCCCCC	11.03	29255136
215	Phosphorylation	SAVQASLSLPATPVG HHHHHHHCCCCCCCC	29.79	28355574
219	Phosphorylation	ASLSLPATPVGKGTE HHHCCCCCCCCCCCC	19.30	29255136
228	Phosphorylation	VGKGTENTFPSPKAI CCCCCCCCCCCCCCC	30.59	30266825
231	Phosphorylation	GTENTFPSPKAIPNG CCCCCCCCCCCCCCC	34.54	30266825
241	Phosphorylation	AIPNGFGTSPLTPSA CCCCCCCCCCCCHHH	25.55	21712546
242	Phosphorylation	IPNGFGTSPLTPSAR CCCCCCCCCCCHHHH	20.49	25159151
245	Phosphorylation	GFGTSPLTPSARISA CCCCCCCCHHHHHHH	20.69	25159151
247	Phosphorylation	GTSPLTPSARISALN CCCCCCHHHHHHHHH	25.58	22199227
251	Phosphorylation	LTPSARISALNIVGD CCHHHHHHHHHHHHH	22.58	28348404
262	Acetylation	IVGDLLRKVGALESK HHHHHHHHHCHHHHH	45.02	26210075
269	Ubiquitination	KVGALESKLAACRNF HHCHHHHHHHHHHHH	32.54	-
269 (in isoform 2)	Ubiquitination	-	32.54	-
273	S-palmitoylation	LESKLAACRNFAKDQ HHHHHHHHHHHHCCH	2.80	19927128
278	Ubiquitination	AACRNFAKDQASRKS HHHHHHHCCHHHCHH	46.35	-
282	Phosphorylation	NFAKDQASRKSYISG HHHCCHHHCHHHHCC	34.31	-
286	Phosphorylation	DQASRKSYISGNVNC CHHHCHHHHCCCCCE	11.35	28555341
301	Phosphorylation	GVLNGNGTKFSRSGH EEECCCCCCCCCCCC	32.68	-
306	Phosphorylation	NGTKFSRSGHTSFFD CCCCCCCCCCCCCCC	33.46	25159151
310	Phosphorylation	FSRSGHTSFFDKGAV CCCCCCCCCCCCCCC	20.45	28555341
331	Phosphorylation	PPPPGLGSSRPSSAP CCCCCCCCCCCCCCC	28.37	28348404
332	Phosphorylation	PPPGLGSSRPSSAPG CCCCCCCCCCCCCCC	46.54	28348404
335	Phosphorylation	GLGSSRPSSAPGMLP CCCCCCCCCCCCCCC	37.71	27732954
336	Phosphorylation	LGSSRPSSAPGMLPL CCCCCCCCCCCCCCC	40.96	27732954
344	Phosphorylation	APGMLPLSV------ CCCCCCCCC------	24.68	25159151
345 (in isoform 2)	Phosphorylation	-	13.82	23090842
351 (in isoform 2)	Phosphorylation	-		23090842
352 (in isoform 2)	Phosphorylation	-		23090842
355 (in isoform 2)	Phosphorylation	-		23090842

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
219	T	Phosphorylation	Kinase	CDK1	P06493	Uniprot
219	T	Phosphorylation	Kinase	ERK2	P28482	PSP
242	S	Phosphorylation	Kinase	CDK1	P06493	Uniprot
245	T	Phosphorylation	Kinase	CDK1	P06493	Uniprot
245	T	Phosphorylation	Kinase	ERK2	P28482	PSP
251	S	Phosphorylation	Kinase	AURKA	O14965	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
273	C	Palmitoylation		15728732
Palmitoylation at Cys-273 reduces affinity for dynein.

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 NDEL1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
1433E_HUMAN	YWHAE	physical	12796778
LIS1_HUMAN	PAFAH1B1	physical	12796778
LIS1_HUMAN	PAFAH1B1	physical	11163260
DYHC1_HUMAN	DYNC1H1	physical	11163260
CDK5_HUMAN	CDK5	physical	11163260
LMNB1_HUMAN	LMNB1	physical	19198602
TACC3_HUMAN	TACC3	physical	17060449
MIC60_HUMAN	IMMT	physical	20880836
GRDN_HUMAN	CCDC88A	physical	17043677
CENPF_HUMAN	CENPF	physical	17043677
CE170_HUMAN	CEP170	physical	17043677
CEP63_HUMAN	CEP63	physical	17043677
KALRN_HUMAN	KALRN	physical	17043677
ZN197_HUMAN	ZNF197	physical	17043677
ANK2_HUMAN	ANK2	physical	17043677
CCSE1_HUMAN	CCSER1	physical	17043677
SYNE1_HUMAN	SYNE1	physical	17043677
LC7L2_HUMAN	LUC7L2	physical	17043677
CCSE2_HUMAN	CCSER2	physical	17043677
AF10_HUMAN	MLLT10	physical	17043677
DIXC1_HUMAN	DIXDC1	physical	17043677
ZNF10_HUMAN	ZNF10	physical	17043677
SNX6_HUMAN	SNX6	physical	17043677
MRC2_HUMAN	MRC2	physical	17043677
ZNF17_HUMAN	ZNF17	physical	17043677
ZN211_HUMAN	ZNF211	physical	17043677
ZN230_HUMAN	ZNF230	physical	17043677
ZNF91_HUMAN	ZNF91	physical	17043677
MS18A_HUMAN	MIS18A	physical	17043677
LIS1_HUMAN	PAFAH1B1	physical	19622634
LIS1_HUMAN	PAFAH1B1	physical	14970193
DYHC1_HUMAN	DYNC1H1	physical	14970193
DCTN2_HUMAN	DCTN2	physical	14970193
TBG1_HUMAN	TUBG1	physical	14970193
TBA1A_HUMAN	TUBA1A	physical	14970193
KTNA1_HUMAN	KATNA1	physical	16203747
KTNB1_HUMAN	KATNB1	physical	16203747
A4_HUMAN	APP	physical	21832049
CENPF_HUMAN	CENPF	physical	17600710
NDEL1_HUMAN	NDEL1	physical	25416956
K1C40_HUMAN	KRT40	physical	25416956
ZN572_HUMAN	ZNF572	physical	25416956
C19L2_HUMAN	CWF19L2	physical	25416956
ZN417_HUMAN	ZNF417	physical	25416956
ZN599_HUMAN	ZNF599	physical	25416956
ZN844_HUMAN	ZNF844	physical	25416956
ZN260_HUMAN	ZNF260	physical	25416956
DC1I1_HUMAN	DYNC1I1	physical	14970193
CCSE1_HUMAN	CCSER1	physical	28514442
DIXC1_HUMAN	DIXDC1	physical	28514442
CCSE2_HUMAN	CCSER2	physical	28514442
DISC1_HUMAN	DISC1	physical	28514442
KI20B_HUMAN	KIF20B	physical	28514442
GRAP1_HUMAN	GRIPAP1	physical	28514442
CP135_HUMAN	CEP135	physical	28514442
ANR26_HUMAN	ANKRD26	physical	28514442
NDE1_HUMAN	NDE1	physical	28514442
NUP54_HUMAN	NUP54	physical	28514442
LIS1_HUMAN	PAFAH1B1	physical	28514442
UTRO_HUMAN	UTRN	physical	28514442
SNTB1_HUMAN	SNTB1	physical	28514442
FBXW5_HUMAN	FBXW5	physical	28514442
SNTB2_HUMAN	SNTB2	physical	28514442
SNTA1_HUMAN	SNTA1	physical	28514442
ZN445_HUMAN	ZNF445	physical	28514442
MTCL1_HUMAN	MTCL1	physical	28514442
CLPX_HUMAN	CLPX	physical	28514442
CCD18_HUMAN	CCDC18	physical	28514442
SHOT1_HUMAN	KIAA1598	physical	28514442
SPF27_HUMAN	BCAS2	physical	28514442
KTN1_HUMAN	KTN1	physical	28514442
OFD1_HUMAN	OFD1	physical	28514442
TRI27_HUMAN	TRIM27	physical	28514442
CCHCR_HUMAN	CCHCR1	physical	28514442
TRIM7_HUMAN	TRIM7	physical	28514442
TARA_HUMAN	TRIOBP	physical	28514442
KS6A3_HUMAN	RPS6KA3	physical	28514442
EVI5_HUMAN	EVI5	physical	28514442
PRP19_HUMAN	PRPF19	physical	28514442

Drug and Disease Associations

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

Regulatory Network of NDEL1_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-273 BY ZDHHC2; ZDHHC3 AND ZDHHC7.	19927128 [Abstract]
Phosphorylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194; SER-197 ANDSER-198, AND MASS SPECTROMETRY.	19413330 [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-215; THR-219; THR-241AND THR-245, AND MASS SPECTROMETRY.	18669648 [Abstract]

show