dbPTM

NEK7_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NEK7_HUMAN
UniProt AC	Q8TDX7
Protein Name	Serine/threonine-protein kinase Nek7
Gene Name	NEK7
Organism	Homo sapiens (Human).
Sequence Length	302
Subcellular Localization	Nucleus. Cytoplasm. Cytoplasm, cytoskeleton, spindle pole. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Present at centrosome throughout the cell cycle. Also detected at spindle midzone of the anaphase cells and eventually conc
Protein Description	Protein kinase which plays an important role in mitotic cell cycle progression. Required for microtubule nucleation activity of the centrosome, robust mitotic spindle formation and cytokinesis. Phosphorylates RPS6KB1..
Protein Sequence	MDEQSQGMQGPPVPQFQPQKALRPDMGYNTLANFRIEKKIGRGQFSEVYRAACLLDGVPVALKKVQIFDLMDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIVLELADAGDLSRMIKHFKKQKRLIPERTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNLYSLCKKIEQCDYPPLPSDHYSEELRQLVNMCINPDPEKRPDVTYVYDVAKRMHACTASS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDEQSQGM -------CCHHCCCC	13.28	19413330
5	Phosphorylation	---MDEQSQGMQGPP ---CCHHCCCCCCCC	27.01	25159151
20	Ubiquitination	VPQFQPQKALRPDMG CCCCCCCCCCCCCCC	56.95	-
26	Sulfoxidation	QKALRPDMGYNTLAN CCCCCCCCCCCHHHC	7.32	30846556
30	Phosphorylation	RPDMGYNTLANFRIE CCCCCCCHHHCCEEE	20.82	-
46	Phosphorylation	KIGRGQFSEVYRAAC EECCCCHHHHHHHHH	20.47	28857561
63	Ubiquitination	DGVPVALKKVQIFDL HCCEEEEEEEEEHHH	40.95	-
64	Ubiquitination	GVPVALKKVQIFDLM CCEEEEEEEEEHHHC	39.98	-
74	Acetylation	IFDLMDAKARADCIK EHHHCCHHHHHHHHH	33.85	25953088
74	Ubiquitination	IFDLMDAKARADCIK EHHHCCHHHHHHHHH	33.85	-
74	2-Hydroxyisobutyrylation	IFDLMDAKARADCIK EHHHCCHHHHHHHHH	33.85	-
81	Ubiquitination	KARADCIKEIDLLKQ HHHHHHHHHHHHHHH	55.75	-
87	Ubiquitination	IKEIDLLKQLNHPNV HHHHHHHHHCCCCCH	61.10	-
97	Phosphorylation	NHPNVIKYYASFIED CCCCHHHHHHHHHCC	7.98	19941817
137	Phosphorylation	KRLIPERTVWKYFVQ CCCCCHHHHHHHHHH	29.11	22210691
141	Phosphorylation	PERTVWKYFVQLCSA CHHHHHHHHHHHHHH	8.02	22210691
147	Phosphorylation	KYFVQLCSALEHMHS HHHHHHHHHHHHHHH	44.47	22210691
163	Ubiquitination	RVMHRDIKPANVFIT CCCCCCCCCCCEEEE	42.22	21890473
170	Phosphorylation	KPANVFITATGVVKL CCCCEEEEECEEEEE	13.50	-
172	Phosphorylation	ANVFITATGVVKLGD CCEEEEECEEEEECC	23.12	-
176	Ubiquitination	ITATGVVKLGDLGLG EEECEEEEECCCCCC	44.33	-
187	Phosphorylation	LGLGRFFSSKTTAAH CCCCHHCCCCCHHHH	28.36	23927012
188	Phosphorylation	GLGRFFSSKTTAAHS CCCHHCCCCCHHHHH	28.94	23927012
189	Ubiquitination	LGRFFSSKTTAAHSL CCHHCCCCCHHHHHC	49.01	-
190	Phosphorylation	GRFFSSKTTAAHSLV CHHCCCCCHHHHHCC	24.50	21945579
191	Phosphorylation	RFFSSKTTAAHSLVG HHCCCCCHHHHHCCC	26.11	21945579
195	Phosphorylation	SKTTAAHSLVGTPYY CCCHHHHHCCCCCCC	21.74	21945579
199	Phosphorylation	AAHSLVGTPYYMSPE HHHHCCCCCCCCCHH	10.71	21945579
201	Phosphorylation	HSLVGTPYYMSPERI HHCCCCCCCCCHHHH	16.19	21945579
202	Phosphorylation	SLVGTPYYMSPERIH HCCCCCCCCCHHHHH	7.72	21945579
204	Phosphorylation	VGTPYYMSPERIHEN CCCCCCCCHHHHHHC	13.90	21945579
213	Phosphorylation	ERIHENGYNFKSDIW HHHHHCCCCCHHHHH	29.07	29496907
244	Phosphorylation	YGDKMNLYSLCKKIE CCCCCCHHHHHHHHH	8.45	21945579
245	Phosphorylation	GDKMNLYSLCKKIEQ CCCCCHHHHHHHHHH	30.38	21945579
248	Acetylation	MNLYSLCKKIEQCDY CCHHHHHHHHHHCCC	63.18	25953088
248	Ubiquitination	MNLYSLCKKIEQCDY CCHHHHHHHHHHCCC	63.18	-
249	Ubiquitination	NLYSLCKKIEQCDYP CHHHHHHHHHHCCCC	50.94	-
260	O-linked_Glycosylation	CDYPPLPSDHYSEEL CCCCCCCCCCCCHHH	44.71	29351928
264	O-linked_Glycosylation	PLPSDHYSEELRQLV CCCCCCCCHHHHHHH	22.60	29351928
281	Ubiquitination	CINPDPEKRPDVTYV HHCCCHHHCCCCEEE	74.70	-
286	Phosphorylation	PEKRPDVTYVYDVAK HHHCCCCEEEECHHH	18.04	27642862
287	Phosphorylation	EKRPDVTYVYDVAKR HHCCCCEEEECHHHH	9.25	-
289	Phosphorylation	RPDVTYVYDVAKRMH CCCCEEEECHHHHHH	8.35	25147952
293	Ubiquitination	TYVYDVAKRMHACTA EEEECHHHHHHHHCC	50.53	-

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
195	S	Phosphorylation	Kinase	NEK9	Q8TD19	Uniprot
204	S	Phosphorylation	Kinase	PLK4	O00444	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
195	S	Phosphorylation		12840024
Phosphorylation at Ser-195 required for its activation.

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 NEK7_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PDIA1_HUMAN	P4HB	physical	27173435
EMAL4_HUMAN	EML4	physical	27173435
CBS_HUMAN	CBS	physical	27173435
NEK9_HUMAN	NEK9	physical	27173435
NEK8_HUMAN	NEK8	physical	27173435
PLK1_HUMAN	PLK1	physical	27173435
WDR19_HUMAN	WDR19	physical	27173435
IF122_HUMAN	IFT122	physical	27173435
WDR35_HUMAN	WDR35	physical	27173435
TERF1_HUMAN	TERF1	physical	28216227
NEK7_HUMAN	NEK7	physical	28216227

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 NEK7_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187; THR-190 ANDSER-195, AND MASS SPECTROMETRY.	19369195 [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-204, 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-187; SER-188; THR-190;SER-195 AND SER-204, AND MASS SPECTROMETRY.	18691976 [Abstract]
"A mitotic cascade of NIMA family kinases. Nercc1/Nek9 activates theNek6 and Nek7 kinases."; Belham C., Roig J., Caldwell J.A., Aoyama Y., Kemp B.E., Comb M.,Avruch J.; J. Biol. Chem. 278:34897-34909(2003). Cited for: PHOSPHORYLATION AT SER-195.	12840024 [Abstract]

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