dbPTM

NEK9_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NEK9_HUMAN
UniProt AC	Q8TD19
Protein Name	Serine/threonine-protein kinase Nek9
Gene Name	NEK9
Organism	Homo sapiens (Human).
Sequence Length	979
Subcellular Localization	Cytoplasm . Nucleus .
Protein Description	Pleiotropic regulator of mitotic progression, participating in the control of spindle dynamics and chromosome separation. Phosphorylates different histones, myelin basic protein, beta-casein, and BICD2. Phosphorylates histone H3 on serine and threonine residues and beta-casein on serine residues. Important for G1/S transition and S phase progression. Phosphorylates NEK6 and NEK7 and stimulates their activity by releasing the autoinhibitory functions of Tyr-108 and Tyr-97 respectively..
Protein Sequence	MSVLGEYERHCDSINSDFGSESGGCGDSSPGPSASQGPRAGGGAAEQEELHYIPIRVLGRGAFGEATLYRRTEDDSLVVWKEVDLTRLSEKERRDALNEIVILALLQHDNIIAYYNHFMDNTTLLIELEYCNGGNLYDKILRQKDKLFEEEMVVWYLFQIVSAVSCIHKAGILHRDIKTLNIFLTKANLIKLGDYGLAKKLNSEYSMAETLVGTPYYMSPELCQGVKYNFKSDIWAVGCVIFELLTLKRTFDATNPLNLCVKIVQGIRAMEVDSSQYSLELIQMVHSCLDQDPEQRPTADELLDRPLLRKRRREMEEKVTLLNAPTKRPRSSTVTEAPIAVVTSRTSEVYVWGGGKSTPQKLDVIKSGCSARQVCAGNTHFAVVTVEKELYTWVNMQGGTKLHGQLGHGDKASYRQPKHVEKLQGKAIRQVSCGDDFTVCVTDEGQLYAFGSDYYGCMGVDKVAGPEVLEPMQLNFFLSNPVEQVSCGDNHVVVLTRNKEVYSWGCGEYGRLGLDSEEDYYTPQKVDVPKALIIVAVQCGCDGTFLLTQSGKVLACGLNEFNKLGLNQCMSGIINHEAYHEVPYTTSFTLAKQLSFYKIRTIAPGKTHTAAIDERGRLLTFGCNKCGQLGVGNYKKRLGINLLGGPLGGKQVIRVSCGDEFTIAATDDNHIFAWGNGGNGRLAMTPTERPHGSDICTSWPRPIFGSLHHVPDLSCRGWHTILIVEKVLNSKTIRSNSSGLSIGTVFQSSSPGGGGGGGGGEEEDSQQESETPDPSGGFRGTMEADRGMEGLISPTEAMGNSNGASSSCPGWLRKELENAEFIPMPDSPSPLSAAFSESEKDTLPYEELQGLKVASEAPLEHKPQVEASSPRLNPAVTCAGKGTPLTPPACACSSLQVEVERLQGLVLKCLAEQQKLQQENLQIFTQLQKLNKKLEGGQQVGMHSKGTQTAKEEMEMDPKPDLDSDSWCLLGTDSCRPSL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSVLGEYER ------CCCCCCHHH	26.50	19369195
2	Phosphorylation	------MSVLGEYER ------CCCCCCHHH	26.50	19369195
7	Phosphorylation	-MSVLGEYERHCDSI -CCCCCCHHHHHCCC	19.23	27642862
13	Phosphorylation	EYERHCDSINSDFGS CHHHHHCCCCCCCCC	29.12	23401153
16	Phosphorylation	RHCDSINSDFGSESG HHHCCCCCCCCCCCC	32.42	23927012
20	O-linked_Glycosylation	SINSDFGSESGGCGD CCCCCCCCCCCCCCC	28.69	OGP
20	Phosphorylation	SINSDFGSESGGCGD CCCCCCCCCCCCCCC	28.69	23927012
22	Phosphorylation	NSDFGSESGGCGDSS CCCCCCCCCCCCCCC	42.03	23927012
28	Phosphorylation	ESGGCGDSSPGPSAS CCCCCCCCCCCCCHH	24.58	23401153
29	Phosphorylation	SGGCGDSSPGPSASQ CCCCCCCCCCCCHHC	38.32	23401153
33	Phosphorylation	GDSSPGPSASQGPRA CCCCCCCCHHCCCCC	46.60	30278072
35	Phosphorylation	SSPGPSASQGPRAGG CCCCCCHHCCCCCCC	39.75	17525332
52	Phosphorylation	AEQEELHYIPIRVLG CCCCCEEEEEEEEEC	22.48	22817900
60	Methylation	IPIRVLGRGAFGEAT EEEEEECCCCCCEEE	29.16	115484801
67	Phosphorylation	RGAFGEATLYRRTED CCCCCEEEEEEECCC	21.74	28857561
72	Phosphorylation	EATLYRRTEDDSLVV EEEEEEECCCCCEEE	34.46	-
76	Phosphorylation	YRRTEDDSLVVWKEV EEECCCCCEEEEEEE	35.07	17192257
81	Ubiquitination	DDSLVVWKEVDLTRL CCCEEEEEEEEHHHC	35.93	-
186	Ubiquitination	TLNIFLTKANLIKLG HHEEEEEHHHHHHHC	37.11	-
191	Ubiquitination	LTKANLIKLGDYGLA EEHHHHHHHCHHHHH	49.97	21890473
199	Ubiquitination	LGDYGLAKKLNSEYS HCHHHHHHHHCCCCC	63.94	21890473
200	Ubiquitination	GDYGLAKKLNSEYSM CHHHHHHHHCCCCCH	47.49	-
203	Phosphorylation	GLAKKLNSEYSMAET HHHHHHCCCCCHHHH	48.63	19060867
205	Phosphorylation	AKKLNSEYSMAETLV HHHHCCCCCHHHHHC	11.99	19060867
206	Phosphorylation	KKLNSEYSMAETLVG HHHCCCCCHHHHHCC	13.89	20071362
210	Phosphorylation	SEYSMAETLVGTPYY CCCCHHHHHCCCCCC	19.73	14660563
214	Phosphorylation	MAETLVGTPYYMSPE HHHHHCCCCCCCCHH	10.71	28857561
216	Phosphorylation	ETLVGTPYYMSPELC HHHCCCCCCCCHHHH	16.19	27251275
217	Phosphorylation	TLVGTPYYMSPELCQ HHCCCCCCCCHHHHC	7.72	24719451
232	Phosphorylation	GVKYNFKSDIWAVGC CCCCCCCCCHHHHHH	30.14	20068231
246	Phosphorylation	CVIFELLTLKRTFDA HHHHHHHHCHHHCCC	42.74	20068231
250	Phosphorylation	ELLTLKRTFDATNPL HHHHCHHHCCCCCCH	25.04	23403867
254	Phosphorylation	LKRTFDATNPLNLCV CHHHCCCCCCHHHHH	38.93	25159151
262	Ubiquitination	NPLNLCVKIVQGIRA CCHHHHHHHHHHCCE	35.84	-
318	Acetylation	RRREMEEKVTLLNAP HHHHHHHHHHHHCCC	27.49	25953088
318	Malonylation	RRREMEEKVTLLNAP HHHHHHHHHHHHCCC	27.49	26320211
318	Ubiquitination	RRREMEEKVTLLNAP HHHHHHHHHHHHCCC	27.49	-
326	Phosphorylation	VTLLNAPTKRPRSST HHHHCCCCCCCCCCC	36.96	-
327	Acetylation	TLLNAPTKRPRSSTV HHHCCCCCCCCCCCC	60.38	25953088
327	Ubiquitination	TLLNAPTKRPRSSTV HHHCCCCCCCCCCCC	60.38	21890473
331	Phosphorylation	APTKRPRSSTVTEAP CCCCCCCCCCCCCCC	32.80	29255136
332	Phosphorylation	PTKRPRSSTVTEAPI CCCCCCCCCCCCCCE	28.33	29255136
333	Phosphorylation	TKRPRSSTVTEAPIA CCCCCCCCCCCCCEE	32.47	29255136
335	Phosphorylation	RPRSSTVTEAPIAVV CCCCCCCCCCCEEEE	26.90	30266825
343	Phosphorylation	EAPIAVVTSRTSEVY CCCEEEEEECCCEEE	13.09	23403867
344	Phosphorylation	APIAVVTSRTSEVYV CCEEEEEECCCEEEE	23.19	23403867
346	Phosphorylation	IAVVTSRTSEVYVWG EEEEEECCCEEEEEC	29.07	30206219
347	Phosphorylation	AVVTSRTSEVYVWGG EEEEECCCEEEEECC	24.77	30206219
350	Phosphorylation	TSRTSEVYVWGGGKS EECCCEEEEECCCCC	6.09	28450419
356	Ubiquitination	VYVWGGGKSTPQKLD EEEECCCCCCCHHHH	55.20	-
357	Phosphorylation	YVWGGGKSTPQKLDV EEECCCCCCCHHHHH	48.90	21712546
358	Phosphorylation	VWGGGKSTPQKLDVI EECCCCCCCHHHHHH	32.97	21712546
361	Acetylation	GGKSTPQKLDVIKSG CCCCCCHHHHHHHCC	48.10	25953088
361	Ubiquitination	GGKSTPQKLDVIKSG CCCCCCHHHHHHHCC	48.10	-
366	Ubiquitination	PQKLDVIKSGCSARQ CHHHHHHHCCCCCCH	40.41	-
391	Phosphorylation	VTVEKELYTWVNMQG EEEEEEEEEEEECCC	10.31	27642862
411	Ubiquitination	GQLGHGDKASYRQPK CCCCCCCCCCCCCCH	43.77	-
413	Phosphorylation	LGHGDKASYRQPKHV CCCCCCCCCCCCHHH	26.96	22817900
414	Phosphorylation	GHGDKASYRQPKHVE CCCCCCCCCCCHHHH	20.37	23828894
422	Ubiquitination	RQPKHVEKLQGKAIR CCCHHHHHHCCCEEE	45.05	-
499	Ubiquitination	VVVLTRNKEVYSWGC EEEEECCCEEEEECC	45.31	-
509	Phosphorylation	YSWGCGEYGRLGLDS EEECCCCCCCCCCCC	7.88	-
516	Phosphorylation	YGRLGLDSEEDYYTP CCCCCCCCCCCCCCC	48.18	-
520	Phosphorylation	GLDSEEDYYTPQKVD CCCCCCCCCCCCCCC	16.71	22817900
521	Phosphorylation	LDSEEDYYTPQKVDV CCCCCCCCCCCCCCC	25.02	27642862
522	Phosphorylation	DSEEDYYTPQKVDVP CCCCCCCCCCCCCCC	17.02	27642862
525	Ubiquitination	EDYYTPQKVDVPKAL CCCCCCCCCCCCCEE	41.42	21890473
563	Ubiquitination	CGLNEFNKLGLNQCM ECCCHHHHHCHHHHH	49.61	-
606	Ubiquitination	IRTIAPGKTHTAAID EEEECCCCCCCEEEC	35.75	-
625	Ubiquitination	LLTFGCNKCGQLGVG EEEEECCCCCCCCCC	43.76	-
635	Acetylation	QLGVGNYKKRLGINL CCCCCCCHHCEECEE	35.10	25953088
635	Ubiquitination	QLGVGNYKKRLGINL CCCCCCCHHCEECEE	35.10	-
650	Ubiquitination	LGGPLGGKQVIRVSC CCCCCCCEEEEEEEE	39.32	-
662	Phosphorylation	VSCGDEFTIAATDDN EEECCEEEEEEECCC	13.99	30257219
685	Phosphorylation	GNGRLAMTPTERPHG CCCCCCCCCCCCCCC	22.81	18691976
698	Phosphorylation	HGSDICTSWPRPIFG CCCCCCCCCCCCCCC	30.58	24719451
731	Acetylation	VEKVLNSKTIRSNSS EEEHHHCCCHHCCCC	47.07	19608861
731	Ubiquitination	VEKVLNSKTIRSNSS EEEHHHCCCHHCCCC	47.07	19608861
732	Phosphorylation	EKVLNSKTIRSNSSG EEHHHCCCHHCCCCC	22.80	-
735	Phosphorylation	LNSKTIRSNSSGLSI HHCCCHHCCCCCCEE	36.89	19369195
737	Phosphorylation	SKTIRSNSSGLSIGT CCCHHCCCCCCEEEE	27.34	28450419
738	Phosphorylation	KTIRSNSSGLSIGTV CCHHCCCCCCEEEEE	48.26	28450419
741	Phosphorylation	RSNSSGLSIGTVFQS HCCCCCCEEEEEEEC	23.61	17192257
744	Phosphorylation	SSGLSIGTVFQSSSP CCCCEEEEEEECCCC	19.24	28450419
748	Phosphorylation	SIGTVFQSSSPGGGG EEEEEEECCCCCCCC	22.71	28450419
749	Phosphorylation	IGTVFQSSSPGGGGG EEEEEECCCCCCCCC	29.75	28450419
750	Phosphorylation	GTVFQSSSPGGGGGG EEEEECCCCCCCCCC	32.58	19369195
765	Phosphorylation	GGGEEEDSQQESETP CCCCCCCCCCCCCCC	36.72	18691976
769	Phosphorylation	EEDSQQESETPDPSG CCCCCCCCCCCCCCC	42.29	18691976
771	Phosphorylation	DSQQESETPDPSGGF CCCCCCCCCCCCCCC	42.12	24144214
775	Phosphorylation	ESETPDPSGGFRGTM CCCCCCCCCCCCCCC	59.95	24144214
793	Phosphorylation	RGMEGLISPTEAMGN CCCCCCCCCHHHCCC	30.71	21082442
795	Phosphorylation	MEGLISPTEAMGNSN CCCCCCCHHHCCCCC	29.59	21082442
801	Phosphorylation	PTEAMGNSNGASSSC CHHHCCCCCCCCCCC	30.80	21082442
805	Phosphorylation	MGNSNGASSSCPGWL CCCCCCCCCCCCCHH	24.96	28450419
806	Phosphorylation	GNSNGASSSCPGWLR CCCCCCCCCCCCHHH	35.11	26074081
807	Phosphorylation	NSNGASSSCPGWLRK CCCCCCCCCCCHHHH	23.10	26074081
827	Phosphorylation	EFIPMPDSPSPLSAA EECCCCCCCCCCHHC	22.77	25159151
829	Phosphorylation	IPMPDSPSPLSAAFS CCCCCCCCCCHHCCC	42.28	21082442
832	Phosphorylation	PDSPSPLSAAFSESE CCCCCCCHHCCCCCC	22.42	21082442
836	Phosphorylation	SPLSAAFSESEKDTL CCCHHCCCCCCCCCC	35.17	21082442
838	Phosphorylation	LSAAFSESEKDTLPY CHHCCCCCCCCCCCH	49.07	21082442
842	Phosphorylation	FSESEKDTLPYEELQ CCCCCCCCCCHHHHH	40.47	21945579
845	Phosphorylation	SEKDTLPYEELQGLK CCCCCCCHHHHHCCE	25.75	21945579
852	Ubiquitination	YEELQGLKVASEAPL HHHHHCCEECCCCCC	42.45	-
855	Phosphorylation	LQGLKVASEAPLEHK HHCCEECCCCCCCCC	36.96	23927012
862	Ubiquitination	SEAPLEHKPQVEASS CCCCCCCCCCCCCCC	27.98	-
868	Phosphorylation	HKPQVEASSPRLNPA CCCCCCCCCCCCCCC	27.63	29255136
869	Phosphorylation	KPQVEASSPRLNPAV CCCCCCCCCCCCCCC	22.53	29255136
877	O-linked_Glycosylation	PRLNPAVTCAGKGTP CCCCCCCCCCCCCCC	9.95	23301498
877	Phosphorylation	PRLNPAVTCAGKGTP CCCCCCCCCCCCCCC	9.95	25849741
883	Phosphorylation	VTCAGKGTPLTPPAC CCCCCCCCCCCCCCC	20.72	17192257
886	Phosphorylation	AGKGTPLTPPACACS CCCCCCCCCCCCCCC	28.56	25159151
893	Phosphorylation	TPPACACSSLQVEVE CCCCCCCCCCHHHHH	18.63	26074081
894	Phosphorylation	PPACACSSLQVEVER CCCCCCCCCHHHHHH	23.78	26074081
929	Ubiquitination	QIFTQLQKLNKKLEG HHHHHHHHHHHHCCC	63.72	21890473
933	Ubiquitination	QLQKLNKKLEGGQQV HHHHHHHHCCCCCCC	51.18	-
942	Sulfoxidation	EGGQQVGMHSKGTQT CCCCCCCCCCCCCHH	3.20	30846556
944	Phosphorylation	GQQVGMHSKGTQTAK CCCCCCCCCCCHHHH	24.72	25159151
945	Ubiquitination	QQVGMHSKGTQTAKE CCCCCCCCCCHHHHH	51.83	-
947	Phosphorylation	VGMHSKGTQTAKEEM CCCCCCCCHHHHHHH	26.87	20068231
949	Phosphorylation	MHSKGTQTAKEEMEM CCCCCCHHHHHHHCC	39.26	20068231
964	Phosphorylation	DPKPDLDSDSWCLLG CCCCCCCCCCEEEEC	40.62	18691976
966	Phosphorylation	KPDLDSDSWCLLGTD CCCCCCCCEEEECCC	24.52	27251275
972	Phosphorylation	DSWCLLGTDSCRPSL CCEEEECCCCCCCCC	25.39	28450419
974	Phosphorylation	WCLLGTDSCRPSL-- EEEECCCCCCCCC--	16.32	28450419
978	Phosphorylation	GTDSCRPSL------ CCCCCCCCC------	100.00	25159151

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
210	T	Phosphorylation	Kinase	CDK1	P06493	PSP
210	T	Phosphorylation	Kinase	NEK9	Q8TD19	PSP
210	T	Phosphorylation	Kinase	PLK1	P53350	PSP
944	S	Phosphorylation	Kinase	NEK9	Q8TD19	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
210	T	Phosphorylation	11864968
During mitosis, not phosphorylated on Thr-210.
210	T	Phosphorylation	11864968
When complexed with FACT, exhibits markedly elevated phosphorylation on Thr-210.

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 NEK9_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SSRP1_HUMAN	SSRP1	physical	14660563
NEK6_HUMAN	NEK6	physical	12840024
NEK7_HUMAN	NEK7	physical	12840024
RAN_HUMAN	RAN	physical	12101123
NEK7_HUMAN	NEK7	physical	20562859
DYL1_HUMAN	DYNLL1	physical	20562859
CHK1_HUMAN	CHEK1	physical	20562859
HS90A_HUMAN	HSP90AA1	physical	22939624
CAP1_HUMAN	CAP1	physical	22863883
DYL1_HUMAN	DYNLL1	physical	25852190
CASB_HUMAN	CSN2	physical	11864968
NEK8_HUMAN	NEK8	physical	11864968
BICD2_HUMAN	BICD2	physical	11864968

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 NEK9_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-731, AND MASS SPECTROMETRY.	19608861 [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-2; SER-13; SER-16;SER-20; SER-28; SER-29; TYR-52; SER-76; SER-203; TYR-205; THR-254;SER-331; SER-332; THR-333; THR-335; SER-357; THR-358; SER-413;SER-735; SER-749; SER-750; SER-793; THR-795; SER-801; SER-827;SER-829; SER-832; SER-836; SER-838; SER-868; SER-869; THR-886;SER-944; SER-974 AND SER-978, AND MASS SPECTROMETRY.	19369195 [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-2; SER-13; SER-16;SER-20; SER-29; SER-76; THR-254; SER-331; SER-332; SER-741; SER-750;SER-793; SER-827; SER-829; SER-836; SER-868; THR-886; SER-944 ANDSER-978, AND MASS SPECTROMETRY.	18691976 [Abstract]
"Proteomics analysis of protein kinases by target class-selectiveprefractionation and tandem mass spectrometry."; Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R.,Keri G., Wehland J., Daub H.; Mol. Cell. Proteomics 6:537-547(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332; THR-333; THR-358AND SER-868, AND MASS SPECTROMETRY.	17192257 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-869, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-333, AND MASSSPECTROMETRY.	19690332 [Abstract]
"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 THR-333, AND MASSSPECTROMETRY.	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 THR-333, AND MASSSPECTROMETRY.	18669648 [Abstract]

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