dbPTM

NEK3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NEK3_HUMAN
UniProt AC	P51956
Protein Name	Serine/threonine-protein kinase Nek3
Gene Name	NEK3
Organism	Homo sapiens (Human).
Sequence Length	506
Subcellular Localization	Cytoplasm. Cell projection, axon.
Protein Description	Protein kinase which influences neuronal morphogenesis and polarity through effects on microtubules. Regulates microtubule acetylation in neurons. Contributes to prolactin-mediated phosphorylation of PXN and VAV2. Implicated in prolactin-mediated cytoskeletal reorganization and motility of breast cancer cells through mechanisms involving RAC1 activation and phosphorylation of PXN and VAV2..
Protein Sequence	MDDYMVLRMIGEGSFGRALLVQHESSNQMFAMKEIRLPKSFSNTQNSRKEAVLLAKMKHPNIVAFKESFEAEGHLYIVMEYCDGGDLMQKIKQQKGKLFPEDMILNWFTQMCLGVNHIHKKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLSNPMAFACTYVGTPYYVPPEIWENLPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGCISPLPSHYSYELQFLVKQMFKRNPSHRPSATTLLSRGIVARLVQKCLPPEIIMEYGEEVLEEIKNSKHNTPRKKTNPSRIRIALGNEASTVQEEEQDRKGSHTDLESINENLVESALRRVNREEKGNKSVHLRKASSPNLHRRQWEKNVPNTALTALENASILTSSLTAEDDRGGSVIKYSKNTTRKQWLKETPDTLLNILKNADLSLAFQTYTIYRPGSEGFLKGPLSEETEASDSVDGGHDSVILDPERLEPGLDEEDTDFEEEDDNPDWVSELKKRAGWQGLCDR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDDYMVLR -------CCCCEEEE	8.80	22814378
25	Phosphorylation	ALLVQHESSNQMFAM EEEEEECCCCCEEEE	32.25	28111955
26	Phosphorylation	LLVQHESSNQMFAMK EEEEECCCCCEEEEE	28.26	28111955
39	Ubiquitination	MKEIRLPKSFSNTQN EEEEECCCCCCCCCC	69.58	-
40	Phosphorylation	KEIRLPKSFSNTQNS EEEECCCCCCCCCCH	31.78	20068231
42	Phosphorylation	IRLPKSFSNTQNSRK EECCCCCCCCCCHHH	46.16	20068231
44	Phosphorylation	LPKSFSNTQNSRKEA CCCCCCCCCCHHHHH	28.12	20068231
47	Phosphorylation	SFSNTQNSRKEAVLL CCCCCCCHHHHHHHH	34.61	20068231
161	Phosphorylation	NPMAFACTYVGTPYY CCCEEEEEECCCCCC	20.15	-
165	Phosphorylation	FACTYVGTPYYVPPE EEEEECCCCCCCCHH	9.70	-
243	Phosphorylation	QMFKRNPSHRPSATT HHHHHCCCCCCCHHH	35.36	20873877
247	Phosphorylation	RNPSHRPSATTLLSR HCCCCCCCHHHHHHH	37.90	20071362
249	Phosphorylation	PSHRPSATTLLSRGI CCCCCCHHHHHHHHH	23.47	20068231
250	Phosphorylation	SHRPSATTLLSRGIV CCCCCHHHHHHHHHH	25.97	20071362
253	Phosphorylation	PSATTLLSRGIVARL CCHHHHHHHHHHHHH	31.41	20068231
273	Phosphorylation	PPEIIMEYGEEVLEE CHHHHHHHHHHHHHH	16.68	-
284	Phosphorylation	VLEEIKNSKHNTPRK HHHHHHCCCCCCCCC	30.23	28348404
288	Phosphorylation	IKNSKHNTPRKKTNP HHCCCCCCCCCCCCH	24.96	-
319	Phosphorylation	EEQDRKGSHTDLESI HHHHCCCCCCCHHHH	26.67	28450419
321	Phosphorylation	QDRKGSHTDLESINE HHCCCCCCCHHHHHH	43.93	29496963
325	Phosphorylation	GSHTDLESINENLVE CCCCCHHHHHHHHHH	37.70	28450419
333	Phosphorylation	INENLVESALRRVNR HHHHHHHHHHHHHCH	25.73	23312004
354	Phosphorylation	SVHLRKASSPNLHRR CCCCEECCCCCHHHH	49.73	28102081
355	Phosphorylation	VHLRKASSPNLHRRQ CCCEECCCCCHHHHH	23.75	28102081
394	Phosphorylation	AEDDRGGSVIKYSKN EECCCCCCEEEECCC	24.40	17924679
402	Phosphorylation	VIKYSKNTTRKQWLK EEEECCCCCCHHHHH	31.54	17924679
435	Methylation	FQTYTIYRPGSEGFL EEEEEEECCCCCCCC	25.83	115385841
453	Phosphorylation	LSEETEASDSVDGGH CCCCCCCCCCCCCCC	24.96	27251275
455	Phosphorylation	EETEASDSVDGGHDS CCCCCCCCCCCCCCC	21.44	27251275
462	Phosphorylation	SVDGGHDSVILDPER CCCCCCCCEEECHHH	12.84	26657352
479	Phosphorylation	PGLDEEDTDFEEEDD CCCCHHCCCCCCCCC	45.96	30175587

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
165	T	Phosphorylation	Kinase	NEK3	P51956	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
479	T	Phosphorylation		19369195
Phosphorylation at Thr-479 regulates its catalytic activity.

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 NEK3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
NMNA1_HUMAN	NMNAT1	physical	21988832

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 NEK3_HUMAN

Related Literatures of Post-Translational Modification

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-354 AND THR-479, ANDMASS SPECTROMETRY.	19369195 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394 AND THR-402, ANDMASS SPECTROMETRY.	17924679 [Abstract]

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