dbPTM

NEK11_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NEK11_HUMAN
UniProt AC	Q8NG66
Protein Name	Serine/threonine-protein kinase Nek11
Gene Name	NEK11 {ECO:0000312\|HGNC:HGNC:18593}
Organism	Homo sapiens (Human).
Sequence Length	645
Subcellular Localization	Nucleus. Nucleus, nucleolus. Nuclear during interphase but moves to the polar microtubules during prometaphase and metaphase. Accumulates in the nucleolus in G1/S-arrested cells.
Protein Description	Protein kinase which plays an important role in the G2/M checkpoint response to DNA damage. Controls degradation of CDC25A by directly phosphorylating it on residues whose phosphorylation is required for BTRC-mediated polyubiquitination and degradation..
Protein Sequence	MLKFQEAAKCVSGSTAISTYPKTLIARRYVLQQKLGSGSFGTVYLVSDKKAKRGEELKVLKEISVGELNPNETVQANLEAQLLSKLDHPAIVKFHASFVEQDNFCIITEYCEGRDLDDKIQEYKQAGKIFPENQIIEWFIQLLLGVDYMHERRILHRDLKSKNVFLKNNLLKIGDFGVSRLLMGSCDLATTLTGTPHYMSPEALKHQGYDTKSDIWSLACILYEMCCMNHAFAGSNFLSIVLKIVEGDTPSLPERYPKELNAIMESMLNKNPSLRPSAIEILKIPYLDEQLQNLMCRYSEMTLEDKNLDCQKEAAHIINAMQKRIHLQTLRALSEVQKMTPRERMRLRKLQAADEKARKLKKIVEEKYEENSKRMQELRSRNFQQLSVDVLHEKTHLKGMEEKEEQPEGRLSCSPQDEDEERWQGREEESDEPTLENLPESQPIPSMDLHELESIVEDATSDLGYHEIPEDPLVAEEYYADAFDSYCEESDEEEEEIALERPEKEIRNEGSQPAYRTNQQDSDIEALARCLENVLGCTSLDTKTITTMAEDMSPGPPIFNSVMARTKMKRMRESAMQKLGTEVFEEVYNYLKRARHQNASEAEIRECLEKVVPQASDCFEVDQLLYFEEQLLITMGKEPTLQNHL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
44	Phosphorylation	SGSFGTVYLVSDKKA CCCCCEEEEECCCCC	10.96	-
47	Phosphorylation	FGTVYLVSDKKAKRG CCEEEEECCCCCCCC	40.91	-
84	Phosphorylation	NLEAQLLSKLDHPAI HHHHHHHHCCCCCHH	39.50	24719451
85	Ubiquitination	LEAQLLSKLDHPAIV HHHHHHHCCCCCHHH	58.88	-
273	Phosphorylation	SMLNKNPSLRPSAIE HHHCCCCCCCHHHHH	46.53	14702039
312	Acetylation	DKNLDCQKEAAHIIN CCCCCHHHHHHHHHH	56.50	19825773
334	Phosphorylation	LQTLRALSEVQKMTP HHHHHHHHHHHHCCH	34.43	28857561
387	Phosphorylation	SRNFQQLSVDVLHEK HCCHHHHHHHHHHHH	16.37	27966365
412	Phosphorylation	EQPEGRLSCSPQDED CCCCCCCCCCCCCCC	15.93	27794612
414	Phosphorylation	PEGRLSCSPQDEDEE CCCCCCCCCCCCCHH	23.40	23927012
585 (in isoform 4)	Phosphorylation	-	52.29	-

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
273	S	Phosphorylation	Kinase	CHK1	O14757	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
273	S	Phosphorylation		19734889
Phosphorylation at Ser-273 is important 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
312	Acetylation	304 (8)	E ⇒ V	rs3738000	Carotid intima media thickness	26343869

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
BLM_HUMAN	BLM	physical	24239288
FKBP5_HUMAN	FKBP5	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
DB08912	Dabrafenib

Regulatory Network of NEK11_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"NEK11: linking CHK1 and CDC25A in DNA damage checkpoint signaling."; Soerensen C.S., Melixetian M., Klein D.K., Helin K.; Cell Cycle 9:450-455(2010). Cited for: FUNCTION, AND PHOSPHORYLATION AT SER-273.	20090422 [Abstract]
"NEK11 regulates CDC25A degradation and the IR-induced G2/Mcheckpoint."; Melixetian M., Klein D.K., Soerensen C.S., Helin K.; Nat. Cell Biol. 11:1247-1253(2009). Cited for: FUNCTION, AND PHOSPHORYLATION AT SER-273.	19734889 [Abstract]