NEK6_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NEK6_MOUSE
• UniProt AC: Q9ES70
• Protein Name: Serine/threonine-protein kinase Nek6
• Gene Name: Nek6
• Organism: Mus musculus (Mouse).
• Sequence Length: 313
• Subcellular Localization: Cytoplasm. Nucleus. Nucleus speckle. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle pole. Co- localizes with APBB1 at the nuclear speckles. Colocalizes with PIN1 in the nucleus. Colocalizes with A
• Protein Description: Protein kinase which plays an important role in mitotic cell cycle progression. Required for chromosome segregation at metaphase-anaphase transition, robust mitotic spindle formation and cytokinesis. Phosphorylates ATF4, CIR1, PTN, RAD26L, RBBP6, RPS7, TRIP4, RPS6KB1 and histones H1 and H3. Phosphorylates KIF11 to promote mitotic spindle formation. Involved in G2/M phase cell cycle arrest induced by DNA damage. Inhibition of activity results in apoptosis. May contribute to tumorigenesis by suppressing p53/TP53-induced cancer cell senescence (By similarity). Phosphorylates STAT3..
• Protein Sequence: MAGQPSHMPHGGSPNHLCHALGPAPPPDPQRLPNTLSFRCSLADFQIEKKIGRGQFSEVYKATCLLDRKTVALKKVQIFEMMDAKARQDCVKEIGLLKQLNHPNIIKYLDSFIEDNELNIVLELADAGDLSQMIKYFKKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGIVKLGDLGLGRFFSSETTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNLFSLCQKIEQCDYPPLPGEHYSEKLRELVSMCIYPDPDHRPDIVYVHQVARQMHVWTSST

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MAGQPSHM -------CCCCCCCC	9.49	-
6	Phosphorylation	--MAGQPSHMPHGGS --CCCCCCCCCCCCC	25.24	29233185
13	Phosphorylation	SHMPHGGSPNHLCHA CCCCCCCCCCCCHHH	27.41	30352176
35	Phosphorylation	DPQRLPNTLSFRCSL CCCCCCCCEEEEEEH	23.10	29472430
37	Phosphorylation	QRLPNTLSFRCSLAD CCCCCCEEEEEEHHH	14.49	29472430
198	Phosphorylation	LGLGRFFSSETTAAH CCCCCCCCCCCHHHH	25.26	17242355
199	Phosphorylation	GLGRFFSSETTAAHS CCCCCCCCCCHHHHH	33.53	17242355
201	Phosphorylation	GRFFSSETTAAHSLV CCCCCCCCHHHHHCC	24.55	28833060
202	Phosphorylation	RFFSSETTAAHSLVG CCCCCCCHHHHHCCC	20.14	28833060
206	Phosphorylation	SETTAAHSLVGTPYY CCCHHHHHCCCCCCC	21.74	21082442
210	Phosphorylation	AAHSLVGTPYYMSPE HHHHCCCCCCCCCHH	10.71	23984901
283	Phosphorylation	EKLRELVSMCIYPDP HHHHHHHHCCCCCCC	22.14	-
298	Phosphorylation	DHRPDIVYVHQVARQ CCCCCEEEEEHHHHH	7.79	-

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
206	S	Phosphorylation	Kinase	NEK9	Q8K1R7	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
206	S	Phosphorylation	Phosphorylation at Ser-206 is required for its activation.	-
210	T	Phosphorylation	Interaction with APBB1 down-regulates phosphorylation at Thr-210 (By similarity).	-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of NEK6_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of NEK6_MOUSE !!

Drug and Disease Associations

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