ExplorEnz: EC 2.7.11.38

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2.7.11.38

Accepted name:

NEK9 subfamily protein kinase

Reaction:

(1) ATP + [protein]-L-serine = ADP + [protein]-O-phospho-L-serine
(2) ATP + [protein]-L-threonine = ADP + [protein]-O-phospho-L-threonine

Other name(s):

NEK9 subfamily kinase (misleading); serine/threonine-protein kinase Nek9; NEK9 (gene name); NERCC1 (gene name)

Systematic name:

ATP:protein Ser/(Thr)-phosphotransferase (NEK9 subfamily)

Comments:

This enzyme is found in animals and choanoflagellates, although it has been lost in arthropods and nematodes. It is implicated in centrosome separation [1] and cilium formation [6]. In peptide arrays, the enzyme prefers to phosphorylate Ser, with acidic residues at -2 and -4/-5, similar to that of the NEK6 protein kinase subfamily [4]. NEK9 can autophosphorylate. Substrates in humans include the microtubule-associated protein kinases NEK6/7 [1], the microtubule-associated protein spindle assembly protein TPX2 [3], the γ-tubulin associated protein NEDD1, which is required for mitotic spindle assembly and function [2] and the LC3B protein, which is involved in autophagy substrate selection and autophagosome biogenesis [5].

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Bertran, M.T., Sdelci, S., Regue, L., Avruch, J., Caelles, C. and Roig, J. Nek9 is a Plk1-activated kinase that controls early centrosome separation through Nek6/7 and Eg5. EMBO J. 30 (2011) 2634–2647. [DOI] [PMID: 21642957]
2.	Sdelci, S., Schutz, M., Pinyol, R., Bertran, M.T., Regue, L., Caelles, C., Vernos, I. and Roig, J. Nek9 phosphorylation of NEDD1/GCP-WD contributes to Plk1 control of γ-tubulin recruitment to the mitotic centrosome. Curr. Biol. 22 (2012) 1516–1523. [DOI] [PMID: 22818914]
3.	Eibes, S., Gallisa-Sune, N., Rosas-Salvans, M., Martinez-Delgado, P., Vernos, I. and Roig, J. Nek9 Phosphorylation Defines a New Role for TPX2 in Eg5-Dependent Centrosome Separation before Nuclear Envelope Breakdown. Curr. Biol. 28 (2018) 121–129.e4. [DOI] [PMID: 29276125]
4.	van de Kooij, B., Creixell, P., van Vlimmeren, A., Joughin, B.A., Miller, C.J., Haider, N., Simpson, C.D., Linding, R., Stambolic, V., Turk, B.E. and Yaffe, M.B. Comprehensive substrate specificity profiling of the human Nek kinome reveals unexpected signaling outputs. Elife 8 (2019) . [DOI] [PMID: 31124786]
5.	Shrestha, B.K., Skytte Rasmussen, M., Abudu, Y.P., Bruun, J.A., Larsen, K.B., Alemu, E.A., Sjottem, E., Lamark, T. and Johansen, T. NIMA-related kinase 9-mediated phosphorylation of the microtubule-associated LC3B protein at Thr-50 suppresses selective autophagy of p62/sequestosome 1. J. Biol. Chem. 295 (2020) 1240–1260. [DOI] [PMID: 31857374]
6.	Yamamoto, Y., Chino, H., Tsukamoto, S., Ode, K.L., Ueda, H.R. and Mizushima, N. NEK9 regulates primary cilia formation by acting as a selective autophagy adaptor for MYH9/myosin IIA. Nat. Commun. 12:3292 (2021). [DOI] [PMID: 34078910]

[EC 2.7.11.38 created 2024]