SRPK1/2 phosphorylates nucleoprotein

Stable Identifier
R-HSA-9729330
Type
Reaction [transition]
Species
Homo sapiens
Related Species
Severe acute respiratory syndrome coronavirus 2
Compartment
ReviewStatus
5/5
Locations in the PathwayBrowser
General
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Full phosphorylation of SARS-CoV-2 nucleoprotein (N) depends on priming phosphorylations on at least two sites by SRPK1/2 protein kinases (Heaton et al, 2020; Carlson et al, 2020). Both kinases are monomers that need a magnesium cofactor to work, and are activated through phosphorylation by CK2 kinase (Daub et al, 2002).
Literature References
PubMed ID Title Journal Year
33248025 Phosphoregulation of Phase Separation by the SARS-CoV-2 N Protein Suggests a Biophysical Basis for its Dual Functions

Howard, CJ, Hartooni, N, Ghent, CM, Carlson, CR, Morgan, DO, Frankel, AD, Asfaha, JB, Safari, M

Mol Cell 2020
32817937 The FDA-approved drug Alectinib compromises SARS-CoV-2 nucleocapsid phosphorylation and inhibits viral infection in vitro

Chaparian, RR, Bulaon, DK, Anand, SK, Johnson, JL, Shobana-Ganesh, K, Trimarco, JD, Liberatore, KM, Levy, TM, Nilsson-Payant, BE, Getz, G, Beausoleil, SA, Weinstein, H, Tata, PR, Kavanagh-Williamson, M, Matthews, D, Yaron, TM, Chen, SB, Lee, G, Kerelsky, A, Lin, TY, Heesom, K, Cohen, BM, Mercadante, MN, Blenis, J, Possemato, AP, Zhu, X, Tkachev, SL, Hamele, CE, Piskounova, E, Smith, CM, Davidson, AD, Harding, AT, He, L, Heaton, BE, Jordan, TX, Burke, KN, Cantley, LC, Kastenhuber, ER, tenOever, BR, Tata, A, Aguet, F, Elemento, O, Hornbeck, PV, Schwartz, RE, Heaton, NS

bioRxiv 2020
Participants
Participates
Catalyst Activity

protein serine kinase activity of SRPK1/2 [cytosol]

Disease
Name Identifier Synonyms
COVID-19 DOID:0080600 2019 Novel Coronavirus (2019-nCoV), Wuhan seafood market pneumonia virus infection, 2019-nCoV infection, Wuhan coronavirus infection
Authored
Reviewed
Created
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