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Ribosomal protein S6 kinase alpha-2 is an enzyme that in humans is encoded by the RPS6KA2gene.[5][6]
This gene encodes a member of the RSK (ribosomal S6 kinase) family of serine and threoninekinases. This kinase contains 2 non-identical kinase catalytic domains and phosphorylates various substrates, including members of the mitogen-activated kinase (MAPK) signalling pathway. The activity of this protein has been implicated in controlling cell growth and differentiation. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.[6]
Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin". J. Infect. 24 (3): 317–20. doi:10.1016/S0163-4453(05)80037-4. PMID1602151.
Schimenti JC (2000). "ORFless, intronless, and mutant transcription units in the mouse t complex responder (Tcr) locus". Mamm. Genome. 10 (10): 969–76. doi:10.1007/s003359901142. PMID10501965. S2CID23157540.
Gudi T, Casteel DE, Vinson C, et al. (2001). "NO activation of fos promoter elements requires nuclear translocation of G-kinase I and CREB phosphorylation but is independent of MAP kinase activation". Oncogene. 19 (54): 6324–33. doi:10.1038/sj.onc.1204007. PMID11175347. S2CID20150481.
Willard FS, Crouch MF (2001). "MEK, ERK, and p90RSK are present on mitotic tubulin in Swiss 3T3 cells: a role for the MAP kinase pathway in regulating mitotic exit". Cell. Signal. 13 (9): 653–64. doi:10.1016/S0898-6568(01)00185-1. PMID11495723.
This page was last edited on 23 December 2023, at 18:53