Rps6ka2 Peptide - C-Terminal Region Blocking Peptide

Function: Serine/threonine-protein kinase that acts downstream of ERK (MAPK1/ERK2 and MAPK3/ERK1) signaling and mediates mitogenic and stress-induced activation of transcription factors, regulates translation, and mediates cellular proliferation, survival, and differentiation. May function as tumor suppressor in epithelial ovarian cancer cells

By similarity.

Catalytic activity: ATP + a protein = ADP + a phosphoprotein.

Cofactor: Magnesium

By similarity.

Enzyme regulation: Upon extracellular signal or mitogen stimulation, phosphorylated at Thr-570 in the C-terminal kinase domain (CTKD) by MAPK1/ERK2 and MAPK3/ERK1. The activated CTKD then autophosphorylates Ser-377, allowing binding of PDPK1, which in turn phosphorylates Ser-218 in the N-terminal kinase domain (NTDK) leading to the full activation of the protein and subsequent phosphorylation of the substrates by the NTKD.

Subunit structure: Forms a complex with either MAPK1/ERK2 or MAPK3/ERK1 in quiescent cells. Transiently dissociates following mitogenic stimulation

By similarity.

Subcellular location: Nucleus

By similarity. Cytoplasm

By similarity.

Post-translational modification: Activated by phosphorylation at Ser-218 by PDPK1. Autophosphorylated on Ser-377, as part of the activation process. May be phosphorylated at Thr-356 and Ser-360 by MAPK1/ERK2 and MAPK3/ERK1

By similarity.N-terminal myristoylation results in an activated kinase in the absence of added growth factors

By similarity.

Sequence similarities: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. S6 kinase subfamily.Contains 1 AGC-kinase C-terminal domain.Contains 2 protein kinase domains.