Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Site-directed mutants of the beta subunit of protein kinase CK2 demonstrate the important role of Pro-58.

FEBS letters - 17 Jul 1995

Hinrichs M V, Gatica M, Allende C C, Allende J E

Abstract excerpt

The following amino acids of the Xenopus laevis beta subunit of protein kinase CK2 (casein kinase 2) were changed to alanine: Pro-58 (beta P-->A); Asp-59 and Glu-60 and Glu-61 (beta DEE-->AAA); His-151-153 (beta HHH-->AAA). The last 37 amino acids of the carboxyl end were deleted (beta delta 179-215). Stimulation of CK2 alpha catalytic subunit activity was measured with casein as substrate and the following...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Base Sequence
Share to DNA
Share to DNA-Binding Proteins

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Molecular Sequence Data

Share to Mutagenesis, Site-Directed

Share to Mutation

Share to Phosphorylation

Share to Protein Conformation

Source

Identifiers

PMID: 7628607
DOI: 10.1016/0014-5793(95)00647-r

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Site-directed mutants of the beta subunit of protein kinase CK2 demonstrate the important role of Pro-58.PMID 7628607Read ↗

Role of the carboxyl terminus on the catalytic activity of protein kinase CK2alpha subunit.Semantic proximity Read ↗

C-terminal region of protein kinase CK2 alpha: How the structure can affect function and stability of the catalytic subunit.Semantic proximity Read ↗

Basic residues in the 74-83 and 191-198 segments of protein kinase CK2 catalytic subunit are implicated in negative but not in positive regulation by the beta-subunit.Semantic proximity Read ↗

Catalytic activity of mutants of yeast protein kinase CK2alpha.Semantic proximity Read ↗

Mapping of the interaction sites of the growth suppressor protein p53 with the regulatory beta-subunit of protein kinase CK2.Semantic proximity Read ↗

Crystal structure of a C-terminal deletion mutant of human protein kinase CK2 catalytic subunit.Semantic proximity Read ↗

Casein kinase 2 down-regulation and activation by polybasic peptides are mediated by acidic residues in the 55-64 region of the beta-subunit. A study with calmodulin as phosphorylatable substrate.Semantic proximity Read ↗

Structure of the human protein kinase CK2 catalytic subunit CK2α' and interaction thermodynamics with the regulatory subunit CK2β.Semantic proximity Read ↗

Drosophila protein kinase CK2 is rendered temperature-sensitive by mutations of highly conserved residues flanking the activation segment.Semantic proximity Read ↗

The role of the N-terminal domain in the regulation of the "constitutively active" conformation of protein kinase CK2α: insight from a molecular dynamics investigation.Semantic proximity Read ↗

Interactions of protein kinase CK2 subunits.Semantic proximity Read ↗

Mapping of the interaction sites between Wee1 kinase and the regulatory beta-subunit of protein kinase CK2.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.