{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Byrne DP"],"funding":["NCI NIH HHS","Biotechnology and Biological Sciences Research Council"],"pagination":["141-160"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9988210"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["480(2)"],"pubmed_abstract":["Pseudokinases, so named because they lack one or more conserved canonical amino acids that define their catalytically active relatives, have evolved a variety of biological functions in both prokaryotic and eukaryotic organisms. Human PSKH2 is closely related to the canonical kinase PSKH1, which maps to the CAMK family of protein kinases. Primates encode PSKH2 in the form of a pseudokinase, which is predicted to be catalytically inactive due to loss of the invariant catalytic Asp residue. Although the biological role(s) of vertebrate PSKH2 proteins remains unclear, we previously identified species-level adaptions in PSKH2 that have led to the appearance of kinase or pseudokinase variants in vertebrate genomes alongside a canonical PSKH1 paralog. In this paper we confirm that, as predicted,"],"journal":["The Biochemical journal"],"pubmed_title":["Evolutionary and cellular analysis of the 'dark' pseudokinase PSKH2."],"pmcid":["PMC9988210"],"funding_grant_id":["U01 CA239106","BB/S018514/1","BB/N021703/1"],"pubmed_authors":["Ramakrishnan K","Kannan N","Eyers CE","Marensi V","Eyers PA","Daly LA","Shrestha S","Byrne DP"],"additional_accession":[]},"is_claimable":false,"name":"Evolutionary and cellular analysis of the 'dark' pseudokinase PSKH2.","description":"Pseudokinases, so named because they lack one or more conserved canonical amino acids that define their catalytically active relatives, have evolved a variety of biological functions in both prokaryotic and eukaryotic organisms. Human PSKH2 is closely related to the canonical kinase PSKH1, which maps to the CAMK family of protein kinases. Primates encode PSKH2 in the form of a pseudokinase, which is predicted to be catalytically inactive due to loss of the invariant catalytic Asp residue. Although the biological role(s) of vertebrate PSKH2 proteins remains unclear, we previously identified species-level adaptions in PSKH2 that have led to the appearance of kinase or pseudokinase variants in vertebrate genomes alongside a canonical PSKH1 paralog. In this paper we confirm that, as predicted,","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Jan","modification":"2026-05-29T05:31:34.227Z","creation":"2025-02-18T23:44:33.904Z"},"accession":"S-EPMC9988210","cross_references":{"pubmed":["36520605"],"doi":["10.1042/BCJ20220474"]}}