Figure 1.
(A) Canonical and pseudokinase PSKH2 orthologs mapped to the SwissTree reference species tree. (B) Alphafold models for full length PSKH2 from Human (Q96QS6), Orangutan (H2PQQ4), Guinea Pig (H0VF24), and Opossum (F7ELA1). (C) Immunoblot showing expression of full length and truncated N-terminal (NT) or (D) C-terminal (CT)-MYC tagged PSKH2 variants in HEK-293T cells. (E) Expression of full-length (1–385) and truncated (62–385) PSKH2 in the presence/absence of MG132. (F) Expression of WT PSKH2 and mutants containing amino acid substitutions at putative sites of N-terminal acylation. (G) Immunoblot showing changes in PSKH2 stability with incremental truncations at the N-terminus. Two independently repeated experiments are provided. All immunoblots constitute whole cell lysates processed with SDS–PAGE sample buffer. Transfection using a plasmid expressing EGFP was used as a control.
Informatics and Biochemical characterisation of PSKH2.

(A) Canonical and pseudokinase PSKH2 orthologs mapped to the SwissTree reference species tree. (B) Alphafold models for full length PSKH2 from Human (Q96QS6), Orangutan (H2PQQ4), Guinea Pig (H0VF24), and Opossum (F7ELA1). (C) Immunoblot showing expression of full length and truncated N-terminal (NT) or (D) C-terminal (CT)-MYC tagged PSKH2 variants in HEK-293T cells. (E) Expression of full-length (1–385) and truncated (62–385) PSKH2 in the presence/absence of MG132. (F) Expression of WT PSKH2 and mutants containing amino acid substitutions at putative sites of N-terminal acylation. (G) Immunoblot showing changes in PSKH2 stability with incremental truncations at the N-terminus. Two independently repeated experiments are provided. All immunoblots constitute whole cell lysates processed with SDS–PAGE sample buffer. Transfection using a plasmid expressing EGFP was used as a control.

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