Protein Serine/threonine-protein kinase H1 is a Ser/Thr protein kinase that is encoded by the PSKH1 gene in humans and is associated with organelle membranes. PSKH1 resides within, and transits between, organelles in the human secretory pathway notably the Endoplasmic Reticulum.[5][6]
Interactions
PSKH1 is a regulated protein kinase with a defined substrate specificity, which has been shown to interact with (and be regulated by) proteins of the Cab45, reticulocalbin, Erc55, and calumenin family of calcium-binding proteins and calmodulin. It is also activated by UNC119B, an acyl chain binding protein.[7] PSKH1 is closely related to the catalytically-inactive pseudokinase PSKH2, which is also membrane-localised within the secretory pathway.[8]
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000159792 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000048310 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ Larsen F, Solheim J, Kristensen T, Kolstø AB, Prydz H (February 1994). "A tight cluster of five unrelated human genes on chromosome 16q22.1". Hum Mol Genet. 2 (10): 1589–95. doi:10.1093/hmg/2.10.1589. PMID 8268911.
- ^ "Entrez Gene: PSKH1 protein serine kinase H1".
- ^ Horne CR, Young SY, Mather LJ, Dagley LF, Johnson JL, Yaron-Barir TM, Huntsman EM, Daly LA, Byrne DP, Cadell AL, Ng BH, Yousef J, Multari DH, Shen L, McAloon LM, Manning G, Febbraio MA, Means AR, Cantley LC, Tanzer MC, Croucher DR, Eyers CE, Eyers PA, Scott JW, and Murphy JM (February 2025). "PSKH1 kinase activity is differentially modulated via allosteric binding of Ca2+ sensor proteins". PNAS. 122 (8). doi:10.1073/pnas.2420961122. PMC 11873932. PMID 39964718.
- ^ Byrne DP, Shrestha S, Daly LA, Marensi V, Ramakrishnan K, Eyers CE, Kannan N, and Eyers PA (January 2023). "Evolutionary and cellular analysis of the 'dark' pseudokinase PSKH2". Biochemical Journal. 480 (2): 141–160. doi:10.1042/BCJ20220474. PMC 11873932. PMID 39964718.
Further reading
- Hanks SK (1987). "Homology probing: identification of cDNA clones encoding members of the protein-serine kinase family". Proc. Natl. Acad. Sci. U.S.A. 84 (2): 388–92. Bibcode:1987PNAS...84..388H. doi:10.1073/pnas.84.2.388. PMC 304212. PMID 2948189.
- Petersen BO, Lukas J, Sørensen CS, Bartek J, Helin K (1999). "Phosphorylation of mammalian CDC6 by cyclin A/CDK2 regulates its subcellular localization". EMBO J. 18 (2): 396–410. doi:10.1093/emboj/18.2.396. PMC 1171134. PMID 9889196.
- Amarzguioui M, Brede G, Babaie E, Grotli M, Sproat B, Prydz H (2000). "Secondary structure prediction and in vitro accessibility of mRNA as tools in the selection of target sites for ribozymes". Nucleic Acids Res. 28 (21): 4113–24. doi:10.1093/nar/28.21.4113. PMC 113158. PMID 11058107.
- Brede G, Solheim J, Tröen G, Prydz H (2001). "Characterization of PSKH1, a novel human protein serine kinase with centrosomal, golgi, and nuclear localization". Genomics. 70 (1): 82–92. doi:10.1006/geno.2000.6365. PMID 11087665.
- Brede G, Solheim J, Prydz H (2002). "PSKH1, a novel splice factor compartment-associated serine kinase". Nucleic Acids Res. 30 (23): 5301–9. doi:10.1093/nar/gkf648. PMC 137962. PMID 12466556.
- Brede G, Solheim J, Stang E, Prydz H (2004). "Mutants of the protein serine kinase PSKH1 disassemble the Golgi apparatus". Exp. Cell Res. 291 (2): 299–312. doi:10.1016/j.yexcr.2003.07.009. PMID 14644153.
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