OXSR1

OXSR1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2V3S, 2VWI, 3DAK
Identifiers
Aliases	OXSR1, OSR1, oxidative stress responsive 1, oxidative stress responsive kinase 1
External IDs	OMIM: 604046 MGI: 1917378 HomoloGene: 31288 GeneCards: OXSR1
Gene location (Human) Chr. Chromosome 3 (human) Band 3p22.2 Start 38,165,089 bp End 38,255,484 bp
Gene location (Mouse) Chr. Chromosome 9 (mouse) Band 9|9 F3 Start 119,067,498 bp End 119,151,493 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in body of tongue saphenous vein gastrocnemius muscle embryo ganglionic eminence deltoid muscle bone marrow monocyte secondary oocyte biceps brachii Top expressed in skeletal muscle tissue quadriceps femoris muscle cumulus cell knee joint triceps brachii muscle ankle medullary collecting duct gastrocnemius muscle thoracic diaphragm ureter More reference expression data BioGPS More reference expression data
Gene ontology Molecular function magnesium ion binding protein kinase activity protein binding kinase activity metal ion binding nucleotide binding transferase activity ATP binding protein serine/threonine kinase activity identical protein binding protein kinase binding Cellular component extracellular exosome cytoplasm cytosol Biological process response to oxidative stress negative regulation of potassium ion transmembrane transport cellular hypotonic response phosphorylation negative regulation of potassium ion transmembrane transporter activity protein phosphorylation peptidyl-threonine phosphorylation intracellular signal transduction regulation of mitotic cell cycle signal transduction stress-activated protein kinase signaling cascade activation of protein kinase activity regulation of apoptotic process osmosensory signaling pathway positive regulation of T cell chemotaxis chemokine (C-C motif) ligand 21 signaling pathway chemokine (C-X-C motif) ligand 12 signaling pathway protein autophosphorylation cellular response to chemokine Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 9943 108737 Ensembl ENSG00000172939 ENSMUSG00000036737 UniProt O95747 Q6P9R2 RefSeq (mRNA) NM_005109 NM_133985 NM_001359582 RefSeq (protein) NP_005100 NP_598746 NP_001346511 Location (UCSC) Chr 3: 38.17 – 38.26 Mb Chr 9: 119.07 – 119.15 Mb PubMed search
Wikidata
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Serine/threonine-protein kinase OSR1 is an enzyme that in humans is encoded by the OXSR1 gene.

The product of this gene belongs to the Ser/Thr protein kinase family of proteins. It regulates downstream kinases in response to environmental stress, and may play a role in regulating the actin cytoskeleton.

Further reading

• Daigo Y, Isomura M, Nishiwaki T, et al. (1999). "Characterization of a 1200-kb genomic segment of chromosome 3p22-p21.3". DNA Res. 6 (1): 37–44. doi:10.1093/dnares/6.1.37. PMID 10231028.
• Kikuno R, Nagase T, Ishikawa K, et al. (1999). "Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 6 (3): 197–205. doi:10.1093/dnares/6.3.197. PMID 10470851.
• Piechotta K, Lu J, Delpire E (2003). "Cation chloride cotransporters interact with the stress-related kinases Ste20-related proline-alanine-rich kinase (SPAK) and oxidative stress response 1 (OSR1)". J. Biol. Chem. 277 (52): 50812–9. doi:10.1074/jbc.M208108200. PMID 12386165.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Chen W, Yazicioglu M, Cobb MH (2004). "Characterization of OSR1, a member of the mammalian Ste20p/germinal center kinase subfamily". J. Biol. Chem. 279 (12): 11129–36. doi:10.1074/jbc.M313562200. PMID 14707132.
• Beausoleil SA, Jedrychowski M, Schwartz D, et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. Bibcode:2004PNAS..10112130B. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
• Ballif BA, Villén J, Beausoleil SA, et al. (2005). "Phosphoproteomic analysis of the developing mouse brain". Mol. Cell. Proteomics. 3 (11): 1093–101. doi:10.1074/mcp.M400085-MCP200. PMID 15345747.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Barrios-Rodiles M, Brown KR, Ozdamar B, et al. (2005). "High-throughput mapping of a dynamic signaling network in mammalian cells". Science. 307 (5715): 1621–5. Bibcode:2005Sci...307.1621B. doi:10.1126/science.1105776. PMID 15761153. S2CID 39457788.
• Moriguchi T, Urushiyama S, Hisamoto N, et al. (2006). "WNK1 regulates phosphorylation of cation-chloride-coupled cotransporters via the STE20-related kinases, SPAK and OSR1". J. Biol. Chem. 280 (52): 42685–93. doi:10.1074/jbc.M510042200. PMID 16263722.
• Cusick JK, Xu LG, Bin LH, et al. (2006). "Identification of RELT homologues that associate with RELT and are phosphorylated by OSR1". Biochem. Biophys. Res. Commun. 340 (2): 535–43. doi:10.1016/j.bbrc.2005.12.033. PMID 16389068.
• Vitari AC, Thastrup J, Rafiqi FH, et al. (2006). "Functional interactions of the SPAK/OSR1 kinases with their upstream activator WNK1 and downstream substrate NKCC1". Biochem. J. 397 (1): 223–31. doi:10.1042/BJ20060220. PMC 1479760. PMID 16669787.
• Anselmo AN, Earnest S, Chen W, et al. (2006). "WNK1 and OSR1 regulate the Na+, K+, 2Cl- cotransporter in HeLa cells". Proc. Natl. Acad. Sci. U.S.A. 103 (29): 10883–8. Bibcode:2006PNAS..10310883A. doi:10.1073/pnas.0604607103. PMC 1544143. PMID 16832045.
• Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983. S2CID 7827573.
• Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
• Villa F, Goebel J, Rafiqi FH, et al. (2007). "Structural insights into the recognition of substrates and activators by the OSR1 kinase". EMBO Rep. 8 (9): 839–45. doi:10.1038/sj.embor.7401048. PMC 1973955. PMID 17721439.