Biology:JMJD6
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Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6 is an enzyme that in humans is encoded by the JMJD6 gene.[1][2]
Function
This gene encodes a nuclear protein with a JmjC domain. JmjC domain-containing proteins belong to the alpha-ketoglutarate-dependent hydroxylase superfamily. They are predicted to function as protein hydroxylases or histone demethylases. This protein was first identified as a putative phosphatidylserine receptor involved in phagocytosis of apoptotic cells. Subsequent studies suggest that the protein may cross-react with a monoclonal antibody that recognizes the phosphatidylserine receptor and does not directly function in the clearance of apoptotic cells. Multiple transcript variants encoding different isoforms have been found for this gene.[2] On a physiological level JMJD6 has a role in angiogenesis, the process of vessel formation, whereas further roles of JMJD6 in pathophysiological processes were implicated, such as mammary tumorigenesis.[3] Here, elevated JMJD6 level were found in breast cancer associated with aggressiveness and metastasis in mice.[4]
References
- ↑ "Elastase-mediated phosphatidylserine receptor cleavage impairs apoptotic cell clearance in cystic fibrosis and bronchiectasis". The Journal of Clinical Investigation 109 (5): 661–70. March 2002. doi:10.1172/JCI13572. PMID 11877474.
- ↑ 2.0 2.1 "Entrez Gene: JMJD6 jumonji domain containing 6". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23210.
- ↑ "Jumonji domain-containing protein 6 (Jmjd6) is required for angiogenic sprouting and regulates splicing of VEGF-receptor 1". Proceedings of the National Academy of Sciences of the United States of America 108 (8): 3276–81. February 2011. doi:10.1073/pnas.1008098108. PMID 21300889. Bibcode: 2011PNAS..108.3276B.
- ↑ "The epigenetic modifier JMJD6 is amplified in mammary tumors and cooperates with c-Myc to enhance cellular transformation, tumor progression, and metastasis". Clin Epigenetics 8 (38): 38. 14 Apr 2016. doi:10.1186/s13148-016-0205-6. PMID 27081402.
Further reading
- "Jumonji domain-containing protein 6 (Jmjd6) is required for angiogenic sprouting and regulates splicing of VEGF-receptor 1". Proceedings of the National Academy of Sciences of the United States of America 108 (8): 3276–81. February 2011. doi:10.1073/pnas.1008098108. PMID 21300889. Bibcode: 2011PNAS..108.3276B.
- "Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated with RNA splicing". Science 325 (5936): 90–3. July 2009. doi:10.1126/science.1175865. PMID 19574390. Bibcode: 2009Sci...325...90W. https://hzi.openrepository.com/hzi/bitstream/10033/78493/1/Webby%20et%20al_final.pdf.
- "Endogenous Jmjd6 gene product is expressed at the cell surface and regulates phagocytosis in immature monocyte-like activated THP-1 cells". Journal of Cellular Physiology 221 (1): 84–91. October 2009. doi:10.1002/jcp.21829. PMID 19492415.
- "Genomic structure and expression of Jmjd6 and evolutionary analysis in the context of related JmjC domain containing proteins". BMC Genomics 9: 293. 2008. doi:10.1186/1471-2164-9-293. PMID 18564434.
- "JMJD6 is a histone arginine demethylase". Science 318 (5849): 444–7. October 2007. doi:10.1126/science.1145801. PMID 17947579. Bibcode: 2007Sci...318..444C.
- "JmjC-domain-containing proteins and histone demethylation". Nature Reviews Genetics 7 (9): 715–27. September 2006. doi:10.1038/nrg1945. PMID 16983801.
- "Hide and seek: the secret identity of the phosphatidylserine receptor". Journal of Biology 3 (4): 14. 2005. doi:10.1186/jbiol14. PMID 15453906.
- "The phosphatidylserine receptor has essential functions during embryogenesis but not in apoptotic cell removal". Journal of Biology 3 (4): 15. 2005. doi:10.1186/jbiol10. PMID 15345036.
- "Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro". DNA Research 5 (1): 31–9. February 1998. doi:10.1093/dnares/5.1.31. PMID 9628581.
- "A receptor for phosphatidylserine-specific clearance of apoptotic cells". Nature 405 (6782): 85–90. May 2000. doi:10.1038/35011084. PMID 10811223. Bibcode: 2000Natur.405...85F.
- "Effects of phosphatidylserine on p38 mitogen activated protein kinase, cyclic AMP responding element binding protein and nuclear factor-kappaB activation in resting and activated microglial cells". Journal of Neurochemistry 84 (2): 413–6. January 2003. doi:10.1046/j.1471-4159.2003.01562.x. PMID 12559004.
- "Phagocytosis of apoptotic inflammatory cells by microglia and its therapeutic implications: termination of CNS autoimmune inflammation and modulation by interferon-beta". Glia 43 (3): 231–42. September 2003. doi:10.1002/glia.10258. PMID 12898702.
- "Cell corpse engulfment mediated by C. elegans phosphatidylserine receptor through CED-5 and CED-12". Science 302 (5650): 1563–6. November 2003. doi:10.1126/science.1087641. PMID 14645848. Bibcode: 2003Sci...302.1563W. http://ntur.lib.ntu.edu.tw/bitstream/246246/161415/1/06.pdf.
- "Nuclear localization of the phosphatidylserine receptor protein via multiple nuclear localization signals". Experimental Cell Research 293 (1): 154–63. February 2004. doi:10.1016/j.yexcr.2003.09.023. PMID 14729065.
- "Phosphatidylserine receptor cooperates with high-density lipoprotein receptor in recognition of apoptotic cells by thymic nurse cells". Journal of Molecular Endocrinology 32 (2): 497–505. April 2004. doi:10.1677/jme.0.0320497. PMID 15072554.
- "The phosphatidylserine receptor from Hydra is a nuclear protein with potential Fe(II) dependent oxygenase activity". BMC Cell Biology 5: 26. June 2004. doi:10.1186/1471-2121-5-26. PMID 15193161.
- "Phosphatidylserine receptor is required for the engulfment of dead apoptotic cells and for normal embryonic development in zebrafish". Development 131 (21): 5417–27. November 2004. doi:10.1242/dev.01409. PMID 15469976.
- "Phosphatidylserine receptor in chronic pancreatitis: evidence for a macrophage independent role". Annals of Surgery 241 (1): 144–51. January 2005. doi:10.1097/01.sla.0000149304.89456.5a. PMID 15622002.
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