BMP2K

{{Short description|Protein-coding gene in the species Homo sapiens}}

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BMP-2-inducible protein kinase is an enzyme in humans encoded by the BMP2K gene.{{cite web | title = Entrez Gene: BMP2K BMP2 inducible kinase| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=55589}}

Function

This gene is the human homolog of mouse BMP-2-inducible kinase. Bone morphogenic proteins (BMPs) play a key role in skeletal development and patterning. Expression of the mouse gene is increased during BMP-2 induced differentiation and the gene product is a putative serine/threonine protein kinase containing a nuclear localization signal. Therefore, the protein encoded by this human homolog is thought to be a protein kinase with a putative regulatory role in attenuating the program of osteoblast differentiation. Two transcript variants encoding different isoforms have been found for this gene.

References

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Further reading

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  • {{cite journal | vauthors = Hoffmann A, Gross G | title = BMP signaling pathways in cartilage and bone formation | journal = Critical Reviews in Eukaryotic Gene Expression | volume = 11 | issue = 1–3 | pages = 23–45 | year = 2002 | pmid = 11693963 }}
  • {{cite journal | vauthors = Ueki N, Oda T, Kondo M, Yano K, Noguchi T, Muramatsu M | title = Selection system for genes encoding nuclear-targeted proteins | journal = Nature Biotechnology | volume = 16 | issue = 13 | pages = 1338–42 | date = Dec 1998 | pmid = 9853615 | doi = 10.1038/4315 | s2cid = 20001769 }}
  • {{cite journal | vauthors = Kearns AE, Donohue MM, Sanyal B, Demay MB | title = Cloning and characterization of a novel protein kinase that impairs osteoblast differentiation in vitro | journal = The Journal of Biological Chemistry | volume = 276 | issue = 45 | pages = 42213–8 | date = Nov 2001 | pmid = 11500515 | doi = 10.1074/jbc.M106163200 | doi-access = free }}
  • {{cite journal | vauthors = Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J | title = Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides | journal = Nature Biotechnology | volume = 21 | issue = 5 | pages = 566–9 | date = May 2003 | pmid = 12665801 | doi = 10.1038/nbt810 | s2cid = 23783563 }}
  • {{cite journal | vauthors = Arikawa T, Omura K, Morita I | title = Regulation of bone morphogenetic protein-2 expression by endogenous prostaglandin E2 in human mesenchymal stem cells | journal = Journal of Cellular Physiology | volume = 200 | issue = 3 | pages = 400–6 | date = Sep 2004 | pmid = 15254968 | doi = 10.1002/jcp.20031 | s2cid = 28129401 }}
  • {{cite journal | vauthors = Medici M, van Meurs JB, Rivadeneira F, Zhao H, Arp PP, Hofman A, Pols HA, Uitterlinden AG | title = BMP-2 gene polymorphisms and osteoporosis: the Rotterdam Study | journal = Journal of Bone and Mineral Research | volume = 21 | issue = 6 | pages = 845–54 | date = Jun 2006 | pmid = 16753015 | doi = 10.1359/jbmr.060306 | s2cid = 25680897 | doi-access = free }}
  • {{cite journal | vauthors = Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M | title = Global, in vivo, and site-specific phosphorylation dynamics in signaling networks | journal = Cell | volume = 127 | issue = 3 | pages = 635–48 | date = Nov 2006 | pmid = 17081983 | doi = 10.1016/j.cell.2006.09.026 | s2cid = 7827573 | doi-access = free }}

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