MYL9

Myosin, light chain 9, regulatory
Identifiers
Symbols	MYL9 ; LC20; MLC-2C; MLC2; MRLC1; MYRL2
External IDs	OMIM: 609905 MGI: 1914518 HomoloGene: 21230 GeneCards: MYL9 Gene
Gene ontology Molecular function • calcium ion binding • structural constituent of muscle • myosin heavy chain binding Cellular component • stress fiber • cytosol • muscle myosin complex • Z disc Biological process • muscle contraction • regulation of muscle contraction • small GTPase mediated signal transduction • axon guidance • ephrin receptor signaling pathway • platelet aggregation Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	10398	98932
Ensembl	ENSG00000101335	ENSMUSG00000067818
UniProt	P24844	Q9CQ19
RefSeq (mRNA)	NM_006097	NM_172118
RefSeq (protein)	NP_006088	NP_742116
Location (UCSC)	Chr 20: 36.54 – 36.55 Mb	Chr 2: 156.78 – 156.78 Mb
PubMed search

Myosin regulatory light polypeptide 9 is a protein that in humans is encoded by the MYL9 gene.^[1]

Function

Myosin, a structural component of muscle, consists of two heavy chains and four light chains. The protein encoded by this gene is a myosin light chain that may regulate muscle contraction by modulating the ATPase activity of myosin heads. The encoded protein binds calcium and is activated by myosin light chain kinase. Two transcript variants encoding different isoforms have been found for this gene.^[2]

References

1. Kumar CC, Mohan SR, Zavodny PJ, Narula SK, Leibowitz PJ (May 1989). "Characterization and differential expression of human vascular smooth muscle myosin light chain 2 isoform in nonmuscle cells". Biochemistry 28 (9): 4027–35. doi:10.1021/bi00435a059. PMID 2526655.
2. "Entrez Gene: myosin".

Further reading

• Stelzl U, Worm U, Lalowski M, et al. (2005). "A human protein-protein interaction network: a resource for annotating the proteome.". Cell 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. PMID 16169070.
• Szczesna-Cordary D, Guzman G, Zhao J, et al. (2005). "The E22K mutation of myosin RLC that causes familial hypertrophic cardiomyopathy increases calcium sensitivity of force and ATPase in transgenic mice.". J. Cell. Sci. 118 (Pt 16): 3675–83. doi:10.1242/jcs.02492. PMID 16076902.
• Deloukas P, Matthews LH, Ashurst J, et al. (2001). "The DNA sequence and comparative analysis of human chromosome 20.". Nature 414 (6866): 865–71. doi:10.1038/414865a. PMID 11780052.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Iwasaki T, Murata-Hori M, Ishitobi S, Hosoya H (2001). "Diphosphorylated MRLC is required for organization of stress fibers in interphase cells and the contractile ring in dividing cells.". Cell Struct. Funct. 26 (6): 677–83. doi:10.1247/csf.26.677. PMID 11942626.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Higashihara M, Watanabe M, Usuda S, Miyazaki K (2008). "Smooth muscle type isoform of 20 kDa myosin light chain is expressed in monocyte/macrophage cell lineage". Journal of smooth muscle research = Nihon Heikatsukin Gakkai kikanshi 44 (1): 29–40. doi:10.1540/jsmr.44.29. PMID 18480596.
• Kumar CC, Mohan SR, Zavodny PJ, et al. (1989). "Characterization and differential expression of human vascular smooth muscle myosin light chain 2 isoform in nonmuscle cells". Biochemistry 28 (9): 4027–35. doi:10.1021/bi00435a059. PMID 2526655.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.