MYL9

MYL9
Identifiers
Aliases	MYL9, LC20, MLC-2C, MLC2, MRLC1, MYRL2, myosin light chain 9, MMIHS4
External IDs	OMIM: 609905 MGI: 2138915 HomoloGene: 21230 GeneCards: MYL9
Gene location (Human) Chr. Chromosome 20 (human) Band 20q11.23 Start 36,541,497 bp End 36,551,447 bp
Gene location (Mouse) Chr. Chromosome 2 (mouse) Band 2|2 H1 Start 156,617,340 bp End 156,623,578 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in popliteal artery right coronary artery thoracic aorta ascending aorta left coronary artery saphenous vein gastric mucosa left uterine tube myometrium urethra Top expressed in ascending aorta aortic valve atrium cervix blood belly cord calvaria external carotid artery left colon pyloric antrum More reference expression data BioGPS n/a
Gene ontology Molecular function calcium ion binding structural constituent of muscle metal ion binding Cellular component myosin complex cytosol muscle myosin complex Biological process platelet aggregation regulation of muscle contraction muscle contraction regulation of megakaryocyte differentiation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 10398 98932 Ensembl ENSG00000101335 ENSMUSG00000067818 UniProt P24844 Q9CQ19 RefSeq (mRNA) NM_181526 NM_006097 NM_172118 RefSeq (protein) NP_006088 NP_852667 NP_742116 Location (UCSC) Chr 20: 36.54 – 36.55 Mb Chr 2: 156.62 – 156.62 Mb PubMed search
Wikidata
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Myosin regulatory light polypeptide 9 is a protein that in humans is encoded by the MYL9 gene.

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.

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. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070. S2CID 8235923.
• 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. S2CID 19633613.
• Deloukas P, Matthews LH, Ashurst J, et al. (2001). "The DNA sequence and comparative analysis of human chromosome 20". Nature. 414 (6866): 865–71. Bibcode:2001Natur.414..865D. 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. Bibcode:2002PNAS...9916899M. 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.