MYLK2 (original) (raw)

From Wikipedia, the free encyclopedia

Protein-coding gene in the species Homo sapiens

MYLK2
Available structuresPDBOrtholog search: PDBe RCSB List of PDB id codes2LV6, 3KF9
Identifiers
Aliases	MYLK2, KMLC, MLCK, MLCK2, skMLCK, myosin light chain kinase 2
External IDs	OMIM: 606566; MGI: 2139434; HomoloGene: 13223; GeneCards: MYLK2; OMA:MYLK2 - orthologs
Gene location (Human)Chr.Chromosome 20 (human)[1]Band20q11.21Start31,819,308 bp[1]End31,834,689 bp[1]
Gene location (Mouse)Chr.Chromosome 2 (mouse)[2]Band2|2 H1Start152,753,272 bp[2]End152,764,988 bp[2]
RNA expression patternBgeeHuman Mouse (ortholog)Top expressed inmuscle of thighSkeletal muscle tissue of rectus abdominisgastrocnemius musclevastus lateralis musclebiceps brachiiSkeletal muscle tissue of biceps brachiitibialis anterior muscledeltoid musclebody of pancreastesticleTop expressed inmuscle of thightriceps brachii muscletemporal musclesternocleidomastoid muscleskeletal muscle tissuequadriceps femoris musclemedial head of gastrocnemius muscledigastric muscletibialis anterior muscleknee jointMore reference expression dataBioGPSn/a
Gene ontologyMolecular function transferase activity nucleotide binding protein kinase activity calmodulin binding myosin light chain kinase activity kinase activity protein serine/threonine kinase activity protein binding calmodulin-dependent protein kinase activity ATP binding myosin light chain binding Cellular component cytoplasm sarcomere nucleus Biological process regulation of muscle filament sliding cardiac muscle contraction phosphorylation cardiac muscle tissue morphogenesis skeletal muscle satellite cell differentiation protein phosphorylation neuromuscular synaptic transmission positive regulation of gene expression skeletal muscle cell differentiation protein autophosphorylation peptidyl-threonine phosphorylation striated muscle contraction peptidyl-serine phosphorylation intracellular signal transduction Sources:Amigo / QuickGO
OrthologsSpeciesHuman MouseEntrez85366228785EnsemblENSG00000101306ENSMUSG00000027470UniProtQ9H1R3Q8VCR8RefSeq (mRNA)NM_033118NM_001081044RefSeq (protein)NP_149109NP_001074513Location (UCSC)Chr 20: 31.82 – 31.83 MbChr 2: 152.75 – 152.76 MbPubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Myosin light chain kinase 2 also known as MYLK2 is an enzyme which in humans is encoded by the MYLK2 gene.[5]

This gene encodes a myosin light chain kinase, a calcium / calmodulin dependent enzyme, that is exclusively expressed in adult skeletal muscle.[6] The MYLK2 gene expresses skMLCK more prevalently in fast twitch muscle fibers as compared to slow twitch muscle fibers. Calmodulin is composed of two terminal domains (N,C) each containing two E-F hand motifs that bind to Ca2+. Upon saturation of Ca2+, Calmodulin undergoes a conformation change allowing it to bind with a target protein such as skMLCK. An image depicting a similar complex (sdCen/skMLCK2) is shown under myosin light chain kinase. This binding to skMLCK increases the affinity of Ca2+ and ultimately leads to a sustained muscle action.[7]

Clinical significance

[edit]

Mutations in the MYLK2 gene have been linked to midventricular hypertrophic cardiomyopathy.[5]

1. ^ a b c GRCh38: Ensembl release 89: ENSG00000101306 – Ensembl, May 2017
2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000027470 – Ensembl, May 2017
3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. ^ a b Davis JS, Hassanzadeh S, Winitsky S, Lin H, Satorius C, Vemuri R, Aletras AH, Wen H, Epstein ND (November 2001). "The overall pattern of cardiac contraction depends on a spatial gradient of myosin regulatory light chain phosphorylation". Cell. 107 (5): 631–41. doi:10.1016/S0092-8674(01)00586-4. PMID 11733062. S2CID 778253.
6. ^ "Entrez Gene: MYLK2 myosin light chain kinase 2, skeletal muscle".
7. ^ Stull JT, Kamm KE, Vandenboom R (February 2011). "Myosin light chain kinase and the role of myosin light chain phosphorylation in skeletal muscle". Arch Biochem Biophys. 510 (2): 120–8. doi:10.1016/j.abb.2011.01.017. PMC 3101293. PMID 21284933.

• Jeronimo C, Forget D, Bouchard A (2007). "Systematic analysis of the protein interaction network for the human transcription machinery reveals the identity of the 7SK capping enzyme". Mol. Cell. 27 (2): 262–74. doi:10.1016/j.molcel.2007.06.027. PMC 4498903. PMID 17643375.
• Junker JP, Rief M (2009). "Single-molecule force spectroscopy distinguishes target binding modes of calmodulin". Proc. Natl. Acad. Sci. U.S.A. 106 (34): 14361–6. Bibcode:2009PNAS..10614361J. doi:10.1073/pnas.0904654106. PMC 2732892. PMID 19667195.
• Roush CL, Kennelly PJ, Glaccum MB (1988). "Isolation of the cDNA encoding rat skeletal muscle myosin light chain kinase. Sequence and tissue distribution". J. Biol. Chem. 263 (21): 10510–6. doi:10.1016/S0021-9258(19)81545-4. PMID 2839493.
• Christie JD, Ma SF, Aplenc R (2008). "Variation in the myosin light chain kinase gene is associated with development of acute lung injury after major trauma". Crit. Care Med. 36 (10): 2794–800. doi:10.1097/CCM.0b013e318186b843. PMID 18828194. S2CID 6567908.
• Lazar V, Garcia JG (1999). "A single human myosin light chain kinase gene (MLCK; MYLK)". Genomics. 57 (2): 256–67. doi:10.1006/geno.1999.5774. PMID 10198165.
• Gerhard DS, Wagner L, Feingold EA (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.
• Deloukas P, Matthews LH, Ashurst J (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.}
• Soung YH, Lee JW, Kim SY (2006). "Mutational analysis of the kinase domain of MYLK2 gene in common human cancers". Pathol. Res. Pract. 202 (3): 137–40. doi:10.1016/j.prp.2005.12.003. PMID 16448786.
• Gallagher PJ, Herring BP, Stull JT (1997). "Myosin light chain kinases". J. Muscle Res. Cell. Motil. 18 (1): 1–16. doi:10.1023/A:1018616814417. PMID 9147985. S2CID 11975486.
• Strausberg RL, Feingold EA, Grouse LH (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.
• Lanfranchi G, Muraro T, Caldara F (1996). "Identification of 4370 expressed sequence tags from a 3'-end-specific cDNA library of human skeletal muscle by DNA sequencing and filter hybridization". Genome Res. 6 (1): 35–42. doi:10.1101/gr.6.1.35. PMID 8681137.
• Toth-Zsamboki E, Oury C, Cornelissen H (2003). "P2X1-mediated ERK2 activation amplifies the collagen-induced platelet secretion by enhancing myosin light chain kinase activation". J. Biol. Chem. 278 (47): 46661–7. doi:10.1074/jbc.M308452200. PMID 14500714.

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