MYH13

MYH13
Identifiers
Aliases	MYH13, MyHC-IIL, MyHC-eo, myosin, heavy chain 13, skeletal muscle, myosin heavy chain 13
External IDs	MGI: 1339967 HomoloGene: 55780 GeneCards: MYH13
Gene ontology Molecular function • nucleotide binding • actin binding • microfilament motor activity • motor activity • ATP binding • calmodulin binding Cellular component • cytoplasm • myosin filament • muscle myosin complex • myofibril • extracellular exosome • myosin complex Biological process • cellular response to starvation • muscle contraction Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	8735	544791
Ensembl	ENSG00000006788	ENSMUSG00000060180
UniProt	Q9UKX3	n/a
RefSeq (mRNA)	NM_003802	NM_001081250
RefSeq (protein)	NP_003793.2	n/a
Location (UCSC)	Chr 17: 10.3 – 10.37 Mb	Chr 11: 67.32 – 67.37 Mb
PubMed search	[1]	[2]
Wikidata

View/Edit Human

View/Edit Mouse

Myosin-13 also known as myosin, heavy chain 13 is a protein which in humans is encoded by the MYH13 gene.^[3]

Function

MYH13 is a myosin whose expression is restricted primarily to the extrinsic eye muscles which are specialized for function in eye movement.^[4]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. Winters LM, Briggs MM, Schachat F (November 1998). "The human extraocular muscle myosin heavy chain gene (MYH13) maps to the cluster of fast and developmental myosin genes on chromosome 17". Genomics. 54 (1): 188–9. doi:10.1006/geno.1998.5558. PMID 9806854.
4. Weiss A, Schiaffino S, Leinwand LA (July 1999). "Comparative sequence analysis of the complete human sarcomeric myosin heavy chain family: implications for functional diversity". J. Mol. Biol. 290 (1): 61–75. doi:10.1006/jmbi.1999.2865. PMID 10388558.

Further reading

• Weiss A, McDonough D, Wertman B, et al. (1999). "Organization of human and mouse skeletal myosin heavy chain gene clusters is highly conserved.". Proc. Natl. Acad. Sci. U.S.A. 96 (6): 2958–63. doi:10.1073/pnas.96.6.2958. PMC 15877. PMID 10077619.
• Schachat F, Briggs MM (2002). "Phylogenetic implications of the superfast myosin in extraocular muscles.". J. Exp. Biol. 205 (Pt 15): 2189–201. PMID 12110653.
• Trynka G, Zhernakova A, Romanos J, et al. (2009). "Coeliac disease-associated risk variants in TNFAIP3 and REL implicate altered NF-kappaB signalling.". Gut. 58 (8): 1078–83. doi:10.1136/gut.2008.169052. PMID 19240061.
• Lehner B, Sanderson CM (2004). "A protein interaction framework for human mRNA degradation.". Genome Res. 14 (7): 1315–23. doi:10.1101/gr.2122004. PMC 442147. PMID 15231747.
• Schjeide BM, McQueen MB, Mullin K, et al. (2009). "Assessment of Alzheimer's disease case-control associations using family-based methods.". Neurogenetics. 10 (1): 19–25. doi:10.1007/s10048-008-0151-3. PMC 2841132. PMID 18830724.
• Shoeman RL, Sachse C, Höner B, et al. (1993). "Cleavage of human and mouse cytoskeletal and sarcomeric proteins by human immunodeficiency virus type 1 protease. Actin, desmin, myosin, and tropomyosin.". Am. J. Pathol. 142 (1): 221–30. PMC 1886840. PMID 8424456.