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{{Infobox_gene}}
{{PBB_Controls
'''Myosin-1''', also known as 'striated muscle myosin heavy chain 1', is a [[protein]] that in humans is encoded by the ''MYH1'' [[gene]].<ref name="pmid6304733">{{cite journal | vauthors = Leinwand LA, Saez L, McNally E, Nadal-Ginard B | title = Isolation and characterization of human myosin heavy chain genes | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 80 | issue = 12 | pages = 3716–20 | date = June 1983 | pmid = 6304733 | pmc = 394121 | doi = 10.1073/pnas.80.12.3716 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: MYH1 myosin, heavy chain 1, skeletal muscle, adult| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4619| accessdate = }}</ref>  This gene is most highly expressed in fast type IIX/D muscle fibres of vertebrates and encodes a protein found uniquely in striated muscle; it is a class II myosin with a long coiled coil tail that dimerizes and should not be confused with 'Myosin 1' encoded by the MYO1 family of genes (''[[MYO1A]]-[[MYO1H]]''). Class I MYO1 genes function in many cell types throughout biology and are single-headed membrane-binding myosins that lack a long coiled coil tail.
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_MYH1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1m8q.
| PDB = {{PDB2|1m8q}}, {{PDB2|1mvw}}, {{PDB2|1o18}}, {{PDB2|1o19}}, {{PDB2|1o1a}}, {{PDB2|1o1b}}, {{PDB2|1o1c}}, {{PDB2|1o1d}}, {{PDB2|1o1e}}, {{PDB2|1o1f}}, {{PDB2|1o1g}}
| Name = Myosin, heavy chain 1, skeletal muscle, adult
| HGNCid = 7567
| Symbol = MYH1
| AltSymbols =; MGC133384; MYHSA1; MYHa; MyHC-2X/D
| OMIM = 160730
| ECnumber = 
| Homologene = 68493
| MGIid = 1339711
| GeneAtlas_image1 = PBB_GE_MYH1_205951_at_tn.png
| Function = {{GNF_GO|id=GO:0000146 |text = microfilament motor activity}} {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003774 |text = motor activity}} {{GNF_GO|id=GO:0003779 |text = actin binding}} {{GNF_GO|id=GO:0005516 |text = calmodulin binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}}
| Component = {{GNF_GO|id=GO:0005859 |text = muscle myosin complex}} {{GNF_GO|id=GO:0005863 |text = striated muscle thick filament}} {{GNF_GO|id=GO:0016459 |text = myosin complex}}
| Process = {{GNF_GO|id=GO:0006941 |text = striated muscle contraction}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 4619
    | Hs_Ensembl = ENSG00000109061
    | Hs_RefseqProtein = NP_005954
    | Hs_RefseqmRNA = NM_005963
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 17
    | Hs_GenLoc_start = 10336353
    | Hs_GenLoc_end = 10360684
    | Hs_Uniprot = P12882
    | Mm_EntrezGene = 17879
    | Mm_Ensembl = ENSMUSG00000056328
    | Mm_RefseqmRNA = NM_030679
    | Mm_RefseqProtein = NP_109604
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 11
    | Mm_GenLoc_start = 67016297
    | Mm_GenLoc_end = 67040772
    | Mm_Uniprot = Q9WUS6
  }}
}}
'''Myosin, heavy chain 1, skeletal muscle, adult''', also known as '''MYH1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MYH1 myosin, heavy chain 1, skeletal muscle, adult| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4619| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
[[Myosin]] is a major contractile protein that converts chemical energy into mechanical energy through the hydrolysis of [[Adenosine triphosphate|ATP]]. Class II Myosins are hexameric proteins composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. Myosin heavy chains are encoded by a multigene family. In mammals, at least ten different myosin heavy chain (MYH) [[isoform]]s have been described from striated, smooth, but rarely in non-muscle cells. These isoforms show expression that is spatially and temporally regulated during development.<ref name="entrez" />
{{PBB_Summary
| section_title =
| summary_text = Myosin is a major contractile protein which converts chemical energy into mechanical energy through the hydrolysis of ATP. Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. Myosin heavy chains are encoded by a multigene family. In mammals at least 10 different myosin heavy chain (MYH) isoforms have been described from striated, smooth, and nonmuscle cells. These isoforms show expression that is spatially and temporally regulated during development.<ref name="entrez">{{cite web | title = Entrez Gene: MYH1 myosin, heavy chain 1, skeletal muscle, adult| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4619| accessdate = }}</ref>
}}


==References==
== References ==
{{reflist|2}}
{{reflist}}
==Further reading==
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Yoon SJ, Seiler SH, Kucherlapati R, Leinwand L | title = Organization of the human skeletal myosin heavy chain gene cluster | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 89 | issue = 24 | pages = 12078–82 | date = December 1992 | pmid = 1465443 | pmc = 50701 | doi = 10.1073/pnas.89.24.12078 }}
| citations =
* {{cite journal | vauthors = Saez L, Leinwand LA | title = Characterization of diverse forms of myosin heavy chain expressed in adult human skeletal muscle | journal = Nucleic Acids Research | volume = 14 | issue = 7 | pages = 2951–69 | date = April 1986 | pmid = 2421254 | pmc = 339714 | doi = 10.1093/nar/14.7.2951 }}
*{{cite journal | author=Yoon SJ, Seiler SH, Kucherlapati R, Leinwand L |title=Organization of the human skeletal myosin heavy chain gene cluster. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 24 |pages= 12078-82 |year= 1993 |pmid= 1465443 |doi= }}
* {{cite journal | vauthors = Smerdu V, Karsch-Mizrachi I, Campione M, Leinwand L, Schiaffino S | title = Type IIx myosin heavy chain transcripts are expressed in type IIb fibers of human skeletal muscle | journal = The American Journal of Physiology | volume = 267 | issue = 6 Pt 1 | pages = C1723-8 | date = December 1994 | pmid = 7545970 | doi =  }}
*{{cite journal | author=Saez L, Leinwand LA |title=Characterization of diverse forms of myosin heavy chain expressed in adult human skeletal muscle. |journal=Nucleic Acids Res. |volume=14 |issue= 7 |pages= 2951-69 |year= 1986 |pmid= 2421254 |doi= }}
* {{cite journal | vauthors = Weiss A, McDonough D, Wertman B, Acakpo-Satchivi L, Montgomery K, Kucherlapati R, Leinwand L, Krauter K | title = Organization of human and mouse skeletal myosin heavy chain gene clusters is highly conserved | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 96 | issue = 6 | pages = 2958–63 | date = March 1999 | pmid = 10077619 | pmc = 15877 | doi = 10.1073/pnas.96.6.2958 }}
*{{cite journal  | author=Leinwand LA, Saez L, McNally E, Nadal-Ginard B |title=Isolation and characterization of human myosin heavy chain genes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=80 |issue= 12 |pages= 3716-20 |year= 1983 |pmid= 6304733 |doi=  }}
* {{cite journal | vauthors = Weiss A, Schiaffino S, Leinwand LA | title = Comparative sequence analysis of the complete human sarcomeric myosin heavy chain family: implications for functional diversity | journal = Journal of Molecular Biology | volume = 290 | issue = 1 | pages = 61–75 | date = July 1999 | pmid = 10388558 | doi = 10.1006/jmbi.1999.2865 }}
*{{cite journal | author=Smerdu V, Karsch-Mizrachi I, Campione M, ''et al.'' |title=Type IIx myosin heavy chain transcripts are expressed in type IIb fibers of human skeletal muscle. |journal=Am. J. Physiol. |volume=267 |issue= 6 Pt 1 |pages= C1723-8 |year= 1995 |pmid= 7545970 |doi=  }}
* {{cite journal | vauthors = Daugaard JR, Nielsen JN, Kristiansen S, Andersen JL, Hargreaves M, Richter EA | title = Fiber type-specific expression of GLUT4 in human skeletal muscle: influence of exercise training | journal = Diabetes | volume = 49 | issue = 7 | pages = 1092–5 | date = July 2000 | pmid = 10909963 | doi = 10.2337/diabetes.49.7.1092 }}
*{{cite journal | author=Weiss A, McDonough D, Wertman B, ''et al.'' |title=Organization of human and mouse skeletal myosin heavy chain gene clusters is highly conserved. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 6 |pages= 2958-63 |year= 1999 |pmid= 10077619 |doi= }}
* {{cite journal | vauthors = Korfage JA, Brugman P, Van Eijden TM | title = Intermuscular and intramuscular differences in myosin heavy chain composition of the human masticatory muscles | journal = Journal of the Neurological Sciences | volume = 178 | issue = 2 | pages = 95–106 | date = September 2000 | pmid = 11018701 | doi = 10.1016/S0022-510X(00)00372-5 }}
*{{cite journal | author=Weiss A, Schiaffino S, Leinwand LA |title=Comparative sequence analysis of the complete human sarcomeric myosin heavy chain family: implications for functional diversity. |journal=J. Mol. Biol. |volume=290 |issue= 1 |pages= 61-75 |year= 1999 |pmid= 10388558 |doi= 10.1006/jmbi.1999.2865 }}
* {{cite journal | vauthors = Konig S, Burkman J, Fitzgerald J, Mitchell M, Su L, Stedman H | title = Modular organization of phylogenetically conserved domains controlling developmental regulation of the human skeletal myosin heavy chain gene family | journal = The Journal of Biological Chemistry | volume = 277 | issue = 31 | pages = 27593–605 | date = August 2002 | pmid = 11971910 | doi = 10.1074/jbc.M203162200 }}
*{{cite journal | author=Daugaard JR, Nielsen JN, Kristiansen S, ''et al.'' |title=Fiber type-specific expression of GLUT4 in human skeletal muscle: influence of exercise training. |journal=Diabetes |volume=49 |issue= 7 |pages= 1092-5 |year= 2000 |pmid= 10909963 |doi= }}
* {{cite journal | vauthors = Villacé P, Marión RM, Ortín J | title = The composition of Staufen-containing RNA granules from human cells indicates their role in the regulated transport and translation of messenger RNAs | journal = Nucleic Acids Research | volume = 32 | issue = 8 | pages = 2411–20 | year = 2004 | pmid = 15121898 | pmc = 419443 | doi = 10.1093/nar/gkh552 }}
*{{cite journal | author=Korfage JA, Brugman P, Van Eijden TM |title=Intermuscular and intramuscular differences in myosin heavy chain composition of the human masticatory muscles. |journal=J. Neurol. Sci. |volume=178 |issue= 2 |pages= 95-106 |year= 2000 |pmid= 11018701 |doi= }}
* {{cite journal | vauthors = Pontén EM, Stål PS | title = Decreased capillarization and a shift to fast myosin heavy chain IIx in the biceps brachii muscle from young adults with spastic paresis | journal = Journal of the Neurological Sciences | volume = 253 | issue = 1-2 | pages = 25–33 | date = February 2007 | pmid = 17196619 | doi = 10.1016/j.jns.2006.11.006 }}
*{{cite journal | author=Konig S, Burkman J, Fitzgerald J, ''et al.'' |title=Modular organization of phylogenetically conserved domains controlling developmental regulation of the human skeletal myosin heavy chain gene family. |journal=J. Biol. Chem. |volume=277 |issue= 31 |pages= 27593-605 |year= 2002 |pmid= 11971910 |doi= 10.1074/jbc.M203162200 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Villacé P, Marión RM, Ortín J |title=The composition of Staufen-containing RNA granules from human cells indicates their role in the regulated transport and translation of messenger RNAs. |journal=Nucleic Acids Res. |volume=32 |issue= 8 |pages= 2411-20 |year= 2004 |pmid= 15121898 |doi= 10.1093/nar/gkh552 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  | author=Kimura K, Wakamatsu A, Suzuki Y, ''et al.'' |title=Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes. |journal=Genome Res. |volume=16 |issue= 1 |pages= 55-65 |year= 2006 |pmid= 16344560 |doi= 10.1101/gr.4039406 }}
*{{cite journal  | author=Pontén EM, Stål PS |title=Decreased capillarization and a shift to fast myosin heavy chain IIx in the biceps brachii muscle from young adults with spastic paresis. |journal=J. Neurol. Sci. |volume=253 |issue= 1-2 |pages= 25-33 |year= 2007 |pmid= 17196619 |doi= 10.1016/j.jns.2006.11.006 }}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=4619}}
{{Cytoskeletal Proteins}}


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{{gene-17-stub}}
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Latest revision as of 02:29, 27 October 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Myosin-1, also known as 'striated muscle myosin heavy chain 1', is a protein that in humans is encoded by the MYH1 gene.[1][2] This gene is most highly expressed in fast type IIX/D muscle fibres of vertebrates and encodes a protein found uniquely in striated muscle; it is a class II myosin with a long coiled coil tail that dimerizes and should not be confused with 'Myosin 1' encoded by the MYO1 family of genes (MYO1A-MYO1H). Class I MYO1 genes function in many cell types throughout biology and are single-headed membrane-binding myosins that lack a long coiled coil tail.

Function

Myosin is a major contractile protein that converts chemical energy into mechanical energy through the hydrolysis of ATP. Class II Myosins are hexameric proteins composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. Myosin heavy chains are encoded by a multigene family. In mammals, at least ten different myosin heavy chain (MYH) isoforms have been described from striated, smooth, but rarely in non-muscle cells. These isoforms show expression that is spatially and temporally regulated during development.[2]

References

  1. ↑ Leinwand LA, Saez L, McNally E, Nadal-Ginard B (June 1983). "Isolation and characterization of human myosin heavy chain genes". Proceedings of the National Academy of Sciences of the United States of America. 80 (12): 3716–20. doi:10.1073/pnas.80.12.3716. PMC 394121. PMID 6304733.
  2. ↑ 2.0 2.1 "Entrez Gene: MYH1 myosin, heavy chain 1, skeletal muscle, adult".

Further reading


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