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MYH1

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From Wikipedia, the free encyclopedia

Protein-coding gene in the species Homo sapiens

MYH1

Identifiers

Aliases

MYH1, HEL71, MYHSA1, MYHa, MyHC-2X/D, MyHC-2x, myosin, heavy chain 1, skeletal muscle, adult, myosin heavy chain 1

External IDs

OMIM:160730;MGI:1339711;HomoloGene:133718;GeneCards:MYH1;OMA:MYH1 - orthologs

Gene location (Human)

Chr.	Chromosome 17 (human)^[1]

Band	17p13.1	Start	10,492,307bp^[1]
Band	17p13.1	End	10,518,542bp^[1]

Gene location (Mouse)

Chr.	Chromosome 11 (mouse)^[2]

Band	11 B3\|11 40.59 cM	Start	67,090,878bp^[2]
Band	11 B3\|11 40.59 cM	End	67,115,401bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

Skeletal muscle tissue of rectus abdominis

biceps brachii

vastus lateralis muscle

Skeletal muscle tissue of biceps brachii

muscle of thigh

thoracic diaphragm

gastrocnemius muscle

deltoid muscle

triceps brachii muscle

larynx

Top expressed in

masseter muscle

digastric muscle

intercostal muscle

extraocular muscle

ankle

temporal muscle

tibialis anterior muscle

vastus lateralis muscle

sternocleidomastoid muscle

body of femur

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	nucleotide binding actin binding cytoskeletal motor activity protein binding ATP binding calmodulin binding actin filament binding microtubule motor activity microtubule binding
Cellular component	cytoplasm myosin filament cytoplasmic ribonucleoprotein granule myofibril myosin complex muscle myosin complex intercalated disc A band
Biological process	microtubule-based movement muscle contraction
Sources:Amigo /QuickGO

Orthologs

Species

Human

Mouse

Entrez


4619


17879

Ensembl


ENSG00000109061


ENSMUSG00000056328

UniProt


P12882


Q5SX40

RefSeq (mRNA)


NM_005963


NM_030679

RefSeq (protein)


NP_005954


NP_109604

Location (UCSC)

Chr 17: 10.49 – 10.52 Mb

Chr 11: 67.09 – 67.12 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Myosin-1, also known as 'striated muscle myosin heavy chain 1', is aprotein that in humans is encoded by theMYH1gene.^[5]^[6] 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

[edit]

Myosin is a major contractile protein that converts chemical energy into mechanical energy through the hydrolysis ofATP. 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.^[6]

References

[edit]

^^a ^b ^cGRCh38: Ensembl release 89: ENSG00000109061 –Ensembl, May 2017
^^a ^b ^cGRCm38: Ensembl release 89: ENSMUSG00000056328 –Ensembl, May 2017
^"Human PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^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.Bibcode:1983PNAS...80.3716L.doi:10.1073/pnas.80.12.3716.PMC 394121.PMID 6304733.
^^a ^b"Entrez Gene: MYH1 myosin, heavy chain 1, skeletal muscle, adult".

Yoon SJ, Seiler SH, Kucherlapati R, Leinwand L (December 1992)."Organization of the human skeletal myosin heavy chain gene cluster".Proceedings of the National Academy of Sciences of the United States of America.89 (24):12078–82.Bibcode:1992PNAS...8912078Y.doi:10.1073/pnas.89.24.12078.PMC 50701.PMID 1465443.
Saez L, Leinwand LA (April 1986)."Characterization of diverse forms of myosin heavy chain expressed in adult human skeletal muscle".Nucleic Acids Research.14 (7):2951–69.doi:10.1093/nar/14.7.2951.PMC 339714.PMID 2421254.
Smerdu V, Karsch-Mizrachi I, Campione M, Leinwand L, Schiaffino S (December 1994). "Type IIx myosin heavy chain transcripts are expressed in type IIb fibers of human skeletal muscle".The American Journal of Physiology.267 (6 Pt 1): C1723–8.doi:10.1152/ajpcell.1994.267.6.C1723.PMID 7545970.
Weiss A, McDonough D, Wertman B, Acakpo-Satchivi L, Montgomery K, Kucherlapati R, Leinwand L, Krauter K (March 1999)."Organization of human and mouse skeletal myosin heavy chain gene clusters is highly conserved".Proceedings of the National Academy of Sciences of the United States of America.96 (6):2958–63.Bibcode:1999PNAS...96.2958W.doi:10.1073/pnas.96.6.2958.PMC 15877.PMID 10077619.
Weiss A, Schiaffino S, Leinwand LA (July 1999). "Comparative sequence analysis of the complete human sarcomeric myosin heavy chain family: implications for functional diversity".Journal of Molecular Biology.290 (1):61–75.doi:10.1006/jmbi.1999.2865.PMID 10388558.
Daugaard JR, Nielsen JN, Kristiansen S, Andersen JL, Hargreaves M, Richter EA (July 2000)."Fiber type-specific expression of GLUT4 in human skeletal muscle: influence of exercise training".Diabetes.49 (7):1092–5.doi:10.2337/diabetes.49.7.1092.PMID 10909963.
Korfage JA, Brugman P, Van Eijden TM (September 2000). "Intermuscular and intramuscular differences in myosin heavy chain composition of the human masticatory muscles".Journal of the Neurological Sciences.178 (2):95–106.doi:10.1016/S0022-510X(00)00372-5.PMID 11018701.S2CID 24218883.
Konig S, Burkman J, Fitzgerald J, Mitchell M, Su L, Stedman H (August 2002)."Modular organization of phylogenetically conserved domains controlling developmental regulation of the human skeletal myosin heavy chain gene family".The Journal of Biological Chemistry.277 (31):27593–605.doi:10.1074/jbc.M203162200.PMID 11971910.
Villacé P, Marión RM, Ortín J (2004)."The composition of Staufen-containing RNA granules from human cells indicates their role in the regulated transport and translation of messenger RNAs".Nucleic Acids Research.32 (8):2411–20.doi:10.1093/nar/gkh552.PMC 419443.PMID 15121898.
Pontén EM, Stål PS (February 2007). "Decreased capillarization and a shift to fast myosin heavy chain IIx in the biceps brachii muscle from young adults with spastic paresis".Journal of the Neurological Sciences.253 (1–2):25–33.doi:10.1016/j.jns.2006.11.006.PMID 17196619.S2CID 23299020.

v t e PDB gallery
1m8q: Molecular Models of Averaged Rigor Crossbridges from Tomograms of Insect Flight Muscle 1mvw: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE 1o18: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE 1o19: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE 1o1a: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE 1o1b: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE 1o1c: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE 1o1d: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE 1o1e: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE 1o1f: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE 1o1g: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE

PDB gallery

1m8q: Molecular Models of Averaged Rigor Crossbridges from Tomograms of Insect Flight Muscle
1mvw: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE
1o18: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE
1o19: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE
1o1a: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE
1o1b: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE
1o1c: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE
1o1d: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE
1o1e: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE
1o1f: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE
1o1g: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE

Proteins of thecytoskeleton

Human

Microfilaments
andABPs

Myofilament

Actins	A1 A2 B C1 G1 G2
Myosins	I MYO1A MYO1B MYO1C MYO1D MYO1E MYO1F MYO1G MYO1H) II MYH1 MYH2 MYH3 MYH4 MYH6 MYH7 MYH7B MYH8 MYH9 MYH10 MYH11 MYH13 MYH14 MYH15 MYH16 III MYO3A MYO3B V MYO5A MYO5B MYO5C VI MYO6 VII MYO7A MYO7B IX MYO9A MYO9B X MYO10 XV MYO15A XVIII MYO18A MYO18B LC MYL1 MYL2 MYL3 MYL4 MYL5 MYL6 MYL6B MYL7 MYL9 MYLIP MYLK MYLK2 MYLL1
Other	Tropomodulin 1 2 3 4 Troponin T 1 2 3 C 1 2 I 1 2 3 Tropomyosin 1 2 3 4 Actinin 1 2 3 4 Arp2/3 complex actin depolymerizing factors Cofilin 1 2 Destrin Gelsolin Profilin 1 2 Titin

Other

Intermediate
filaments

Type 1/2
(Keratin,
Cytokeratin)

Epithelial keratins (soft alpha-keratins)	type I/chromosome 17 9 10 12 13 14 15 16 17 19 20 chromosome 12 18 none 21 type II/chromosome 12 1 2A 3 4 5 6A 6B 6C 7 8
Hair keratins (hard alpha-keratins)	type I/chromosome 17 31 32 33A 33B 34 35 36 37 38 type II/chromosome 12 81 82 83 84 85 86
Ungrouped alpha	chromosome 17 23 24 25 26 27 28 39 40 chromosome 12 71 72 73 74 75 76 77 78 79 80
Not alpha	Beta-keratin

Type 3

Type 4

Type 5

Microtubules
andMAPs

Tubulins	TUBA1A TUBA1B TUBA1C TUBA3C TUBA3D TUBA3E TUBA4A TUBA8 TUBB TUBB1 TUBB2A TUBB2B TUBB2C TUBB3 TUBB4 TUBB4Q TUBB6 TUBB8 TUBG1 TUBG2 TUBGCP2 TUBGCP3 TUBGCP4 TUBGCP5 TUBGCP6 TUBD1 TUBE1
MAPs	EB1 EB2 EB3 MAP1A MAP1B MAP2 MAP4
Kinesins	KIF1A KIF1B KIF2A KIF2C KIF3B KIF3C KIF4A KIF4B KIF5A KIF5B KIF5C KIF6 KIF7 KIF9 KIF11 KIF12 KIF13A KIF13B KIF14 KIF15 KIF16B KIF17 KIF18A KIF18B KIF19 KIF20A KIF20B KIF21A KIF21B KIF22 KIF23 KIF24 KIF25 KIF26A KIF26B KIF27 KIFC1 KIFC2 KIFC3
Dyneins	axonemal:DNAH1 DNAH2 DNAH3 DNAH5 DNAH6 DNAH7 DNAH8 DNAH9 DNAH10 DNAH11 DNAH12 DNAH13 DNAH14 DNAH17 DNAI1 DNAI2 DNALI1 DNAL1 DNAL4 cytoplasmic:DYNC1H1 DYNC2H1 DYNC1I1 DYNC1I2 DYNC1LI1 DYNC1LI2 DYNC2LI1 DYNLL1 DYNLL2 DYNLRB1 DYNLRB2 DYNLT1 DYNLT3
Microtubule organising proteins	CAMSAP1 CAMSAP2 CAMSAP3 Centrin 1 Centrin 2 Centrin 3 PCM1
Microtubule severing proteins	Katanin Spastin
Other	Tau protein Dynactin DCTN1 Stathmin Tektin TEKT1 TEKT2 TEKT3 TEKT4 TEKT5 Dynamin DNM1 DNM2 DNM3