MYH9

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
2LNK, 3ZWH, 4CFQ, 4CFR, 4ETO

Identifiers

Aliases

MYH9, BDPLT6, DFNA17, EPSTS, FTNS, MHA, NMHC-II-A, NMMHC-IIA, NMMHCA, myosin, heavy chain 9, non-muscle

External IDs

MGI: 107717 HomoloGene: 129835 GeneCards: MYH9

Gene ontology
Molecular function	• protein homodimerization activity • nucleotide binding • microfilament motor activity • protein binding • poly(A) RNA binding • ADP binding • protein anchor • actin-dependent ATPase activity • calmodulin binding • ATPase activity • protein domain specific binding • actin filament binding • actin binding • motor activity • ATP binding • cadherin binding involved in cell-cell adhesion
Cellular component	• myosin II filament • cell cortex • brush border • actomyosin • myosin complex • integrin complex • ruffle • nucleus • cell leading edge • protein complex • actomyosin contractile ring • cytoskeleton • cleavage furrow • cortical cytoskeleton • actin cytoskeleton • spindle • membrane • COP9 signalosome • extracellular exosome • neuromuscular junction • cytoplasm • cytosol • focal adhesion • plasma membrane • stress fiber • uropod • immunological synapse • myosin II complex • extracellular matrix • cell-cell adherens junction
Biological process	• in utero embryonic development • protein transport • monocyte differentiation • uropod organization • cell adhesion • cell morphogenesis involved in differentiation • platelet formation • leukocyte migration • cytokinesis • establishment of meiotic spindle localization • blood vessel endothelial cell migration • establishment of T cell polarity • myoblast fusion • membrane protein ectodomain proteolysis • actomyosin structure organization • angiogenesis • integrin-mediated signaling pathway • actin cytoskeleton reorganization • regulation of cell shape • actin filament-based movement • platelet aggregation • single organismal cell-cell adhesion • meiotic spindle organization • phagocytosis, engulfment • negative regulation of actin filament severing • positive regulation of protein processing in phagocytic vesicle
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


4627


17886

Ensembl


ENSG00000100345


ENSMUSG00000022443

UniProt


P35579 Q5BKV1


Q8VDD5

RefSeq (mRNA)


NM_002473


NM_022410

RefSeq (protein)


NP_002464.1 NP_002464.1


NP_071855.2

Location (UCSC)

Chr 22: 36.28 – 36.39 Mb

Chr 15: 77.76 – 77.84 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

Myosin, heavy chain 9, non-muscle is a protein which in humans is encoded by the MYH9 gene.^[3]^[4]

Clinical significance

MYH9 polymorphisms have been shown to associate with glomerulosclerosis^[5] and non-diabetic end stage renal disease^[6] in African Americans and in Hispanic Americans,^[7] though it was later shown that two independent variants in the nearby APOL1 gene were responsible for the increased risk of disease.^[8]^[9]

Model organisms

*Myh9* knockout mouse phenotype
Characteristic	Phenotype
Homozygote viability	Abnormal
Recessive lethal study	Abnormal
Fertility	Normal
Body weight	Normal
Anxiety	Normal
Neurological assessment	Normal
Grip strength	Normal
Hot plate	Normal
Dysmorphology	Normal
Indirect calorimetry	Normal
Glucose tolerance test	Normal
Auditory brainstem response	Normal
DEXA	Normal
Radiography	Normal
Body temperature	Normal
Eye morphology	Normal
Clinical chemistry	Normal
Plasma immunoglobulins	Normal
Haematology	Normal
Peripheral blood lymphocytes	Normal
Micronucleus test	Normal
Heart weight	Normal
Skin Histopathology	Normal
Eye Histopathology	Normal
Salmonella infection	Normal^[10]
Citrobacter infection	Normal^[11]
All tests and analysis from^[12]^[13]

Model organisms have been used in the study of MYH9 function. A conditional knockout mouse line, called Myh9^{tm1a(EUCOMM)Wtsi}^[14]^[15] was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.^[16]^[17]^[18]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.^[12]^[19] Twenty six tests were carried out on mutant mice and two significant abnormalities were observed.^[12] No homozygous mutant embryos were identified during gestation, and therefore none survived until weaning. The remaining tests were carried out on heterozygous mutant adult mice; no additional significant abnormalities were observed in these animals.^[12]

Interactions

MYH9 has been shown to interact with PRKCE.^[20]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Simons M, Wang M, McBride OW, Kawamoto S, Yamakawa K, Gdula D, Adelstein RS, Weir L (August 1991). "Human nonmuscle myosin heavy chains are encoded by two genes located on different chromosomes". Circulation Research. 69 (2): 530–9. doi:10.1161/01.res.69.2.530. PMID 1860190.
↑ Lalwani AK, Goldstein JA, Kelley MJ, Luxford W, Castelein CM, Mhatre AN (November 2000). "Human nonsyndromic hereditary deafness DFNA17 is due to a mutation in nonmuscle myosin MYH9". American Journal of Human Genetics. 67 (5): 1121–8. doi:10.1016/S0002-9297(07)62942-5. PMC 1288554. PMID 11023810.
↑ Kopp JB, Smith MW, Nelson GW, Johnson RC, Freedman BI, Bowden DW, Oleksyk T, McKenzie LM, Kajiyama H, Ahuja TS, Berns JS, Briggs W, Cho ME, Dart RA, Kimmel PL, Korbet SM, Michel DM, Mokrzycki MH, Schelling JR, Simon E, Trachtman H, Vlahov D, Winkler CA (October 2008). "MYH9 is a major-effect risk gene for focal segmental glomerulosclerosis". Nature Genetics. 40 (10): 1175–84. doi:10.1038/ng.226. PMC 2827354. PMID 18794856.
↑ Kao WH, Klag MJ, Meoni LA, Reich D, Berthier-Schaad Y, Li M, Coresh J, Patterson N, Tandon A, Powe NR, Fink NE, Sadler JH, Weir MR, Abboud HE, Adler SG, Divers J, Iyengar SK, Freedman BI, Kimmel PL, Knowler WC, Kohn OF, Kramp K, Leehey DJ, Nicholas SB, Pahl MV, Schelling JR, Sedor JR, Thornley-Brown D, Winkler CA, Smith MW, Parekh RS; Family Investigation of Nephropathy and Diabetes Research Group (October 2008). "MYH9 is associated with nondiabetic end-stage renal disease in African Americans". Nature Genetics. 40 (10): 1185–92. doi:10.1038/ng.232. PMC 2614692. PMID 18794854.
↑ Behar DM, Rosset S, Tzur S, Selig S, Yudkovsky G, Bercovici S, Kopp JB, Winkler CA, Nelson GW, Wasser WG, Skorecki K (2010). "African ancestry allelic variation at the MYH9 gene contributes to increased susceptibility to non-diabetic end-stage kidney disease in Hispanic Americans.". Hum Mol Genet. 19 (9): 1816–27. doi:10.1093/hmg/ddq040. PMC 2850615. PMID 20144966.
↑ Genovese G, Friedman DJ, Ross MD, Lecordier L, Uzureau P, Freedman BI, Bowden DW, Langefeld CD, Oleksyk TK, Uscinski Knob AL, Bernhardy AJ, Hicks PJ, Nelson GW, Vanhollebeke B, Winkler CA, Kopp JB, Pays E, Pollak MR (July 2010). "Association of Trypanolytic ApoL1 Variants with Kidney Disease in African-Americans". Science. 329 (5993): 841–5. doi:10.1126/science.1193032. PMC 2980843. PMID 20647424.
↑ Tzur S, Rosset S, Shemer R, Yudkovsky G, Selig S, Tarekegn A, Bekele E, Bradman N, Wasser WG, Behar DM, Skorecki K (July 2010). "Missense mutations in the APOL1 gene are highly associated with end stage kidney disease risk previously attributed to the MYH9 gene.". Human Genetics. 128 (3): 345–50. doi:10.1007/s00439-010-0861-0. PMC 2921485. PMID 20635188.
↑ "Salmonella infection data for Myh9". Wellcome Trust Sanger Institute.
↑ "Citrobacter infection data for Myh9". Wellcome Trust Sanger Institute.
1 2 3 4 Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica. 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x.
↑ Mouse Resources Portal, Wellcome Trust Sanger Institute.
↑ "International Knockout Mouse Consortium".
↑ "Mouse Genome Informatics".
↑ Skarnes, W. C.; Rosen, B.; West, A. P.; Koutsourakis, M.; Bushell, W.; Iyer, V.; Mujica, A. O.; Thomas, M.; Harrow, J.; Cox, T.; Jackson, D.; Severin, J.; Biggs, P.; Fu, J.; Nefedov, M.; De Jong, P. J.; Stewart, A. F.; Bradley, A. (2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–342. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
↑ Dolgin E (2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
↑ Collins FS, Rossant J, Wurst W (2007). "A Mouse for All Reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
↑ van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism.". Genome Biol. 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.
↑ England, Karen; Ashford David; Kidd Daniel; Rumsby Martin (June 2002). "PKC epsilon is associated with myosin IIA and actin in fibroblasts". Cell. Signal. England. 14 (6): 529–36. doi:10.1016/S0898-6568(01)00277-7. ISSN 0898-6568. PMID 11897493.

External links

GeneReview/NIH/UW entry on MYH9-Related Disorders

Starr R, Offer G (1978). "The interaction of C-protein with heavy meromyosin and subfragment-2.". Biochem. J. 171 (3): 813–6. PMC 1184031. PMID 352343.
Lee CL, Atassi MZ (1978). "Enzymic and immunochemical properties of lysozyme. Accurate definition of the antigenic site around the disulphide bridge 30-115 (site 3) by 'surface-simulation' synthesis.". Biochem. J. 167 (3): 571–81. PMC 1183703. PMID 603622.
Tweed WA, Phua WT, Chong KY, et al. (1992). "Large tidal volume ventilation improves pulmonary gas exchange during lower abdominal surgery in Trendelenburg's position.". Canadian Journal of Anesthesia. 38 (8): 989–95. doi:10.1007/BF03008617. PMID 1752022.
Simons M, Wang M, McBride OW, et al. (1991). "Human nonmuscle myosin heavy chains are encoded by two genes located on different chromosomes.". Circ. Res. 69 (2): 530–9. doi:10.1161/01.res.69.2.530. PMID 1860190.
Toothaker LE, Gonzalez DA, Tung N, et al. (1991). "Cellular myosin heavy chain in human leukocytes: isolation of 5' cDNA clones, characterization of the protein, chromosomal localization, and upregulation during myeloid differentiation.". Blood. 78 (7): 1826–33. PMID 1912569.
Saez CG, Myers JC, Shows TB, Leinwand LA (1990). "Human nonmuscle myosin heavy chain mRNA: generation of diversity through alternative polyadenylylation.". Proc. Natl. Acad. Sci. U.S.A. 87 (3): 1164–8. doi:10.1073/pnas.87.3.1164. PMC 53431. PMID 1967836.
Moos C, Feng IN (1980). "Effect of C-protein on actomyosin ATPase.". Biochim. Biophys. Acta. 632 (2): 141–9. doi:10.1016/0304-4165(80)90071-9. PMID 6448079.
Obermann WM, Plessmann U, Weber K, Fürst DO (1995). "Purification and biochemical characterization of myomesin, a myosin-binding and titin-binding protein, from bovine skeletal muscle.". Eur. J. Biochem. 233 (1): 110–5. doi:10.1111/j.1432-1033.1995.110_1.x. PMID 7588733.
Maupin P, Phillips CL, Adelstein RS, Pollard TD (1995). "Differential localization of myosin-II isozymes in human cultured cells and blood cells.". J. Cell. Sci. 107 (11): 3077–90. PMID 7699007.
Bement WM, Hasson T, Wirth JA, et al. (1994). "Identification and overlapping expression of multiple unconventional myosin genes in vertebrate cell types.". Proc. Natl. Acad. Sci. U.S.A. 91 (14): 6549–53. doi:10.1073/pnas.91.14.6549. PMC 44240. PMID 8022818.
Eilertsen KJ, Kazmierski ST, Keller TC (1994). "Cellular titin localization in stress fibers and interaction with myosin II filaments in vitro.". J. Cell Biol. 126 (5): 1201–10. doi:10.1083/jcb.126.5.1201. PMC 2120159. PMID 8063857.
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.
Lalwani AK, Linthicum FH, Wilcox ER, et al. (1998). "A five-generation family with late-onset progressive hereditary hearing impairment due to cochleosaccular degeneration.". Audiol. Neurootol. 2 (3): 139–54. doi:10.1159/000259237. PMID 9390828.
Ford HL, Silver DL, Kachar B, et al. (1998). "Effect of Mts1 on the structure and activity of nonmuscle myosin II.". Biochemistry. 36 (51): 16321–7. doi:10.1021/bi971182l. PMID 9405067.
Obermann WM, van der Ven PF, Steiner F, et al. (1998). "Mapping of a myosin-binding domain and a regulatory phosphorylation site in M-protein, a structural protein of the sarcomeric M band.". Mol. Biol. Cell. 9 (4): 829–40. doi:10.1091/mbc.9.4.829. PMC 25310. PMID 9529381.
Dunham I, Shimizu N, Roe BA, et al. (1999). "The DNA sequence of human chromosome 22.". Nature. 402 (6761): 489–95. doi:10.1038/990031. PMID 10591208.
Miyamoto CA, Fischman DA, Reinach FC (2000). "The interface between MyBP-C and myosin: site-directed mutagenesis of the CX myosin-binding domain of MyBP-C.". J. Muscle Res. Cell. Motil. 20 (7): 703–15. doi:10.1023/A:1005513312939. PMID 10672519.
Sajid M, Hu Z, Lele M, Stouffer GA (2000). "Protein complexes involving alpha v beta 3 integrins, nonmuscle myosin heavy chain-A, and focal adhesion kinase from in thrombospondin-treated smooth muscle cells.". J. Investig. Med. 48 (3): 190–7. PMID 10822899.
Husi H, Ward MA, Choudhary JS, et al. (2000). "Proteomic analysis of NMDA receptor-adhesion protein signaling complexes.". Nat. Neurosci. 3 (7): 661–9. doi:10.1038/76615. PMID 10862698.
Kelley MJ, Jawien W, Lin A, et al. (2000). "Autosomal dominant macrothrombocytopenia with leukocyte inclusions (May-Hegglin anomaly) is linked to chromosome 22q12-13.". Hum. Genet. 106 (5): 557–64. doi:10.1007/s004390050025. PMID 10914687.

Proteins of the cytoskeleton

Human

Microfilaments
and ABPs

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 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 7 8 9

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
and MAPs

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

Other	Tau protein Dynactin DCTN1 Tubulins TUBA1A TUBA1B TUBA1C TUBA3C TUBA3D TUBA3E TUBA4A TUBA8 Stathmin Tektin TEKT1 TEKT2 TEKT3 TEKT4 TEKT5 Dynamin DNM1 DNM2 DNM3

Catenins

Membrane

Dystrophin
- Dystroglycan
Utrophin
Ankyrin
- ANK1
- ANK2
- ANK3
Spectrin
- SPTA1
- SPTAN1
- SPTB
- SPTBN1
- SPTBN2
- SPTBN4
- SPTBN5

Other

Plakins
- Corneodesmosin
- Desmoplakin
- Dystonin
- Envoplakin
- MACF1
- Periplakin
- Plectin
Talin
- TLN1
Vinculin
Plakophilin
- PKP1
- PKP2

Nonhuman

See also: cytoskeletal defects

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

This article is issued from Wikipedia - version of the 6/3/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.