protein

Recombinant Human Myosin-9

MBS717396

0.05 mg (E-Coli)

Recombinant Protein

Recombinant Human Myosin-9

Myosin-9

Cellular myosin heavy chain, type A; Myosin heavy chain 9; Myosin heavy chain, non-muscle Iia; Non-muscle myosin heavy chain A; NMMHC-A; Non-muscle myosin heavy chain IIa; NMMHC II-a; NMMHC-IIA

myosin-9; Myosin-9; myosin-9; myosin, heavy chain 9, non-muscle; Cellular myosin heavy chain, type A; Myosin heavy chain 9; Myosin heavy chain, non-muscle IIa; Non-muscle myosin heavy chain A; NMMHC-A; Non-muscle myosin heavy chain IIa; NMMHC II-a; NMMHC-IIA

MYH9

MYH9; MYH9; MHA; FTNS; EPSTS; BDPLT6; DFNA17; NMMHCA; NMHC-II-A; NMMHC-IIA; NMMHC-A; NMMHC II-a; NMMHC-IIA

MYH9_HUMAN

E Coli

2-241, partial.

241

AQQAADKYLYVDKNFINNPLAQADWAAKKLVWVPSDKSG
FEPASLKEEVGEEAIVELVENGKKVKVNKDDIQKMNPPK
FSKVEDMAELTCLNEASVLHNLKERYYSGLIYTYSGLFC
VVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTA
YRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVAS
SHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRF
GKFIRI

Greater than 90% as determined by SDS-PAGE.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Cell Cycle

Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping. During cell spreading, plays an important role in cytoskeleton reorganization, focal contacts formation (in the margins but not the central part of spreading cells), and lamellipodial retraction; this function is mechanically antagonized by MYH10.

A genome annotation-driven approach to cloning the human ORFeome.Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.Genome Biol. 5:R84.1-R84.11(2004) Vector-capping a simple method for preparing a high-quality full-length cDNA library.Kato S., Ohtoko K., Ohtake H., Kimura T.DNA Res. 12:53-62(2005) The full-ORF clone resource of the German cDNA consortium.Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.BMC Genomics 8:399-399(2007) Multiplex amplification and cloning of 5'-ends of cDNA by ligase-free recombination Preparation of full-lemgth cDNA clones encoding motor proteins.Yamakawa H., Kikuno R.F., Nagase T., Ohara O.The DNA sequence of human chromosome 22.Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.Nature 402:489-495(1999) Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.Cellular myosin heavy chain in human leukocytes isolation of 5' cDNA clones, characterization of the protein, chromosomal localization, and upregulation during myeloid differentiation.Toothaker L.E., Gonzalez D.A., Tung N., Lemons R.S., le Beau M.M., Arnaout M.A., Clayton L.K., Tenen D.G.Blood 78:1826-1833(1991) Complete sequencing and characterization of 21,243 full-length human cDNAs.Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.Nat. Genet. 36:40-45(2004) Human nonmuscle myosin heavy chains are encoded by two genes located on different chromosomes.Simons M., Wang M., McBride O.W., Kawamoto S., Yamakawa K., Gdula D., Adelstein R.S., Weir L.Circ. Res. 69:530-539(1991) Bienvenut W.V., Claeys R.Submitted (AUG-2005) to UniProtKB Human nonmuscle myosin heavy chain mRNA generation of diversity through alternative polyadenylylation.Saez C.G., Myers J.C., Shows T.B., Leinwand L.A.Proc. Natl. Acad. Sci. U.S.A. 87:1164-1168(1990) F-actin and myosin II binding domains in supervillin.Chen Y., Takizawa N., Crowley J.L., Oh S.W., Gatto C.L., Kambara T., Sato O., Li X.-D., Ikebe M., Luna E.J.J. Biol. Chem. 278:46094-46106(2003) Proteomic identification of proteins conjugated to ISG15 in mouse and human cells.Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J., Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.Biochem. Biophys. Res. Commun. 336:496-506(2005) Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.Cell 127:635-648(2006) A probability-based approach for high-throughput protein phosphorylation analysis and site localization.Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.Nat. Biotechnol. 24:1285-1292(2006) Toward a global characterization of the phosphoproteome in prostate cancer cells identification of phosphoproteins in the LNCaP cell line.Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.Electrophoresis 28:2027-2034(2007) Supervillin slows cell spreading by facilitating myosin II activation at the cell periphery.Takizawa N., Ikebe R., Ikebe M., Luna E.J.J. Cell Sci. 120:3792-3803(2007) Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment.Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.J. Proteome Res. 7:5167-5176(2008) Phosphoproteome of resting human platelets.Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.J. Proteome Res. 7:526-534(2008) MYH9 is a major-effect risk gene for focal segmental glomerulosclerosis.Kopp J.B., Smith M.W., Nelson G.W., Johnson R.C., Freedman B.I., Bowden D.W., Oleksyk T., McKenzie L.M., Kajiyama H., Ahuja T.S., Berns J.S., Briggs W., Cho M.E., Dart R.A., Kimmel P.L., Korbet S.M., Michel D.M., Mokrzycki M.H., Schelling J.R., Simon E., Trachtman H., Vlahov D., Winkler C.A.Nat. Genet. 40:1175-1184(2008) MYH9 is associated with nondiabetic end-stage renal disease in African Americans.Kao W.H., Klag M.J., Meoni L.A., Reich D., Berthier-Schaad Y., Li M., Coresh J., Patterson N., Tandon A., Powe N.R., Fink N.E., Sadler J.H., Weir M.R., Abboud H.E., Adler S.G., Divers J., Iyengar S.K., Freedman B.I., Kimmel P.L., Knowler W.C., Kohn O.F., Kramp K., Leehey D.J., Nicholas S.B., Pahl M.V., Schelling J.R., Sedor J.R., Thornley-Brown D., Winkler C.A., Smith M.W., Parekh R.S.Nat. Genet. 40:1185-1192(2008) A quantitative atlas of mitotic phosphorylation.Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography.Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.Proteomics 8:1346-1361(2008) Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.Anal. Chem. 81:4493-4501(2009) Polymorphisms in the non-muscle myosin heavy chain 9 gene (MYH9) are strongly associated with end-stage renal disease historically attributed to hypertension in African Americans.Freedman B.I., Hicks P.J., Bostrom M.A., Cunningham M.E., Liu Y., Divers J., Kopp J.B., Winkler C.A., Nelson G.W., Langefeld C.D., Bowden D.W.Kidney Int. 75:736-745(2009) Large-scale proteomics analysis of the human kinome.Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.Mol. Cell. Proteomics 8:1751-1764(2009) Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.Sci. Signal. 2:RA46-RA46(2009) Lysine acetylation targets protein complexes and co-regulates major cellular functions.Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.Science 325:834-840(2009) Myosin II motor proteins with different functions determine the fate of lamellipodia extension during cell spreading.Betapudi V.PLoS ONE 5:E8560-E8560(2010) Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.Sci. Signal. 3:RA3-RA3(2010) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011) System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.Sci. Signal. 4:RS3-RS3(2011) Application of the wheat-germ cell-free translation system to produce high temperature requirement A3 (HtrA3) proteases.Singh H., Makino S., Endo Y., Li Y., Stephens A.N., Nie G.BioTechniques 52:23-28(2012) N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014) Human nonsyndromic hereditary deafness DFNA17 is due to a mutation in nonmuscle myosin MYH9.Lalwani A.K., Goldstein J.A., Kelley M.J., Luxford W., Castelein C.M., Mhatre A.N.Am. J. Hum. Genet. 67:1121-1128(2000) Mutations in MYH9 result in the May-Hegglin anomaly, and Fechtner and Sebastian syndromes.Seri M., Cusano M., Gangarossa S., Caridi G., Bordo D., Lo Nigro C., Ghiggeri G.M., Ravazzolo R., Savino M., Del Vecchio M., d'Apolito M., Iolascon A., Zelante L.L., Savoia A., Balduini C.L., Noris P., Magrini U., Belletti S., Heath K.E., Babcock M., Glucksman M.J., Aliprandis E., Bizzaro N., Desnick R.J., Martignetti J.A.Nat. Genet. 26:103-105(2000) Mutation of MYH9, encoding non-muscle myosin heavy chain A, in May-Hegglin anomaly.Kelley M.J., Jawien W., Ortel T.L., Korczak J.F.Nat. Genet. 26:106-108(2000) Nonmuscle myosin heavy chain IIA mutations define a spectrum of autosomal dominant macrothrombocytopenias May-Hegglin anomaly and Fechtner, Sebastian, Epstein, and Alport-like syndromes.Heath K.E., Campos-Barros A., Toren A., Rozenfeld-Granot G., Carlsson L.E., Savige J., Denison J.C., Gregory M.C., White J.G., Barker D.F., Greinacher A., Epstein C.J., Glucksman M.J., Martignetti J.A.Am. J. Hum. Genet. 69:1033-1045(2001) Identification of six novel MYH9 mutations and genotype-phenotype relationships in autosomal dominant macrothrombocytopenia with leukocyte inclusions.Kunishima S., Matsushita T., Kojima T., Amemiya N., Choi Y.M., Hosaka N., Inoue M., Jung Y., Mamiya S., Matsumoto K., Miyajima Y., Zhang G., Ruan C., Saito K., Song K.S., Yoon H.-J., Kamiya T., Saito H.J. Hum. Genet. 46:722-729(2001) Epstein syndrome another renal disorder with mutations in the nonmuscle myosin heavy chain 9 gene.Seri M., Savino M., Bordo D., Cusano R., Rocca B., Meloni I., Di Bari F., Koivisto P.A., Bolognesi M., Ghiggeri G.M., Landolfi R., Balduini C.L., Zelante L., Ravazzolo R., Renieri A., Savoia A.Hum. Genet. 110:182-186(2002) Expression of the nonmuscle myosin heavy chain IIA in the human kidney and screening for MYH9 mutations in Epstein and Fechtner syndromes.Arrondel C., Vodovar N., Knebelmann B., Gruenfeld J.-P., Gubler M.-C., Antignac C., Heidet L.J. Am. Soc. Nephrol. 13:65-74(2002) Asp1424Asn MYH9 mutation results in an unstable protein responsible for the phenotypes in May-Hegglin anomaly/Fechtner syndrome.Deutsch S., Rideau A., Bochaton-Piallat M.-L., Merla G., Geinoz A., Gabbiani G., Schwede T., Matthes T., Antonarakis S.E., Beris P.Blood 102:529-534(2003) Immunofluorescence analysis of neutrophil nonmuscle myosin heavy chain-A in MYH9 disorders association of subcellular localization with MYH9 mutations.Kunishima S., Matsushita T., Kojima T., Sako M., Kimura F., Jo E.-K., Inoue C., Kamiya T., Saito H.Lab. Invest. 83:115-122(2003) MYH9-related disease may-Hegglin anomaly, Sebastian syndrome, Fechtner syndrome, and Epstein syndrome are not distinct entities but represent a variable expression of a single illness.Seri M., Pecci A., Di Bari F., Cusano R., Savino M., Panza E., Nigro A., Noris P., Gangarossa S., Rocca B., Gresele P., Bizzaro N., Malatesta P., Koivisto P.A., Longo I., Musso R., Pecoraro C., Iolascon A., Magrini U., Rodriguez Soriano J., Renieri A., Ghiggeri G.M., Ravazzolo R., Balduini C.L., Savoia A.Medicine (Baltimore) 82:203-215(2003) Macrothrombocytopenia and progressive deafness is due to a mutation in MYH9.Mhatre A.N., Kim Y., Brodie H.A., Lalwani A.K.Otol. Neurotol. 24:205-209(2003) Bladder exstrophy and Epstein type congenital macrothrombocytopenia evidence for a common cause?Utsch B., DiFeo A., Kujat A., Karle S., Schuster V., Lenk H., Jacobs U., Mueller M., Doetsch J., Rascher W., Reutter H., Martignetti J.A., Ludwig M., Troebs R.-B.Am. J. Med. Genet. A 140:2251-2253(2006) The consensus coding sequences of human breast and colorectal cancers.Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.Science 314:268-274(2006) Position of nonmuscle myosin heavy chain IIA (NMMHC-IIA) mutations predicts the natural history of MYH9-related disease.Pecci A., Panza E., Pujol-Moix N., Klersy C., Di Bari F., Bozzi V., Gresele P., Lethagen S., Fabris F., Dufour C., Granata A., Doubek M., Pecoraro C., Koivisto P.A., Heller P.G., Iolascon A., Alvisi P., Schwabe D., De Candia E., Rocca B., Russo U., Ramenghi U., Noris P., Seri M., Balduini C.L., Savoia A.Hum. Mutat. 29:409-417(2008) +Additional computationally mapped references. p>Provides general information on the entry.

12667788

NP_002464.1

NM_002473.5

P35579

54.6kD

Axon Guidance Pathway (1270303); Developmental Biology Pathway (1270302); EPH-Ephrin Signaling Pathway (1270330); EPHA-mediated Growth Cone Collapse Pathway (1270331); Fcgamma Receptor (FCGR) Dependent Phagocytosis Pathway (1269279); Immune System Pathway (1269170); Innate Immune System Pathway (1269203); RHO GTPase Effectors Pathway (1269509); RHO GTPases Activate ROCKs Pathway (1269510); RHO GTPases Activate CIT Pathway (1269514)

This gene encodes a conventional non-muscle myosin; this protein should not be confused with the unconventional myosin-9a or 9b (MYO9A or MYO9B). The encoded protein is a myosin IIA heavy chain that contains an IQ domain and a myosin head-like domain which is involved in several important functions, including cytokinesis, cell motility and maintenance of cell shape. Defects in this gene have been associated with non-syndromic sensorineural deafness autosomal dominant type 17, Epstein syndrome, Alport syndrome with macrothrombocytopenia, Sebastian syndrome, Fechtner syndrome and macrothrombocytopenia with progressive sensorineural deafness. [provided by RefSeq, Dec 2011]

MYH9: Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping. Interacts with PDLIM2. Interacts with SLC6A4. Myosin is a hexameric protein that consists of 2 heavy chain subunits (MHC), 2 alkali light chain subunits (MLC) and 2 regulatory light chain subunits (MLC-2). Interacts with RASIP1. Interacts with DDR1. Interacts with SVIL and HTRA3. In the kidney, expressed in the glomeruli. Also expressed in leukocytes. 2 isoforms of the human protein are produced by alternative splicing. Protein type: Motility/polarity/chemotaxis; Actin-binding; Motor. Chromosomal Location of Human Ortholog: 22q13.1. Cellular Component: actin cytoskeleton; actomyosin; brush border; cell-cell adherens junction; cleavage furrow; contractile ring; cytoplasm; cytosol; focal adhesion; immunological synapse; integrin complex; leading edge; membrane; myosin II complex; neuromuscular junction; nucleus; plasma membrane; protein complex; ruffle; signalosome; spindle; stress fiber; uropod. Molecular Function: actin binding; actin filament binding; actin-dependent ATPase activity; ADP binding; ATP binding; ATPase activity; calmodulin binding; microfilament motor activity; motor activity; protein anchor; protein binding; protein domain specific binding; protein homodimerization activity. Biological Process: actin cytoskeleton reorganization; actin filament-based movement; actomyosin structure organization and biogenesis; angiogenesis; axon guidance; blood vessel endothelial cell migration; cytokinesis; ephrin receptor signaling pathway; establishment of meiotic spindle localization; establishment of T cell polarity; in utero embryonic development; integrin-mediated signaling pathway; leukocyte migration; meiotic spindle organization and biogenesis; membrane protein ectodomain proteolysis; monocyte differentiation; myoblast fusion; phagocytosis, engulfment; platelet formation; protein transport; regulation of cell shape; small GTPase mediated signal transduction; uropod organization and biogenesis. Disease: Deafness, Autosomal Dominant 17; Epstein Syndrome; Fechtner Syndrome; Macrothrombocytopenia And Progressive Sensorineural Deafness; May-hegglin Anomaly; Sebastian Syndrome

0.05 mg (E-Coli)

0.2 mg (E-Coli)

460

0.5 mg (E-Coli)

750

1 mg (E-Coli)

1180