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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)

 MYH9_HUMAN              Reviewed;        1960 AA.
P35579; A8K6E4; O60805; Q60FE2; Q86T83;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
30-AUG-2017, entry version 207.
RecName: Full=Myosin-9;
AltName: Full=Cellular myosin heavy chain, type A;
AltName: Full=Myosin heavy chain 9;
AltName: Full=Myosin heavy chain, non-muscle IIa;
AltName: Full=Non-muscle myosin heavy chain A;
Short=NMMHC-A;
AltName: Full=Non-muscle myosin heavy chain IIa;
Short=NMMHC II-a;
Short=NMMHC-IIA;
Name=MYH9;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
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.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=16106752; DOI=10.1093/dnares/12.1.53;
Kato S., Ohtoko K., Ohtake H., Kimura T.;
"Vector-capping: a simple method for preparing a high-quality full-
length cDNA library.";
DNA Res. 12:53-62(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Spinal cord;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
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.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Yamakawa H., Kikuno R.F., Nagase T., Ohara O.;
"Multiplex amplification and cloning of 5'-ends of cDNA by ligase-free
recombination: Preparation of full-lemgth cDNA clones encoding motor
proteins.";
Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
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.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-1337, AND TISSUE SPECIFICITY.
PubMed=1912569;
Toothaker L.E., Gonzalez D.A., Tung N., Lemons R.S., le Beau M.M.,
Arnaout M.A., Clayton L.K., Tenen D.G.;
"Cellular myosin heavy chain in human leukocytes: isolation of 5' cDNA
clones, characterization of the protein, chromosomal localization, and
upregulation during myeloid differentiation.";
Blood 78:1826-1833(1991).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1009.
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-715.
PubMed=1860190; DOI=10.1161/01.RES.69.2.530;
Simons M., Wang M., McBride O.W., Kawamoto S., Yamakawa K., Gdula D.,
Adelstein R.S., Weir L.;
"Human nonmuscle myosin heavy chains are encoded by two genes located
on different chromosomes.";
Circ. Res. 69:530-539(1991).
[10]
PROTEIN SEQUENCE OF 2-47; 67-74; 126-139; 187-199; 203-225; 241-261;
290-299; 328-355; 359-387; 408-419; 476-494; 546-555; 581-613;
618-637; 645-651; 657-670; 683-693; 712-718; 721-731; 746-755;
765-775; 802-810; 824-829; 834-842; 861-867; 924-930; 995-1014;
1042-1048; 1052-1075; 1081-1099; 1136-1162; 1166-1191; 1261-1266;
1278-1295; 1302-1322; 1393-1400; 1405-1413; 1418-1433; 1484-1492;
1504-1513; 1519-1525; 1529-1555; 1558-1566; 1606-1612; 1614-1638;
1642-1648; 1662-1669; 1704-1724; 1794-1802; 1807-1828; 1857-1867;
1899-1912; 1923-1932 AND 1951-1960, CLEAVAGE OF INITIATOR METHIONINE,
ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Platelet;
Bienvenut W.V., Claeys R.;
Submitted (AUG-2005) to UniProtKB.
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 714-1960.
PubMed=1967836; DOI=10.1073/pnas.87.3.1164;
Saez C.G., Myers J.C., Shows T.B., Leinwand L.A.;
"Human nonmuscle myosin heavy chain mRNA: generation of diversity
through alternative polyadenylylation.";
Proc. Natl. Acad. Sci. U.S.A. 87:1164-1168(1990).
[12]
INTERACTION WITH SVIL.
PubMed=12917436; DOI=10.1074/jbc.M305311200;
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.;
"F-actin and myosin II binding domains in supervillin.";
J. Biol. Chem. 278:46094-46106(2003).
[13]
ISGYLATION.
PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
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.;
"Proteomic identification of proteins conjugated to ISG15 in mouse and
human cells.";
Biochem. Biophys. Res. Commun. 336:496-506(2005).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Prostate cancer;
PubMed=17487921; DOI=10.1002/elps.200600782;
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
"Toward a global characterization of the phosphoproteome in prostate
cancer cells: identification of phosphoproteins in the LNCaP cell
line.";
Electrophoresis 28:2027-2034(2007).
[17]
INTERACTION WITH SVIL.
PubMed=17925381; DOI=10.1242/jcs.008219;
Takizawa N., Ikebe R., Ikebe M., Luna E.J.;
"Supervillin slows cell spreading by facilitating myosin II activation
at the cell periphery.";
J. Cell Sci. 120:3792-3803(2007).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=T-cell;
PubMed=19367720; DOI=10.1021/pr800500r;
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
"Phosphorylation analysis of primary human T lymphocytes using
sequential IMAC and titanium oxide enrichment.";
J. Proteome Res. 7:5167-5176(2008).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[20]
ASSOCIATION WITH END STAGE RENAL DISEASE.
PubMed=18794856; DOI=10.1038/ng.226;
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.;
"MYH9 is a major-effect risk gene for focal segmental
glomerulosclerosis.";
Nat. Genet. 40:1175-1184(2008).
[21]
ASSOCIATION WITH END STAGE RENAL DISEASE.
PubMed=18794854; DOI=10.1038/ng.232;
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.;
"MYH9 is associated with nondiabetic end-stage renal disease in
African Americans.";
Nat. Genet. 40:1185-1192(2008).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18318008; DOI=10.1002/pmic.200700884;
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by
enrichment and fractionation of phosphopeptides with strong anion
exchange chromatography.";
Proteomics 8:1346-1361(2008).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[25]
ASSOCIATION WITH END STAGE RENAL DISEASE.
PubMed=19177153; DOI=10.1038/ki.2008.701;
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.;
"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.";
Kidney Int. 75:736-745(2009).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-11 AND SER-1943, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[28]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-8; LYS-102; LYS-299;
LYS-1024; LYS-1357; LYS-1392; LYS-1404; LYS-1410; LYS-1459 AND
LYS-1638, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[29]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=20052411; DOI=10.1371/journal.pone.0008560;
Betapudi V.;
"Myosin II motor proteins with different functions determine the fate
of lamellipodia extension during cell spreading.";
PLoS ONE 5:E8560-E8560(2010).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1714 AND SER-1943, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[31]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[33]
INTERACTION WITH HTRA3.
PubMed=22229724; DOI=10.2144/000113798;
Singh H., Makino S., Endo Y., Li Y., Stephens A.N., Nie G.;
"Application of the wheat-germ cell-free translation system to produce
high temperature requirement A3 (HtrA3) proteases.";
BioTechniques 52:23-28(2012).
[34]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
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.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-754; SER-1714 AND
SER-1943, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[36]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-628 AND SER-1943, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[37]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[38]
SUBCELLULAR LOCATION, AND UBIQUITINATION.
PubMed=27331610; DOI=10.7554/eLife.15258;
Li T., Giagtzoglou N., Eberl D.F., Jaiswal S.N., Cai T., Godt D.,
Groves A.K., Bellen H.J.;
"The E3 ligase Ubr3 regulates Usher syndrome and MYH9 disorder
proteins in the auditory organs of Drosophila and mammals.";
Elife 5:E15258-E15258(2016).
[39]
VARIANT DFNA17 HIS-705.
PubMed=11023810; DOI=10.1086/321212;
Lalwani A.K., Goldstein J.A., Kelley M.J., Luxford W., Castelein C.M.,
Mhatre A.N.;
"Human nonsyndromic hereditary deafness DFNA17 is due to a mutation in
nonmuscle myosin MYH9.";
Am. J. Hum. Genet. 67:1121-1128(2000).
[40]
VARIANTS MHA/FTNS/SBS LYS-93; CYS-702; CYS-1165; HIS-1424 AND
LYS-1841.
PubMed=10973259; DOI=10.1038/79063;
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.;
"Mutations in MYH9 result in the May-Hegglin anomaly, and Fechtner and
Sebastian syndromes.";
Nat. Genet. 26:103-105(2000).
[41]
VARIANTS MHA ILE-1155 AND LYS-1841.
PubMed=10973260; DOI=10.1038/79069;
Kelley M.J., Jawien W., Ortel T.L., Korczak J.F.;
"Mutation of MYH9, encoding non-muscle myosin heavy chain A, in May-
Hegglin anomaly.";
Nat. Genet. 26:106-108(2000).
[42]
VARIANTS MHA/SBS/FTNS/EPSTN ASN-373; CYS-702; HIS-702; ASN-1424;
HIS-1424 AND LYS-1841, AND VARIANT EPSTNS PRO-1114.
PubMed=11590545; DOI=10.1086/324267;
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.;
"Nonmuscle myosin heavy chain IIA mutations define a spectrum of
autosomal dominant macrothrombocytopenias: May-Hegglin anomaly and
Fechtner, Sebastian, Epstein, and Alport-like syndromes.";
Am. J. Hum. Genet. 69:1033-1045(2001).
[43]
VARIANTS MHA/FTNS/SBS THR-95; CYS-1165; LEU-1165; 1205-LEU--GLN-1207
DEL; HIS-1424; ASN-1424; TYR-1424 AND LYS-1841, AND VARIANT VAL-1626.
PubMed=11776386; DOI=10.1007/s100380170007;
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.;
"Identification of six novel MYH9 mutations and genotype-phenotype
relationships in autosomal dominant macrothrombocytopenia with
leukocyte inclusions.";
J. Hum. Genet. 46:722-729(2001).
[44]
VARIANT EPSTNS HIS-702.
PubMed=11935325; DOI=10.1007/s00439-001-0659-1;
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.;
"Epstein syndrome: another renal disorder with mutations in the
nonmuscle myosin heavy chain 9 gene.";
Hum. Genet. 110:182-186(2002).
[45]
VARIANTS FTNS LEU-1165; ASN-1424 AND LYS-1841, VARIANTS EPSTNS LEU-96;
TRP-1400 AND LYS-1841, AND TISSUE SPECIFICITY.
PubMed=11752022;
Arrondel C., Vodovar N., Knebelmann B., Gruenfeld J.-P., Gubler M.-C.,
Antignac C., Heidet L.;
"Expression of the nonmuscle myosin heavy chain IIA in the human
kidney and screening for MYH9 mutations in Epstein and Fechtner
syndromes.";
J. Am. Soc. Nephrol. 13:65-74(2002).
[46]
CHARACTERIZATION OF VARIANT ASN-1424.
PubMed=12649151; DOI=10.1182/blood-2002-09-2783;
Deutsch S., Rideau A., Bochaton-Piallat M.-L., Merla G., Geinoz A.,
Gabbiani G., Schwede T., Matthes T., Antonarakis S.E., Beris P.;
"Asp1424Asn MYH9 mutation results in an unstable protein responsible
for the phenotypes in May-Hegglin anomaly/Fechtner syndrome.";
Blood 102:529-534(2003).
[47]
VARIANT FTNS/SBS CYS-1165, VARIANTS SBS LEU-1165 AND
1205-LEU--GLN-1207 DEL, VARIANTS MHA HIS-1424; ASN-1424; TYR-1424 AND
LYS-1841, VARIANT EPS VAL-1816, AND VARIANT FTNS/MHA LYS-1841.
PubMed=12533692;
Kunishima S., Matsushita T., Kojima T., Sako M., Kimura F., Jo E.-K.,
Inoue C., Kamiya T., Saito H.;
"Immunofluorescence analysis of neutrophil nonmuscle myosin heavy
chain-A in MYH9 disorders: association of subcellular localization
with MYH9 mutations.";
Lab. Invest. 83:115-122(2003).
[48]
VARIANT EPSTNS HIS-702, VARIANTS FTNS GLN-910; ILE-1155 AND HIS-1424,
VARIANTS MHA/SBS 1066-GLU--ALA-1072 DEL AND ASN-1424, AND VARIANT
EPSTNS/FTNS/MHA/SBS CYS-702.
PubMed=12792306; DOI=10.1097/00005792-200305000-00006;
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.;
"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.";
Medicine (Baltimore) 82:203-215(2003).
[49]
VARIANT MPSD ASN-1424.
PubMed=12621333; DOI=10.1097/00129492-200303000-00013;
Mhatre A.N., Kim Y., Brodie H.A., Lalwani A.K.;
"Macrothrombocytopenia and progressive deafness is due to a mutation
in MYH9.";
Otol. Neurotol. 24:205-209(2003).
[50]
VARIANT EPSTNS LEU-96.
PubMed=16969870; DOI=10.1002/ajmg.a.31454;
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.;
"Bladder exstrophy and Epstein type congenital macrothrombocytopenia:
evidence for a common cause?";
Am. J. Med. Genet. A 140:2251-2253(2006).
[51]
VARIANT [LARGE SCALE ANALYSIS] ASN-810.
PubMed=16959974; DOI=10.1126/science.1133427;
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.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[52]
POSITION OF MUTATIONS IN MYH9-RELATED DISEASE.
PubMed=18059020; DOI=10.1002/humu.20661;
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.;
"Position of nonmuscle myosin heavy chain IIA (NMMHC-IIA) mutations
predicts the natural history of MYH9-related disease.";
Hum. Mutat. 29:409-417(2008).
-!- FUNCTION: 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. {ECO:0000269|PubMed:20052411}.
-!- SUBUNIT: 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 (By
similarity). Interacts with DDR1 (By similarity). Interacts with
SLC6A4 (By similarity). Interacts with PDLIM2 (By similarity).
Interacts with SVIL (PubMed:12917436, PubMed:17925381). Interacts
with HTRA3 (PubMed:22229724). Interacts with Myo7a (By
similarity). {ECO:0000250|UniProtKB:Q62812,
ECO:0000250|UniProtKB:Q8VDD5, ECO:0000269|PubMed:12917436,
ECO:0000269|PubMed:17925381, ECO:0000269|PubMed:22229724}.
-!- INTERACTION:
P61073:CXCR4; NbExp=5; IntAct=EBI-350338, EBI-489411;
P62993:GRB2; NbExp=3; IntAct=EBI-350338, EBI-401755;
O00255:MEN1; NbExp=3; IntAct=EBI-350338, EBI-592789;
O00255-2:MEN1; NbExp=4; IntAct=EBI-350338, EBI-9869387;
P19338:NCL; NbExp=3; IntAct=EBI-350338, EBI-346967;
O46385:SVIL (xeno); NbExp=2; IntAct=EBI-350338, EBI-6995105;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000250|UniProtKB:Q8VDD5}. Cytoplasm, cell cortex
{ECO:0000250|UniProtKB:Q8VDD5}. Note=Colocalizes with actin
filaments at lamellipodia margins and at the leading edge of
migrating cells (PubMed:20052411). In retinal pigment epthelial
cells, predominantly localized to stress fiber-like structures
with some localization to cytoplasmic puncta (PubMed:27331610).
{ECO:0000269|PubMed:20052411, ECO:0000269|PubMed:27331610}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P35579-1; Sequence=Displayed;
Name=2;
IsoId=P35579-2; Sequence=VSP_035409, VSP_035410;
-!- TISSUE SPECIFICITY: In the kidney, expressed in the glomeruli.
Also expressed in leukocytes. {ECO:0000269|PubMed:11752022,
ECO:0000269|PubMed:1912569}.
-!- DOMAIN: The rodlike tail sequence is highly repetitive, showing
cycles of a 28-residue repeat pattern composed of 4 heptapeptides,
characteristic for alpha-helical coiled coils.
-!- PTM: ISGylated. {ECO:0000269|PubMed:16139798}.
-!- PTM: Ubiquitination. {ECO:0000269|PubMed:27331610}.
-!- DISEASE: May-Hegglin anomaly (MHA) [MIM:155100]: A disorder
characterized by thrombocytopenia, giant platelets and Dohle body-
like inclusions in peripheral blood leukocytes. appearing as
highly parallel paracrystalline bodies.
{ECO:0000269|PubMed:10973259, ECO:0000269|PubMed:10973260,
ECO:0000269|PubMed:11590545, ECO:0000269|PubMed:11776386,
ECO:0000269|PubMed:12533692, ECO:0000269|PubMed:12792306}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Sebastian syndrome (SBS) [MIM:605249]: Autosomal dominant
macrothrombocytopenia characterized by thrombocytopenia, giant
platelets and leukocyte inclusions that are smaller and less
organized than in May-Hegglin anomaly.
{ECO:0000269|PubMed:12533692}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Fechtner syndrome (FTNS) [MIM:153640]: Autosomal dominant
macrothrombocytopenia characterized by thrombocytopenia, giant
platelets and leukocyte inclusions that are small and poorly
organized. Additionally, FTNS is distinguished by Alport-like
clinical features of sensorineural deafness, cataracts and
nephritis. {ECO:0000269|PubMed:10973259,
ECO:0000269|PubMed:11752022, ECO:0000269|PubMed:11776386,
ECO:0000269|PubMed:12533692, ECO:0000269|PubMed:12792306}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Epstein syndrome (EPSTNS) [MIM:153650]: An autosomal
dominant disorder characterized by the association of
macrothrombocytopathy, sensorineural hearing loss and nephritis.
{ECO:0000269|PubMed:11590545, ECO:0000269|PubMed:11752022,
ECO:0000269|PubMed:11935325, ECO:0000269|PubMed:12533692,
ECO:0000269|PubMed:12792306, ECO:0000269|PubMed:16969870}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Deafness, autosomal dominant, 17 (DFNA17) [MIM:603622]: A
form of deafness characterized by progressive high frequency
hearing impairment and cochleosaccular degeneration.
{ECO:0000269|PubMed:11023810}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Macrothrombocytopenia and progressive sensorineural
deafness (MPSD) [MIM:600208]: An autosomal dominant disorder
characterized by the association of macrothrombocytopathy and
progressive sensorineural hearing loss without renal dysfunction.
{ECO:0000269|PubMed:12621333}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Note=Subjects with mutations in the motor domain of MYH9
present with severe thrombocytopenia and develop nephritis and
deafness before the age of 40 years, while those with mutations in
the tail domain have a much lower risk of noncongenital
complications and significantly higher platelet counts. The
clinical course of patients with mutations in the four most
frequently affected residues of MYH9 (responsible for 70% of MYH9-
related cases) were evaluated. Mutations at residue 1933 do not
induce kidney damage or cataracts and cause deafness only in the
elderly, those in position 702 result in severe thrombocytopenia
and produce nephritis and deafness at a juvenile age, while
alterations at residue 1424 or 1841 result in intermediate
clinical pictures.
-!- DISEASE: Note=Genetic variations in MYH9 are associated with non-
diabetic end stage renal disease (ESRD).
-!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
superfamily. Myosin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAD89954.1; Type=Frameshift; Positions=1890; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/MYH9ID481.html";
-----------------------------------------------------------------------
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EMBL; CR456526; CAG30412.1; -; mRNA.
EMBL; AB191263; BAD52439.1; -; mRNA.
EMBL; AL832639; CAD89954.1; ALT_FRAME; mRNA.
EMBL; AB290175; BAG06729.1; -; mRNA.
EMBL; Z82215; CAB05105.1; -; Genomic_DNA.
EMBL; CH471095; EAW60096.1; -; Genomic_DNA.
EMBL; M81105; AAA59888.1; -; mRNA.
EMBL; AK291609; BAF84298.1; -; mRNA.
EMBL; M69180; AAA61765.1; -; mRNA.
EMBL; M31013; AAA36349.1; -; mRNA.
CCDS; CCDS13927.1; -. [P35579-1]
PIR; A61231; A61231.
RefSeq; NP_002464.1; NM_002473.5. [P35579-1]
RefSeq; XP_011528499.1; XM_011530197.2. [P35579-1]
RefSeq; XP_016884292.1; XM_017028803.1. [P35579-1]
RefSeq; XP_016884293.1; XM_017028804.1. [P35579-1]
RefSeq; XP_016884294.1; XM_017028805.1. [P35579-1]
RefSeq; XP_016884295.1; XM_017028806.1. [P35579-1]
UniGene; Hs.474751; -.
PDB; 2LNK; NMR; -; C=1897-1935.
PDB; 3ZWH; X-ray; 1.94 A; Q=1893-1937.
PDB; 4CFQ; X-ray; 1.37 A; Q/R=1893-1937.
PDB; 4CFR; X-ray; 1.40 A; Q=1893-1937.
PDB; 4ETO; X-ray; 1.54 A; P=1908-1923.
PDBsum; 2LNK; -.
PDBsum; 3ZWH; -.
PDBsum; 4CFQ; -.
PDBsum; 4CFR; -.
PDBsum; 4ETO; -.
ProteinModelPortal; P35579; -.
SMR; P35579; -.
BioGrid; 110712; 314.
DIP; DIP-33103N; -.
IntAct; P35579; 269.
MINT; MINT-7901706; -.
STRING; 9606.ENSP00000216181; -.
ChEMBL; CHEMBL2189151; -.
iPTMnet; P35579; -.
PhosphoSitePlus; P35579; -.
SwissPalm; P35579; -.
BioMuta; MYH9; -.
DMDM; 6166599; -.
EPD; P35579; -.
PaxDb; P35579; -.
PeptideAtlas; P35579; -.
PRIDE; P35579; -.
TopDownProteomics; P35579-1; -. [P35579-1]
DNASU; 4627; -.
Ensembl; ENST00000216181; ENSP00000216181; ENSG00000100345. [P35579-1]
GeneID; 4627; -.
KEGG; hsa:4627; -.
UCSC; uc003apg.4; human. [P35579-1]
CTD; 4627; -.
DisGeNET; 4627; -.
GeneCards; MYH9; -.
GeneReviews; MYH9; -.
HGNC; HGNC:7579; MYH9.
HPA; CAB015386; -.
HPA; HPA001644; -.
MalaCards; MYH9; -.
MIM; 153640; phenotype.
MIM; 153650; phenotype.
MIM; 155100; phenotype.
MIM; 160775; gene.
MIM; 600208; phenotype.
MIM; 603622; phenotype.
MIM; 605249; phenotype.
neXtProt; NX_P35579; -.
OpenTargets; ENSG00000100345; -.
Orphanet; 90635; Autosomal dominant non-syndromic sensorineural deafness type DFNA.
Orphanet; 182050; MYH9-related disease.
PharmGKB; PA31377; -.
eggNOG; KOG0161; Eukaryota.
eggNOG; COG5022; LUCA.
GeneTree; ENSGT00760000118919; -.
HOGENOM; HOG000173958; -.
HOVERGEN; HBG004704; -.
InParanoid; P35579; -.
KO; K10352; -.
OMA; GDSEHKR; -.
OrthoDB; EOG091G009J; -.
PhylomeDB; P35579; -.
TreeFam; TF333601; -.
Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-HSA-3928663; EPHA-mediated growth cone collapse.
Reactome; R-HSA-416572; Sema4D induced cell migration and growth-cone collapse.
Reactome; R-HSA-5625740; RHO GTPases activate PKNs.
Reactome; R-HSA-5625900; RHO GTPases activate CIT.
Reactome; R-HSA-5627117; RHO GTPases Activate ROCKs.
Reactome; R-HSA-5627123; RHO GTPases activate PAKs.
SIGNOR; P35579; -.
ChiTaRS; MYH9; human.
GeneWiki; MYH9; -.
GenomeRNAi; 4627; -.
PMAP-CutDB; P35579; -.
PRO; PR:P35579; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000100345; -.
CleanEx; HS_MYH9; -.
ExpressionAtlas; P35579; baseline and differential.
Genevisible; P35579; HS.
GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
GO; GO:0042641; C:actomyosin; IDA:UniProtKB.
GO; GO:0005826; C:actomyosin contractile ring; IDA:UniProtKB.
GO; GO:0005903; C:brush border; IEA:Ensembl.
GO; GO:0031252; C:cell leading edge; IDA:UniProtKB.
GO; GO:0005913; C:cell-cell adherens junction; IEA:Ensembl.
GO; GO:0032154; C:cleavage furrow; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IDA:BHF-UCL.
GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
GO; GO:0001772; C:immunological synapse; IEA:Ensembl.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0016460; C:myosin II complex; IDA:UniProtKB.
GO; GO:0097513; C:myosin II filament; IDA:UniProtKB.
GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0001726; C:ruffle; IDA:UniProtKB.
GO; GO:0005819; C:spindle; IEA:Ensembl.
GO; GO:0001725; C:stress fiber; IDA:UniProtKB.
GO; GO:0001931; C:uropod; IDA:MGI.
GO; GO:0003779; F:actin binding; IDA:MGI.
GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
GO; GO:0030898; F:actin-dependent ATPase activity; IDA:MGI.
GO; GO:0043531; F:ADP binding; IDA:MGI.
GO; GO:0005524; F:ATP binding; IDA:MGI.
GO; GO:0016887; F:ATPase activity; IDA:UniProtKB.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
GO; GO:0000146; F:microfilament motor activity; IDA:UniProtKB.
GO; GO:0003774; F:motor activity; NAS:UniProtKB.
GO; GO:0043495; F:protein anchor; IMP:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0031532; P:actin cytoskeleton reorganization; IMP:UniProtKB.
GO; GO:0030048; P:actin filament-based movement; IDA:UniProtKB.
GO; GO:0031032; P:actomyosin structure organization; IDA:UniProtKB.
GO; GO:0001525; P:angiogenesis; IDA:UniProtKB.
GO; GO:0043534; P:blood vessel endothelial cell migration; IMP:UniProtKB.
GO; GO:0032506; P:cytokinetic process; IMP:UniProtKB.
GO; GO:0051295; P:establishment of meiotic spindle localization; IEA:Ensembl.
GO; GO:0001768; P:establishment of T cell polarity; IEA:Ensembl.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0007229; P:integrin-mediated signaling pathway; NAS:UniProtKB.
GO; GO:0050900; P:leukocyte migration; NAS:UniProtKB.
GO; GO:0000212; P:meiotic spindle organization; IEA:Ensembl.
GO; GO:0006509; P:membrane protein ectodomain proteolysis; IDA:UniProtKB.
GO; GO:0030224; P:monocyte differentiation; IEP:UniProtKB.
GO; GO:0007520; P:myoblast fusion; IEA:Ensembl.
GO; GO:1903919; P:negative regulation of actin filament severing; IMP:UniProtKB.
GO; GO:0006911; P:phagocytosis, engulfment; ISS:UniProtKB.
GO; GO:0070527; P:platelet aggregation; IMP:UniProtKB.
GO; GO:0030220; P:platelet formation; IMP:UniProtKB.
GO; GO:1903923; P:positive regulation of protein processing in phagocytic vesicle; ISS:UniProtKB.
GO; GO:0015031; P:protein transport; IMP:UniProtKB.
GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
GO; GO:0032796; P:uropod organization; IEA:Ensembl.
InterPro; IPR000048; IQ_motif_EF-hand-BS.
InterPro; IPR001609; Myosin_head_motor_dom.
InterPro; IPR004009; Myosin_N.
InterPro; IPR002928; Myosin_tail.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR016137; RGS.
Pfam; PF00063; Myosin_head; 1.
Pfam; PF02736; Myosin_N; 1.
Pfam; PF01576; Myosin_tail_1; 1.
PRINTS; PR00193; MYOSINHEAVY.
SMART; SM00015; IQ; 1.
SMART; SM00242; MYSc; 1.
SUPFAM; SSF48097; SSF48097; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS50096; IQ; 1.
PROSITE; PS51456; MYOSIN_MOTOR; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Actin-binding; Alport syndrome;
Alternative splicing; ATP-binding; Calmodulin-binding; Cataract;
Cell adhesion; Cell shape; Coiled coil; Complete proteome; Cytoplasm;
Cytoskeleton; Deafness; Direct protein sequencing; Disease mutation;
Methylation; Motor protein; Myosin; Non-syndromic deafness;
Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|Ref.10}.
CHAIN 2 1960 Myosin-9.
/FTId=PRO_0000123416.
DOMAIN 81 776 Myosin motor.
DOMAIN 779 808 IQ. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
NP_BIND 174 181 ATP. {ECO:0000255}.
REGION 654 676 Actin-binding.
COILED 837 1926 {ECO:0000255}.
MOD_RES 2 2 N-acetylalanine. {ECO:0000269|Ref.10}.
MOD_RES 8 8 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 11 11 Phosphotyrosine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 102 102 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 299 299 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 435 435 N6-acetyllysine.
{ECO:0000250|UniProtKB:P35580}.
MOD_RES 613 613 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8VDD5}.
MOD_RES 628 628 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 754 754 Phosphotyrosine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 850 850 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q8VDD5}.
MOD_RES 860 860 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8VDD5}.
MOD_RES 975 975 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8VDD5}.
MOD_RES 1024 1024 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1114 1114 Phosphoserine.
{ECO:0000250|UniProtKB:Q8VDD5}.
MOD_RES 1234 1234 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q61879}.
MOD_RES 1249 1249 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8VDD5}.
MOD_RES 1357 1357 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1392 1392 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1404 1404 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1410 1410 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1459 1459 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1638 1638 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1669 1669 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q8VDD5}.
MOD_RES 1714 1714 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1793 1793 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8VDD5}.
MOD_RES 1802 1802 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8VDD5}.
MOD_RES 1845 1845 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8VDD5}.
MOD_RES 1923 1923 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q61879}.
MOD_RES 1943 1943 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:17487921,
ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:18318008,
ECO:0000244|PubMed:19367720,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
VAR_SEQ 1 136 Missing (in isoform 2).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_035409.
VAR_SEQ 980 1421 Missing (in isoform 2).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_035410.
VARIANT 93 93 N -> K (in MHA; dbSNP:rs121913655).
{ECO:0000269|PubMed:10973259}.
/FTId=VAR_010791.
VARIANT 95 95 A -> T (in MHA).
{ECO:0000269|PubMed:11776386}.
/FTId=VAR_018308.
VARIANT 96 96 S -> L (in EPSTNS; dbSNP:rs121913657).
{ECO:0000269|PubMed:11752022,
ECO:0000269|PubMed:16969870}.
/FTId=VAR_018309.
VARIANT 373 373 K -> N (in MHA and SBS).
{ECO:0000269|PubMed:11590545}.
/FTId=VAR_018310.
VARIANT 702 702 R -> C (in EPSTNS, FTNS, MHA and SBS;
dbSNP:rs80338826).
{ECO:0000269|PubMed:10973259,
ECO:0000269|PubMed:11590545,
ECO:0000269|PubMed:12792306}.
/FTId=VAR_010792.
VARIANT 702 702 R -> H (in EPSTNS; dbSNP:rs80338827).
{ECO:0000269|PubMed:11590545,
ECO:0000269|PubMed:11935325,
ECO:0000269|PubMed:12792306}.
/FTId=VAR_018311.
VARIANT 705 705 R -> H (in DFNA17; dbSNP:rs80338828).
{ECO:0000269|PubMed:11023810}.
/FTId=VAR_010793.
VARIANT 810 810 K -> N (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036006.
VARIANT 910 910 K -> Q (in FTNS; dbSNP:rs554332083).
{ECO:0000269|PubMed:12792306}.
/FTId=VAR_044226.
VARIANT 967 967 V -> E (in dbSNP:rs16996652).
/FTId=VAR_044227.
VARIANT 1066 1072 Missing (in MHA and SBS).
{ECO:0000269|PubMed:12792306}.
/FTId=VAR_044228.
VARIANT 1114 1114 S -> P (in EPSTNS; dbSNP:rs200901330).
{ECO:0000269|PubMed:11590545}.
/FTId=VAR_018312.
VARIANT 1155 1155 T -> I (in MHA and FTNS;
dbSNP:rs121913656).
{ECO:0000269|PubMed:10973260,
ECO:0000269|PubMed:12792306}.
/FTId=VAR_010794.
VARIANT 1165 1165 R -> C (in FTNS and SBS;
dbSNP:rs80338829).
{ECO:0000269|PubMed:10973259,
ECO:0000269|PubMed:11776386,
ECO:0000269|PubMed:12533692}.
/FTId=VAR_010795.
VARIANT 1165 1165 R -> L (in FTNS, MHA and SBS;
dbSNP:rs80338830).
{ECO:0000269|PubMed:11752022,
ECO:0000269|PubMed:11776386,
ECO:0000269|PubMed:12533692}.
/FTId=VAR_018313.
VARIANT 1205 1207 Missing (in SBS).
{ECO:0000269|PubMed:11776386,
ECO:0000269|PubMed:12533692}.
/FTId=VAR_018314.
VARIANT 1400 1400 R -> W (in EPSTNS; unknown pathological
significance; might contribute to
pathogenicity when associated with L-96;
dbSNP:rs76368635).
{ECO:0000269|PubMed:11752022}.
/FTId=VAR_018315.
VARIANT 1424 1424 D -> H (in FTNS and MHA;
dbSNP:rs80338831).
{ECO:0000269|PubMed:10973259,
ECO:0000269|PubMed:11590545,
ECO:0000269|PubMed:11776386,
ECO:0000269|PubMed:12533692,
ECO:0000269|PubMed:12792306}.
/FTId=VAR_010796.
VARIANT 1424 1424 D -> N (in FTNS, MHA, SBS and MPSD;
results in reduced protein levels;
dbSNP:rs80338831).
{ECO:0000269|PubMed:11590545,
ECO:0000269|PubMed:11752022,
ECO:0000269|PubMed:11776386,
ECO:0000269|PubMed:12533692,
ECO:0000269|PubMed:12621333,
ECO:0000269|PubMed:12649151,
ECO:0000269|PubMed:12792306}.
/FTId=VAR_018316.
VARIANT 1424 1424 D -> Y (in MHA; dbSNP:rs80338831).
{ECO:0000269|PubMed:11776386,
ECO:0000269|PubMed:12533692}.
/FTId=VAR_018317.
VARIANT 1626 1626 I -> V (in dbSNP:rs2269529).
{ECO:0000269|PubMed:11776386}.
/FTId=VAR_018318.
VARIANT 1816 1816 I -> V (in EPSTNS; dbSNP:rs762773112).
{ECO:0000269|PubMed:12533692}.
/FTId=VAR_030385.
VARIANT 1841 1841 E -> K (in FTNS, SBS, MHA and EPSTNS;
dbSNP:rs80338834).
{ECO:0000269|PubMed:10973259,
ECO:0000269|PubMed:10973260,
ECO:0000269|PubMed:11590545,
ECO:0000269|PubMed:11752022,
ECO:0000269|PubMed:11776386,
ECO:0000269|PubMed:12533692}.
/FTId=VAR_010797.
CONFLICT 53 55 EAI -> RGH (in Ref. 9). {ECO:0000305}.
CONFLICT 660 660 T -> S (in Ref. 9). {ECO:0000305}.
CONFLICT 869 869 T -> M (in Ref. 11; AAA36349).
{ECO:0000305}.
CONFLICT 931 931 C -> Y (in Ref. 11; AAA36349).
{ECO:0000305}.
CONFLICT 1000 1000 R -> I (in Ref. 8; BAF84298).
{ECO:0000305}.
CONFLICT 1240 1241 KG -> GR (in Ref. 11; AAA36349).
{ECO:0000305}.
CONFLICT 1350 1350 E -> EE (in Ref. 11). {ECO:0000305}.
CONFLICT 1462 1462 E -> G (in Ref. 1; CAD89954).
{ECO:0000305}.
CONFLICT 1546 1546 D -> G (in Ref. 1; CAD89954).
{ECO:0000305}.
CONFLICT 1764 1764 T -> A (in Ref. 11; AAA36349).
{ECO:0000305}.
CONFLICT 1771 1771 S -> G (in Ref. 11; AAA36349).
{ECO:0000305}.
STRAND 1895 1897 {ECO:0000244|PDB:4CFR}.
HELIX 1899 1903 {ECO:0000244|PDB:4CFR}.
HELIX 1904 1921 {ECO:0000244|PDB:4CFQ}.
STRAND 1922 1925 {ECO:0000244|PDB:2LNK}.
SEQUENCE 1960 AA; 226532 MW; 588F84BB8C106E6F CRC64;
MAQQAADKYL YVDKNFINNP LAQADWAAKK LVWVPSDKSG FEPASLKEEV GEEAIVELVE
NGKKVKVNKD DIQKMNPPKF SKVEDMAELT CLNEASVLHN LKERYYSGLI YTYSGLFCVV
INPYKNLPIY SEEIVEMYKG KKRHEMPPHI YAITDTAYRS MMQDREDQSI LCTGESGAGK
TENTKKVIQY LAYVASSHKS KKDQGELERQ LLQANPILEA FGNAKTVKND NSSRFGKFIR
INFDVNGYIV GANIETYLLE KSRAIRQAKE ERTFHIFYYL LSGAGEHLKT DLLLEPYNKY
RFLSNGHVTI PGQQDKDMFQ ETMEAMRIMG IPEEEQMGLL RVISGVLQLG NIVFKKERNT
DQASMPDNTA AQKVSHLLGI NVTDFTRGIL TPRIKVGRDY VQKAQTKEQA DFAIEALAKA
TYERMFRWLV LRINKALDKT KRQGASFIGI LDIAGFEIFD LNSFEQLCIN YTNEKLQQLF
NHTMFILEQE EYQREGIEWN FIDFGLDLQP CIDLIEKPAG PPGILALLDE ECWFPKATDK
SFVEKVMQEQ GTHPKFQKPK QLKDKADFCI IHYAGKVDYK ADEWLMKNMD PLNDNIATLL
HQSSDKFVSE LWKDVDRIIG LDQVAGMSET ALPGAFKTRK GMFRTVGQLY KEQLAKLMAT
LRNTNPNFVR CIIPNHEKKA GKLDPHLVLD QLRCNGVLEG IRICRQGFPN RVVFQEFRQR
YEILTPNSIP KGFMDGKQAC VLMIKALELD SNLYRIGQSK VFFRAGVLAH LEEERDLKIT
DVIIGFQACC RGYLARKAFA KRQQQLTAMK VLQRNCAAYL KLRNWQWWRL FTKVKPLLQV
SRQEEEMMAK EEELVKVREK QLAAENRLTE METLQSQLMA EKLQLQEQLQ AETELCAEAE
ELRARLTAKK QELEEICHDL EARVEEEEER CQHLQAEKKK MQQNIQELEE QLEEEESARQ
KLQLEKVTTE AKLKKLEEEQ IILEDQNCKL AKEKKLLEDR IAEFTTNLTE EEEKSKSLAK
LKNKHEAMIT DLEERLRREE KQRQELEKTR RKLEGDSTDL SDQIAELQAQ IAELKMQLAK
KEEELQAALA RVEEEAAQKN MALKKIRELE SQISELQEDL ESERASRNKA EKQKRDLGEE
LEALKTELED TLDSTAAQQE LRSKREQEVN ILKKTLEEEA KTHEAQIQEM RQKHSQAVEE
LAEQLEQTKR VKANLEKAKQ TLENERGELA NEVKVLLQGK GDSEHKRKKV EAQLQELQVK
FNEGERVRTE LADKVTKLQV ELDNVTGLLS QSDSKSSKLT KDFSALESQL QDTQELLQEE
NRQKLSLSTK LKQVEDEKNS FREQLEEEEE AKHNLEKQIA TLHAQVADMK KKMEDSVGCL
ETAEEVKRKL QKDLEGLSQR HEEKVAAYDK LEKTKTRLQQ ELDDLLVDLD HQRQSACNLE
KKQKKFDQLL AEEKTISAKY AEERDRAEAE AREKETKALS LARALEEAME QKAELERLNK
QFRTEMEDLM SSKDDVGKSV HELEKSKRAL EQQVEEMKTQ LEELEDELQA TEDAKLRLEV
NLQAMKAQFE RDLQGRDEQS EEKKKQLVRQ VREMEAELED ERKQRSMAVA ARKKLEMDLK
DLEAHIDSAN KNRDEAIKQL RKLQAQMKDC MRELDDTRAS REEILAQAKE NEKKLKSMEA
EMIQLQEELA AAERAKRQAQ QERDELADEI ANSSGKGALA LEEKRRLEAR IAQLEEELEE
EQGNTELIND RLKKANLQID QINTDLNLER SHAQKNENAR QQLERQNKEL KVKLQEMEGT
VKSKYKASIT ALEAKIAQLE EQLDNETKER QAACKQVRRT EKKLKDVLLQ VDDERRNAEQ
YKDQADKAST RLKQLKRQLE EAEEEAQRAN ASRRKLQREL EDATETADAM NREVSSLKNK
LRRGDLPFVV PRRMARKGAG DGSDEEVDGK ADGAEAKPAE


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