MYH9_HUMAN
ID MYH9_HUMAN Reviewed; 1960 AA.
AC P35579; A8K6E4; O60805; Q60FE2; Q86T83;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 245.
DE RecName: Full=Myosin-9;
DE AltName: Full=Cellular myosin heavy chain, type A;
DE AltName: Full=Myosin heavy chain 9;
DE AltName: Full=Myosin heavy chain, non-muscle IIa;
DE AltName: Full=Non-muscle myosin heavy chain A;
DE Short=NMMHC-A;
DE AltName: Full=Non-muscle myosin heavy chain IIa;
DE Short=NMMHC II-a;
DE Short=NMMHC-IIA;
GN Name=MYH9;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16106752; DOI=10.1093/dnares/12.1.53;
RA Kato S., Ohtoko K., Ohtake H., Kimura T.;
RT "Vector-capping: a simple method for preparing a high-quality full-length
RT cDNA library.";
RL DNA Res. 12:53-62(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Spinal cord;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Yamakawa H., Kikuno R.F., Nagase T., Ohara O.;
RT "Multiplex amplification and cloning of 5'-ends of cDNA by ligase-free
RT recombination: Preparation of full-lemgth cDNA clones encoding motor
RT proteins.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-1337, AND TISSUE SPECIFICITY.
RX PubMed=1912569;
RA Toothaker L.E., Gonzalez D.A., Tung N., Lemons R.S., le Beau M.M.,
RA Arnaout M.A., Clayton L.K., Tenen D.G.;
RT "Cellular myosin heavy chain in human leukocytes: isolation of 5' cDNA
RT clones, characterization of the protein, chromosomal localization, and
RT upregulation during myeloid differentiation.";
RL Blood 78:1826-1833(1991).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1009.
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-715.
RX PubMed=1860190; DOI=10.1161/01.res.69.2.530;
RA Simons M., Wang M., McBride O.W., Kawamoto S., Yamakawa K., Gdula D.,
RA Adelstein R.S., Weir L.;
RT "Human nonmuscle myosin heavy chains are encoded by two genes located on
RT different chromosomes.";
RL Circ. Res. 69:530-539(1991).
RN [10]
RP PROTEIN SEQUENCE OF 2-47; 67-74; 126-139; 187-199; 203-225; 241-261;
RP 290-299; 328-355; 359-387; 408-419; 476-494; 546-555; 581-613; 618-637;
RP 645-651; 657-670; 683-693; 712-718; 721-731; 746-755; 765-775; 802-810;
RP 824-829; 834-842; 861-867; 924-930; 995-1014; 1042-1048; 1052-1075;
RP 1081-1099; 1136-1162; 1166-1191; 1261-1266; 1278-1295; 1302-1322;
RP 1393-1400; 1405-1413; 1418-1433; 1484-1492; 1504-1513; 1519-1525;
RP 1529-1555; 1558-1566; 1606-1612; 1614-1638; 1642-1648; 1662-1669;
RP 1704-1724; 1794-1802; 1807-1828; 1857-1867; 1899-1912; 1923-1932 AND
RP 1951-1960, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Platelet;
RA Bienvenut W.V., Claeys R.;
RL Submitted (AUG-2005) to UniProtKB.
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 714-1960.
RX PubMed=1967836; DOI=10.1073/pnas.87.3.1164;
RA Saez C.G., Myers J.C., Shows T.B., Leinwand L.A.;
RT "Human nonmuscle myosin heavy chain mRNA: generation of diversity through
RT alternative polyadenylylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:1164-1168(1990).
RN [12]
RP INTERACTION WITH SVIL.
RX PubMed=12917436; DOI=10.1074/jbc.m305311200;
RA Chen Y., Takizawa N., Crowley J.L., Oh S.W., Gatto C.L., Kambara T.,
RA Sato O., Li X.-D., Ikebe M., Luna E.J.;
RT "F-actin and myosin II binding domains in supervillin.";
RL J. Biol. Chem. 278:46094-46106(2003).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [14]
RP ISGYLATION.
RX PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
RA Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
RA Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
RT "Proteomic identification of proteins conjugated to ISG15 in mouse and
RT human cells.";
RL Biochem. Biophys. Res. Commun. 336:496-506(2005).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [17]
RP INTERACTION WITH S100A4, AND FUNCTION.
RX PubMed=16707441; DOI=10.1158/0008-5472.can-05-3087;
RA Li Z.H., Bresnick A.R.;
RT "The S100A4 metastasis factor regulates cellular motility via a direct
RT interaction with myosin-IIA.";
RL Cancer Res. 66:5173-5180(2006).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Prostate cancer;
RX PubMed=17487921; DOI=10.1002/elps.200600782;
RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
RT "Toward a global characterization of the phosphoproteome in prostate cancer
RT cells: identification of phosphoproteins in the LNCaP cell line.";
RL Electrophoresis 28:2027-2034(2007).
RN [19]
RP INTERACTION WITH SVIL.
RX PubMed=17925381; DOI=10.1242/jcs.008219;
RA Takizawa N., Ikebe R., Ikebe M., Luna E.J.;
RT "Supervillin slows cell spreading by facilitating myosin II activation at
RT the cell periphery.";
RL J. Cell Sci. 120:3792-3803(2007).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [22]
RP ASSOCIATION WITH END STAGE RENAL DISEASE.
RX PubMed=18794856; DOI=10.1038/ng.226;
RA Kopp J.B., Smith M.W., Nelson G.W., Johnson R.C., Freedman B.I.,
RA Bowden D.W., Oleksyk T., McKenzie L.M., Kajiyama H., Ahuja T.S.,
RA Berns J.S., Briggs W., Cho M.E., Dart R.A., Kimmel P.L., Korbet S.M.,
RA Michel D.M., Mokrzycki M.H., Schelling J.R., Simon E., Trachtman H.,
RA Vlahov D., Winkler C.A.;
RT "MYH9 is a major-effect risk gene for focal segmental glomerulosclerosis.";
RL Nat. Genet. 40:1175-1184(2008).
RN [23]
RP ASSOCIATION WITH END STAGE RENAL DISEASE.
RX PubMed=18794854; DOI=10.1038/ng.232;
RA Kao W.H., Klag M.J., Meoni L.A., Reich D., Berthier-Schaad Y., Li M.,
RA Coresh J., Patterson N., Tandon A., Powe N.R., Fink N.E., Sadler J.H.,
RA Weir M.R., Abboud H.E., Adler S.G., Divers J., Iyengar S.K., Freedman B.I.,
RA Kimmel P.L., Knowler W.C., Kohn O.F., Kramp K., Leehey D.J., Nicholas S.B.,
RA Pahl M.V., Schelling J.R., Sedor J.R., Thornley-Brown D., Winkler C.A.,
RA Smith M.W., Parekh R.S.;
RT "MYH9 is associated with nondiabetic end-stage renal disease in African
RT Americans.";
RL Nat. Genet. 40:1185-1192(2008).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [26]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [27]
RP ASSOCIATION WITH END STAGE RENAL DISEASE.
RX PubMed=19177153; DOI=10.1038/ki.2008.701;
RA Freedman B.I., Hicks P.J., Bostrom M.A., Cunningham M.E., Liu Y.,
RA Divers J., Kopp J.B., Winkler C.A., Nelson G.W., Langefeld C.D.,
RA Bowden D.W.;
RT "Polymorphisms in the non-muscle myosin heavy chain 9 gene (MYH9) are
RT strongly associated with end-stage renal disease historically attributed to
RT hypertension in African Americans.";
RL Kidney Int. 75:736-745(2009).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-11 AND SER-1943, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [30]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-8; LYS-102; LYS-299; LYS-1024;
RP LYS-1357; LYS-1392; LYS-1404; LYS-1410; LYS-1459 AND LYS-1638, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [31]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20052411; DOI=10.1371/journal.pone.0008560;
RA Betapudi V.;
RT "Myosin II motor proteins with different functions determine the fate of
RT lamellipodia extension during cell spreading.";
RL PLoS ONE 5:E8560-E8560(2010).
RN [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1714 AND SER-1943, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [33]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [34]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [35]
RP INTERACTION WITH HTRA3.
RX PubMed=22229724; DOI=10.2144/000113798;
RA Singh H., Makino S., Endo Y., Li Y., Stephens A.N., Nie G.;
RT "Application of the wheat-germ cell-free translation system to produce high
RT temperature requirement A3 (HtrA3) proteases.";
RL BioTechniques 52:23-28(2012).
RN [36]
RP INTERACTION WITH ZBED4, AND SUBCELLULAR LOCATION.
RX PubMed=22693546; DOI=10.1371/journal.pone.0035317;
RA Mokhonov V.V., Theendakara V.P., Gribanova Y.E., Ahmedli N.B., Farber D.B.;
RT "Sequence-specific binding of recombinant Zbed4 to DNA: insights into Zbed4
RT participation in gene transcription and its association with other
RT proteins.";
RL PLoS ONE 7:e35317-e35317(2012).
RN [37]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [38]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-754; SER-1714 AND SER-1943,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [39]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-628 AND SER-1943, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [40]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [41]
RP INTERACTION WITH RAB3A.
RX PubMed=27325790; DOI=10.1083/jcb.201511093;
RA Encarnacao M., Espada L., Escrevente C., Mateus D., Ramalho J.,
RA Michelet X., Santarino I., Hsu V.W., Brenner M.B., Barral D.C.,
RA Vieira O.V.;
RT "A Rab3a-dependent complex essential for lysosome positioning and plasma
RT membrane repair.";
RL J. Cell Biol. 213:631-640(2016).
RN [42]
RP SUBCELLULAR LOCATION, AND UBIQUITINATION.
RX PubMed=27331610; DOI=10.7554/elife.15258;
RA Li T., Giagtzoglou N., Eberl D.F., Jaiswal S.N., Cai T., Godt D.,
RA Groves A.K., Bellen H.J.;
RT "The E3 ligase Ubr3 regulates Usher syndrome and MYH9 disorder proteins in
RT the auditory organs of Drosophila and mammals.";
RL Elife 5:E15258-E15258(2016).
RN [43]
RP INTERACTION WITH LIMCH1, AND REGION.
RX PubMed=28228547; DOI=10.1091/mbc.e15-04-0218;
RA Lin Y.H., Zhen Y.Y., Chien K.Y., Lee I.C., Lin W.C., Chen M.Y., Pai L.M.;
RT "LIMCH1 regulates nonmuscle myosin-II activity and suppresses cell
RT migration.";
RL Mol. Biol. Cell 28:1054-1065(2017).
RN [44]
RP INTERACTION WITH CFAP95.
RX PubMed=28345668; DOI=10.1038/srep45311;
RA Zhou S., Liu Y., Ma Y., Zhang X., Li Y., Wen J.;
RT "C9ORF135 encodes a membrane protein whose expression is related to
RT pluripotency in human embryonic stem cells.";
RL Sci. Rep. 7:45311-45311(2017).
RN [45]
RP VARIANT DFNA17 HIS-705.
RX PubMed=11023810; DOI=10.1086/321212;
RA Lalwani A.K., Goldstein J.A., Kelley M.J., Luxford W., Castelein C.M.,
RA Mhatre A.N.;
RT "Human nonsyndromic hereditary deafness DFNA17 is due to a mutation in
RT nonmuscle myosin MYH9.";
RL Am. J. Hum. Genet. 67:1121-1128(2000).
RN [46]
RP VARIANTS MATINS LYS-93; CYS-702; CYS-1165; HIS-1424 AND LYS-1841.
RX PubMed=10973259; DOI=10.1038/79063;
RA Seri M., Cusano M., Gangarossa S., Caridi G., Bordo D., Lo Nigro C.,
RA Ghiggeri G.M., Ravazzolo R., Savino M., Del Vecchio M., d'Apolito M.,
RA Iolascon A., Zelante L.L., Savoia A., Balduini C.L., Noris P., Magrini U.,
RA Belletti S., Heath K.E., Babcock M., Glucksman M.J., Aliprandis E.,
RA Bizzaro N., Desnick R.J., Martignetti J.A.;
RT "Mutations in MYH9 result in the May-Hegglin anomaly, and Fechtner and
RT Sebastian syndromes.";
RL Nat. Genet. 26:103-105(2000).
RN [47]
RP VARIANTS MATINS ILE-1155 AND LYS-1841.
RX PubMed=10973260; DOI=10.1038/79069;
RA Kelley M.J., Jawien W., Ortel T.L., Korczak J.F.;
RT "Mutation of MYH9, encoding non-muscle myosin heavy chain A, in May-Hegglin
RT anomaly.";
RL Nat. Genet. 26:106-108(2000).
RN [48]
RP VARIANTS MATINS ASN-373; CYS-702; HIS-702; PRO-1114; ASN-1424; HIS-1424 AND
RP LYS-1841.
RX PubMed=11590545; DOI=10.1086/324267;
RA Heath K.E., Campos-Barros A., Toren A., Rozenfeld-Granot G., Carlsson L.E.,
RA Savige J., Denison J.C., Gregory M.C., White J.G., Barker D.F.,
RA Greinacher A., Epstein C.J., Glucksman M.J., Martignetti J.A.;
RT "Nonmuscle myosin heavy chain IIA mutations define a spectrum of autosomal
RT dominant macrothrombocytopenias: May-Hegglin anomaly and Fechtner,
RT Sebastian, Epstein, and Alport-like syndromes.";
RL Am. J. Hum. Genet. 69:1033-1045(2001).
RN [49]
RP VARIANTS MATINS THR-95; CYS-1165; LEU-1165; 1205-LEU--GLN-1207 DEL;
RP HIS-1424; ASN-1424; TYR-1424 AND LYS-1841, AND VARIANT VAL-1626.
RX PubMed=11776386; DOI=10.1007/s100380170007;
RA Kunishima S., Matsushita T., Kojima T., Amemiya N., Choi Y.M., Hosaka N.,
RA Inoue M., Jung Y., Mamiya S., Matsumoto K., Miyajima Y., Zhang G., Ruan C.,
RA Saito K., Song K.S., Yoon H.-J., Kamiya T., Saito H.;
RT "Identification of six novel MYH9 mutations and genotype-phenotype
RT relationships in autosomal dominant macrothrombocytopenia with leukocyte
RT inclusions.";
RL J. Hum. Genet. 46:722-729(2001).
RN [50]
RP VARIANT MATINS HIS-702.
RX PubMed=11935325; DOI=10.1007/s00439-001-0659-1;
RA Seri M., Savino M., Bordo D., Cusano R., Rocca B., Meloni I., Di Bari F.,
RA Koivisto P.A., Bolognesi M., Ghiggeri G.M., Landolfi R., Balduini C.L.,
RA Zelante L., Ravazzolo R., Renieri A., Savoia A.;
RT "Epstein syndrome: another renal disorder with mutations in the nonmuscle
RT myosin heavy chain 9 gene.";
RL Hum. Genet. 110:182-186(2002).
RN [51]
RP VARIANTS MATINS LEU-96; LEU-1165; TRP-1400; ASN-1424 AND LYS-1841, AND
RP TISSUE SPECIFICITY.
RX PubMed=11752022; DOI=10.1681/asn.v13165;
RA Arrondel C., Vodovar N., Knebelmann B., Gruenfeld J.-P., Gubler M.-C.,
RA Antignac C., Heidet L.;
RT "Expression of the nonmuscle myosin heavy chain IIA in the human kidney and
RT screening for MYH9 mutations in Epstein and Fechtner syndromes.";
RL J. Am. Soc. Nephrol. 13:65-74(2002).
RN [52]
RP CHARACTERIZATION OF VARIANT MATINS ASN-1424.
RX PubMed=12649151; DOI=10.1182/blood-2002-09-2783;
RA Deutsch S., Rideau A., Bochaton-Piallat M.-L., Merla G., Geinoz A.,
RA Gabbiani G., Schwede T., Matthes T., Antonarakis S.E., Beris P.;
RT "Asp1424Asn MYH9 mutation results in an unstable protein responsible for
RT the phenotypes in May-Hegglin anomaly/Fechtner syndrome.";
RL Blood 102:529-534(2003).
RN [53]
RP VARIANTS MATINS CYS-1165; LEU-1165; 1205-LEU--GLN-1207 DEL; HIS-1424;
RP ASN-1424; TYR-1424; VAL-1816 AND LYS-1841.
RX PubMed=12533692; DOI=10.1097/01.lab.0000050960.48774.17;
RA Kunishima S., Matsushita T., Kojima T., Sako M., Kimura F., Jo E.-K.,
RA Inoue C., Kamiya T., Saito H.;
RT "Immunofluorescence analysis of neutrophil nonmuscle myosin heavy chain-A
RT in MYH9 disorders: association of subcellular localization with MYH9
RT mutations.";
RL Lab. Invest. 83:115-122(2003).
RN [54]
RP VARIANTS MATINS CYS-702; HIS-702; GLN-910; 1066-GLU--ALA-1072 DEL;
RP ILE-1155; ASN-1424 AND HIS-1424.
RX PubMed=12792306; DOI=10.1097/01.md.0000076006.64510.5c;
RA Seri M., Pecci A., Di Bari F., Cusano R., Savino M., Panza E., Nigro A.,
RA Noris P., Gangarossa S., Rocca B., Gresele P., Bizzaro N., Malatesta P.,
RA Koivisto P.A., Longo I., Musso R., Pecoraro C., Iolascon A., Magrini U.,
RA Rodriguez Soriano J., Renieri A., Ghiggeri G.M., Ravazzolo R.,
RA Balduini C.L., Savoia A.;
RT "MYH9-related disease: may-Hegglin anomaly, Sebastian syndrome, Fechtner
RT syndrome, and Epstein syndrome are not distinct entities but represent a
RT variable expression of a single illness.";
RL Medicine (Baltimore) 82:203-215(2003).
RN [55]
RP VARIANT MATINS ASN-1424.
RX PubMed=12621333; DOI=10.1097/00129492-200303000-00013;
RA Mhatre A.N., Kim Y., Brodie H.A., Lalwani A.K.;
RT "Macrothrombocytopenia and progressive deafness is due to a mutation in
RT MYH9.";
RL Otol. Neurotol. 24:205-209(2003).
RN [56]
RP VARIANT MATINS LEU-96.
RX PubMed=16969870; DOI=10.1002/ajmg.a.31454;
RA Utsch B., DiFeo A., Kujat A., Karle S., Schuster V., Lenk H., Jacobs U.,
RA Mueller M., Doetsch J., Rascher W., Reutter H., Martignetti J.A.,
RA Ludwig M., Troebs R.-B.;
RT "Bladder exstrophy and Epstein type congenital macrothrombocytopenia:
RT evidence for a common cause?";
RL Am. J. Med. Genet. A 140:2251-2253(2006).
RN [57]
RP VARIANT [LARGE SCALE ANALYSIS] ASN-810.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [58]
RP POSITION OF MUTATIONS IN MYH9-RELATED DISEASE.
RX PubMed=18059020; DOI=10.1002/humu.20661;
RA Pecci A., Panza E., Pujol-Moix N., Klersy C., Di Bari F., Bozzi V.,
RA Gresele P., Lethagen S., Fabris F., Dufour C., Granata A., Doubek M.,
RA Pecoraro C., Koivisto P.A., Heller P.G., Iolascon A., Alvisi P.,
RA Schwabe D., De Candia E., Rocca B., Russo U., Ramenghi U., Noris P.,
RA Seri M., Balduini C.L., Savoia A.;
RT "Position of nonmuscle myosin heavy chain IIA (NMMHC-IIA) mutations
RT predicts the natural history of MYH9-related disease.";
RL Hum. Mutat. 29:409-417(2008).
RN [59]
RP VARIANT DFNA17 LYS-1228.
RX PubMed=30872814; DOI=10.1038/s41431-019-0372-y;
RA Schrauwen I., Melegh B.I., Chakchouk I., Acharya A., Nasir A., Poston A.,
RA Cornejo-Sanchez D.M., Szabo Z., Karosi T., Bene J., Melegh B., Leal S.M.;
RT "Hearing impairment locus heterogeneity and identification of PLS1 as a new
RT autosomal dominant gene in Hungarian Roma.";
RL Eur. J. Hum. Genet. 27:869-878(2019).
CC -!- FUNCTION: Cellular myosin that appears to play a role in cytokinesis,
CC cell shape, and specialized functions such as secretion and capping.
CC Required for cortical actin clearance prior to oocyte exocytosis (By
CC similarity). Promotes cell motility in conjunction with S100A4
CC (PubMed:16707441). During cell spreading, plays an important role in
CC cytoskeleton reorganization, focal contact formation (in the margins
CC but not the central part of spreading cells), and lamellipodial
CC retraction; this function is mechanically antagonized by MYH10
CC (PubMed:20052411). {ECO:0000250|UniProtKB:Q8VDD5,
CC ECO:0000269|PubMed:16707441, ECO:0000269|PubMed:20052411}.
CC -!- SUBUNIT: Myosin is a hexameric protein that consists of 2 heavy chain
CC subunits (MHC), 2 alkali light chain subunits (MLC) and 2 regulatory
CC light chain subunits (MLC-2). Interacts with RASIP1 (By similarity).
CC Interacts with DDR1 (By similarity). Interacts with PDLIM2 (By
CC similarity). Interacts with SVIL (PubMed:12917436, PubMed:17925381).
CC Interacts with HTRA3 (PubMed:22229724). Interacts with Myo7a (By
CC similarity). Interacts with CFAP95 (PubMed:28345668). Interacts with
CC LIMCH1; independently of the integration of MYH9 into the myosin
CC complex (PubMed:28228547). Interacts with RAB3A (PubMed:27325790).
CC Interacts with ZBED4 (PubMed:22693546). Interacts with S100A4; this
CC interaction increases cell motility (PubMed:16707441).
CC {ECO:0000250|UniProtKB:Q62812, ECO:0000250|UniProtKB:Q8VDD5,
CC ECO:0000269|PubMed:12917436, ECO:0000269|PubMed:16707441,
CC ECO:0000269|PubMed:17925381, ECO:0000269|PubMed:22229724,
CC ECO:0000269|PubMed:22693546, ECO:0000269|PubMed:27325790,
CC ECO:0000269|PubMed:28228547, ECO:0000269|PubMed:28345668}.
CC -!- INTERACTION:
CC P35579; P61073: CXCR4; NbExp=5; IntAct=EBI-350338, EBI-489411;
CC P35579; P62993: GRB2; NbExp=3; IntAct=EBI-350338, EBI-401755;
CC P35579; O00255: MEN1; NbExp=3; IntAct=EBI-350338, EBI-592789;
CC P35579; O00255-2: MEN1; NbExp=4; IntAct=EBI-350338, EBI-9869387;
CC P35579; P35579: MYH9; NbExp=8; IntAct=EBI-350338, EBI-350338;
CC P35579; P19338: NCL; NbExp=3; IntAct=EBI-350338, EBI-346967;
CC P35579; P23297: S100A1; NbExp=3; IntAct=EBI-350338, EBI-743686;
CC P35579; P29034: S100A2; NbExp=2; IntAct=EBI-350338, EBI-752230;
CC P35579; P26447: S100A4; NbExp=18; IntAct=EBI-350338, EBI-717058;
CC P35579; P33763: S100A5; NbExp=2; IntAct=EBI-350338, EBI-7211732;
CC P35579; P06703: S100A6; NbExp=2; IntAct=EBI-350338, EBI-352877;
CC P35579; P04271: S100B; NbExp=2; IntAct=EBI-350338, EBI-458391;
CC P35579; P25815: S100P; NbExp=3; IntAct=EBI-350338, EBI-743700;
CC P35579; P0DTC2: S; Xeno; NbExp=7; IntAct=EBI-350338, EBI-25474821;
CC P35579; O46385: SVIL; Xeno; NbExp=2; IntAct=EBI-350338, EBI-6995105;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:22693546}. Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:Q8VDD5}. Cytoplasmic vesicle, secretory vesicle,
CC Cortical granule {ECO:0000250|UniProtKB:Q8VDD5}. Note=Colocalizes with
CC actin filaments at lamellipodia margins and at the leading edge of
CC migrating cells (PubMed:20052411). In retinal pigment epithelial cells,
CC predominantly localized to stress fiber-like structures with some
CC localization to cytoplasmic puncta (PubMed:27331610).
CC {ECO:0000269|PubMed:20052411, ECO:0000269|PubMed:27331610}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P35579-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P35579-2; Sequence=VSP_035409, VSP_035410;
CC -!- TISSUE SPECIFICITY: In the kidney, expressed in the glomeruli. Also
CC expressed in leukocytes. {ECO:0000269|PubMed:11752022,
CC ECO:0000269|PubMed:1912569}.
CC -!- DOMAIN: The rodlike tail sequence is highly repetitive, showing cycles
CC of a 28-residue repeat pattern composed of 4 heptapeptides,
CC characteristic for alpha-helical coiled coils.
CC -!- PTM: ISGylated. {ECO:0000269|PubMed:16139798}.
CC -!- PTM: Ubiquitination. {ECO:0000269|PubMed:27331610}.
CC -!- DISEASE: Macrothrombocytopenia and granulocyte inclusions with or
CC without nephritis or sensorineural hearing loss (MATINS) [MIM:155100]:
CC An autosomal dominant disorder characterized by thrombocytopenia, giant
CC platelets and Dohle body-like inclusions in peripheral blood leukocytes
CC with variable ultrastructural appearance. Some affected individuals
CC lack leukocyte inclusion bodies on classic staining of peripheral blood
CC smears. Alport syndrome-like features of nephritis, hearing loss, and
CC eye abnormalities are present in some patients.
CC {ECO:0000269|PubMed:10973259, ECO:0000269|PubMed:10973260,
CC ECO:0000269|PubMed:11590545, ECO:0000269|PubMed:11752022,
CC ECO:0000269|PubMed:11776386, ECO:0000269|PubMed:11935325,
CC ECO:0000269|PubMed:12533692, ECO:0000269|PubMed:12621333,
CC ECO:0000269|PubMed:12649151, ECO:0000269|PubMed:12792306,
CC ECO:0000269|PubMed:16969870}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Deafness, autosomal dominant, 17 (DFNA17) [MIM:603622]: A form
CC of deafness characterized by progressive high frequency hearing
CC impairment and cochleosaccular degeneration.
CC {ECO:0000269|PubMed:11023810, ECO:0000269|PubMed:30872814}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Note=Subjects with mutations in the motor domain of MYH9
CC present with severe thrombocytopenia and develop nephritis and deafness
CC before the age of 40 years, while those with mutations in the tail
CC domain have a much lower risk of noncongenital complications and
CC significantly higher platelet counts. The clinical course of patients
CC with mutations in the four most frequently affected residues of MYH9
CC (responsible for 70% of MYH9-related cases) were evaluated. Mutations
CC at residue 1933 do not induce kidney damage or cataracts and cause
CC deafness only in the elderly, those in position 702 result in severe
CC thrombocytopenia and produce nephritis and deafness at a juvenile age,
CC while alterations at residue 1424 or 1841 result in intermediate
CC clinical pictures.
CC -!- DISEASE: Note=Genetic variations in MYH9 are associated with non-
CC diabetic end stage renal disease (ESRD).
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD89954.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/MYH9ID481.html";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR456526; CAG30412.1; -; mRNA.
DR EMBL; AB191263; BAD52439.1; -; mRNA.
DR EMBL; AL832639; CAD89954.1; ALT_FRAME; mRNA.
DR EMBL; AB290175; BAG06729.1; -; mRNA.
DR EMBL; Z82215; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW60096.1; -; Genomic_DNA.
DR EMBL; M81105; AAA59888.1; -; mRNA.
DR EMBL; AK291609; BAF84298.1; -; mRNA.
DR EMBL; M69180; AAA61765.1; -; mRNA.
DR EMBL; M31013; AAA36349.1; -; mRNA.
DR CCDS; CCDS13927.1; -. [P35579-1]
DR PIR; A61231; A61231.
DR RefSeq; NP_002464.1; NM_002473.5. [P35579-1]
DR RefSeq; XP_011528499.1; XM_011530197.2.
DR RefSeq; XP_016884292.1; XM_017028803.1.
DR RefSeq; XP_016884293.1; XM_017028804.1.
DR RefSeq; XP_016884294.1; XM_017028805.1.
DR RefSeq; XP_016884295.1; XM_017028806.1.
DR PDB; 2LNK; NMR; -; C=1897-1935.
DR PDB; 3ZWH; X-ray; 1.94 A; Q=1893-1937.
DR PDB; 4CFQ; X-ray; 1.37 A; Q/R=1893-1937.
DR PDB; 4CFR; X-ray; 1.40 A; Q=1893-1937.
DR PDB; 4ETO; X-ray; 1.54 A; P=1908-1923.
DR PDBsum; 2LNK; -.
DR PDBsum; 3ZWH; -.
DR PDBsum; 4CFQ; -.
DR PDBsum; 4CFR; -.
DR PDBsum; 4ETO; -.
DR AlphaFoldDB; P35579; -.
DR BMRB; P35579; -.
DR SMR; P35579; -.
DR BioGRID; 110712; 487.
DR CORUM; P35579; -.
DR DIP; DIP-33103N; -.
DR IntAct; P35579; 338.
DR MINT; P35579; -.
DR STRING; 9606.ENSP00000216181; -.
DR BindingDB; P35579; -.
DR ChEMBL; CHEMBL2189151; -.
DR DrugBank; DB11638; Artenimol.
DR CarbonylDB; P35579; -.
DR GlyGen; P35579; 6 sites, 2 O-linked glycans (6 sites).
DR iPTMnet; P35579; -.
DR MetOSite; P35579; -.
DR PhosphoSitePlus; P35579; -.
DR SwissPalm; P35579; -.
DR BioMuta; MYH9; -.
DR DMDM; 6166599; -.
DR EPD; P35579; -.
DR jPOST; P35579; -.
DR MassIVE; P35579; -.
DR MaxQB; P35579; -.
DR PaxDb; P35579; -.
DR PeptideAtlas; P35579; -.
DR PRIDE; P35579; -.
DR ProteomicsDB; 55093; -. [P35579-1]
DR ProteomicsDB; 55094; -. [P35579-2]
DR TopDownProteomics; P35579-1; -. [P35579-1]
DR ABCD; P35579; 5 sequenced antibodies.
DR Antibodypedia; 887; 494 antibodies from 42 providers.
DR DNASU; 4627; -.
DR Ensembl; ENST00000216181.11; ENSP00000216181.6; ENSG00000100345.23. [P35579-1]
DR GeneID; 4627; -.
DR KEGG; hsa:4627; -.
DR MANE-Select; ENST00000216181.11; ENSP00000216181.6; NM_002473.6; NP_002464.1.
DR UCSC; uc003apg.4; human. [P35579-1]
DR CTD; 4627; -.
DR DisGeNET; 4627; -.
DR GeneCards; MYH9; -.
DR GeneReviews; MYH9; -.
DR HGNC; HGNC:7579; MYH9.
DR HPA; ENSG00000100345; Low tissue specificity.
DR MalaCards; MYH9; -.
DR MIM; 155100; phenotype.
DR MIM; 160775; gene.
DR MIM; 603622; phenotype.
DR neXtProt; NX_P35579; -.
DR OpenTargets; ENSG00000100345; -.
DR Orphanet; 90635; Autosomal dominant non-syndromic sensorineural deafness type DFNA.
DR Orphanet; 182050; MYH9-related disease.
DR Orphanet; 477742; Nodular fasciitis.
DR PharmGKB; PA31377; -.
DR VEuPathDB; HostDB:ENSG00000100345; -.
DR eggNOG; KOG0161; Eukaryota.
DR GeneTree; ENSGT00940000155632; -.
DR HOGENOM; CLU_000192_4_0_1; -.
DR InParanoid; P35579; -.
DR OMA; NAHNEAQ; -.
DR PhylomeDB; P35579; -.
DR TreeFam; TF333601; -.
DR PathwayCommons; P35579; -.
DR Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane.
DR Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-HSA-3928663; EPHA-mediated growth cone collapse.
DR Reactome; R-HSA-416572; Sema4D induced cell migration and growth-cone collapse.
DR Reactome; R-HSA-5625740; RHO GTPases activate PKNs.
DR Reactome; R-HSA-5625900; RHO GTPases activate CIT.
DR Reactome; R-HSA-5627117; RHO GTPases Activate ROCKs.
DR Reactome; R-HSA-5627123; RHO GTPases activate PAKs.
DR Reactome; R-HSA-9662360; Sensory processing of sound by inner hair cells of the cochlea.
DR Reactome; R-HSA-9662361; Sensory processing of sound by outer hair cells of the cochlea.
DR Reactome; R-HSA-9662834; CD163 mediating an anti-inflammatory response.
DR Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis.
DR Reactome; R-HSA-9725370; Signaling by ALK fusions and activated point mutants.
DR SignaLink; P35579; -.
DR SIGNOR; P35579; -.
DR BioGRID-ORCS; 4627; 364 hits in 1099 CRISPR screens.
DR ChiTaRS; MYH9; human.
DR GeneWiki; MYH9; -.
DR GenomeRNAi; 4627; -.
DR Pharos; P35579; Tbio.
DR PRO; PR:P35579; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P35579; protein.
DR Bgee; ENSG00000100345; Expressed in ascending aorta and 186 other tissues.
DR ExpressionAtlas; P35579; baseline and differential.
DR Genevisible; P35579; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
DR GO; GO:0042641; C:actomyosin; IDA:UniProtKB.
DR GO; GO:0005826; C:actomyosin contractile ring; IDA:UniProtKB.
DR GO; GO:0005912; C:adherens junction; IEA:Ensembl.
DR GO; GO:0005903; C:brush border; IEA:Ensembl.
DR GO; GO:0031252; C:cell leading edge; IDA:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; IDA:UniProtKB.
DR GO; GO:0060473; C:cortical granule; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:0001772; C:immunological synapse; IDA:MGI.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0032982; C:myosin filament; IBA:GO_Central.
DR GO; GO:0016460; C:myosin II complex; IDA:UniProtKB.
DR GO; GO:0097513; C:myosin II filament; IDA:UniProtKB.
DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0001726; C:ruffle; IDA:UniProtKB.
DR GO; GO:0005819; C:spindle; IEA:Ensembl.
DR GO; GO:0001725; C:stress fiber; IDA:UniProtKB.
DR GO; GO:0001931; C:uropod; IDA:MGI.
DR GO; GO:0003779; F:actin binding; IDA:MGI.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0043531; F:ADP binding; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IDA:MGI.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0003774; F:cytoskeletal motor activity; NAS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005178; F:integrin binding; IDA:UniProtKB.
DR GO; GO:0000146; F:microfilament motor activity; IDA:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0043495; F:protein-membrane adaptor activity; IMP:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IMP:UniProtKB.
DR GO; GO:0030048; P:actin filament-based movement; IDA:UniProtKB.
DR GO; GO:0031032; P:actomyosin structure organization; IDA:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IDA:UniProtKB.
DR GO; GO:0043534; P:blood vessel endothelial cell migration; IMP:UniProtKB.
DR GO; GO:0060471; P:cortical granule exocytosis; ISS:UniProtKB.
DR GO; GO:0032506; P:cytokinetic process; IMP:UniProtKB.
DR GO; GO:0051295; P:establishment of meiotic spindle localization; IEA:Ensembl.
DR GO; GO:0001768; P:establishment of T cell polarity; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; NAS:UniProtKB.
DR GO; GO:0050900; P:leukocyte migration; NAS:UniProtKB.
DR GO; GO:0032418; P:lysosome localization; IMP:UniProtKB.
DR GO; GO:0000212; P:meiotic spindle organization; IEA:Ensembl.
DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; IDA:UniProtKB.
DR GO; GO:0030224; P:monocyte differentiation; IEP:UniProtKB.
DR GO; GO:0007520; P:myoblast fusion; IEA:Ensembl.
DR GO; GO:1903919; P:negative regulation of actin filament severing; IMP:UniProtKB.
DR GO; GO:0006911; P:phagocytosis, engulfment; ISS:UniProtKB.
DR GO; GO:0001778; P:plasma membrane repair; IDA:UniProtKB.
DR GO; GO:0070527; P:platelet aggregation; HMP:UniProtKB.
DR GO; GO:0030220; P:platelet formation; IMP:UniProtKB.
DR GO; GO:1903923; P:positive regulation of protein processing in phagocytic vesicle; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IMP:UniProtKB.
DR GO; GO:0045055; P:regulated exocytosis; IMP:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
DR GO; GO:1905684; P:regulation of plasma membrane repair; IMP:UniProtKB.
DR GO; GO:0032796; P:uropod organization; IEA:Ensembl.
DR Gene3D; 2.30.30.360; -; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR004009; Myosin_N.
DR InterPro; IPR008989; Myosin_S1_N.
DR InterPro; IPR002928; Myosin_tail.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036305; RGS_sf.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF02736; Myosin_N; 1.
DR Pfam; PF01576; Myosin_tail_1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 1.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF48097; SSF48097; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Alport syndrome;
KW Alternative splicing; ATP-binding; Calmodulin-binding; Cataract;
KW Cell adhesion; Cell shape; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW Cytoskeleton; Deafness; Direct protein sequencing; Disease variant;
KW Methylation; Motor protein; Myosin; Non-syndromic deafness;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.10"
FT CHAIN 2..1960
FT /note="Myosin-9"
FT /id="PRO_0000123416"
FT DOMAIN 27..77
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 81..776
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 779..808
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 2..838
FT /note="Mediates interaction with LIMCH1"
FT /evidence="ECO:0000269|PubMed:28228547"
FT REGION 654..676
FT /note="Actin-binding"
FT REGION 1035..1057
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1118..1137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1877..1960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 837..1926
FT /evidence="ECO:0000255"
FT COMPBIAS 1877..1908
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1915..1930
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1937..1960
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 174..181
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.10"
FT MOD_RES 8
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 11
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 102
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 299
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 435
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P35580"
FT MOD_RES 613
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDD5"
FT MOD_RES 628
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 754
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 850
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDD5"
FT MOD_RES 860
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDD5"
FT MOD_RES 975
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDD5"
FT MOD_RES 1024
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1114
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDD5"
FT MOD_RES 1234
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q61879"
FT MOD_RES 1249
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDD5"
FT MOD_RES 1357
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1392
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1404
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1410
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1459
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1638
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1669
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDD5"
FT MOD_RES 1714
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1793
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDD5"
FT MOD_RES 1802
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDD5"
FT MOD_RES 1845
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDD5"
FT MOD_RES 1923
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q61879"
FT MOD_RES 1943
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:17487921,
FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..136
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_035409"
FT VAR_SEQ 980..1421
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_035410"
FT VARIANT 93
FT /note="N -> K (in MATINS; dbSNP:rs121913655)"
FT /evidence="ECO:0000269|PubMed:10973259"
FT /id="VAR_010791"
FT VARIANT 95
FT /note="A -> T (in MATINS; dbSNP:rs1603484047)"
FT /evidence="ECO:0000269|PubMed:11776386"
FT /id="VAR_018308"
FT VARIANT 96
FT /note="S -> L (in MATINS; dbSNP:rs121913657)"
FT /evidence="ECO:0000269|PubMed:11752022,
FT ECO:0000269|PubMed:16969870"
FT /id="VAR_018309"
FT VARIANT 373
FT /note="K -> N (in MATINS; dbSNP:rs1603483388)"
FT /evidence="ECO:0000269|PubMed:11590545"
FT /id="VAR_018310"
FT VARIANT 702
FT /note="R -> C (in MATINS; dbSNP:rs80338826)"
FT /evidence="ECO:0000269|PubMed:10973259,
FT ECO:0000269|PubMed:11590545, ECO:0000269|PubMed:12792306"
FT /id="VAR_010792"
FT VARIANT 702
FT /note="R -> H (in MATINS; dbSNP:rs80338827)"
FT /evidence="ECO:0000269|PubMed:11590545,
FT ECO:0000269|PubMed:11935325, ECO:0000269|PubMed:12792306"
FT /id="VAR_018311"
FT VARIANT 705
FT /note="R -> H (in DFNA17; dbSNP:rs80338828)"
FT /evidence="ECO:0000269|PubMed:11023810"
FT /id="VAR_010793"
FT VARIANT 810
FT /note="K -> N (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036006"
FT VARIANT 910
FT /note="K -> Q (in MATINS; dbSNP:rs554332083)"
FT /evidence="ECO:0000269|PubMed:12792306"
FT /id="VAR_044226"
FT VARIANT 967
FT /note="V -> E (in dbSNP:rs16996652)"
FT /id="VAR_044227"
FT VARIANT 1066..1072
FT /note="Missing (in MATINS)"
FT /evidence="ECO:0000269|PubMed:12792306"
FT /id="VAR_044228"
FT VARIANT 1114
FT /note="S -> P (in MATINS; dbSNP:rs200901330)"
FT /evidence="ECO:0000269|PubMed:11590545"
FT /id="VAR_018312"
FT VARIANT 1155
FT /note="T -> I (in MATINS; dbSNP:rs121913656)"
FT /evidence="ECO:0000269|PubMed:10973260,
FT ECO:0000269|PubMed:12792306"
FT /id="VAR_010794"
FT VARIANT 1165
FT /note="R -> C (in MATINS; dbSNP:rs80338829)"
FT /evidence="ECO:0000269|PubMed:10973259,
FT ECO:0000269|PubMed:11776386, ECO:0000269|PubMed:12533692"
FT /id="VAR_010795"
FT VARIANT 1165
FT /note="R -> L (in MATINS; dbSNP:rs80338830)"
FT /evidence="ECO:0000269|PubMed:11752022,
FT ECO:0000269|PubMed:11776386, ECO:0000269|PubMed:12533692"
FT /id="VAR_018313"
FT VARIANT 1205..1207
FT /note="Missing (in MATINS)"
FT /evidence="ECO:0000269|PubMed:11776386,
FT ECO:0000269|PubMed:12533692"
FT /id="VAR_018314"
FT VARIANT 1228
FT /note="E -> K (in DFNA17; unknown pathological
FT significance; dbSNP:rs746956415)"
FT /evidence="ECO:0000269|PubMed:30872814"
FT /id="VAR_083825"
FT VARIANT 1400
FT /note="R -> W (in MATINS; likely benign variant;
FT dbSNP:rs76368635)"
FT /evidence="ECO:0000269|PubMed:11752022"
FT /id="VAR_018315"
FT VARIANT 1424
FT /note="D -> H (in MATINS; dbSNP:rs80338831)"
FT /evidence="ECO:0000269|PubMed:10973259,
FT ECO:0000269|PubMed:11590545, ECO:0000269|PubMed:11776386,
FT ECO:0000269|PubMed:12533692, ECO:0000269|PubMed:12792306"
FT /id="VAR_010796"
FT VARIANT 1424
FT /note="D -> N (in MATINS; results in reduced protein
FT levels; dbSNP:rs80338831)"
FT /evidence="ECO:0000269|PubMed:11590545,
FT ECO:0000269|PubMed:11752022, ECO:0000269|PubMed:11776386,
FT ECO:0000269|PubMed:12533692, ECO:0000269|PubMed:12621333,
FT ECO:0000269|PubMed:12649151, ECO:0000269|PubMed:12792306"
FT /id="VAR_018316"
FT VARIANT 1424
FT /note="D -> Y (in MATINS; dbSNP:rs80338831)"
FT /evidence="ECO:0000269|PubMed:11776386,
FT ECO:0000269|PubMed:12533692"
FT /id="VAR_018317"
FT VARIANT 1626
FT /note="I -> V (in dbSNP:rs2269529)"
FT /evidence="ECO:0000269|PubMed:11776386"
FT /id="VAR_018318"
FT VARIANT 1816
FT /note="I -> V (in MATINS; dbSNP:rs762773112)"
FT /evidence="ECO:0000269|PubMed:12533692"
FT /id="VAR_030385"
FT VARIANT 1841
FT /note="E -> K (in MATINS; dbSNP:rs80338834)"
FT /evidence="ECO:0000269|PubMed:10973259,
FT ECO:0000269|PubMed:10973260, ECO:0000269|PubMed:11590545,
FT ECO:0000269|PubMed:11752022, ECO:0000269|PubMed:11776386,
FT ECO:0000269|PubMed:12533692"
FT /id="VAR_010797"
FT CONFLICT 53..55
FT /note="EAI -> RGH (in Ref. 9)"
FT /evidence="ECO:0000305"
FT CONFLICT 660
FT /note="T -> S (in Ref. 9)"
FT /evidence="ECO:0000305"
FT CONFLICT 869
FT /note="T -> M (in Ref. 11; AAA36349)"
FT /evidence="ECO:0000305"
FT CONFLICT 931
FT /note="C -> Y (in Ref. 11; AAA36349)"
FT /evidence="ECO:0000305"
FT CONFLICT 1000
FT /note="R -> I (in Ref. 8; BAF84298)"
FT /evidence="ECO:0000305"
FT CONFLICT 1240..1241
FT /note="KG -> GR (in Ref. 11; AAA36349)"
FT /evidence="ECO:0000305"
FT CONFLICT 1350
FT /note="E -> EE (in Ref. 11)"
FT /evidence="ECO:0000305"
FT CONFLICT 1462
FT /note="E -> G (in Ref. 1; CAD89954)"
FT /evidence="ECO:0000305"
FT CONFLICT 1546
FT /note="D -> G (in Ref. 1; CAD89954)"
FT /evidence="ECO:0000305"
FT CONFLICT 1764
FT /note="T -> A (in Ref. 11; AAA36349)"
FT /evidence="ECO:0000305"
FT CONFLICT 1771
FT /note="S -> G (in Ref. 11; AAA36349)"
FT /evidence="ECO:0000305"
FT STRAND 1895..1897
FT /evidence="ECO:0007829|PDB:4CFR"
FT HELIX 1899..1903
FT /evidence="ECO:0007829|PDB:4CFR"
FT HELIX 1904..1921
FT /evidence="ECO:0007829|PDB:4CFQ"
FT STRAND 1922..1925
FT /evidence="ECO:0007829|PDB:2LNK"
SQ 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
