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

Gene name

Name:

MYH9

From

Homo sapiens (Human)

[TaxID: 9606]

Taxonomy

Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Protein existence

1: Evidence at protein level;

References

[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). TISSUE=Spinal cord; The German cDNA consortium; Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). DOI=10.1186/gb-2004-5-10-r84; PubMed=15461802 [NCBI, ExPASy, EBI, Israel, Japan] 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:RESEARCH84.1-RESEARCH84.11(2004).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1038/990031; PubMed=10591208 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[4]	NUCLEOTIDE SEQUENCE [MRNA] OF 1-1337, AND TISSUE SPECIFICITY. PubMed=1912569 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[5]	NUCLEOTIDE SEQUENCE [MRNA] OF 1-715. PubMed=1860190 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[6]	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 MASS SPECTROMETRY. TISSUE=Platelet; Bienvenut W.V., Claeys R.; Submitted (AUG-2005) to UniProtKB.
[7]	NUCLEOTIDE SEQUENCE [MRNA] OF 714-1960. PubMed=1967836 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[8]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, AND MASS SPECTROMETRY. DOI=10.1021/pr050048h; PubMed=16083285 [NCBI, ExPASy, EBI, Israel, Japan] Kim J.-E., Tannenbaum S.R., White F.M.; "Global phosphoproteome of HT-29 human colon adenocarcinoma cells."; J. Proteome Res. 4:1339-1346(2005).
[9]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, AND MASS SPECTROMETRY. TISSUE=T-cell; DOI=10.1038/nmeth776; PubMed=16094384 [NCBI, ExPASy, EBI, Israel, Japan] Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J., Bodenmiller B., Watts J.D., Hood L., Aebersold R.; "Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry."; Nat. Methods 2:591-598(2005).
[10]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[11]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[12]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-754 AND TYR-1408, AND MASS SPECTROMETRY. DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan] Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; "Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."; Cell 131:1190-1203(2007).
[13]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, AND MASS SPECTROMETRY. DOI=10.1002/elps.200600782; PubMed=17487921 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[14]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, AND MASS SPECTROMETRY. DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan] Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; "Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
[15]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1714 AND SER-1943, AND MASS SPECTROMETRY. TISSUE=Platelet; DOI=10.1021/pr0704130; PubMed=18088087 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[16]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, AND MASS SPECTROMETRY. DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[17]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, AND MASS SPECTROMETRY. TISSUE=Liver; DOI=10.1002/pmic.200700884; PubMed=18318008 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[18]	VARIANT DFNA17 HIS-705. PubMed=11023810 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[19]	VARIANTS MHA/FTNS/SBS LYS-93; CYS-702; CYS-1165; HIS-1424 AND LYS-1841. DOI=10.1038/79063; PubMed=10973259 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[20]	VARIANTS MHA ILE-1155 AND LYS-1841. DOI=10.1038/79069; PubMed=10973260 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[21]	VARIANTS MHA/SBS/FTNS/EPS/APSM ASN-373; CYS-702; HIS-702; PRO-1114; ASN-1424; HIS-1424 AND LYS-1841. DOI=10.1086/324267; PubMed=11590545 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[22]	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. DOI=10.1007/s100380170007; PubMed=11776386 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[23]	VARIANT EPS HIS-702. DOI=10.1007/s00439-001-0659-1; PubMed=11935325 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[24]	VARIANTS FTNS/EPS LEU-96; LEU-1165; ASN-1424 AND LYS-1841, VARIANT TRP-1400, AND TISSUE SPECIFICITY. PubMed=11752022 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[25]	CHARACTERIZATION OF VARIANT ASN-1424. DOI=10.1182/blood-2002-09-2783; PubMed=12649151 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[26]	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 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[27]	VARIANT EPS HIS-702, VARIANTS FTNS GLN-910; ILE-1155 AND HIS-1424, VARIANTS MHA/SBS 1066-GLU--ALA-1072 DEL AND ASN-1424, AND VARIANT EPS/FTNS/MHA/SBS CYS-702. DOI=10.1097/00005792-200305000-00006; PubMed=12792306 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[28]	VARIANT MPSD ASN-1424. DOI=10.1097/00129492-200303000-00013; PubMed=12621333 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[29]	VARIANT EPS LEU-96. DOI=10.1002/ajmg.a.31454; PubMed=16969870 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[30]	VARIANT [LARGE SCALE ANALYSIS] ASN-810. DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[31]	POSITION OF MUTATIONS IN MYH9-RELATED DISEASE. DOI=10.1002/humu.20661; PubMed=18059020 [NCBI, ExPASy, EBI, Israel, Japan] 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).

Comments

FUNCTION: Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping.
SUBUNIT: Interacts with PDLIM2 (By similarity). 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).
INTERACTION:
P51681:CCR5; NbExp=1; IntAct=EBI-350338, EBI-489374;
P61073:CXCR4; NbExp=4; IntAct=EBI-350338, EBI-489411;
P11171:EPB41; NbExp=1; IntAct=EBI-350338, EBI-1050906;
O00255:MEN1; NbExp=5; IntAct=EBI-350338, EBI-592789;
P19338:NCL; NbExp=2; IntAct=EBI-350338, EBI-352553;
P25815:S100P; NbExp=1; IntAct=EBI-350338, EBI-743700;
ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name 1

Isoform ID P35579-1

This is the isoform sequence displayed in this entry.

Name 2

Isoform ID P35579-2

Features which should be applied to build the isoform sequence: VSP_035409, VSP_035410.
TISSUE SPECIFICITY: In the kidney, expressed in the glomeruli. Also expressed in leukocytes.
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.
DISEASE: Defects in MYH9 are the cause of May-Hegglin anomaly (MHA) [MIM:155100]. MHA is an autosomal dominant macrothrombocytopenia characterized by thrombocytopenia, giant platelets and leukokyte inclusions appearing as highly parallel paracrystalline bodies.
DISEASE: Defects in MYH9 are the cause of Sebastian syndrome (SBS) [MIM:605249]. SBS is an autosomal dominant macrothrombocytopenia characterized by thrombocytopenia, giant platelets and leukocyte inclusions that are smaller and less organized than in May-Hegglin anomaly.
DISEASE: Defects in MYH9 are the cause of Fechtner syndrome (FTNS) [MIM:153640]. FTNS is an 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.
DISEASE: Defects in MYH9 are the cause of Alport syndrome with macrothrombocytopenia (APSM) [MIM:153650]. APSM is an autosomal dominant disorder characterized by the association of ocular lesions, sensorineural hearing loss and nephritis (Alport syndrome) with platelet defects.
DISEASE: Defects in MYH9 are the cause of Epstein syndrome (EPS) [MIM:153650]. EPS is an autosomal dominant disorder characterized by the association of macrothrombocytopathy, sensorineural hearing loss and nephritis.
DISEASE: Defects in MYH9 are the cause of non-syndromic sensorineural deafness autosomal dominant type 17 (DFNA17) [MIM:603622]. DFNA17 is a form of sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. DFNA17 is characterized by progressive hearing impairment and cochleosaccular degeneration.
DISEASE: Defects in MYH9 are the cause of macrothrombocytopenia with progressive sensorineural deafness (MPSD) [MIM:600208]. MPSD is an autosomal dominant disorder characterized by the association of macrothrombocytopathy and progressive sensorineural hearing loss without renal dysfunction.
DISEASE: 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.
SIMILARITY: Contains 1 IQ domain.
SIMILARITY: Contains 1 myosin head-like domain.
SEQUENCE CAUTION:
- Sequence=CAD89954.1; Type=Frameshift; Positions=1890;
WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/MYH9ID481.html";.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=MYH9";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AL832639; CAD89954.1; ALT_FRAME; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CR456526; CAG30412.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z82215; CAB05105.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M81105; AAA59888.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M69180; AAA61765.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M31013; AAA36349.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A61231; A61231.

NP_002464.1; -.

3D structure databases

HSSP

P10587; 1BR2. [HSSP ENTRY / PDB]

ModBase

P35579.

Protein-protein interaction databases

IntAct

P35579; -.

PTM databases

PhosphoSite

P35579; -.

Organism-specific databases

HIX0016424; -.

HGNC:7579; MYH9.

CAB015386; -.
HPA001644; -.

MIM

153640; phenotype. [NCBI / EBI]
153650; phenotype. [NCBI / EBI]
155100; phenotype. [NCBI / EBI]
160775; gene. [NCBI / EBI]
600208; phenotype. [NCBI / EBI]
603622; phenotype. [NCBI / EBI]
605249; phenotype. [NCBI / EBI]

Orphanet

1019; Epstein syndrome.
1984; Fechtner syndrome.
850; May-Hegglin thrombocytopenia.
807; Sebastian syndrome.

PharmGKB

PA31377; -.

GeneCards

P35579.

Gene expression databases

ArrayExpress

P35579; -.

CleanEx

HS_MYH9; -.

GermOnline

ENSG00000100345; Homo sapiens.

Ontologies

GO:0032154;	Cellular component: cleavage furrow (inferred from direct assay from UniProtKB).
GO:0005826;	Cellular component: contractile ring (inferred from direct assay from UniProtKB).
GO:0005829;	Cellular component: cytosol (inferred from direct assay from UniProtKB).
GO:0001772;	Cellular component: immunological synapse (inferred from direct assay from MGI).
GO:0016459;	Cellular component: myosin complex (inferred from electronic annotation from InterPro).
GO:0005634;	Cellular component: nucleus (inferred from direct assay from UniProtKB).
GO:0001726;	Cellular component: ruffle (inferred from direct assay from UniProtKB).
GO:0001725;	Cellular component: stress fiber (inferred from direct assay from UniProtKB).
GO:0001931;	Cellular component: uropod (inferred from direct assay from MGI).
GO:0051015;	Molecular function: actin filament binding (inferred from direct assay from UniProtKB).
GO:0030898;	Molecular function: actin-dependent ATPase activity (inferred from direct assay from MGI).
GO:0043531;	Molecular function: ADP binding (inferred from direct assay from MGI).
GO:0005524;	Molecular function: ATP binding (inferred from direct assay from MGI).
GO:0005516;	Molecular function: calmodulin binding (inferred from electronic annotation from UniProtKB-KW).
GO:0000146;	Molecular function: microfilament motor activity (inferred from direct assay from UniProtKB).
GO:0043495;	Molecular function: protein anchor (inferred from mutant phenotype from UniProtKB).
GO:0042803;	Molecular function: protein homodimerization activity (inferred from direct assay from UniProtKB).
GO:0031532;	Biological process: actin cytoskeleton reorganization (inferred from mutant phenotype from UniProtKB).
GO:0030048;	Biological process: actin filament-based movement (inferred from direct assay from UniProtKB).
GO:0001525;	Biological process: angiogenesis (inferred from direct assay from UniProtKB).
GO:0043534;	Biological process: blood vessel endothelial cell migration (inferred from mutant phenotype from UniProtKB).
GO:0000910;	Biological process: cytokinesis (inferred from mutant phenotype from UniProtKB).
GO:0007229;	Biological process: integrin-mediated signaling pathway (non-traceable author statement from UniProtKB).
GO:0050900;	Biological process: leukocyte migration (non-traceable author statement from UniProtKB).
GO:0006509;	Biological process: membrane protein ectodomain proteolysis (inferred from direct assay from UniProtKB).
GO:0030224;	Biological process: monocyte differentiation (inferred from expression pattern from UniProtKB).
GO:0030220;	Biological process: platelet formation (inferred from mutant phenotype from UniProtKB).
GO:0015031;	Biological process: protein transport (inferred from mutant phenotype from UniProtKB).
GO:0008360;	Biological process: regulation of cell shape (inferred from mutant phenotype from UniProtKB).
GO:0007605;	Biological process: sensory perception of sound (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000048; IQ_CaM_bd_region.
IPR001609; Myosin_head.
IPR004009; Myosin_N.
IPR002928; Myosin_tail.
Graphical view of domain structure.

Pfam

PF00612; IQ; 1.
PF00063; Myosin_head; 1.
PF02736; Myosin_N; 1.
PF01576; Myosin_tail_1; 1.
Pfam graphical view of domain structure.

PRINTS

PR00193; MYOSINHEAVY.

ProDom

PD000355; Myosin_head; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00015; IQ; 1.
SM00242; MYSc; 1.
SMART graphical view of domain structure.

PROSITE

PS50096; IQ; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P35579.

Proteomic databases

PeptideAtlas

P35579; -.

Genome annotation databases

Ensembl

ENSG00000100345; Homo sapiens. [Contig view]

GeneID

4627; -.

KEGG

hsa:4627; -.

Phylogenomic databases

HOGENOM

P35579; -.

HOVERGEN

P35579; -.

Other

P35579; -.

17810; -.

MYH9; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acetylation; Actin-binding; Alport syndrome; Alternative splicing; ATP-binding; Calmodulin-binding; Cataract; Cell shape; Coiled coil; Deafness; Direct protein sequencing; Disease mutation; Motor protein; Myosin; Non-syndromic deafness; Nucleotide-binding; Phosphoprotein; Polymorphism.

Features

Feature table viewer

Feature aligner

Key From To Length Description FTId