ID MYH11_HUMAN Reviewed; 1972 AA. AC P35749; D2JYH7; O00396; O94944; P78422; Q3MIV8; Q3MNF0; Q3MNF1; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 27-APR-2001, sequence version 3. DT 04-NOV-2026, entry version 238. DE RecName: Full=Myosin-11; DE AltName: Full=Myosin heavy chain 11; DE AltName: Full=Myosin heavy chain, smooth muscle isoform; DE AltName: Full=SMMHC; GN Name=MYH11; Synonyms=KIAA0866; 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 [MRNA] (ISOFORMS 2 AND 3), AND TISSUE SPECIFICITY. RX PubMed=16000639; DOI=10.1152/ajpcell.00244.2004; RA Leguillette R., Gil F.R., Zitouni N., Lajoie-Kadoch S., Sobieszek A., RA Lauzon A.M.; RT "(+)Insert smooth muscle myosin heavy chain (SM-B) isoform expression in RT human tissues."; RL Am. J. Physiol. 289:C1277-C1285(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10493829; DOI=10.1006/geno.1999.5927; RA Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J., RA Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X., RA Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C., RA Adams M.D.; RT "Genome duplications and other features in 12 Mb of DNA sequence from human RT chromosome 16p and 16q."; RL Genomics 60:295-308(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=10048485; DOI=10.1093/dnares/5.6.355; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., RA Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XII. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 5:355-364(1998). RN [4] RP SEQUENCE REVISION. RA Nagase T., Kikuno R., Yamakawa H., Ohara O.; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NHLBI resequencing and genotyping service (RS&G); RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [7] 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 [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4). RC TISSUE=Colon; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 885-1972 (ISOFORM 1/2). RX PubMed=7684189; DOI=10.1002/ajmg.1320460110; RA Matsuoka R., Yoshida M.C., Furutani Y., Imamura S., Kanda N., RA Yanagisawa M., Masaki T., Takao A.; RT "Human smooth muscle myosin heavy chain gene mapped to chromosomal region RT 16q12."; RL Am. J. Med. Genet. 46:61-67(1993). RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1093-1972 (ISOFORM 1/2). RC TISSUE=Hippocampus; RA Okajima K.; RL Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases. RN [11] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC TISSUE=Melanoma; RX PubMed=17081065; DOI=10.1021/pr060363j; RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., RA Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.; RT "Proteomic and bioinformatic characterization of the biogenesis and RT function of melanosomes."; RL J. Proteome Res. 5:3135-3144(2006). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1954, 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 [13] 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-23; SER-1954 AND RP THR-1958, AND 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 [15] RP VARIANTS AAT4 1241-ARG--LEU-1264 DEL AND GLN-1758. RX PubMed=16444274; DOI=10.1038/ng1721; RA Zhu L., Vranckx R., Khau Van Kien P., Lalande A., Boisset N., Mathieu F., RA Wegman M., Glancy L., Gasc J.-M., Brunotte F., Bruneval P., Wolf J.-E., RA Michel J.-B., Jeunemaitre X.; RT "Mutations in myosin heavy chain 11 cause a syndrome associating thoracic RT aortic aneurysm/aortic dissection and patent ductus arteriosus."; RL Nat. Genet. 38:343-349(2006). RN [16] RP VARIANT MMIHS2 1200-LYS--GLU-1972 DEL, AND INVOLVEMENT IN MMIHS2. RX PubMed=25407000; DOI=10.1038/ejhg.2014.256; RA Gauthier J., Ouled Amar Bencheikh B., Hamdan F.F., Harrison S.M., RA Baker L.A., Couture F., Thiffault I., Ouazzani R., Samuels M.E., RA Mitchell G.A., Rouleau G.A., Michaud J.L., Soucy J.F.; RT "A homozygous loss-of-function variant in MYH11 in a case with megacystis- RT microcolon-intestinal hypoperistalsis syndrome."; RL Eur. J. Hum. Genet. 23:1266-1268(2015). RN [17] RP INVOLVEMENT IN MMIHS2. RX PubMed=29575632; DOI=10.1002/ajmg.a.38647; RA Yetman A.T., Starr L.J.; RT "Newly described recessive MYH11 disorder with clinical overlap of RT multisystemic smooth muscle dysfunction and megacystis microcolon RT hypoperistalsis syndromes."; RL Am. J. Med. Genet. A 176:1011-1014(2018). RN [18] RP INVOLVEMENT IN VSCM2. RX PubMed=31389005; DOI=10.1111/cge.13617; RA Dong W., Baldwin C., Choi J., Milunsky J.M., Zhang J., Bilguvar K., RA Lifton R.P., Milunsky A.; RT "Identification of a dominant MYH11 causal variant in chronic intestinal RT pseudo-obstruction: Results of whole-exome sequencing."; RL Clin. Genet. 96:473-477(2019). RN [19] RP VARIANT GLY-616. RX PubMed=29781137; DOI=10.1111/nmo.13371; RA Ravenscroft G., Pannell S., O'Grady G., Ong R., Ee H.C., Faiz F., Marns L., RA Goel H., Kumarasinghe P., Sollis E., Sivadorai P., Wilson M., Magoffin A., RA Nightingale S., Freckmann M.L., Kirk E.P., Sachdev R., Lemberg D.A., RA Delatycki M.B., Kamm M.A., Basnayake C., Lamont P.J., Amor D.J., Jones K., RA Schilperoort J., Davis M.R., Laing N.G.; RT "Variants in ACTG2 underlie a substantial number of Australasian patients RT with primary chronic intestinal pseudo-obstruction."; RL Neurogastroenterol. Motil. 30:e13371-e13371(2018). RN [20] RP VARIANT MMIHS2 HIS-677, AND INVOLVEMENT IN MMIHS2. RX PubMed=31427716; DOI=10.1038/s10038-019-0651-z; RA Wang Q., Zhang J., Wang H., Feng Q., Luo F., Xie J.; RT "Compound heterozygous variants in MYH11 underlie autosomal recessive RT megacystis-microcolon-intestinal hypoperistalsis syndrome in a Chinese RT family."; RL J. Hum. Genet. 64:1067-1073(2019). RN [21] RP VARIANT VSCM2 VAL-1555, AND INVOLVEMENT IN VSCM2. RX PubMed=31944481; DOI=10.1002/humu.23986; RA Gilbert M.A., Schultz-Rogers L., Rajagopalan R., Grochowski C.M., RA Wilkins B.J., Biswas S., Conlin L.K., Fiorino K.N., Dhamija R., Pack M.A., RA Klee E.W., Piccoli D.A., Spinner N.B.; RT "Protein-elongating mutations in MYH11 are implicated in a dominantly RT inherited smooth muscle dysmotility syndrome with severe esophageal, RT gastric, and intestinal disease."; RL Hum. Mutat. 41:973-982(2020). CC -!- FUNCTION: Muscle contraction. CC -!- SUBUNIT: Muscle myosin is a hexameric protein that consists of 2 heavy CC chain subunits (MHC), 2 alkali light chain subunits (MLC) and 2 CC regulatory light chain subunits (MLC-2). CC -!- INTERACTION: CC P35749; O14950: MYL12B; NbExp=3; IntAct=EBI-1052928, EBI-1642165; CC -!- SUBCELLULAR LOCATION: Melanosome {ECO:0000269|PubMed:17081065}. CC Note=Identified by mass spectrometry in melanosome fractions from stage CC I to stage IV. Thick filaments of the myofibrils. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=SM-A; CC IsoId=P35749-1; Sequence=Displayed; CC Name=2; Synonyms=SM-B1; CC IsoId=P35749-2; Sequence=VSP_043017; CC Name=3; Synonyms=SM-B2; CC IsoId=P35749-3; Sequence=VSP_043017, VSP_043018; CC Name=4; CC IsoId=P35749-4; Sequence=VSP_043018; CC -!- TISSUE SPECIFICITY: Smooth muscle; expressed in the umbilical artery, CC bladder, esophagus and trachea. Isoform 1 is mostly found in slowly CC contracting tonic muscles. {ECO:0000269|PubMed:16000639}. 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 -!- DOMAIN: Limited proteolysis of myosin heavy chain produces 1 light CC meromyosin (LMM) and 1 heavy meromyosin (HMM). HMM can be further CC cleaved into 2 globular subfragments (S1) and 1 rod-shaped subfragment CC (S2). {ECO:0000305}. CC -!- DISEASE: Note=A chromosomal aberration involving MYH11 is found in CC acute myeloid leukemia of M4EO subtype. Pericentric inversion CC inv(16)(p13;q22). The inversion produces a fusion protein consisting of CC the 165 N-terminal residues of CBF-beta (PEPB2) and the tail region of CC MYH11. CC -!- DISEASE: Aortic aneurysm, familial thoracic 4 (AAT4) [MIM:132900]: A CC disease characterized by permanent dilation of the thoracic aorta CC usually due to degenerative changes in the aortic wall. It is primarily CC associated with a characteristic histologic appearance known as 'medial CC necrosis' or 'Erdheim cystic medial necrosis' in which there is CC degeneration and fragmentation of elastic fibers, loss of smooth muscle CC cells, and an accumulation of basophilic ground substance. CC {ECO:0000269|PubMed:16444274}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Megacystis-microcolon-intestinal hypoperistalsis syndrome 2 CC (MMIHS2) [MIM:619351]: A form of megacystis-microcolon-intestinal CC hypoperistalsis syndrome, a congenital visceral myopathy primarily CC affecting females, and characterized by loss of smooth muscle CC contraction in the bladder and intestine. Affected individuals present CC at birth with functional obstruction of intestine, microcolon, dilation CC of bladder, and secondary hydronephrosis. The majority of cases have a CC fatal outcome due to malnutrition and sepsis, followed by multiorgan CC failure. MMIHS2 inheritance is autosomal recessive. CC {ECO:0000269|PubMed:25407000, ECO:0000269|PubMed:29575632, CC ECO:0000269|PubMed:31427716}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Visceral myopathy 2 (VSCM2) [MIM:619350]: A form of visceral CC myopathy, a gastrointestinal pseudo-obstruction disorder characterized CC by impaired function of enteric smooth muscle cells, intestinal CC dysmotility and paresis, severe abdominal pain, and malnutrition. The CC disease shows inter- and intrafamilial variability. VSCM2 inheritance CC is autosomal dominant. {ECO:0000269|PubMed:31389005, CC ECO:0000269|PubMed:31944481}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- MISCELLANEOUS: [Isoform 2]: This isoform with a 7 AA insert in the head CC domain is predominantly expressed in rapidly contracting phasic CC muscles. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 3]: This isoform with a 7 AA insert in the head CC domain is predominantly expressed in rapidly contracting phasic CC muscles. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase CC superfamily. Myosin family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA74889.2; Type=Erroneous initiation; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/43/MYH11"; 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; AY520816; AAS98910.1; -; mRNA. DR EMBL; AY520817; AAS98911.1; -; mRNA. DR EMBL; AF001548; AAC31665.1; -; Genomic_DNA. DR EMBL; U91323; AAC35212.1; -; Genomic_DNA. DR EMBL; AB020673; BAA74889.2; ALT_INIT; mRNA. DR EMBL; GU143399; ACZ58373.1; -; Genomic_DNA. DR EMBL; GU143400; ACZ58374.1; -; Genomic_DNA. DR EMBL; AC024120; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC026401; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC130651; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471226; EAW53924.1; -; Genomic_DNA. DR EMBL; CH471226; EAW53926.1; -; Genomic_DNA. DR EMBL; BC101677; AAI01678.1; -; mRNA. DR EMBL; BC104906; AAI04907.1; -; mRNA. DR EMBL; BC143364; AAI43365.1; -; mRNA. DR EMBL; D10667; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; X69292; CAA49154.1; -; mRNA. DR CCDS; CCDS10565.1; -. [P35749-1] DR CCDS; CCDS10566.1; -. [P35749-4] DR CCDS; CCDS45423.1; -. [P35749-2] DR CCDS; CCDS45424.1; -. [P35749-3] DR RefSeq; NP_001035202.1; NM_001040113.2. [P35749-3] DR RefSeq; NP_001035203.1; NM_001040114.2. [P35749-2] DR RefSeq; NP_002465.1; NM_002474.3. [P35749-1] DR RefSeq; NP_074035.1; NM_022844.3. [P35749-4] DR RefSeq; XP_054185070.1; XM_054329095.1. [P35749-3] DR PDB; 9FU2; X-ray; 2.58 A; A=1-1972. DR AlphaFoldDB; P35749; -. DR SMR; P35749; -. DR BioGRID; 110714; 152. DR DIP; DIP-47268N; -. DR FunCoup; P35749; 365. DR IntAct; P35749; 69. DR NDEx; IQUERY-CP-MYH11; 3 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000379616; -. DR DrugBank; DB04444; Tetrafluoroaluminate Ion. DR GlyCosmos; P35749; 1 site, 2 glycans. DR GlyGen; P35749; 1 site, 2 O-linked glycans (1 site). DR iPTMnet; P35749; -. DR MetOSite; P35749; -. DR PhosphoSitePlus; P35749; -. DR SwissPalm; P35749; -. DR BioMuta; MYH11; -. DR DMDM; 13432177; -. DR jPOST; P35749; -. DR MassIVE; P35749; -. DR PaxDb; 9606-ENSP00000379616; -. DR PeptideAtlas; P35749; -. DR PRIDE; P35749; -. DR ProteomicsDB; 55147; -. [P35749-1] DR ProteomicsDB; 55148; -. [P35749-2] DR ProteomicsDB; 55149; -. [P35749-3] DR ProteomicsDB; 61796; -. DR Pumba; P35749; -. DR Antibodypedia; 1966; 911 antibodies from 37 providers. DR DNASU; 4629; -. DR Ensembl; ENST00000300036.6; ENSP00000300036.5; ENSG00000133392.20. [P35749-1] DR Ensembl; ENST00000396324.7; ENSP00000379616.3; ENSG00000133392.20. [P35749-2] DR Ensembl; ENST00000452625.7; ENSP00000407821.2; ENSG00000133392.20. [P35749-3] DR Ensembl; ENST00000576790.7; ENSP00000458731.1; ENSG00000133392.20. [P35749-4] DR Ensembl; ENST00000612165.4; ENSP00000478092.1; ENSG00000276480.5. [P35749-3] DR Ensembl; ENST00000616422.4; ENSP00000478816.1; ENSG00000276480.5. [P35749-4] DR Ensembl; ENST00000621545.2; ENSP00000478109.1; ENSG00000276480.5. [P35749-2] DR Ensembl; ENST00000634050.1; ENSP00000488461.1; ENSG00000276480.5. [P35749-1] DR Ensembl; ENST00000713757.1; ENSP00000519058.1; ENSG00000133392.20. [P35749-1] DR Ensembl; ENST00000911134.1; ENSP00000581193.1; ENSG00000133392.20. [P35749-1] DR Ensembl; ENST00000911140.1; ENSP00000581199.1; ENSG00000133392.20. [P35749-1] DR Ensembl; ENST00000963701.1; ENSP00000633760.1; ENSG00000133392.20. [P35749-1] DR GeneID; 4629; -. DR KEGG; hsa:4629; -. DR MANE-Select; ENST00000300036.6; ENSP00000300036.5; NM_002474.3; NP_002465.1. DR UCSC; uc002ddv.4; human. [P35749-1] DR AGR; HGNC:7569; -. DR ClinPGx; PA31367; -. DR CTD; 4629; -. DR DisGeNET; 4629; -. DR GeneCards; MYH11; -. DR GeneReviews; MYH11; -. DR HGNC; HGNC:7569; MYH11. DR HPA; ENSG00000133392; Tissue enhanced (blood vessel, intestine, urinary bladder). DR MalaCards; MYH11; -. DR MIM; 132900; phenotype. DR MIM; 160745; gene. DR MIM; 619350; phenotype. DR MIM; 619351; phenotype. DR OpenTargets; ENSG00000133392; -. DR Orphanet; 98829; Acute myeloid leukemia with abnormal bone marrow eosinophils inv(16)(p13q22) or t(16;16)(p13;q22). DR Orphanet; 229; Familial aortic dissection. DR Orphanet; 91387; Familial thoracic aortic aneurysm and aortic dissection. DR Orphanet; 2241; Megacystis-microcolon-intestinal hypoperistalsis syndrome. DR VEuPathDB; HostDB:ENSG00000133392; -. DR eggNOG; KOG0161; Eukaryota. DR GeneTree; ENSGT00940000155421; -. DR HOGENOM; CLU_000192_4_2_1; -. DR InParanoid; P35749; -. DR OMA; AAQKCCH; -. DR OrthoDB; 10254995at2759; -. DR PAN-GO; P35749; 6 GO annotations based on evolutionary models. DR PhylomeDB; P35749; -. DR PathwayCommons; P35749; -. 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-445355; Smooth Muscle Contraction. 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-9927432; Developmental Lineage of Mammary Gland Myoepithelial Cells. DR SignaLink; P35749; -. DR Agora; ENSG00000133392; -. DR Agora; ENSG00000276480; -. DR BioGRID-ORCS; 4629; 10 hits in 1155 CRISPR screens. DR CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities. DR ChiTaRS; MYH11; human. DR GeneWiki; MYH11; -. DR GenomeRNAi; 4629; -. DR Pharos; P35749; Tbio. DR PRO; PR:P35749; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; P35749; protein. DR Bgee; ENSG00000133392; Expressed in lower esophagus muscularis layer and 103 other cell types or tissues. DR ExpressionAtlas; P35749; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0005859; C:muscle myosin complex; TAS:ProtInc. DR GO; GO:0032982; C:myosin filament; IBA:GO_Central. DR GO; GO:0016460; C:myosin II complex; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central. DR GO; GO:0008307; F:structural constituent of muscle; IMP:UniProtKB. DR GO; GO:0031032; P:actomyosin structure organization; IBA:GO_Central. DR GO; GO:0055013; P:cardiac muscle cell development; IMP:UniProtKB. DR GO; GO:0048251; P:elastic fiber assembly; IMP:UniProtKB. DR GO; GO:0030241; P:skeletal muscle myosin thick filament assembly; ISS:UniProtKB. DR GO; GO:0006939; P:smooth muscle contraction; ISS:UniProtKB. DR CDD; cd14921; MYSc_Myh11; 1. DR FunFam; 2.30.30.360:FF:000001; Myosin heavy chain; 1. DR FunFam; 3.30.70.1590:FF:000001; Myosin heavy chain; 1. DR FunFam; 1.10.10.820:FF:000002; Myosin heavy chain 10; 1. DR FunFam; 1.20.120.720:FF:000002; Myosin heavy chain 10; 1. DR FunFam; 1.20.58.530:FF:000003; Myosin heavy chain 10; 1. DR FunFam; 1.20.5.340:FF:000008; Myosin heavy chain 11; 1. DR FunFam; 1.20.5.340:FF:000007; Myosin heavy chain, non-muscle; 1. DR FunFam; 4.10.270.10:FF:000001; Myosin heavy chain, non-muscle; 1. DR FunFam; 1.20.5.340:FF:000009; myosin-11 isoform X2; 1. DR FunFam; 1.20.5.340:FF:000027; myosin-11 isoform X2; 1. DR FunFam; 3.40.850.10:FF:000101; Slow myosin heavy chain 2; 1. DR Gene3D; 1.10.10.820; -; 1. DR Gene3D; 1.20.5.340; -; 4. DR Gene3D; 1.20.58.530; -; 1. DR Gene3D; 3.30.70.1590; -; 1. DR Gene3D; 6.10.250.2420; -; 1. DR Gene3D; 3.40.850.10; Kinesin motor domain; 1. DR Gene3D; 2.30.30.360; Myosin S1 fragment, N-terminal; 1. DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1. DR Gene3D; 4.10.270.10; Myosin, subunit A; 1. DR InterPro; IPR000048; IQ_motif_EF-hand-BS. DR InterPro; IPR036961; Kinesin_motor_dom_sf. DR InterPro; IPR001609; Myosin_head_motor_dom-like. DR InterPro; IPR008989; Myosin_S1_N. DR InterPro; IPR002928; Myosin_tail. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR004009; SH3_Myosin. DR PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1. DR PANTHER; PTHR45615:SF23; MYOSIN-11; 1. 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; SSF90257; Myosin rod fragments; 6. DR SUPFAM; SSF50084; Myosin S1 fragment, N-terminal domain; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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; Actin-binding; Alternative splicing; Aortic aneurysm; KW ATP-binding; Calmodulin-binding; Chromosomal rearrangement; Coiled coil; KW Disease variant; Methylation; Motor protein; Muscle protein; Myosin; KW Nucleotide-binding; Phosphoprotein; Proteomics identification; KW Proto-oncogene; Reference proteome; Thick filament. FT CHAIN 1..1972 FT /note="Myosin-11" FT /id="PRO_0000123424" FT DOMAIN 31..81 FT /note="Myosin N-terminal SH3-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190" FT DOMAIN 85..783 FT /note="Myosin motor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782" FT DOMAIN 786..815 FT /note="IQ" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116" FT REGION 661..683 FT /note="Actin-binding" FT /evidence="ECO:0000250" FT REGION 762..776 FT /note="Actin-binding" FT /evidence="ECO:0000250" FT REGION 858..882 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1744..1800 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1866..1972 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1935..1972 FT /note="C-terminal" FT COILED 844..1934 FT /evidence="ECO:0000255" FT COMPBIAS 858..882 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1762..1788 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1789..1800 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1866..1876 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 178..185 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255" FT MOD_RES 8 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 23 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 40 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q7Z406" FT MOD_RES 129 FT /note="N6,N6,N6-trimethyllysine" FT /evidence="ECO:0000255" FT MOD_RES 1177 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q7Z406" FT MOD_RES 1684 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q63862" FT MOD_RES 1722 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q63862" FT MOD_RES 1954 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18318008, FT ECO:0007744|PubMed:24275569" FT MOD_RES 1958 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 1971 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O08638" FT VAR_SEQ 211 FT /note="T -> TQGPSFAY (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:16000639" FT /id="VSP_043017" FT VAR_SEQ 1930..1972 FT /note="RGNETSFVPSRRSGGRRVIENADGSEEETDTRDADFNGTKASE -> GPPPQ FT ETSQ (in isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:16000639" FT /id="VSP_043018" FT VARIANT 616 FT /note="A -> G" FT /evidence="ECO:0000269|PubMed:29781137" FT /id="VAR_085875" FT VARIANT 677 FT /note="R -> H (in MMIHS2)" FT /evidence="ECO:0000269|PubMed:31427716" FT /id="VAR_085645" FT VARIANT 1104 FT /note="A -> T (in dbSNP:rs34263860)" FT /id="VAR_050205" FT VARIANT 1200..1972 FT /note="Missing (in MMIHS2)" FT /evidence="ECO:0000269|PubMed:25407000" FT /id="VAR_085646" FT VARIANT 1234 FT /note="A -> T (in dbSNP:rs16967494)" FT /id="VAR_030239" FT VARIANT 1241..1264 FT /note="Missing (in AAT4)" FT /evidence="ECO:0000269|PubMed:16444274" FT /id="VAR_031734" FT VARIANT 1289 FT /note="V -> A (in dbSNP:rs16967510)" FT /id="VAR_030240" FT VARIANT 1310 FT /note="V -> M (in dbSNP:rs7196804)" FT /id="VAR_030241" FT VARIANT 1508 FT /note="M -> V (in dbSNP:rs35176378)" FT /id="VAR_050206" FT VARIANT 1555 FT /note="L -> V (in VSCM2; uncertain significance)" FT /evidence="ECO:0000269|PubMed:31944481" FT /id="VAR_085647" FT VARIANT 1758 FT /note="R -> Q (in AAT4; dbSNP:rs142546324)" FT /evidence="ECO:0000269|PubMed:16444274" FT /id="VAR_031735" FT CONFLICT 887..889 FT /note="EEK -> NSE (in Ref. 9; D10667)" FT /evidence="ECO:0000305" FT CONFLICT 1558 FT /note="T -> S (in Ref. 9; D10667)" FT /evidence="ECO:0000305" FT CONFLICT 1610..1611 FT /note="KQ -> NE (in Ref. 9; D10667)" FT /evidence="ECO:0000305" FT CONFLICT 1786 FT /note="A -> S (in Ref. 10; CAA49154)" FT /evidence="ECO:0000305" FT CONFLICT 1958 FT /note="T -> L (in Ref. 9; D10667)" FT /evidence="ECO:0000305" FT STRAND 36..39 FT /evidence="ECO:0007829|PDB:9FU2" FT STRAND 41..48 FT /evidence="ECO:0007829|PDB:9FU2" FT STRAND 55..57 FT /evidence="ECO:0007829|PDB:9FU2" FT TURN 73..75 FT /evidence="ECO:0007829|PDB:9FU2" FT HELIX 82..84 FT /evidence="ECO:0007829|PDB:9FU2" FT HELIX 90..92 FT /evidence="ECO:0007829|PDB:9FU2" FT HELIX 98..109 FT /evidence="ECO:0007829|PDB:9FU2" FT TURN 110..112 FT /evidence="ECO:0007829|PDB:9FU2" FT STRAND 115..118 FT /evidence="ECO:0007829|PDB:9FU2" FT STRAND 121..125 FT /evidence="ECO:0007829|PDB:9FU2" FT HELIX 136..141 FT /evidence="ECO:0007829|PDB:9FU2" FT TURN 142..144 FT /evidence="ECO:0007829|PDB:9FU2" FT HELIX 147..149 FT /evidence="ECO:0007829|PDB:9FU2" FT HELIX 154..168 FT /evidence="ECO:0007829|PDB:9FU2" FT STRAND 172..177 FT /evidence="ECO:0007829|PDB:9FU2" FT HELIX 184..198 FT /evidence="ECO:0007829|PDB:9FU2" FT HELIX 213..219 FT /evidence="ECO:0007829|PDB:9FU2" FT HELIX 221..229 FT /evidence="ECO:0007829|PDB:9FU2" FT STRAND 239..242 FT /evidence="ECO:0007829|PDB:9FU2" FT STRAND 244..250 FT /evidence="ECO:0007829|PDB:9FU2" FT STRAND 252..254 FT /evidence="ECO:0007829|PDB:9FU2" FT STRAND 256..263 FT /evidence="ECO:0007829|PDB:9FU2" FT HELIX 268..271 FT /evidence="ECO:0007829|PDB:9FU2" FT HELIX 282..290 FT /evidence="ECO:0007829|PDB:9FU2" FT HELIX 293..298 FT /evidence="ECO:0007829|PDB:9FU2" FT HELIX 304..306 FT /evidence="ECO:0007829|PDB:9FU2" FT HELIX 322..336 FT /evidence="ECO:0007829|PDB:9FU2" FT HELIX 340..357 FT /evidence="ECO:0007829|PDB:9FU2" FT HELIX 376..385 FT /evidence="ECO:0007829|PDB:9FU2" FT HELIX 389..397 FT /evidence="ECO:0007829|PDB:9FU2" FT STRAND 400..409 FT /evidence="ECO:0007829|PDB:9FU2" FT HELIX 414..444 FT /evidence="ECO:0007829|PDB:9FU2" FT STRAND 453..459 FT /evidence="ECO:0007829|PDB:9FU2" FT STRAND 467..469 FT /evidence="ECO:0007829|PDB:9FU2" FT HELIX 471..488 FT /evidence="ECO:0007829|PDB:9FU2" FT HELIX 489..494 FT /evidence="ECO:0007829|PDB:9FU2" FT HELIX 495..501 FT /evidence="ECO:0007829|PDB:9FU2" FT HELIX 516..523 FT /evidence="ECO:0007829|PDB:9FU2" FT STRAND 526..528 FT /evidence="ECO:0007829|PDB:9FU2" FT HELIX 531..539 FT /evidence="ECO:0007829|PDB:9FU2" FT HELIX 546..557 FT /evidence="ECO:0007829|PDB:9FU2" FT STRAND 574..578 FT /evidence="ECO:0007829|PDB:9FU2" FT STRAND 583..587 FT /evidence="ECO:0007829|PDB:9FU2" FT HELIX 591..596 FT /evidence="ECO:0007829|PDB:9FU2" FT HELIX 601..608 FT /evidence="ECO:0007829|PDB:9FU2" FT HELIX 613..618 FT /evidence="ECO:0007829|PDB:9FU2" FT HELIX 653..669 FT /evidence="ECO:0007829|PDB:9FU2" FT STRAND 671..679 FT /evidence="ECO:0007829|PDB:9FU2" FT HELIX 692..702 FT /evidence="ECO:0007829|PDB:9FU2" FT HELIX 704..713 FT /evidence="ECO:0007829|PDB:9FU2" FT STRAND 717..720 FT /evidence="ECO:0007829|PDB:9FU2" FT HELIX 721..728 FT /evidence="ECO:0007829|PDB:9FU2" FT HELIX 729..732 FT /evidence="ECO:0007829|PDB:9FU2" FT HELIX 743..754 FT /evidence="ECO:0007829|PDB:9FU2" FT HELIX 758..760 FT /evidence="ECO:0007829|PDB:9FU2" FT STRAND 761..763 FT /evidence="ECO:0007829|PDB:9FU2" FT STRAND 765..770 FT /evidence="ECO:0007829|PDB:9FU2" FT HELIX 774..784 FT /evidence="ECO:0007829|PDB:9FU2" SQ SEQUENCE 1972 AA; 227339 MW; 67665BB2AECE1277 CRC64; MAQKGQLSDD EKFLFVDKNF INSPVAQADW AAKRLVWVPS EKQGFEAASI KEEKGDEVVV ELVENGKKVT VGKDDIQKMN PPKFSKVEDM AELTCLNEAS VLHNLRERYF SGLIYTYSGL FCVVVNPYKH LPIYSEKIVD MYKGKKRHEM PPHIYAIADT AYRSMLQDRE DQSILCTGES GAGKTENTKK VIQYLAVVAS SHKGKKDTSI TGELEKQLLQ ANPILEAFGN AKTVKNDNSS RFGKFIRINF DVTGYIVGAN IETYLLEKSR AIRQARDERT FHIFYYMIAG AKEKMRSDLL LEGFNNYTFL SNGFVPIPAA QDDEMFQETV EAMAIMGFSE EEQLSILKVV SSVLQLGNIV FKKERNTDQA SMPDNTAAQK VCHLMGINVT DFTRSILTPR IKVGRDVVQK AQTKEQADFA VEALAKATYE RLFRWILTRV NKALDKTHRQ GASFLGILDI AGFEIFEVNS FEQLCINYTN EKLQQLFNHT MFILEQEEYQ REGIEWNFID FGLDLQPCIE LIERPNNPPG VLALLDEECW FPKATDKSFV EKLCTEQGSH PKFQKPKQLK DKTEFSIIHY AGKVDYNASA WLTKNMDPLN DNVTSLLNAS SDKFVADLWK DVDRIVGLDQ MAKMTESSLP SASKTKKGMF RTVGQLYKEQ LGKLMTTLRN TTPNFVRCII PNHEKRSGKL DAFLVLEQLR CNGVLEGIRI CRQGFPNRIV FQEFRQRYEI LAANAIPKGF MDGKQACILM IKALELDPNL YRIGQSKIFF RTGVLAHLEE ERDLKITDVI MAFQAMCRGY LARKAFAKRQ QQLTAMKVIQ RNCAAYLKLR NWQWWRLFTK VKPLLQVTRQ EEEMQAKEDE LQKTKERQQK AENELKELEQ KHSQLTEEKN LLQEQLQAET ELYAEAEEMR VRLAAKKQEL EEILHEMEAR LEEEEDRGQQ LQAERKKMAQ QMLDLEEQLE EEEAARQKLQ LEKVTAEAKI KKLEDEILVM DDQNNKLSKE RKLLEERISD LTTNLAEEEE KAKNLTKLKN KHESMISELE VRLKKEEKSR QELEKLKRKL EGDASDFHEQ IADLQAQIAE LKMQLAKKEE ELQAALARLD DEIAQKNNAL KKIRELEGHI SDLQEDLDSE RAARNKAEKQ KRDLGEELEA LKTELEDTLD STATQQELRA KREQEVTVLK KALDEETRSH EAQVQEMRQK HAQAVEELTE QLEQFKRAKA NLDKNKQTLE KENADLAGEL RVLGQAKQEV EHKKKKLEAQ VQELQSKCSD GERARAELND KVHKLQNEVE SVTGMLNEAE GKAIKLAKDV ASLSSQLQDT QELLQEETRQ KLNVSTKLRQ LEEERNSLQD QLDEEMEAKQ NLERHISTLN IQLSDSKKKL QDFASTVEAL EEGKKRFQKE IENLTQQYEE KAAAYDKLEK TKNRLQQELD DLVVDLDNQR QLVSNLEKKQ RKFDQLLAEE KNISSKYADE RDRAEAEARE KETKALSLAR ALEEALEAKE ELERTNKMLK AEMEDLVSSK DDVGKNVHEL EKSKRALETQ MEEMKTQLEE LEDELQATED AKLRLEVNMQ ALKGQFERDL QARDEQNEEK RRQLQRQLHE YETELEDERK QRALAAAAKK KLEGDLKDLE LQADSAIKGR EEAIKQLRKL QAQMKDFQRE LEDARASRDE IFATAKENEK KAKSLEADLM QLQEDLAAAE RARKQADLEK EELAEELASS LSGRNALQDE KRRLEARIAQ LEEELEEEQG NMEAMSDRVR KATQQAEQLS NELATERSTA QKNESARQQL ERQNKELRSK LHEMEGAVKS KFKSTIAALE AKIAQLEEQV EQEAREKQAA TKSLKQKDKK LKEILLQVED ERKMAEQYKE QAEKGNARVK QLKRQLEEAE EESQRINANR RKLQRELDEA TESNEAMGRE VNALKSKLRR GNETSFVPSR RSGGRRVIEN ADGSEEETDT RDADFNGTKA SE //