MYH11_HUMAN
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 03-AUG-2022, entry version 219.
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=2; 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="http://atlasgeneticsoncology.org/Genes/MYH11ID43.html";
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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_001040113.1. [P35749-3]
DR RefSeq; NP_001035203.1; NM_001040114.1. [P35749-2]
DR RefSeq; NP_002465.1; NM_002474.2. [P35749-1]
DR RefSeq; NP_074035.1; NM_022844.2. [P35749-4]
DR RefSeq; XP_016878739.1; XM_017023250.1. [P35749-3]
DR AlphaFoldDB; P35749; -.
DR SMR; P35749; -.
DR BioGRID; 110714; 102.
DR DIP; DIP-47268N; -.
DR IntAct; P35749; 52.
DR MINT; P35749; -.
DR STRING; 9606.ENSP00000379616; -.
DR DrugBank; DB04444; Tetrafluoroaluminate Ion.
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 EPD; P35749; -.
DR jPOST; P35749; -.
DR MassIVE; P35749; -.
DR MaxQB; P35749; -.
DR PaxDb; P35749; -.
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 Antibodypedia; 1966; 769 antibodies from 33 providers.
DR DNASU; 4629; -.
DR Ensembl; ENST00000300036.6; ENSP00000300036.5; ENSG00000133392.18. [P35749-1]
DR Ensembl; ENST00000396324.7; ENSP00000379616.3; ENSG00000133392.18. [P35749-2]
DR Ensembl; ENST00000452625.7; ENSP00000407821.2; ENSG00000133392.18. [P35749-3]
DR Ensembl; ENST00000576790.7; ENSP00000458731.1; ENSG00000133392.18. [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 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 CTD; 4629; -.
DR DisGeNET; 4629; -.
DR GeneCards; MYH11; -.
DR GeneReviews; MYH11; -.
DR HGNC; HGNC:7569; MYH11.
DR HPA; ENSG00000133392; Tissue enhanced (intestine, seminal vesicle, urinary bladder).
DR MalaCards; MYH11; -.
DR MIM; 132900; phenotype.
DR MIM; 160745; gene.
DR MIM; 619350; phenotype.
DR MIM; 619351; phenotype.
DR neXtProt; NX_P35749; -.
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 Orphanet; 706; NON RARE IN EUROPE: Patent arterial duct.
DR PharmGKB; PA31367; -.
DR VEuPathDB; HostDB:ENSG00000133392; -.
DR eggNOG; KOG0161; Eukaryota.
DR GeneTree; ENSGT00940000155421; -.
DR HOGENOM; CLU_000192_4_2_1; -.
DR InParanoid; P35749; -.
DR OMA; RCYFASK; -.
DR OrthoDB; 47111at2759; -.
DR PhylomeDB; P35749; -.
DR TreeFam; TF333601; -.
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 SignaLink; P35749; -.
DR BioGRID-ORCS; 4629; 9 hits in 1070 CRISPR screens.
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 101 other tissues.
DR ExpressionAtlas; P35749; baseline and differential.
DR Genevisible; P35749; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
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:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
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 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 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; 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 Actin-binding; Alternative splicing; Aortic aneurysm; ATP-binding;
KW Calmodulin-binding; Chromosomal rearrangement; Coiled coil;
KW Disease variant; Methylation; Motor protein; Muscle protein; Myosin;
KW Nucleotide-binding; Phosphoprotein; Proto-oncogene; Reference proteome;
KW 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 1761..1787
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1866..1915
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1945..1972
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; unknown pathological
FT 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"
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
