ID MYH10_HUMAN Reviewed; 1976 AA. AC P35580; B2RWP9; D3DTS1; F8VTL3; Q12989; Q149N3; Q149N4; Q16087; Q4LE45; AC Q6PK16; Q9BWG0; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 3. DT 27-MAR-2024, entry version 227. DE RecName: Full=Myosin-10; DE AltName: Full=Cellular myosin heavy chain, type B; DE AltName: Full=Myosin heavy chain 10; DE AltName: Full=Myosin heavy chain, non-muscle IIb; DE AltName: Full=Non-muscle myosin heavy chain B; DE Short=NMMHC-B; DE AltName: Full=Non-muscle myosin heavy chain IIb; DE Short=NMMHC II-b; DE Short=NMMHC-IIB; GN Name=MYH10; 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] (ISOFORM 1). RX PubMed=7499478; DOI=10.1007/bf00114503; RA Phillips C.L., Yamakawa K., Adelstein R.S.; RT "Cloning of the cDNA encoding human nonmuscle myosin heavy chain-B and RT analysis of human tissues with isoform-specific antibodies."; RL J. Muscle Res. Cell Motil. 16:379-389(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=8690889; RA Abdelhaleem M.M., Hameed S., Klassen D., Greenberg A.H.; RT "Leukophysin: an RNA helicase A-related molecule identified in cytotoxic T RT cell granules and vesicles."; RL J. Immunol. 156:2026-2035(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Brain; RA Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R., RA Okazaki N., Koga H., Nagase T., Ohara O.; RT "Preparation of a set of expression-ready clones of mammalian long cDNAs RT encoding large proteins by the ORF trap cloning method."; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5). RC TISSUE=Eye, and Muscle; 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 [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 63-722 (ISOFORM 1). 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 [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 211-301 (ISOFORM 2), ALTERNATIVE SPLICING RP (ISOFORM 3), AND TISSUE SPECIFICITY. RX PubMed=7782316; DOI=10.1074/jbc.270.24.14533; RA Itoh K., Adelstein R.S.; RT "Neuronal cell expression of inserted isoforms of vertebrate nonmuscle RT myosin heavy chain II-B."; RL J. Biol. Chem. 270:14533-14540(1995). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1751-1976. RX PubMed=7916668; DOI=10.1161/01.res.73.6.1000; RA Aikawa M., Sivam P.N., Kuro-O M., Kimura K., Nakahara K., Takewaki S., RA Ueda M., Yamaguchi H., Yazaki Y., Periasamy M.; RT "Human smooth muscle myosin heavy chain isoforms as molecular markers for RT vascular development and atherosclerosis."; RL Circ. Res. 73:1000-1012(1993). RN [10] 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 [11] RP IDENTIFICATION BY 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 [12] RP INTERACTION WITH PLEKHG6. RX PubMed=16721066; DOI=10.4161/cc.5.11.2815; RA Wu D., Asiedu M., Adelstein R.S., Wei Q.; RT "A novel guanine nucleotide exchange factor MyoGEF is required for RT cytokinesis."; RL Cell Cycle 5:1234-1239(2006). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1939; SER-1952 AND SER-1956, RP AND 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 [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1956, 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 [16] 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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1939 AND SER-1956, 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 [18] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-442 AND LYS-1645, 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 [19] RP INTERACTION WITH ECPAS. RX PubMed=20682791; DOI=10.1074/jbc.m110.154120; RA Gorbea C., Pratt G., Ustrell V., Bell R., Sahasrabudhe S., Hughes R.E., RA Rechsteiner M.; RT "A protein interaction network for Ecm29 links the 26 S proteasome to RT molecular motors and endosomal components."; RL J. Biol. Chem. 285:31616-31633(2010). RN [20] RP FUNCTION, AND INTERACTION WITH LARP6. RX PubMed=20603131; DOI=10.1016/j.jmb.2010.06.057; RA Cai L., Fritz D., Stefanovic L., Stefanovic B.; RT "Nonmuscle myosin-dependent synthesis of type I collagen."; RL J. Mol. Biol. 401:564-578(2010). RN [21] 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 [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1956, PHOSPHORYLATION [LARGE RP SCALE ANALYSIS] AT SER-214 (ISOFORMS 2 AND 4), AND IDENTIFICATION BY MASS RP 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 [23] 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 [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1145 AND SER-1938, RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214 (ISOFORMS 2 AND 4), AND RP IDENTIFICATION BY 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 [25] RP INTERACTION WITH MCC, AND SUBCELLULAR LOCATION. RX PubMed=22480440; DOI=10.1016/j.bbamcr.2012.03.011; RA Pangon L., Van Kralingen C., Abas M., Daly R.J., Musgrove E.A., RA Kohonen-Corish M.R.; RT "The PDZ-binding motif of MCC is phosphorylated at position -1 and controls RT lamellipodia formation in colon epithelial cells."; RL Biochim. Biophys. Acta 1823:1058-1067(2012). RN [26] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1935; SER-1937; SER-1952 AND RP SER-1956, 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 [27] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1935; SER-1939; SER-1952; RP SER-1956 AND THR-1960, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214 RP (ISOFORMS 2 AND 4), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [28] 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 [29] RP VARIANT 908-GLU--GLU-1976 DEL. RX PubMed=25003005; DOI=10.4161/rdis.26144; RA Tuzovic L., Yu L., Zeng W., Li X., Lu H., Lu H.M., Gonzalez K.D., RA Chung W.K.; RT "A human de novo mutation in MYH10 phenocopies the loss of function RT mutation in mice."; RL Rare Dis. 1:E26144-E26144(2013). RN [30] RP VARIANT CYS-270. RX PubMed=25356899; DOI=10.1371/journal.pgen.1004772; RA Hamdan F.F., Srour M., Capo-Chichi J.M., Daoud H., Nassif C., Patry L., RA Massicotte C., Ambalavanan A., Spiegelman D., Diallo O., Henrion E., RA Dionne-Laporte A., Fougerat A., Pshezhetsky A.V., Venkateswaran S., RA Rouleau G.A., Michaud J.L.; RT "De novo mutations in moderate or severe intellectual disability."; RL PLoS Genet. 10:E1004772-E1004772(2014). CC -!- FUNCTION: Cellular myosin that appears to play a role in cytokinesis, CC cell shape, and specialized functions such as secretion and capping. CC Involved with LARP6 in the stabilization of type I collagen mRNAs for CC CO1A1 and CO1A2. During cell spreading, plays an important role in CC cytoskeleton reorganization, focal contacts formation (in the central CC part but not the margins of spreading cells), and lamellipodial CC extension; this function is mechanically antagonized by MYH9. CC {ECO:0000269|PubMed:20052411, ECO:0000269|PubMed:20603131}. 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 PLEKHG6 (PubMed:16721066). CC Interacts with ECPAS (PubMed:20682791). Interacts with KIF26B (By CC similarity). Interacts with LARP6 (PubMed:20603131). Interacts with MCC CC (PubMed:22480440). Interacts with CFAP95 (PubMed:28345668). CC {ECO:0000250|UniProtKB:Q61879, ECO:0000269|PubMed:16721066, CC ECO:0000269|PubMed:20603131, ECO:0000269|PubMed:20682791, CC ECO:0000269|PubMed:22480440, ECO:0000269|PubMed:28345668}. CC -!- SUBCELLULAR LOCATION: Cell projection, lamellipodium CC {ECO:0000269|PubMed:20052411, ECO:0000269|PubMed:22480440}. CC Note=Colocalizes with MCC at the leading edge of migrating cells. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=P35580-1; Sequence=Displayed; CC Name=2; CC IsoId=P35580-2; Sequence=VSP_022013; CC Name=3; CC IsoId=P35580-3; Sequence=VSP_022014; CC Name=4; CC IsoId=P35580-4; Sequence=VSP_046033, VSP_022014; CC Name=5; CC IsoId=P35580-5; Sequence=VSP_054974; CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed in cerebellum and spinal CC chord. Isoform 2 is expressed in cerebrum and retina. Isoform 3 is CC expressed in the cerebrum and to a much lower extent in cerebellum. CC {ECO:0000269|PubMed:7782316}. 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: Phosphorylated by ABL2. {ECO:0000250}. CC -!- DISEASE: Note=Associated with severe intellectual disability, CC microcephaly, and feeding difficulties as well as cerebral atrophy. CC {ECO:0000269|PubMed:25003005, ECO:0000269|PubMed:25356899}. CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase CC superfamily. Myosin family. {ECO:0000305}. CC -!- CAUTION: Represents a conventional non-muscle myosin. This protein CC should not be confused with the unconventional myosin-10 (MYO10). CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAE06108.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; 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; M69181; AAA99177.1; -; mRNA. DR EMBL; AB210026; BAE06108.1; ALT_INIT; mRNA. DR EMBL; AC011061; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC025518; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC026130; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471108; EAW90046.1; -; Genomic_DNA. DR EMBL; CH471108; EAW90047.1; -; Genomic_DNA. DR EMBL; CH471108; EAW90048.1; -; Genomic_DNA. DR EMBL; CH471108; EAW90049.1; -; Genomic_DNA. DR EMBL; BC000280; AAH00280.1; -; mRNA. DR EMBL; BC008968; AAH08968.1; -; mRNA. DR EMBL; BC117690; AAI17691.1; -; mRNA. DR EMBL; BC117691; AAI17692.1; -; mRNA. DR EMBL; BC144668; AAI44669.1; -; mRNA. DR EMBL; BC150634; AAI50635.1; -; mRNA. DR EMBL; U15618; AAA87712.1; -; mRNA. DR EMBL; S67247; AAB28952.1; -; mRNA. DR CCDS; CCDS11144.1; -. [P35580-1] DR CCDS; CCDS58515.1; -. [P35580-4] DR CCDS; CCDS73984.1; -. [P35580-5] DR PIR; A59252; A59252. DR PIR; I65769; I65769. DR RefSeq; NP_001242941.1; NM_001256012.1. [P35580-4] DR RefSeq; NP_001243024.1; NM_001256095.1. [P35580-5] DR RefSeq; NP_005955.3; NM_005964.3. [P35580-1] DR RefSeq; XP_016880169.1; XM_017024680.1. DR RefSeq; XP_016880170.1; XM_017024681.1. DR RefSeq; XP_016880171.1; XM_017024682.1. DR PDB; 4PD3; X-ray; 2.84 A; A/B=1-782. DR PDBsum; 4PD3; -. DR AlphaFoldDB; P35580; -. DR SMR; P35580; -. DR BioGRID; 110713; 341. DR CORUM; P35580; -. DR DIP; DIP-31110N; -. DR IntAct; P35580; 90. DR MINT; P35580; -. DR STRING; 9606.ENSP00000353590; -. DR BindingDB; P35580; -. DR ChEMBL; CHEMBL4105746; -. DR CarbonylDB; P35580; -. DR GlyCosmos; P35580; 1 site, 2 glycans. DR GlyGen; P35580; 2 sites, 2 O-linked glycans (2 sites). DR iPTMnet; P35580; -. DR MetOSite; P35580; -. DR PhosphoSitePlus; P35580; -. DR SwissPalm; P35580; -. DR BioMuta; MYH10; -. DR DMDM; 215274129; -. DR EPD; P35580; -. DR jPOST; P35580; -. DR MassIVE; P35580; -. DR MaxQB; P35580; -. DR PaxDb; 9606-ENSP00000353590; -. DR PeptideAtlas; P35580; -. DR PRIDE; P35580; -. DR ProteomicsDB; 28641; -. DR ProteomicsDB; 55095; -. [P35580-1] DR ProteomicsDB; 55096; -. [P35580-2] DR ProteomicsDB; 55097; -. [P35580-3] DR Pumba; P35580; -. DR Antibodypedia; 24686; 200 antibodies from 31 providers. DR DNASU; 4628; -. DR Ensembl; ENST00000269243.8; ENSP00000269243.4; ENSG00000133026.14. [P35580-1] DR Ensembl; ENST00000360416.8; ENSP00000353590.4; ENSG00000133026.14. [P35580-4] DR Ensembl; ENST00000379980.8; ENSP00000369315.5; ENSG00000133026.14. [P35580-5] DR Ensembl; ENST00000686654.1; ENSP00000508862.1; ENSG00000133026.14. [P35580-4] DR Ensembl; ENST00000687178.1; ENSP00000509748.1; ENSG00000133026.14. [P35580-5] DR Ensembl; ENST00000688902.1; ENSP00000509091.1; ENSG00000133026.14. [P35580-4] DR Ensembl; ENST00000693441.1; ENSP00000509241.1; ENSG00000133026.14. [P35580-4] DR GeneID; 4628; -. DR KEGG; hsa:4628; -. DR MANE-Select; ENST00000360416.8; ENSP00000353590.4; NM_001256012.3; NP_001242941.1. [P35580-4] DR UCSC; uc002gll.5; human. [P35580-1] DR AGR; HGNC:7568; -. DR CTD; 4628; -. DR DisGeNET; 4628; -. DR GeneCards; MYH10; -. DR HGNC; HGNC:7568; MYH10. DR HPA; ENSG00000133026; Low tissue specificity. DR MalaCards; MYH10; -. DR MIM; 160776; gene. DR neXtProt; NX_P35580; -. DR OpenTargets; ENSG00000133026; -. DR PharmGKB; PA31366; -. DR VEuPathDB; HostDB:ENSG00000133026; -. DR eggNOG; KOG0160; Eukaryota. DR eggNOG; KOG0161; Eukaryota. DR GeneTree; ENSGT00940000155159; -. DR HOGENOM; CLU_000192_8_0_1; -. DR InParanoid; P35580; -. DR OMA; MQAHIQX; -. DR OrthoDB; 2877572at2759; -. DR PhylomeDB; P35580; -. DR TreeFam; TF333601; -. DR PathwayCommons; P35580; -. 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 SignaLink; P35580; -. DR SIGNOR; P35580; -. DR BioGRID-ORCS; 4628; 20 hits in 1164 CRISPR screens. DR ChiTaRS; MYH10; human. DR GeneWiki; MYH10; -. DR GenomeRNAi; 4628; -. DR Pharos; P35580; Tchem. DR PRO; PR:P35580; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; P35580; Protein. DR Bgee; ENSG00000133026; Expressed in blood vessel layer and 213 other cell types or tissues. DR ExpressionAtlas; P35580; baseline and differential. DR GO; GO:0042641; C:actomyosin; IDA:UniProtKB. DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB. DR GO; GO:0032154; C:cleavage furrow; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IMP:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell. DR GO; GO:0030496; C:midbody; IDA:UniProtKB. DR GO; GO:0016459; C:myosin complex; NAS: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:0005634; C:nucleus; HDA:UniProtKB. DR GO; GO:0001725; C:stress fiber; IDA:UniProtKB. DR GO; GO:0003779; F:actin binding; NAS:UniProtKB. DR GO; GO:0051015; F:actin filament binding; IDA:MGI. DR GO; GO:0043531; F:ADP binding; IDA:MGI. DR GO; GO:0005524; F:ATP binding; IDA:MGI. DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW. DR GO; GO:0000146; F:microfilament motor activity; IDA:MGI. DR GO; GO:0048027; F:mRNA 5'-UTR binding; IDA:UniProtKB. DR GO; GO:0035613; F:RNA stem-loop binding; IDA:UniProtKB. DR GO; GO:0030048; P:actin filament-based movement; IDA:MGI. DR GO; GO:0031032; P:actomyosin structure organization; IMP:UniProtKB. DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. DR GO; GO:0000281; P:mitotic cytokinesis; IDA:MGI. DR GO; GO:0050714; P:positive regulation of protein secretion; IMP:UniProtKB. DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central. DR CDD; cd14920; MYSc_Myh10; 1. DR Gene3D; 1.10.10.820; -; 1. DR Gene3D; 1.10.287.1490; -; 1. DR Gene3D; 1.20.5.340; -; 4. DR Gene3D; 1.20.5.4820; -; 1. DR Gene3D; 1.20.58.530; -; 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 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 PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1. DR PANTHER; PTHR45615:SF24; MYOSIN-10; 1. DR Pfam; PF00612; IQ; 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. DR Genevisible; P35580; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Actin-binding; Alternative splicing; KW ATP-binding; Calmodulin-binding; Cell adhesion; Cell projection; KW Cell shape; Coiled coil; Disease variant; Methylation; Motor protein; KW Myosin; Nucleotide-binding; Phosphoprotein; Reference proteome. FT CHAIN 1..1976 FT /note="Myosin-10" FT /id="PRO_0000123421" 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:0000255|PROSITE-ProRule:PRU00782" FT REGION 1127..1147 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1697..1728 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1872..1976 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 845..1976 FT /evidence="ECO:0000255" FT COMPBIAS 1697..1717 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1872..1915 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1950..1965 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 18 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:Q61879" FT MOD_RES 442 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 1145 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 1241 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q61879" FT MOD_RES 1301 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q61879" FT MOD_RES 1645 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 1930 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:Q61879" FT MOD_RES 1935 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 1937 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1938 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 1939 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569" FT MOD_RES 1940 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:Q61879" FT MOD_RES 1952 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 1956 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18318008, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 1960 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 1975 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9JLT0" FT VAR_SEQ 211 FT /note="P -> PQESPKPVKHQSGSLLY (in isoform 2)" FT /evidence="ECO:0000303|PubMed:7782316" FT /id="VSP_022013" FT VAR_SEQ 211 FT /note="P -> PQESPKPVKHQ (in isoform 4)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_046033" FT VAR_SEQ 211 FT /note="P -> PESPKPVKHQ (in isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_054974" FT VAR_SEQ 621 FT /note="D -> DEIQNIQRASFYDSVSGLHEPP (in isoform 3 and FT isoform 4)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_022014" FT VARIANT 270 FT /note="R -> C (found in a patient with severe intellectual FT disease, microcephaly and feeding difficulties as well as FT cerebral atrophy; likely pathogenic; dbSNP:rs727504231)" FT /evidence="ECO:0000269|PubMed:25356899" FT /id="VAR_078649" FT VARIANT 908..1976 FT /note="Missing (found in a patient with intrauterine growth FT restriction, microcephaly, developmental delay, failure to FT thrive, congenital bilateral hip dysplasia, cerebral and FT cerebellar atrophy, hydrocephalus and congenital FT diaphragmatic hernia; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:25003005" FT /id="VAR_078650" FT CONFLICT 800 FT /note="Y -> C (in Ref. 1; AAA99177)" FT /evidence="ECO:0000305" FT CONFLICT 943..944 FT /note="NE -> KK (in Ref. 5; AAH08968)" FT /evidence="ECO:0000305" FT CONFLICT 1429 FT /note="L -> P (in Ref. 5; AAI17691)" FT /evidence="ECO:0000305" FT CONFLICT 1751 FT /note="N -> D (in Ref. 9; AAB28952)" FT /evidence="ECO:0000305" FT TURN 9..14 FT /evidence="ECO:0007829|PDB:4PD3" FT STRAND 36..39 FT /evidence="ECO:0007829|PDB:4PD3" FT STRAND 41..49 FT /evidence="ECO:0007829|PDB:4PD3" FT STRAND 57..65 FT /evidence="ECO:0007829|PDB:4PD3" FT STRAND 68..75 FT /evidence="ECO:0007829|PDB:4PD3" FT HELIX 82..84 FT /evidence="ECO:0007829|PDB:4PD3" FT HELIX 90..92 FT /evidence="ECO:0007829|PDB:4PD3" FT HELIX 98..109 FT /evidence="ECO:0007829|PDB:4PD3" FT TURN 110..112 FT /evidence="ECO:0007829|PDB:4PD3" FT STRAND 115..118 FT /evidence="ECO:0007829|PDB:4PD3" FT STRAND 121..125 FT /evidence="ECO:0007829|PDB:4PD3" FT HELIX 136..141 FT /evidence="ECO:0007829|PDB:4PD3" FT HELIX 154..167 FT /evidence="ECO:0007829|PDB:4PD3" FT STRAND 172..178 FT /evidence="ECO:0007829|PDB:4PD3" FT HELIX 180..182 FT /evidence="ECO:0007829|PDB:4PD3" FT HELIX 184..198 FT /evidence="ECO:0007829|PDB:4PD3" FT HELIX 216..218 FT /evidence="ECO:0007829|PDB:4PD3" FT HELIX 221..229 FT /evidence="ECO:0007829|PDB:4PD3" FT STRAND 237..240 FT /evidence="ECO:0007829|PDB:4PD3" FT STRAND 242..250 FT /evidence="ECO:0007829|PDB:4PD3" FT STRAND 256..264 FT /evidence="ECO:0007829|PDB:4PD3" FT HELIX 269..272 FT /evidence="ECO:0007829|PDB:4PD3" FT HELIX 282..290 FT /evidence="ECO:0007829|PDB:4PD3" FT HELIX 293..298 FT /evidence="ECO:0007829|PDB:4PD3" FT HELIX 304..306 FT /evidence="ECO:0007829|PDB:4PD3" FT HELIX 322..335 FT /evidence="ECO:0007829|PDB:4PD3" FT HELIX 340..357 FT /evidence="ECO:0007829|PDB:4PD3" FT HELIX 379..384 FT /evidence="ECO:0007829|PDB:4PD3" FT HELIX 389..397 FT /evidence="ECO:0007829|PDB:4PD3" FT HELIX 414..442 FT /evidence="ECO:0007829|PDB:4PD3" FT STRAND 453..461 FT /evidence="ECO:0007829|PDB:4PD3" FT HELIX 471..501 FT /evidence="ECO:0007829|PDB:4PD3" FT HELIX 511..514 FT /evidence="ECO:0007829|PDB:4PD3" FT HELIX 516..522 FT /evidence="ECO:0007829|PDB:4PD3" FT HELIX 531..538 FT /evidence="ECO:0007829|PDB:4PD3" FT HELIX 546..556 FT /evidence="ECO:0007829|PDB:4PD3" FT STRAND 567..569 FT /evidence="ECO:0007829|PDB:4PD3" FT STRAND 572..578 FT /evidence="ECO:0007829|PDB:4PD3" FT STRAND 583..586 FT /evidence="ECO:0007829|PDB:4PD3" FT HELIX 591..594 FT /evidence="ECO:0007829|PDB:4PD3" FT HELIX 601..608 FT /evidence="ECO:0007829|PDB:4PD3" FT HELIX 613..618 FT /evidence="ECO:0007829|PDB:4PD3" FT HELIX 653..668 FT /evidence="ECO:0007829|PDB:4PD3" FT STRAND 671..679 FT /evidence="ECO:0007829|PDB:4PD3" FT HELIX 692..702 FT /evidence="ECO:0007829|PDB:4PD3" FT HELIX 704..711 FT /evidence="ECO:0007829|PDB:4PD3" FT STRAND 717..720 FT /evidence="ECO:0007829|PDB:4PD3" FT HELIX 721..728 FT /evidence="ECO:0007829|PDB:4PD3" FT HELIX 729..731 FT /evidence="ECO:0007829|PDB:4PD3" FT TURN 733..735 FT /evidence="ECO:0007829|PDB:4PD3" FT HELIX 745..754 FT /evidence="ECO:0007829|PDB:4PD3" FT STRAND 760..763 FT /evidence="ECO:0007829|PDB:4PD3" FT STRAND 765..770 FT /evidence="ECO:0007829|PDB:4PD3" FT HELIX 774..782 FT /evidence="ECO:0007829|PDB:4PD3" FT MOD_RES P35580-2:214 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569" FT MOD_RES P35580-4:214 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569" SQ SEQUENCE 1976 AA; 228999 MW; A7C91944EBC2368F CRC64; MAQRTGLEDP ERYLFVDRAV IYNPATQADW TAKKLVWIPS ERHGFEAASI KEERGDEVMV ELAENGKKAM VNKDDIQKMN PPKFSKVEDM AELTCLNEAS VLHNLKDRYY SGLIYTYSGL FCVVINPYKN LPIYSENIIE MYRGKKRHEM PPHIYAISES AYRCMLQDRE DQSILCTGES GAGKTENTKK VIQYLAHVAS SHKGRKDHNI PGELERQLLQ ANPILESFGN AKTVKNDNSS RFGKFIRINF DVTGYIVGAN IETYLLEKSR AVRQAKDERT FHIFYQLLSG AGEHLKSDLL LEGFNNYRFL SNGYIPIPGQ QDKDNFQETM EAMHIMGFSH EEILSMLKVV SSVLQFGNIS FKKERNTDQA SMPENTVAQK LCHLLGMNVM EFTRAILTPR IKVGRDYVQK AQTKEQADFA VEALAKATYE RLFRWLVHRI NKALDRTKRQ GASFIGILDI AGFEIFELNS FEQLCINYTN EKLQQLFNHT MFILEQEEYQ REGIEWNFID FGLDLQPCID LIERPANPPG VLALLDEECW FPKATDKTFV EKLVQEQGSH SKFQKPRQLK DKADFCIIHY AGKVDYKADE WLMKNMDPLN DNVATLLHQS SDRFVAELWK DVDRIVGLDQ VTGMTETAFG SAYKTKKGMF RTVGQLYKES LTKLMATLRN TNPNFVRCII PNHEKRAGKL DPHLVLDQLR CNGVLEGIRI CRQGFPNRIV FQEFRQRYEI LTPNAIPKGF MDGKQACERM IRALELDPNL YRIGQSKIFF RAGVLAHLEE ERDLKITDII IFFQAVCRGY LARKAFAKKQ QQLSALKVLQ RNCAAYLKLR HWQWWRVFTK VKPLLQVTRQ EEELQAKDEE LLKVKEKQTK VEGELEEMER KHQQLLEEKN ILAEQLQAET ELFAEAEEMR ARLAAKKQEL EEILHDLESR VEEEEERNQI LQNEKKKMQA HIQDLEEQLD EEEGARQKLQ LEKVTAEAKI KKMEEEILLL EDQNSKFIKE KKLMEDRIAE CSSQLAEEEE KAKNLAKIRN KQEVMISDLE ERLKKEEKTR QELEKAKRKL DGETTDLQDQ IAELQAQIDE LKLQLAKKEE ELQGALARGD DETLHKNNAL KVVRELQAQI AELQEDFESE KASRNKAEKQ KRDLSEELEA LKTELEDTLD TTAAQQELRT KREQEVAELK KALEEETKNH EAQIQDMRQR HATALEELSE QLEQAKRFKA NLEKNKQGLE TDNKELACEV KVLQQVKAES EHKRKKLDAQ VQELHAKVSE GDRLRVELAE KASKLQNELD NVSTLLEEAE KKGIKFAKDA ASLESQLQDT QELLQEETRQ KLNLSSRIRQ LEEEKNSLQE QQEEEEEARK NLEKQVLALQ SQLADTKKKV DDDLGTIESL EEAKKKLLKD AEALSQRLEE KALAYDKLEK TKNRLQQELD DLTVDLDHQR QVASNLEKKQ KKFDQLLAEE KSISARYAEE RDRAEAEARE KETKALSLAR ALEEALEAKE EFERQNKQLR ADMEDLMSSK DDVGKNVHEL EKSKRALEQQ VEEMRTQLEE LEDELQATED AKLRLEVNMQ AMKAQFERDL QTRDEQNEEK KRLLIKQVRE LEAELEDERK QRALAVASKK KMEIDLKDLE AQIEAANKAR DEVIKQLRKL QAQMKDYQRE LEEARASRDE IFAQSKESEK KLKSLEAEIL QLQEELASSE RARRHAEQER DELADEITNS ASGKSALLDE KRRLEARIAQ LEEELEEEQS NMELLNDRFR KTTLQVDTLN AELAAERSAA QKSDNARQQL ERQNKELKAK LQELEGAVKS KFKATISALE AKIGQLEEQL EQEAKERAAA NKLVRRTEKK LKEIFMQVED ERRHADQYKE QMEKANARMK QLKRQLEEAE EEATRANASR RKLQRELDDA TEANEGLSRE VSTLKNRLRR GGPISFSSSR SGRRQLHLEG ASLELSDDDT ESKTSDVNET QPPQSE //