MYH10_HUMAN
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 03-AUG-2022, entry version 218.
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};
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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. [P35580-5]
DR RefSeq; XP_016880170.1; XM_017024681.1. [P35580-1]
DR RefSeq; XP_016880171.1; XM_017024682.1. [P35580-1]
DR PDB; 4PD3; X-ray; 2.84 A; A/B=1-782.
DR PDBsum; 4PD3; -.
DR AlphaFoldDB; P35580; -.
DR SMR; P35580; -.
DR BioGRID; 110713; 231.
DR CORUM; P35580; -.
DR DIP; DIP-31110N; -.
DR IntAct; P35580; 70.
DR MINT; P35580; -.
DR STRING; 9606.ENSP00000353590; -.
DR BindingDB; P35580; -.
DR ChEMBL; CHEMBL4105746; -.
DR CarbonylDB; P35580; -.
DR GlyGen; P35580; 1 site, 2 O-linked glycans (1 site).
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; P35580; -.
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 Antibodypedia; 24686; 168 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 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; XERAAAN; -.
DR OrthoDB; 47111at2759; -.
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; 19 hits in 1086 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 211 other tissues.
DR ExpressionAtlas; P35580; baseline and differential.
DR Genevisible; P35580; HS.
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:0005844; C:polysome; IMP: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 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; 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; SSF52540; SSF52540; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; 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 (probable disease-associated variant found in
FT a patient with severe intellectual disease, microcephaly
FT and feeding difficulties as well as cerebral atrophy;
FT dbSNP:rs727504231)"
FT /evidence="ECO:0000269|PubMed:25356899"
FT /id="VAR_078649"
FT VARIANT 908..1976
FT /note="Missing (probable disease-associated variant found
FT in a patient with intrauterine growth restriction,
FT microcephaly, developmental delay, failure to thrive,
FT congenital bilateral hip dysplasia, cerebral and cerebellar
FT atrophy, hydrocephalus and congenital diaphragmatic
FT hernia)"
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
