Full text data of MYH10
MYH10
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Myosin-10 (Cellular myosin heavy chain, type B; Myosin heavy chain 10; Myosin heavy chain, non-muscle IIb; Non-muscle myosin heavy chain B; NMMHC-B; Non-muscle myosin heavy chain IIb; NMMHC II-b; NMMHC-IIB)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Myosin-10 (Cellular myosin heavy chain, type B; Myosin heavy chain 10; Myosin heavy chain, non-muscle IIb; Non-muscle myosin heavy chain B; NMMHC-B; Non-muscle myosin heavy chain IIb; NMMHC II-b; NMMHC-IIB)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Comments
Isoform P35580-2 was detected.
Isoform P35580-2 was detected.
UniProt
P35580
ID MYH10_HUMAN Reviewed; 1976 AA.
AC P35580; F8VTL3; Q12989; Q149N3; Q149N4; Q16087; Q4LE45; Q6PK16;
read moreDT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 3.
DT 22-JAN-2014, entry version 141.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT cytotoxic T 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.,
RA Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.;
RT "Preparation of a set of expression-ready clones of mammalian long
RT cDNAs 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.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA 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
RT the 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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
RT project: 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;
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
RT on different chromosomes.";
RL Circ. Res. 69:530-539(1991).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 211-301 (ISOFORM 2), ALTERNATIVE
RP SPLICING (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;
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
RT for vascular development and atherosclerosis.";
RL Circ. Res. 73:1000-1012(1993).
RN [10]
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [11]
RP INTERACTION WITH PLEKHG6.
RX PubMed=16721066;
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 [12]
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,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1939; SER-1952 AND
RP SER-1956, AND MASS SPECTROMETRY.
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1956, AND MASS
RP SPECTROMETRY.
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
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [15]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1939 AND SER-1956, AND
RP MASS SPECTROMETRY.
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 [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-442 AND LYS-1645, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [18]
RP INTERACTION WITH ECM29.
RX PubMed=20682791; DOI=10.1074/jbc.M110.154120;
RA Gorbea C., Pratt G., Ustrell V., Bell R., Sahasrabudhe S.,
RA Hughes R.E., 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 [19]
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 [20]
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
RT of lamellipodia extension during cell spreading.";
RL PLoS ONE 5:E8560-E8560(2010).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1956, PHOSPHORYLATION
RP [LARGE SCALE ANALYSIS] AT SER-214 (ISOFORMS 2 AND 4), AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [22]
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.,
RA Buerckstuemmer T., 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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1145; SER-1938 AND
RP SER-1956, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214 (ISOFORMS
RP 2 AND 4), AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [24]
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
RT controls lamellipodia formation in colon epithelial cells.";
RL Biochim. Biophys. Acta 1823:1058-1067(2012).
CC -!- FUNCTION: Cellular myosin that appears to play a role in
CC cytokinesis, cell shape, and specialized functions such as
CC secretion and capping. Involved with LARP6 in the stabilization of
CC type I collagen mRNAs for CO1A1 and CO1A2. During cell spreading,
CC plays an important role in cytoskeleton reorganization, focal
CC contacts formation (in the central part but not the margins of
CC spreading cells), and lamellipodial extension; this function is
CC mechanically antagonized by MYH9.
CC -!- SUBUNIT: 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). Interacts with PLEKHG6.
CC Interacts with ECM29. Interacts with KIF26B (By similarity).
CC Interacts with LARP6. Interacts with MCC.
CC -!- SUBCELLULAR LOCATION: Cell projection, lamellipodium.
CC Note=Colocalizes with MCC at the leading edge of migrating cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P35580-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P35580-2; Sequence=VSP_022013;
CC Note=Contains a phosphoserine at position 214;
CC Name=3;
CC IsoId=P35580-3; Sequence=VSP_022014;
CC Name=4;
CC IsoId=P35580-4; Sequence=VSP_046033, VSP_022014;
CC Note=No experimental confirmation available. Contains a
CC phosphoserine at position 214;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed in cerebellum and
CC spinal chord. Isoform 2 is expressed in cerebrum and retina.
CC Isoform 3 is expressed in the cerebrum and to a much lower extent
CC in cerebellum.
CC -!- DOMAIN: The rodlike tail sequence is highly repetitive, showing
CC cycles of a 28-residue repeat pattern composed of 4 heptapeptides,
CC characteristic for alpha-helical coiled coils.
CC -!- PTM: Phosphorylated by ABL2 (By similarity).
CC -!- SIMILARITY: Contains 1 IQ domain.
CC -!- SIMILARITY: Contains 1 myosin head-like domain.
CC -!- CAUTION: Represents a conventional non-muscle myosin. This protein
CC should not be confused with the unconventional myosin-10 (MYO10).
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE06108.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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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; EAW90049.1; -; Genomic_DNA.
DR EMBL; BC008968; AAH08968.1; -; mRNA.
DR EMBL; BC117690; AAI17691.1; -; mRNA.
DR EMBL; BC117691; AAI17692.1; -; mRNA.
DR EMBL; U15618; AAA87712.1; -; mRNA.
DR EMBL; S67247; AAB28952.1; -; mRNA.
DR PIR; A59252; A59252.
DR PIR; I65769; I65769.
DR RefSeq; NP_001242941.1; NM_001256012.1.
DR RefSeq; NP_001243024.1; NM_001256095.1.
DR RefSeq; NP_005955.3; NM_005964.3.
DR RefSeq; XP_005256708.1; XM_005256651.1.
DR RefSeq; XP_005256709.1; XM_005256652.1.
DR UniGene; Hs.16355; -.
DR ProteinModelPortal; P35580; -.
DR SMR; P35580; 7-963.
DR DIP; DIP-31110N; -.
DR IntAct; P35580; 17.
DR MINT; MINT-7901694; -.
DR STRING; 9606.ENSP00000269243; -.
DR PhosphoSite; P35580; -.
DR DMDM; 215274129; -.
DR PaxDb; P35580; -.
DR PRIDE; P35580; -.
DR Ensembl; ENST00000269243; ENSP00000269243; ENSG00000133026.
DR Ensembl; ENST00000360416; ENSP00000353590; ENSG00000133026.
DR Ensembl; ENST00000396239; ENSP00000379539; ENSG00000133026.
DR GeneID; 4628; -.
DR KEGG; hsa:4628; -.
DR UCSC; uc002glm.4; human.
DR CTD; 4628; -.
DR GeneCards; GC17M008318; -.
DR H-InvDB; HIX0013525; -.
DR HGNC; HGNC:7568; MYH10.
DR HPA; CAB017180; -.
DR MIM; 160776; gene.
DR neXtProt; NX_P35580; -.
DR PharmGKB; PA31366; -.
DR eggNOG; COG5022; -.
DR HOGENOM; HOG000173958; -.
DR HOVERGEN; HBG004704; -.
DR KO; K10352; -.
DR OMA; ASNMESQ; -.
DR PhylomeDB; P35580; -.
DR Reactome; REACT_111045; Developmental Biology.
DR ChiTaRS; MYH10; human.
DR GeneWiki; MYH10; -.
DR GenomeRNAi; 4628; -.
DR NextBio; 17814; -.
DR PRO; PR:P35580; -.
DR ArrayExpress; P35580; -.
DR Bgee; P35580; -.
DR CleanEx; HS_MYH10; -.
DR Genevestigator; P35580; -.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; IDA:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
DR GO; GO:0030426; C:growth cone; IEA:Ensembl.
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:0016460; C:myosin II complex; IEA:Ensembl.
DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0005819; C:spindle; IEA:Ensembl.
DR GO; GO:0001725; C:stress fiber; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IDA:MGI.
DR GO; GO:0030898; F:actin-dependent ATPase activity; IDA:MGI.
DR GO; GO:0043531; F:ADP binding; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; NAS:UniProtKB.
DR GO; GO:0000146; F:microfilament motor activity; IDA:MGI.
DR GO; GO:0030048; P:actin filament-based movement; IDA:MGI.
DR GO; GO:0007512; P:adult heart development; IEA:Ensembl.
DR GO; GO:0007411; P:axon guidance; TAS:Reactome.
DR GO; GO:0055003; P:cardiac myofibril assembly; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
DR GO; GO:0021680; P:cerebellar Purkinje cell layer development; IEA:Ensembl.
DR GO; GO:0006887; P:exocytosis; IEA:Ensembl.
DR GO; GO:0021592; P:fourth ventricle development; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0021670; P:lateral ventricle development; IEA:Ensembl.
DR GO; GO:0000281; P:mitotic cytokinesis; IDA:MGI.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
DR GO; GO:0001764; P:neuron migration; IEA:Ensembl.
DR GO; GO:0007097; P:nuclear migration; IEA:Ensembl.
DR GO; GO:0001778; P:plasma membrane repair; IEA:Ensembl.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR GO; GO:0006930; P:substrate-dependent cell migration, cell extension; IEA:Ensembl.
DR GO; GO:0021678; P:third ventricle development; IEA:Ensembl.
DR GO; GO:0055015; P:ventricular cardiac muscle cell development; IEA:Ensembl.
DR Gene3D; 4.10.270.10; -; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR027401; Myosin-like_IQ_dom.
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; SSF50084; SSF50084; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50096; IQ; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Alternative splicing; ATP-binding;
KW Calmodulin-binding; Cell adhesion; Cell projection; Cell shape;
KW Coiled coil; Complete proteome; Motor protein; Myosin;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1 1976 Myosin-10.
FT /FTId=PRO_0000123421.
FT DOMAIN 2 785 Myosin head-like.
FT DOMAIN 786 815 IQ.
FT NP_BIND 178 185 ATP (Potential).
FT COILED 845 1976 Potential.
FT MOD_RES 442 442 N6-acetyllysine.
FT MOD_RES 1145 1145 Phosphoserine.
FT MOD_RES 1645 1645 N6-acetyllysine.
FT MOD_RES 1938 1938 Phosphoserine.
FT MOD_RES 1939 1939 Phosphoserine.
FT MOD_RES 1952 1952 Phosphoserine.
FT MOD_RES 1956 1956 Phosphoserine.
FT VAR_SEQ 211 211 P -> PQESPKPVKHQSGSLLY (in isoform 2).
FT /FTId=VSP_022013.
FT VAR_SEQ 211 211 P -> PQESPKPVKHQ (in isoform 4).
FT /FTId=VSP_046033.
FT VAR_SEQ 621 621 D -> DEIQNIQRASFYDSVSGLHEPP (in isoform 3
FT and isoform 4).
FT /FTId=VSP_022014.
FT CONFLICT 800 800 Y -> C (in Ref. 1; AAA99177).
FT CONFLICT 943 944 NE -> KK (in Ref. 5; AAH08968).
FT CONFLICT 1429 1429 L -> P (in Ref. 5; AAI17691).
FT CONFLICT 1751 1751 N -> D (in Ref. 9; AAB28952).
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
//
ID MYH10_HUMAN Reviewed; 1976 AA.
AC P35580; F8VTL3; Q12989; Q149N3; Q149N4; Q16087; Q4LE45; Q6PK16;
read moreDT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 3.
DT 22-JAN-2014, entry version 141.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT cytotoxic T 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.,
RA Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.;
RT "Preparation of a set of expression-ready clones of mammalian long
RT cDNAs 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.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA 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
RT the 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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
RT project: 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;
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
RT on different chromosomes.";
RL Circ. Res. 69:530-539(1991).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 211-301 (ISOFORM 2), ALTERNATIVE
RP SPLICING (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;
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
RT for vascular development and atherosclerosis.";
RL Circ. Res. 73:1000-1012(1993).
RN [10]
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [11]
RP INTERACTION WITH PLEKHG6.
RX PubMed=16721066;
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 [12]
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,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1939; SER-1952 AND
RP SER-1956, AND MASS SPECTROMETRY.
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1956, AND MASS
RP SPECTROMETRY.
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
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [15]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1939 AND SER-1956, AND
RP MASS SPECTROMETRY.
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 [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-442 AND LYS-1645, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [18]
RP INTERACTION WITH ECM29.
RX PubMed=20682791; DOI=10.1074/jbc.M110.154120;
RA Gorbea C., Pratt G., Ustrell V., Bell R., Sahasrabudhe S.,
RA Hughes R.E., 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 [19]
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 [20]
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
RT of lamellipodia extension during cell spreading.";
RL PLoS ONE 5:E8560-E8560(2010).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1956, PHOSPHORYLATION
RP [LARGE SCALE ANALYSIS] AT SER-214 (ISOFORMS 2 AND 4), AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [22]
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.,
RA Buerckstuemmer T., 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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1145; SER-1938 AND
RP SER-1956, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214 (ISOFORMS
RP 2 AND 4), AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [24]
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
RT controls lamellipodia formation in colon epithelial cells.";
RL Biochim. Biophys. Acta 1823:1058-1067(2012).
CC -!- FUNCTION: Cellular myosin that appears to play a role in
CC cytokinesis, cell shape, and specialized functions such as
CC secretion and capping. Involved with LARP6 in the stabilization of
CC type I collagen mRNAs for CO1A1 and CO1A2. During cell spreading,
CC plays an important role in cytoskeleton reorganization, focal
CC contacts formation (in the central part but not the margins of
CC spreading cells), and lamellipodial extension; this function is
CC mechanically antagonized by MYH9.
CC -!- SUBUNIT: 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). Interacts with PLEKHG6.
CC Interacts with ECM29. Interacts with KIF26B (By similarity).
CC Interacts with LARP6. Interacts with MCC.
CC -!- SUBCELLULAR LOCATION: Cell projection, lamellipodium.
CC Note=Colocalizes with MCC at the leading edge of migrating cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P35580-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P35580-2; Sequence=VSP_022013;
CC Note=Contains a phosphoserine at position 214;
CC Name=3;
CC IsoId=P35580-3; Sequence=VSP_022014;
CC Name=4;
CC IsoId=P35580-4; Sequence=VSP_046033, VSP_022014;
CC Note=No experimental confirmation available. Contains a
CC phosphoserine at position 214;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed in cerebellum and
CC spinal chord. Isoform 2 is expressed in cerebrum and retina.
CC Isoform 3 is expressed in the cerebrum and to a much lower extent
CC in cerebellum.
CC -!- DOMAIN: The rodlike tail sequence is highly repetitive, showing
CC cycles of a 28-residue repeat pattern composed of 4 heptapeptides,
CC characteristic for alpha-helical coiled coils.
CC -!- PTM: Phosphorylated by ABL2 (By similarity).
CC -!- SIMILARITY: Contains 1 IQ domain.
CC -!- SIMILARITY: Contains 1 myosin head-like domain.
CC -!- CAUTION: Represents a conventional non-muscle myosin. This protein
CC should not be confused with the unconventional myosin-10 (MYO10).
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE06108.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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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; EAW90049.1; -; Genomic_DNA.
DR EMBL; BC008968; AAH08968.1; -; mRNA.
DR EMBL; BC117690; AAI17691.1; -; mRNA.
DR EMBL; BC117691; AAI17692.1; -; mRNA.
DR EMBL; U15618; AAA87712.1; -; mRNA.
DR EMBL; S67247; AAB28952.1; -; mRNA.
DR PIR; A59252; A59252.
DR PIR; I65769; I65769.
DR RefSeq; NP_001242941.1; NM_001256012.1.
DR RefSeq; NP_001243024.1; NM_001256095.1.
DR RefSeq; NP_005955.3; NM_005964.3.
DR RefSeq; XP_005256708.1; XM_005256651.1.
DR RefSeq; XP_005256709.1; XM_005256652.1.
DR UniGene; Hs.16355; -.
DR ProteinModelPortal; P35580; -.
DR SMR; P35580; 7-963.
DR DIP; DIP-31110N; -.
DR IntAct; P35580; 17.
DR MINT; MINT-7901694; -.
DR STRING; 9606.ENSP00000269243; -.
DR PhosphoSite; P35580; -.
DR DMDM; 215274129; -.
DR PaxDb; P35580; -.
DR PRIDE; P35580; -.
DR Ensembl; ENST00000269243; ENSP00000269243; ENSG00000133026.
DR Ensembl; ENST00000360416; ENSP00000353590; ENSG00000133026.
DR Ensembl; ENST00000396239; ENSP00000379539; ENSG00000133026.
DR GeneID; 4628; -.
DR KEGG; hsa:4628; -.
DR UCSC; uc002glm.4; human.
DR CTD; 4628; -.
DR GeneCards; GC17M008318; -.
DR H-InvDB; HIX0013525; -.
DR HGNC; HGNC:7568; MYH10.
DR HPA; CAB017180; -.
DR MIM; 160776; gene.
DR neXtProt; NX_P35580; -.
DR PharmGKB; PA31366; -.
DR eggNOG; COG5022; -.
DR HOGENOM; HOG000173958; -.
DR HOVERGEN; HBG004704; -.
DR KO; K10352; -.
DR OMA; ASNMESQ; -.
DR PhylomeDB; P35580; -.
DR Reactome; REACT_111045; Developmental Biology.
DR ChiTaRS; MYH10; human.
DR GeneWiki; MYH10; -.
DR GenomeRNAi; 4628; -.
DR NextBio; 17814; -.
DR PRO; PR:P35580; -.
DR ArrayExpress; P35580; -.
DR Bgee; P35580; -.
DR CleanEx; HS_MYH10; -.
DR Genevestigator; P35580; -.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; IDA:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
DR GO; GO:0030426; C:growth cone; IEA:Ensembl.
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:0016460; C:myosin II complex; IEA:Ensembl.
DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0005819; C:spindle; IEA:Ensembl.
DR GO; GO:0001725; C:stress fiber; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IDA:MGI.
DR GO; GO:0030898; F:actin-dependent ATPase activity; IDA:MGI.
DR GO; GO:0043531; F:ADP binding; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; NAS:UniProtKB.
DR GO; GO:0000146; F:microfilament motor activity; IDA:MGI.
DR GO; GO:0030048; P:actin filament-based movement; IDA:MGI.
DR GO; GO:0007512; P:adult heart development; IEA:Ensembl.
DR GO; GO:0007411; P:axon guidance; TAS:Reactome.
DR GO; GO:0055003; P:cardiac myofibril assembly; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
DR GO; GO:0021680; P:cerebellar Purkinje cell layer development; IEA:Ensembl.
DR GO; GO:0006887; P:exocytosis; IEA:Ensembl.
DR GO; GO:0021592; P:fourth ventricle development; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0021670; P:lateral ventricle development; IEA:Ensembl.
DR GO; GO:0000281; P:mitotic cytokinesis; IDA:MGI.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
DR GO; GO:0001764; P:neuron migration; IEA:Ensembl.
DR GO; GO:0007097; P:nuclear migration; IEA:Ensembl.
DR GO; GO:0001778; P:plasma membrane repair; IEA:Ensembl.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR GO; GO:0006930; P:substrate-dependent cell migration, cell extension; IEA:Ensembl.
DR GO; GO:0021678; P:third ventricle development; IEA:Ensembl.
DR GO; GO:0055015; P:ventricular cardiac muscle cell development; IEA:Ensembl.
DR Gene3D; 4.10.270.10; -; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR027401; Myosin-like_IQ_dom.
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; SSF50084; SSF50084; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50096; IQ; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Alternative splicing; ATP-binding;
KW Calmodulin-binding; Cell adhesion; Cell projection; Cell shape;
KW Coiled coil; Complete proteome; Motor protein; Myosin;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1 1976 Myosin-10.
FT /FTId=PRO_0000123421.
FT DOMAIN 2 785 Myosin head-like.
FT DOMAIN 786 815 IQ.
FT NP_BIND 178 185 ATP (Potential).
FT COILED 845 1976 Potential.
FT MOD_RES 442 442 N6-acetyllysine.
FT MOD_RES 1145 1145 Phosphoserine.
FT MOD_RES 1645 1645 N6-acetyllysine.
FT MOD_RES 1938 1938 Phosphoserine.
FT MOD_RES 1939 1939 Phosphoserine.
FT MOD_RES 1952 1952 Phosphoserine.
FT MOD_RES 1956 1956 Phosphoserine.
FT VAR_SEQ 211 211 P -> PQESPKPVKHQSGSLLY (in isoform 2).
FT /FTId=VSP_022013.
FT VAR_SEQ 211 211 P -> PQESPKPVKHQ (in isoform 4).
FT /FTId=VSP_046033.
FT VAR_SEQ 621 621 D -> DEIQNIQRASFYDSVSGLHEPP (in isoform 3
FT and isoform 4).
FT /FTId=VSP_022014.
FT CONFLICT 800 800 Y -> C (in Ref. 1; AAA99177).
FT CONFLICT 943 944 NE -> KK (in Ref. 5; AAH08968).
FT CONFLICT 1429 1429 L -> P (in Ref. 5; AAI17691).
FT CONFLICT 1751 1751 N -> D (in Ref. 9; AAB28952).
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
//
MIM
160776
*RECORD*
*FIELD* NO
160776
*FIELD* TI
*160776 MYOSIN, HEAVY CHAIN 10, NONMUSCLE; MYH10
;;CELLULAR MYOSIN HEAVY CHAIN, TYPE B;;
read moreMYOSIN, HEAVY CHAIN, NONMUSCLE, TYPE B; NMMHCB;;
NONMUSCLE MYOSIN IIB;;
NMHC IIB
*FIELD* TX
CLONING
Simons et al. (1991) cloned cDNAs encoding 2 different human nonmuscle
myosin heavy chains, which they designated NMMHCA (MYH9; 160775) and
NMMHCB. Both mRNAs were 7.5 kb long.
By Northern blot analysis, D'Apolito et al. (2002) found that Myh10 was
abundantly expressed in mouse brain and testis. It was also expressed in
heart, lung, liver, and kidney, but not in skeletal muscle or spleen.
GENE FUNCTION
Completion of cell division during cytokinesis requires temporally and
spatially regulated communication from the microtubule cytoskeleton to
the actin cytoskeleton and the cell membrane. Straight et al. (2003)
identified a specific inhibitor of nonmuscle myosin II, blebbistatin,
that inhibited contraction of the cleavage furrow without disrupting
mitosis or contractile ring assembly. Using blebbistatin and other
drugs, Straight et al. (2003) showed that exit from the cytokinetic
phase of the cell cycle depends on ubiquitin-mediated proteolysis.
Continuous signals from microtubules are required to maintain the
position of the cleavage furrow, and these signals control the
localization of myosin II independently of other furrow components.
Turney and Bridgman (2005) found that Myh10 was required by embryonic
rat peripheral nerve growth cones to turn at borders of laminin (see
LAMA2; 156225) stripes in response to signals from laminin-activated
integrin receptors. In the absence of Myh10, neurite outgrowth continued
across laminin borders.
Kim et al. (2005) found that actin-activated MgATPase activity was
decreased in MYH10 with either an asn97-to-lysine (N97K) substitution,
which is homologous to the N93K mutation in MYH9 (160775.0003) that
causes May-Hegglin anomaly (155100), or an arg709-to-cysteine (R709C)
substitution, which causes developmental defects in brain and heart when
present in mouse Myh10. The ability of MYH10 heavy meromyosin to support
the movement of actin filaments over an MYH10-coated surface was reduced
in heavy meromyosin with the N97K mutation and eliminated with the R709C
mutation. Kinetic analysis indicated that the R709C mutation resulted in
extremely tight affinity between MYH10 heavy meromyosin and ADP,
reducing the rate of ADP release.
Ryu et al. (2006) showed that Myh10 was enriched in the postsynaptic
density of rat hippocampal neurons and was essential for normal spine
morphology and dynamics. Pharmacologic or genetic inhibition of Myh10
altered protrusive motility of spines, destabilized their mushroom-head
morphology, and impaired excitatory synaptic transmission.
Using immunofluorescence microscopy, Western blot analysis, and
knockdown strategies with human lung fibroblasts, Hanisch et al. (2011)
showed that Salmonella entered nonphagocytic cells by manipulating 2
machineries of actin-based motility in the host: actin polymerization
through the ARP2/3 complex (604221), and actomyosin-mediated
contractility in a myosin IIA- and myosin IIB-dependent manner. Hanisch
et al. (2011) concluded that Salmonella entry can be effected
independently of membrane ruffling.
MAPPING
By study of hybrid panels and by in situ hybridization, Simons et al.
(1991) localized the MYH10 gene to chromosome 17p13. The assignment is
shared by several other skeletal muscle heavy chain genes.
ANIMAL MODEL
Takeda et al. (2003) studied the development of myocytes in
Myh10-ablated mice. They found that homozygous null mice had 70% fewer,
but larger, myocytes than heterozygous and wildtype mice, with a marked
increase in binucleation. Mice homozygous for an R709C mutation in the
Myh10 gene also showed an increase in binucleation and cell size, but
mice expressing as little as 6% of the normal amount of wildtype Myh10
in the heart did not show these abnormalities. The authors concluded
that these findings were consistent with the occurrence of karyokinesis
in the absence of cytokinesis, and that the increase in cyclin D2
(CCND2; 123833) and D3 (CCND3; 123834) seen in both Myh10 homozygous
null and homozygous R709C mutant mice reflected an abnormality in
earlier steps in the cell cycle.
*FIELD* RF
1. D'Apolito, M.; Guarnieri, V.; Boncristiano, M.; Zelante, L.; Savoia,
A.: Cloning of the murine non-muscle myosin heavy chain IIA gene
ortholog of human MYH9 responsible for May-Hegglin, Sebastian, Fechtner,
and Epstein syndromes. Gene 286: 215-222, 2002.
2. Hanisch, J.; Kolm, R.; Wozniczka, M.; Bumann, D.; Rottner, K.;
Stradal, T. E. B.: Activation of a RhoA/myosin II-dependent but Arp2/3
complex-independent pathway facilitates Salmonella invasion. Cell
Host Microbe 9: 273-285, 2011.
3. Kim, K.-Y.; Kovacs, M.; Kawamoto, S.; Sellers, J. R.; Adelstein,
R. S.: Disease-associated mutations and alternative splicing alter
the enzymatic and motile activity of nonmuscle myosins II-B and II-C. J.
Biol. Chem. 280: 22769-22775, 2005.
4. Ryu, J.; Liu, L.; Wong, T. P.; Wu, D. C.; Burette, A.; Weinberg,
R.; Wang, Y. T.; Sheng, M.: A critical role for myosin IIB in dendritic
spine morphology and synaptic function. Neuron 49: 175-182, 2006.
5. Simons, M.; Wang, M.; McBride, O. W.; Kawamoto, S.; Yamakawa, K.;
Gdula, D.; Adelstein, R. S.; Weir, L.: Human nonmuscle myosin heavy
chains are encoded by two genes located on different chromosomes. Circulation
Res. 69: 530-539, 1991.
6. Straight, A. F.; Cheung, A.; Limouze, J.; Chen, I.; Westwood, N.
J.; Sellers, J. R.; Mitchison, T. J.: Dissecting temporal and spatial
control of cytokinesis with a myosin II inhibitor. Science 299:
1743-1747, 2003.
7. Takeda, K.; Kishi, H.; Ma, X.; Yu, Z.-X.; Adelstein, R. S.: Ablation
and mutation of nonmuscle myosin heavy chain II-B results in a defect
in cardiac myocyte cytokinesis. Circ. Res. 93: 330-337, 2003.
8. Turney, S. G.; Bridgman, P. C.: Laminin stimulates and guides
axonal outgrowth via growth cone myosin II activity. Nature Neurosci. 8:
717-719, 2005.
*FIELD* CN
Paul J. Converse - updated: 3/1/2012
Patricia A. Hartz - updated: 4/25/2007
Patricia A. Hartz - updated: 2/9/2006
Ada Hamosh - updated: 4/3/2003
*FIELD* CD
Victor A. McKusick: 12/14/1992
*FIELD* ED
mgross: 03/02/2012
terry: 3/1/2012
alopez: 3/12/2009
terry: 3/10/2009
wwang: 4/25/2007
mgross: 3/9/2006
terry: 2/9/2006
alopez: 4/7/2003
terry: 4/3/2003
alopez: 4/30/1999
mimadm: 4/14/1994
carol: 12/14/1992
*RECORD*
*FIELD* NO
160776
*FIELD* TI
*160776 MYOSIN, HEAVY CHAIN 10, NONMUSCLE; MYH10
;;CELLULAR MYOSIN HEAVY CHAIN, TYPE B;;
read moreMYOSIN, HEAVY CHAIN, NONMUSCLE, TYPE B; NMMHCB;;
NONMUSCLE MYOSIN IIB;;
NMHC IIB
*FIELD* TX
CLONING
Simons et al. (1991) cloned cDNAs encoding 2 different human nonmuscle
myosin heavy chains, which they designated NMMHCA (MYH9; 160775) and
NMMHCB. Both mRNAs were 7.5 kb long.
By Northern blot analysis, D'Apolito et al. (2002) found that Myh10 was
abundantly expressed in mouse brain and testis. It was also expressed in
heart, lung, liver, and kidney, but not in skeletal muscle or spleen.
GENE FUNCTION
Completion of cell division during cytokinesis requires temporally and
spatially regulated communication from the microtubule cytoskeleton to
the actin cytoskeleton and the cell membrane. Straight et al. (2003)
identified a specific inhibitor of nonmuscle myosin II, blebbistatin,
that inhibited contraction of the cleavage furrow without disrupting
mitosis or contractile ring assembly. Using blebbistatin and other
drugs, Straight et al. (2003) showed that exit from the cytokinetic
phase of the cell cycle depends on ubiquitin-mediated proteolysis.
Continuous signals from microtubules are required to maintain the
position of the cleavage furrow, and these signals control the
localization of myosin II independently of other furrow components.
Turney and Bridgman (2005) found that Myh10 was required by embryonic
rat peripheral nerve growth cones to turn at borders of laminin (see
LAMA2; 156225) stripes in response to signals from laminin-activated
integrin receptors. In the absence of Myh10, neurite outgrowth continued
across laminin borders.
Kim et al. (2005) found that actin-activated MgATPase activity was
decreased in MYH10 with either an asn97-to-lysine (N97K) substitution,
which is homologous to the N93K mutation in MYH9 (160775.0003) that
causes May-Hegglin anomaly (155100), or an arg709-to-cysteine (R709C)
substitution, which causes developmental defects in brain and heart when
present in mouse Myh10. The ability of MYH10 heavy meromyosin to support
the movement of actin filaments over an MYH10-coated surface was reduced
in heavy meromyosin with the N97K mutation and eliminated with the R709C
mutation. Kinetic analysis indicated that the R709C mutation resulted in
extremely tight affinity between MYH10 heavy meromyosin and ADP,
reducing the rate of ADP release.
Ryu et al. (2006) showed that Myh10 was enriched in the postsynaptic
density of rat hippocampal neurons and was essential for normal spine
morphology and dynamics. Pharmacologic or genetic inhibition of Myh10
altered protrusive motility of spines, destabilized their mushroom-head
morphology, and impaired excitatory synaptic transmission.
Using immunofluorescence microscopy, Western blot analysis, and
knockdown strategies with human lung fibroblasts, Hanisch et al. (2011)
showed that Salmonella entered nonphagocytic cells by manipulating 2
machineries of actin-based motility in the host: actin polymerization
through the ARP2/3 complex (604221), and actomyosin-mediated
contractility in a myosin IIA- and myosin IIB-dependent manner. Hanisch
et al. (2011) concluded that Salmonella entry can be effected
independently of membrane ruffling.
MAPPING
By study of hybrid panels and by in situ hybridization, Simons et al.
(1991) localized the MYH10 gene to chromosome 17p13. The assignment is
shared by several other skeletal muscle heavy chain genes.
ANIMAL MODEL
Takeda et al. (2003) studied the development of myocytes in
Myh10-ablated mice. They found that homozygous null mice had 70% fewer,
but larger, myocytes than heterozygous and wildtype mice, with a marked
increase in binucleation. Mice homozygous for an R709C mutation in the
Myh10 gene also showed an increase in binucleation and cell size, but
mice expressing as little as 6% of the normal amount of wildtype Myh10
in the heart did not show these abnormalities. The authors concluded
that these findings were consistent with the occurrence of karyokinesis
in the absence of cytokinesis, and that the increase in cyclin D2
(CCND2; 123833) and D3 (CCND3; 123834) seen in both Myh10 homozygous
null and homozygous R709C mutant mice reflected an abnormality in
earlier steps in the cell cycle.
*FIELD* RF
1. D'Apolito, M.; Guarnieri, V.; Boncristiano, M.; Zelante, L.; Savoia,
A.: Cloning of the murine non-muscle myosin heavy chain IIA gene
ortholog of human MYH9 responsible for May-Hegglin, Sebastian, Fechtner,
and Epstein syndromes. Gene 286: 215-222, 2002.
2. Hanisch, J.; Kolm, R.; Wozniczka, M.; Bumann, D.; Rottner, K.;
Stradal, T. E. B.: Activation of a RhoA/myosin II-dependent but Arp2/3
complex-independent pathway facilitates Salmonella invasion. Cell
Host Microbe 9: 273-285, 2011.
3. Kim, K.-Y.; Kovacs, M.; Kawamoto, S.; Sellers, J. R.; Adelstein,
R. S.: Disease-associated mutations and alternative splicing alter
the enzymatic and motile activity of nonmuscle myosins II-B and II-C. J.
Biol. Chem. 280: 22769-22775, 2005.
4. Ryu, J.; Liu, L.; Wong, T. P.; Wu, D. C.; Burette, A.; Weinberg,
R.; Wang, Y. T.; Sheng, M.: A critical role for myosin IIB in dendritic
spine morphology and synaptic function. Neuron 49: 175-182, 2006.
5. Simons, M.; Wang, M.; McBride, O. W.; Kawamoto, S.; Yamakawa, K.;
Gdula, D.; Adelstein, R. S.; Weir, L.: Human nonmuscle myosin heavy
chains are encoded by two genes located on different chromosomes. Circulation
Res. 69: 530-539, 1991.
6. Straight, A. F.; Cheung, A.; Limouze, J.; Chen, I.; Westwood, N.
J.; Sellers, J. R.; Mitchison, T. J.: Dissecting temporal and spatial
control of cytokinesis with a myosin II inhibitor. Science 299:
1743-1747, 2003.
7. Takeda, K.; Kishi, H.; Ma, X.; Yu, Z.-X.; Adelstein, R. S.: Ablation
and mutation of nonmuscle myosin heavy chain II-B results in a defect
in cardiac myocyte cytokinesis. Circ. Res. 93: 330-337, 2003.
8. Turney, S. G.; Bridgman, P. C.: Laminin stimulates and guides
axonal outgrowth via growth cone myosin II activity. Nature Neurosci. 8:
717-719, 2005.
*FIELD* CN
Paul J. Converse - updated: 3/1/2012
Patricia A. Hartz - updated: 4/25/2007
Patricia A. Hartz - updated: 2/9/2006
Ada Hamosh - updated: 4/3/2003
*FIELD* CD
Victor A. McKusick: 12/14/1992
*FIELD* ED
mgross: 03/02/2012
terry: 3/1/2012
alopez: 3/12/2009
terry: 3/10/2009
wwang: 4/25/2007
mgross: 3/9/2006
terry: 2/9/2006
alopez: 4/7/2003
terry: 4/3/2003
alopez: 4/30/1999
mimadm: 4/14/1994
carol: 12/14/1992