ID MYH10_HUMAN Reviewed; 1976 AA. AC P35580; Q12989; Q149N3; Q16087; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 3. DT 19-JAN-2010, entry version 101. DE RecName: Full=Myosin-10; DE AltName: Full=Myosin heavy chain 10; DE AltName: Full=Myosin heavy chain, non-muscle IIb; DE AltName: Full=Non-muscle myosin heavy chain IIb; DE Short=NMMHC II-b; DE Short=NMMHC-IIB; DE AltName: Full=Cellular myosin heavy chain, type B; DE AltName: Full=Non-muscle myosin heavy chain B; DE Short=NMMHC-B; 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 MEDLINE=96025307; 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 [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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 63-722 (ISOFORM 1). RX MEDLINE=91316803; 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 [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 211-301 (ISOFORM 2), ALTERNATIVE RP SPLICING (ISOFORM 3), AND TISSUE SPECIFICITY. RX MEDLINE=95301542; 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 [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1751-1976. RX MEDLINE=94037315; 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 [7] 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1960, AND MASS RP SPECTROMETRY. RC TISSUE=Epithelium; 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1415, AND MASS RP SPECTROMETRY. RX PubMed=18083107; DOI=10.1016/j.cell.2007.11.025; RA Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., RA Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., RA Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., RA Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., RA Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; RT "Global survey of phosphotyrosine signaling identifies oncogenic RT kinases in lung cancer."; RL Cell 131:1190-1203(2007). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1013, AND MASS RP SPECTROMETRY. 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1956 AND SER-1975, AND RP MASS SPECTROMETRY. RX PubMed=19007248; DOI=10.1021/ac801708p; RA Wang B., Malik R., Nigg E.A., Korner R.; RT "Evaluation of the low-specificity protease elastase for large-scale RT phosphoproteome analysis."; RL Anal. Chem. 80:9526-9533(2008). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1376, AND MASS RP SPECTROMETRY. RX PubMed=18187866; DOI=10.2116/analsci.24.161; RA Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; RT "Automated phosphoproteome analysis for cultured cancer cells by two- RT dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; RL Anal. Sci. 24:161-166(2008). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1939; SER-1952 AND RP SER-1956, AND MASS SPECTROMETRY. 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 [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. RA Colinge J., Superti-Furga G., Bennett K.L.; RL Submitted (OCT-2008) to UniProtKB. RN [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE RP SCALE ANALYSIS] AT THR-1964; SER-1965 AND SER-1975, AND MASS RP SPECTROMETRY. 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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1939; SER-1952 AND RP SER-1956, AND MASS SPECTROMETRY. RC TISSUE=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; LYS-552; LYS-1247 AND RP LYS-1645, AND MASS SPECTROMETRY. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., 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). CC -!- FUNCTION: Cellular myosin that appears to play a role in CC cytokinesis, cell shape, and specialized functions such as CC secretion and capping. 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 -!- INTERACTION: CC Q14164:IKBKE; NbExp=1; IntAct=EBI-351758, EBI-307369; CC Q15334:LLGL1; NbExp=1; IntAct=EBI-351758, EBI-299979; CC P23508:MCC; NbExp=1; IntAct=EBI-351758, EBI-307531; CC Q13177:PAK2; NbExp=1; IntAct=EBI-351758, EBI-1045887; CC Q9Y478:PRKAB1; NbExp=1; IntAct=EBI-351758, EBI-719769; CC Q9UBN6:TNFRSF10D; NbExp=1; IntAct=EBI-351758, EBI-1044859; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; 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 -!- TISSUE SPECIFICITY: In brain, isoform 1 is predominantly CC expresssed in cerebellum and spinal chord, isoform 2 in cerebrum CC and retina; isoform 3 is expressed in the cerebebrum and to a much CC lower extent 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 upon DNA damage, probably by ATM or ATR. CC -!- SIMILARITY: Contains 1 IQ domain. CC -!- SIMILARITY: Contains 1 myosin head-like domain. 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; CH471108; EAW90049.1; -; Genomic_DNA. DR EMBL; BC117691; AAI17692.1; -; mRNA. DR EMBL; U15618; AAA87712.1; -; mRNA. DR EMBL; S67247; AAB28952.1; -; mRNA. DR IPI; IPI00397526; -. DR IPI; IPI00479307; -. DR IPI; IPI00790503; -. DR PIR; A59252; A59252. DR PIR; I65769; I65769. DR RefSeq; NP_005955.1; -. DR UniGene; Hs.16355; -. DR SMR; P35580; 7-815, 26-843, 843-964. DR IntAct; P35580; 19. DR STRING; P35580; -. DR PhosphoSite; P35580; -. DR PRIDE; P35580; -. DR Ensembl; ENST00000269243; ENSP00000269243; ENSG00000133026; Homo sapiens. DR GeneID; 4628; -. DR KEGG; hsa:4628; -. DR CTD; 4628; -. DR GeneCards; GC17M008318; -. DR H-InvDB; HIX0013525; -. DR HGNC; HGNC:7568; MYH10. DR HPA; CAB017180; -. DR MIM; 160776; gene. DR PharmGKB; PA31366; -. DR eggNOG; maNOG15268; -. DR HOVERGEN; P35580; -. DR PhylomeDB; P35580; -. DR Reactome; REACT_18266; Axon guidance. DR NextBio; 17814; -. DR ArrayExpress; P35580; -. DR Bgee; P35580; -. DR CleanEx; HS_MYH10; -. DR Genevestigator; P35580; -. DR GermOnline; ENSG00000133026; Homo sapiens. DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB. DR GO; GO:0032154; C:cleavage furrow; IDA:UniProtKB. DR GO; GO:0030496; C:midbody; IDA:UniProtKB. DR GO; GO:0016459; C:myosin complex; NAS:UniProtKB. 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:0005516; F:calmodulin binding; IEA:UniProtKB-KW. DR GO; GO:0000146; F:microfilament motor activity; IDA:MGI. DR GO; GO:0030048; P:actin filament-based movement; IDA:MGI. DR GO; GO:0000281; P:cytokinesis after mitosis; IDA:MGI. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR InterPro; IPR000048; IQ_CaM_bd_region. DR InterPro; IPR001609; Myosin_head_motor_dom. DR InterPro; IPR004009; Myosin_N. DR InterPro; IPR008989; Myosin_S1_N. DR InterPro; IPR002928; Myosin_tail. 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 PROSITE; PS50096; IQ; 1. PE 1: Evidence at protein level; KW Acetylation; Actin-binding; Alternative splicing; ATP-binding; KW Calmodulin-binding; Cell shape; Coiled coil; Complete proteome; KW Motor protein; Myosin; Nucleotide-binding; Phosphoprotein. FT INIT_MET 1 1 Removed. FT CHAIN 2 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 2 2 N-acetylalanine. FT MOD_RES 442 442 N6-acetyllysine. FT MOD_RES 552 552 N6-acetyllysine. FT MOD_RES 1013 1013 Phosphoserine. FT MOD_RES 1247 1247 N6-acetyllysine. FT MOD_RES 1376 1376 Phosphothreonine. FT MOD_RES 1415 1415 Phosphotyrosine. FT MOD_RES 1645 1645 N6-acetyllysine. FT MOD_RES 1938 1938 Phosphoserine (By similarity). FT MOD_RES 1939 1939 Phosphoserine. FT MOD_RES 1952 1952 Phosphoserine. FT MOD_RES 1956 1956 Phosphoserine. FT MOD_RES 1960 1960 Phosphothreonine. FT MOD_RES 1964 1964 Phosphothreonine. FT MOD_RES 1965 1965 Phosphoserine. FT MOD_RES 1975 1975 Phosphoserine. FT VAR_SEQ 211 211 P -> PQESPKPVKHQSGSLLY (in isoform 2). FT /FTId=VSP_022013. FT VAR_SEQ 621 621 D -> DEIQNIQRASFYDSVSGLHEPP (in isoform FT 3). FT /FTId=VSP_022014. FT CONFLICT 800 800 Y -> C (in Ref. 1; AAA99177). FT CONFLICT 1751 1751 N -> D (in Ref. 6; 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 //