MYO1C

MYO1C
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4BYF
Identifiers
Aliases	MYO1C, MMI-beta, MMIb, NMI, myr2, myosin IC
External IDs	MGI: 106612 HomoloGene: 32046 GeneCards: MYO1C
Gene ontology Molecular function • protein C-terminus binding • nucleotide binding • actin binding • receptor binding • motor activity • calmodulin binding • actin-dependent ATPase activity • ATP binding • Ral GTPase binding • protein binding • microfilament motor activity Cellular component • extracellular exosome • filamentous actin • brush border • nucleolus • cytoplasm • nuclear pore • cell projection • cytosol • nucleus • stress fiber • stereocilium • unconventional myosin complex • cytoplasmic, membrane-bounded vesicle • microvillus • basal plasma membrane • membrane • myosin I complex • ruffle • membrane raft • plasma membrane • myosin complex • cytoplasmic vesicle • stereocilium membrane • lateral plasma membrane • nucleoplasm • ruffle membrane Biological process • Fc-gamma receptor signaling pathway involved in phagocytosis • positive regulation of protein targeting to membrane • positive regulation of cell migration by vascular endothelial growth factor signaling pathway • positive regulation of gene expression, epigenetic • positive regulation of cell migration • protein targeting • regulation of bicellular tight junction assembly • transport • protein transport • protein targeting to membrane • mRNA transport • positive regulation of vascular endothelial growth factor signaling pathway • positive regulation of cellular response to insulin stimulus • positive regulation of actin filament polymerization • metabolic process Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	4641	17913
Ensembl	ENSG00000197879	ENSMUSG00000017774
UniProt	O00159	Q9WTI7
RefSeq (mRNA)	NM_033375 NM_001080779 NM_001080950	NM_001080774 NM_001080775 NM_008659
RefSeq (protein)	NP_001074248.1 NP_001074419.1 NP_203693.3	NP_001074243.1 NP_001074244.1 NP_032685.1
Location (UCSC)	Chr 17: 1.46 – 1.49 Mb	Chr 11: 75.65 – 75.67 Mb
PubMed search	[1]	[2]
Wikidata

View/Edit Human

View/Edit Mouse

Myosin-Ic is a protein that in humans is encoded by the MYO1C gene.^[3][4]

This gene encodes a member of the unconventional myosin protein family, which are actin-based molecular motors. The protein is found in the cytoplasm, and one isoform with a unique N-terminus is also found in the nucleus. The nuclear isoform associates with RNA polymerase I and II and functions in transcription initiation. The mouse ortholog of this protein also functions in intracellular vesicle transport to the plasma membrane. Multiple transcript variants encoding different isoforms have been found for this gene. The related gene myosin IE has been referred to as myosin IC in the literature, but it is a distinct locus on chromosome 19.^[4]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. Crozet F, el Amraoui A, Blanchard S, Lenoir M, Ripoll C, Vago P, Hamel C, Fizames C, Levi-Acobas F, Depetris D, Mattei MG, Weil D, Pujol R, Petit C (Apr 1997). "Cloning of the genes encoding two murine and human cochlear unconventional type I myosins". Genomics. 40 (2): 332–41. doi:10.1006/geno.1996.4526. PMID 9119401.
4. "Entrez Gene: MYO1C myosin IC".

Further reading

• Ruppert C, Godel J, Müller RT, et al. (1997). "Localization of the rat myosin I molecules myr 1 and myr 2 and in vivo targeting of their tail domains.". J. Cell. Sci. 108 (12): 3775–86. PMID 8719884.
• Hasson T, Skowron JF, Gilbert DJ, et al. (1997). "Mapping of unconventional myosins in mouse and human.". Genomics. 36 (3): 431–9. doi:10.1006/geno.1996.0488. PMID 8884266.
• Skowron JF, Bement WM, Mooseker MS (1999). "Human brush border myosin-I and myosin-Ic expression in human intestine and Caco-2BBe cells.". Cell Motil. Cytoskeleton. 41 (4): 308–24. doi:10.1002/(SICI)1097-0169(1998)41:4<308::AID-CM4>3.0.CO;2-J. PMID 9858156.
• Pestic-Dragovich L, Stojiljkovic L, Philimonenko AA, et al. (2000). "A myosin I isoform in the nucleus.". Science. 290 (5490): 337–41. doi:10.1126/science.290.5490.337. PMID 11030652.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Brandenberger R, Wei H, Zhang S, et al. (2005). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation.". Nat. Biotechnol. 22 (6): 707–16. doi:10.1038/nbt971. PMID 15146197.
• Beausoleil SA, Jedrychowski M, Schwartz D, et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins.". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
• Suzuki Y, Yamashita R, Shirota M, et al. (2004). "Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions.". Genome Res. 14 (9): 1711–8. doi:10.1101/gr.2435604. PMC 515316. PMID 15342556.
• Philimonenko VV, Zhao J, Iben S, et al. (2005). "Nuclear actin and myosin I are required for RNA polymerase I transcription.". Nat. Cell Biol. 6 (12): 1165–72. doi:10.1038/ncb1190. PMID 15558034.
• Kyselá K, Philimonenko AA, Philimonenko VV, et al. (2005). "Nuclear distribution of actin and myosin I depends on transcriptional activity of the cell.". Histochem. Cell Biol. 124 (5): 347–58. doi:10.1007/s00418-005-0042-8. PMID 16133118.
• Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes.". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
• Cavellán E, Asp P, Percipalle P, Farrants AK (2006). "The WSTF-SNF2h chromatin remodeling complex interacts with several nuclear proteins in transcription.". J. Biol. Chem. 281 (24): 16264–71. doi:10.1074/jbc.M600233200. PMID 16603771.
• Cisterna B, Necchi D, Prosperi E, Biggiogera M (2006). "Small ribosomal subunits associate with nuclear myosin and actin in transit to the nuclear pores.". FASEB J. 20 (11): 1901–3. doi:10.1096/fj.05-5278fje. PMID 16877530.
• Kahle M, Pridalová J, Spacek M, et al. (2007). "Nuclear myosin is ubiquitously expressed and evolutionary conserved in vertebrates.". Histochem. Cell Biol. 127 (2): 139–48. doi:10.1007/s00418-006-0231-0. PMID 16957816.
• Hofmann WA, Vargas GM, Ramchandran R, et al. (2006). "Nuclear myosin I is necessary for the formation of the first phosphodiester bond during transcription initiation by RNA polymerase II.". J. Cell. Biochem. 99 (4): 1001–9. doi:10.1002/jcb.21035. PMID 16960872.
• Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
• Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry.". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.