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, MyoIC
External IDs	OMIM: 606538 MGI: 106612 HomoloGene: 32046 GeneCards: MYO1C
Gene location (Human) Chr. Chromosome 17 (human) Band 17p13.3 Start 1,464,186 bp End 1,492,686 bp
Gene location (Mouse) Chr. Chromosome 11 (mouse) Band 11 B5|11 45.92 cM Start 75,541,330 bp End 75,564,736 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right lung tibial nerve subcutaneous adipose tissue popliteal artery gastric mucosa right coronary artery sural nerve abdominal fat stromal cell of endometrium olfactory bulb Top expressed in right lung right lung lobe left lung submandibular gland lacrimal gland parotid gland left lung lobe ascending aorta ankle calvaria More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein C-terminus binding nucleotide binding actin binding signaling receptor binding cytoskeletal motor activity calmodulin binding ATP binding protein binding microfilament motor activity actin filament binding microtubule motor activity microtubule binding Cellular component extracellular exosome filamentous actin brush border nucleolus cytoplasm nuclear pore cell projection cytosol nucleus stress fiber stereocilium unconventional myosin complex microvillus basal plasma membrane membrane myosin I complex ruffle membrane raft plasma membrane myosin complex cytoplasmic vesicle stereocilium membrane lateral plasma membrane ruffle membrane nucleoplasm nuclear body stereocilium bundle cytoplasmic vesicle membrane phagocytic vesicle 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 epigenetic maintenance of chromatin in transcription-competent conformation positive regulation of cell migration protein targeting regulation of bicellular tight junction assembly 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 transport vesicle transport along actin filament cellular response to interferon-gamma microtubule-based movement Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 4641 17913 Ensembl ENSG00000197879 ENSMUSG00000017774 UniProt O00159 Q9WTI7 RefSeq (mRNA) NM_033375 NM_001080779 NM_001080950 NM_001363855 NM_001080774 NM_001080775 NM_008659 NM_001370611 RefSeq (protein) NP_001074248 NP_001074419 NP_203693 NP_001350784 NP_001074243 NP_001074244 NP_032685 NP_001357540 Location (UCSC) Chr 17: 1.46 – 1.49 Mb Chr 11: 75.54 – 75.56 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Myosin-Ic is a protein that in humans is encoded by the MYO1C gene.

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.

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. doi:10.1242/jcs.108.12.3775. 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. Bibcode:2000Sci...290..337P. 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. Bibcode:2002PNAS...9916899M. 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. S2CID 27764390.
• 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. Bibcode:2004PNAS..10112130B. 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. S2CID 6633625.
• 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. S2CID 28731167.
• 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. S2CID 24892289.
• 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. S2CID 23325557.
• 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. S2CID 39237955.
• 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. S2CID 7827573.
• 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.

External links

• Overview of all the structural information available in the PDB for UniProt: O00159 (Unconventional myosin-Ic) at the PDBe-KB.