EPB49

Erythrocyte membrane protein band 4.9 (dematin)
PDB rendering based on 1qzp.
Available structures PDB 1QZP, 1ZV6
Identifiers
Symbols	EPB49; DMT; FLJ78462; FLJ98848
External IDs	OMIM: 125305 MGI: 99670 HomoloGene: 1496 GeneCards: EPB49 Gene
Gene Ontology Molecular function • actin binding Cellular component • nucleus • cytoplasm • actin cytoskeleton • membrane • cortical cytoskeleton Biological process • cytoskeleton organization • actin filament bundle assembly • actin filament capping Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	2039	13829
Ensembl	ENSG00000158856	ENSMUSG00000022099
UniProt	Q08495	Q3TYC5
RefSeq (mRNA)	NM_001114135.2	NM_013514.3
RefSeq (protein)	NP_001107607.1	NP_038542.1
Location (UCSC)	Chr 8: 21.91 – 21.94 Mb	Chr 14: 71 – 71.04 Mb
PubMed search	[1]	[2]

Dematin is a protein that in humans is encoded by the EPB49 gene.

Further reading

• Azim AC, Knoll JH, Beggs AH, Chishti AH (1995). "Isoform cloning, actin binding, and chromosomal localization of human erythroid dematin, a member of the villin superfamily". J. Biol. Chem. 270 (29): 17407–13. doi:10.1074/jbc.270.29.17407. PMID 7615546. 
• Azim AC, Marfatia SM, Korsgren C, et al. (1996). "Human erythrocyte dematin and protein 4.2 (pallidin) are ATP binding proteins". Biochemistry 35 (9): 3001–6. doi:10.1021/bi951745y. PMID 8608138. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Millar JK, Christie S, Porteous DJ (2004). "Yeast two-hybrid screens implicate DISC1 in brain development and function". Biochem. Biophys. Res. Commun. 311 (4): 1019–25. doi:10.1016/j.bbrc.2003.10.101. PMID 14623284. 
• Frank BS, Vardar D, Chishti AH, McKnight CJ (2004). "The NMR structure of dematin headpiece reveals a dynamic loop that is conformationally altered upon phosphorylation at a distal site". J. Biol. Chem. 279 (9): 7909–16. doi:10.1074/jbc.M310524200. PMID 14660664. 
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039. 
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928. 
• Vermeulen W, Van Troys M, Bourry D, et al. (2006). "Identification of the PXW sequence as a structural gatekeeper of the headpiece C-terminal subdomain fold". J. Mol. Biol. 359 (5): 1277–92. doi:10.1016/j.jmb.2006.04.042. PMID 16697408.