// Workers AI · dad joke modeWhat did Dematin say to its date? You're a hair above the rest.

Dmtn
Identifiers
Aliases	AI325486Epb4.9Epb49dematindematin actin binding protein
External IDs	HomoloGene: 1496; GeneCards: ; OMA:- orthologs
Gene location (Human) Chr. Chromosome 14 (human) Band 14 D2|14 36.32 cM Start 70,601,263 bp End 70,636,048 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in primary visual cortex superior frontal gyrus dentate gyrus of hippocampal formation granule cell fetal liver hematopoietic progenitor cell entorhinal cortex perirhinal cortex primary motor cortex prefrontal cortex olfactory tubercle CA3 field n/a More reference expression data BioGPS n/a
Gene ontology Molecular function spectrin binding actin binding signaling receptor binding protein self-association actin filament binding Cellular component cytoplasm cytosol cell projection membrane cortical cytoskeleton plasma membrane platelet dense tubular network membrane cell projection membrane actin filament spectrin-associated cytoskeleton perinuclear region of cytoplasm cytoskeleton endomembrane system postsynaptic density cytoplasmic vesicle actin cytoskeleton Biological process negative regulation of cell-substrate adhesion regulation of lamellipodium assembly cellular response to calcium ion regulation of filopodium assembly actin filament reorganization regulation of actin cytoskeleton organization negative regulation of peptidyl-threonine phosphorylation positive regulation of wound healing positive regulation of substrate adhesion-dependent cell spreading negative regulation of protein targeting to membrane negative regulation of peptidyl-tyrosine phosphorylation positive regulation of blood coagulation calcium-mediated signaling using extracellular calcium source cytoskeleton organization actin filament capping regulation of cell shape negative regulation of peptidyl-serine phosphorylation positive regulation of integrin-mediated signaling pathway protein secretion by platelet negative regulation of substrate adhesion-dependent cell spreading calcium-mediated signaling using intracellular calcium source positive regulation of fibroblast migration negative regulation of focal adhesion assembly actin cytoskeleton organization cellular response to cAMP positive regulation of platelet aggregation erythrocyte development actin filament bundle assembly protein-containing complex assembly lamellipodium assembly Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 13829 n/a Ensembl ENSMUSG00000022099 n/a UniProt Q9WV69 Q9WV69 RefSeq (mRNA) NM_001252662 NM_001252663 NM_001252664 NM_001252665 NM_001252666 NM_013514 NM_001360024 NM_001360025 NM_001360026 NM_001360027 NM_001360028 NM_001360029 NM_001360030 n/a RefSeq (protein) NP_001239591 NP_001239592 NP_001239593 NP_001239594 NP_001239595 NP_038542 NP_001346953 NP_001346954 NP_001346955 NP_001346956 NP_001346957 NP_001346958 NP_001346959 NP_001239591 NP_001239592 NP_001239593 NP_001239594 NP_001239595 NP_038542 NP_001346953 NP_001346954 NP_001346955 NP_001346956 NP_001346957 NP_001346958 NP_001346959 Location (UCSC) Chr 14: 70.6 – 70.64 Mb n/a PubMed search n/a
Wikidata
View/Edit Human

Dematin is a protein that in humans is encoded by the DMTN gene (formerly EPB49). Dematin functions to stabilize the cytoskeleton structure of red blood cells. In particular, it binds to actin, and induces bundling.

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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• 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.
• 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.