EPB49

Dematin is a protein that in humans is encoded by the EPB49 gene.^[5][6][7]

DMTN
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1QZP, 1ZV6
Identifiers
Aliases	DMTN, DMT, EPB49, dematin actin binding protein
External IDs	OMIM: 125305; MGI: 99670; HomoloGene: 1496; GeneCards: DMTN; OMA:DMTN - orthologs
Gene location (Human) Chr. Chromosome 8 (human)[1] Band 8p21.3 Start 22,048,995 bp[1] End 22,082,527 bp[1]
Gene location (Mouse) Chr. Chromosome 14 (mouse)[2] Band 14 D2|14 36.32 cM Start 70,601,263 bp[2] End 70,636,048 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right frontal lobe cingulate gyrus anterior cingulate cortex prefrontal cortex Brodmann area 10 nucleus accumbens amygdala Brodmann area 9 caudate nucleus right hemisphere of cerebellum 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 More reference expression data BioGPS More reference expression data
Gene ontology Molecular function spectrin binding protein 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 actin cytoskeleton spectrin-associated cytoskeleton perinuclear region of cytoplasm endomembrane system cytoskeleton postsynaptic density cytoplasmic vesicle 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 actin filament bundle assembly 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 transmembrane transport 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 positive regulation of platelet aggregation cellular response to cAMP erythrocyte development regulation of cell shape protein-containing complex assembly lamellipodium assembly Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 2039 13829 Ensembl ENSG00000158856 ENSMUSG00000022099 UniProt Q08495 Q9WV69 RefSeq (mRNA) NM_001114135 NM_001114136 NM_001114137 NM_001114138 NM_001114139 NM_001302816 NM_001302817 NM_001978 NM_001323378 NM_001323380 NM_001323381 NM_001323382 NM_001323383 NM_001323384 NM_001323385 NM_001323387 NM_001323388 NM_001323389 NM_001323390 NM_001323391 NM_001323392 NM_001323393 NM_001323394 NM_001323395 NM_001323396 NM_001323397 NM_001323398 NM_001323399 NM_001323400 NM_001323401 NM_001323379 NM_001387723 NM_001387726 NM_001387727 NM_001387728 NM_001387730 NM_001387732 NM_001387734 NM_001387735 NM_001387736 NM_001387737 NM_001387742 NM_001387743 NM_001387744 NM_001387745 NM_001387750 NM_001387751 NM_001387752 NM_001387753 NM_001387754 NM_001387755 NM_001387756 NM_001387757 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 RefSeq (protein) NP_001107607 NP_001107608 NP_001107609 NP_001107610 NP_001107611 NP_001289745 NP_001289746 NP_001310307 NP_001310308 NP_001310309 NP_001310310 NP_001310311 NP_001310312 NP_001310313 NP_001310314 NP_001310316 NP_001310317 NP_001310318 NP_001310319 NP_001310320 NP_001310321 NP_001310322 NP_001310323 NP_001310324 NP_001310325 NP_001310326 NP_001310327 NP_001310328 NP_001310329 NP_001310330 NP_001969 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 8: 22.05 – 22.08 Mb Chr 14: 70.6 – 70.64 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

References

1. GRCh38: Ensembl release 89: ENSG00000158856 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000022099 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Rana AP, Ruff P, Maalouf GJ, Speicher DW, Chishti AH (Aug 1993). "Cloning of human erythroid dematin reveals another member of the villin family". Proc Natl Acad Sci U S A. 90 (14): 6651–5. Bibcode:1993PNAS...90.6651R. doi:10.1073/pnas.90.14.6651. PMC 46990. PMID 8341682.
6. Khanna R, Chang SH, Andrabi S, Azam M, Kim A, Rivera A, Brugnara C, Low PS, Liu SC, Chishti AH (May 2002). "Headpiece domain of dematin is required for the stability of the erythrocyte membrane". Proc Natl Acad Sci U S A. 99 (10): 6637–42. Bibcode:2002PNAS...99.6637K. doi:10.1073/pnas.052155999. PMC 124455. PMID 12011427.
7. "Entrez Gene: EPB49 erythrocyte membrane protein band 4.9 (dematin)".

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.