EPB49 Knowpia

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
Gene location (Human)
Chr.	Chromosome 8 (human)
End	22,082,527 bp
Gene location (Mouse)
Chr.	Chromosome 14 (mouse)
End	70,636,048 bp
RNA expression pattern
	Top expressed in
	cingulate gyrus; ; prefrontal cortex; ; Brodmann area 10; ; nucleus accumbens; ; amygdala; ; Brodmann area 9; ; caudate nucleus; ; putamen; ; anterior pituitary; ; frontal pole;
	Top expressed in
	superior frontal gyrus; ; entorhinal cortex; ; primary motor cortex; ; prefrontal cortex; ; olfactory tubercle; ; subiculum; ; superior colliculus; ; dorsal tegmental nucleus; ; inferior colliculus; ; dorsomedial hypothalamic nucleus;
	More reference expression data
	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
	2039
	13829
	ENSG00000158856
	ENSMUSG00000022099
	Q08495
	Q9WV69
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
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
	Wikidata
View/Edit Human	View/Edit Mouse

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

References edit

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000158856 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000022099 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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.
^ 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.
^ "Entrez Gene: EPB49 erythrocyte membrane protein band 4.9 (dematin)".

Further reading edit

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.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000158856 – Ensembl, May 2017

[refGRCm38Ensembl-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.

[pmid8341682-5] 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.

[pmid12011427-6] 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.

[entrez-7] "Entrez Gene: EPB49 erythrocyte membrane protein band 4.9 (dematin)".

[5]

[6]

[7]

[1]

[2]

[3]

[4]

Summary

References edit

Further reading edit