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Dematin (Dematin actin-binding protein) (Erythrocyte membrane protein band 4.9)

 DEMA_HUMAN              Reviewed;         405 AA.
Q08495; A8K0T5; B3KP70; B3KRH3; B4DI75; E9PEJ0; Q13215; Q9BRE3;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
30-AUG-2002, sequence version 3.
25-OCT-2017, entry version 179.
RecName: Full=Dematin;
AltName: Full=Dematin actin-binding protein;
AltName: Full=Erythrocyte membrane protein band 4.9;
Name=DMTN; Synonyms=DMT, EPB49;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Reticulocyte;
PubMed=8341682; DOI=10.1073/pnas.90.14.6651;
Rana A.P., Ruff P., Maalouf G.J., Speicher D.W., Chishti A.H.;
"Cloning of human erythroid dematin reveals another member of the
villin family.";
Proc. Natl. Acad. Sci. U.S.A. 90:6651-6655(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION BY CAPK,
SUBUNIT, AND ALTERNATIVE SPLICING.
TISSUE=Reticulocyte;
PubMed=7615546; DOI=10.1074/jbc.270.29.17407;
Azim A.C., Knoll J.H.M., Beggs A.H., Chishti A.H.;
"Isoform cloning, actin binding, and chromosomal localization of human
erythroid dematin, a member of the villin superfamily.";
J. Biol. Chem. 270:17407-17413(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
TISSUE=Amygdala, Brain, Hippocampus, and Kidney;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain, and Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
FUNCTION.
PubMed=10565303; DOI=10.1016/S0165-4608(99)00081-3;
Lutchman M., Pack S., Kim A.C., Azim A., Emmert-Buck M.,
van Huffel C., Zhuang Z., Chishti A.H.;
"Loss of heterozygosity on 8p in prostate cancer implicates a role for
dematin in tumor progression.";
Cancer Genet. Cytogenet. 115:65-69(1999).
[8]
FUNCTION, INTERACTION WITH RASGRF2, AND SUBCELLULAR LOCATION.
PubMed=11856323; DOI=10.1046/j.0014-2956.2001.02694.x;
Lutchman M., Kim A.C., Cheng L., Whitehead I.P., Oh S.S., Hanspal M.,
Boukharov A.A., Hanada T., Chishti A.H.;
"Dematin interacts with the Ras-guanine nucleotide exchange factor
Ras-GRF2 and modulates mitogen-activated protein kinase pathways.";
Eur. J. Biochem. 269:638-649(2002).
[9]
FUNCTION, IDENTIFICATION IN A COMPLEX WITH ADD2 AND SLC2A1, AND
INTERACTION WITH SLC2A1.
PubMed=18347014; DOI=10.1074/jbc.M707818200;
Khan A.A., Hanada T., Mohseni M., Jeong J.J., Zeng L., Gaetani M.,
Li D., Reed B.C., Speicher D.W., Chishti A.H.;
"Dematin and adducin provide a novel link between the spectrin
cytoskeleton and human erythrocyte membrane by directly interacting
with glucose transporter-1.";
J. Biol. Chem. 283:14600-14609(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=T-cell;
PubMed=19367720; DOI=10.1021/pr800500r;
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
"Phosphorylation analysis of primary human T lymphocytes using
sequential IMAC and titanium oxide enrichment.";
J. Proteome Res. 7:5167-5176(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96; SER-105; SER-156;
SER-226; SER-333 AND SER-372, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18318008; DOI=10.1002/pmic.200700884;
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by
enrichment and fractionation of phosphopeptides with strong anion
exchange chromatography.";
Proteomics 8:1346-1361(2008).
[13]
FUNCTION, AND INTERACTION WITH F-ACTIN.
PubMed=19241372; DOI=10.1002/pro.59;
Chen L., Jiang Z.G., Khan A.A., Chishti A.H., McKnight C.J.;
"Dematin exhibits a natively unfolded core domain and an independently
folded headpiece domain.";
Protein Sci. 18:629-636(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96 AND SER-105, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[16]
INTERACTION WITH PLASMODIUM BERGHEI 14-3-3 PROTEIN, SUBCELLULAR
LOCATION, AND MUTAGENESIS OF SER-124; SER-333 AND SER-403.
PubMed=21084299; DOI=10.1074/jbc.M110.194613;
Lalle M., Curra C., Ciccarone F., Pace T., Cecchetti S., Fantozzi L.,
Ay B., Breton C.B., Ponzi M.;
"Dematin, a component of the erythrocyte membrane skeleton, is
internalized by the malaria parasite and associates with Plasmodium
14-3-3.";
J. Biol. Chem. 286:1227-1236(2011).
[17]
FUNCTION, PHOSPHORYLATION AT SER-403, AND IDENTIFICATION IN A COMPLEX
WITH SPECTRIN AND F-ACTIN.
PubMed=22927433; DOI=10.1074/jbc.M111.305441;
Koshino I., Mohandas N., Takakuwa Y.;
"Identification of a novel role for dematin in regulating red cell
membrane function by modulating spectrin-actin interaction.";
J. Biol. Chem. 287:35244-35250(2012).
[18]
INTERACTION WITH DMTN, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=23060452; DOI=10.1074/jbc.M112.364679;
Wieschhaus A.J., Le Breton G.C., Chishti A.H.;
"Headpiece domain of dematin regulates calcium mobilization and
signaling in platelets.";
J. Biol. Chem. 287:41218-41231(2012).
[19]
FUNCTION, SUBUNIT, PHOSPHORYLATION AT SER-403, AND MUTAGENESIS OF
SER-403.
PubMed=23355471; DOI=10.1074/jbc.M112.438861;
Chen L., Brown J.W., Mok Y.F., Hatters D.M., McKnight C.J.;
"The allosteric mechanism induced by protein kinase A (PKA)
phosphorylation of dematin (band 4.9).";
J. Biol. Chem. 288:8313-8320(2013).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-18; SER-26;
SER-92; SER-96; SER-105; SER-226; SER-269; SER-279; SER-289; SER-303;
SER-333; SER-372 AND SER-383, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-18; SER-105;
SER-289 AND SER-372, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[22]
STRUCTURE BY NMR OF 342-405.
PubMed=14660664; DOI=10.1074/jbc.M310524200;
Frank B.S., Vardar D., Chishti A.H., McKnight C.J.;
"The NMR structure of dematin headpiece reveals a dynamic loop that is
conformationally altered upon phosphorylation at a distal site.";
J. Biol. Chem. 279:7909-7916(2004).
[23]
STRUCTURE BY NMR OF 342-405, AND PHOSPHORYLATION AT SER-403.
PubMed=16472756; DOI=10.1016/j.str.2005.11.007;
Jiang Z.G., McKnight C.J.;
"A phosphorylation-induced conformation change in dematin headpiece.";
Structure 14:379-387(2006).
-!- FUNCTION: Membrane-cytoskeleton-associated protein with F-actin-
binding activity that induces F-actin bundles formation and
stabilization. Its F-actin-bundling activity is reversibly
regulated upon its phosphorylation by the cAMP-dependent protein
kinase A (PKA). Binds to the erythrocyte membrane glucose
transporter-1 SLC2A1/GLUT1, and hence stabilizes and attaches the
spectrin-actin network to the erythrocytic plasma membrane. Plays
a role in maintaining the functional integrity of PKA-activated
erythrocyte shape and the membrane mechanical properties. Plays
also a role as a modulator of actin dynamics in fibroblasts; acts
as a negative regulator of the RhoA activation pathway. In
platelets, functions as a regulator of internal calcium
mobilization across the dense tubular system that affects platelet
granule secretion pathways and aggregation. Also required for the
formation of a diverse set of cell protrusions, such as filopodia
and lamellipodia, necessary for platelet cell spreading, motility
and migration. Acts as a tumor suppressor and inhibits malignant
cell transformation. {ECO:0000269|PubMed:10565303,
ECO:0000269|PubMed:11856323, ECO:0000269|PubMed:18347014,
ECO:0000269|PubMed:19241372, ECO:0000269|PubMed:22927433,
ECO:0000269|PubMed:23355471}.
-!- SUBUNIT: Monomeric (isoform 2); under reducing conditions. Self-
associates. Exists under oxidizing condition as a trimer of two
isoforms 2 and isoform 1 linked by disulfide bonds (Probable).
Found in a complex with DMTN, F-actin and spectrin. Found in a
complex with ADD2, DMTN and SLC2A1. Interacts with F-actin, ITPKB,
RASGRF2 and spectrin. Isoform 2 interacts with SLC2A1 (via C-
terminus cytoplasmic region). Isoform 1 and isoform 2 interact
(phosphorylated form) with plasmodium berghei 14-3-3 protein; the
interaction occurs in a PKA-dependent manner.
{ECO:0000269|PubMed:11856323, ECO:0000269|PubMed:18347014,
ECO:0000269|PubMed:19241372, ECO:0000269|PubMed:21084299,
ECO:0000269|PubMed:22927433, ECO:0000269|PubMed:23060452,
ECO:0000269|PubMed:23355471, ECO:0000269|PubMed:7615546,
ECO:0000305}.
-!- INTERACTION:
Q08379:GOLGA2; NbExp=3; IntAct=EBI-715275, EBI-618309;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytosol. Cytoplasm,
perinuclear region {ECO:0000250}. Cytoplasm, cytoskeleton. Cell
membrane. Membrane {ECO:0000250}. Endomembrane system. Cell
projection {ECO:0000250}. Note=Localized at the spectrin-actin
junction of erythrocyte plasma membrane. Localized to
intracellular membranes and the cytoskeletal network. Localized at
intracellular membrane-bounded organelle compartment in platelets
that likely represent the dense tubular network membrane. Detected
at the cell membrane and at the parasitophorous vacuole in
malaria-infected erythrocytes at late stages of plasmodium berghei
or falciparum development.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=Long;
IsoId=Q08495-1; Sequence=Displayed;
Name=2; Synonyms=Short;
IsoId=Q08495-2; Sequence=VSP_004189;
Name=3;
IsoId=Q08495-3; Sequence=VSP_044803, VSP_004189;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q08495-4; Sequence=VSP_044803, VSP_057428;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in platelets (at protein level).
Expressed in heart, brain, lung, skeletal muscle, and kidney.
{ECO:0000269|PubMed:23060452}.
-!- DOMAIN: Both the N-terminal core domain and the C-terminal
headpiece domain are sufficient for binding to F-actin and
necessary for actin bundling activity.
-!- PTM: Phosphorylated. Phosphorylation at Ser-403 by PKA causes the
C-terminal headpiece domain to associate with the N-terminal core
domain, and leads to the inhibition of its actin bundling
activity. {ECO:0000269|PubMed:16472756,
ECO:0000269|PubMed:22927433, ECO:0000269|PubMed:23355471,
ECO:0000269|PubMed:7615546}.
-!- PTM: The N-terminus is blocked.
-!- SIMILARITY: Belongs to the villin/gelsolin family. {ECO:0000305}.
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EMBL; L19713; AAA58438.1; -; mRNA.
EMBL; U28389; AAC50223.1; -; mRNA.
EMBL; AK055842; BAG51582.1; -; mRNA.
EMBL; AK091581; BAG52385.1; -; mRNA.
EMBL; AK289650; BAF82339.1; -; mRNA.
EMBL; AK295452; BAG58387.1; -; mRNA.
EMBL; BT007396; AAP36060.1; -; mRNA.
EMBL; AC091171; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC006318; AAH06318.1; -; mRNA.
EMBL; BC017445; AAH17445.1; -; mRNA.
EMBL; BC052805; AAH52805.1; -; mRNA.
CCDS; CCDS47820.1; -. [Q08495-2]
CCDS; CCDS47821.1; -. [Q08495-3]
CCDS; CCDS6020.1; -. [Q08495-1]
CCDS; CCDS78311.1; -. [Q08495-4]
PIR; A48222; A48222.
PIR; I39062; I39062.
RefSeq; NP_001107607.1; NM_001114135.4. [Q08495-1]
RefSeq; NP_001107608.1; NM_001114136.2. [Q08495-1]
RefSeq; NP_001107609.1; NM_001114137.3. [Q08495-2]
RefSeq; NP_001107610.1; NM_001114138.2. [Q08495-2]
RefSeq; NP_001107611.1; NM_001114139.3. [Q08495-3]
RefSeq; NP_001289745.1; NM_001302816.2. [Q08495-2]
RefSeq; NP_001289746.1; NM_001302817.2. [Q08495-4]
RefSeq; NP_001310307.1; NM_001323378.1. [Q08495-1]
RefSeq; NP_001310308.1; NM_001323379.1. [Q08495-1]
RefSeq; NP_001310309.1; NM_001323380.1. [Q08495-1]
RefSeq; NP_001310310.1; NM_001323381.1. [Q08495-1]
RefSeq; NP_001310311.1; NM_001323382.1. [Q08495-1]
RefSeq; NP_001310312.1; NM_001323383.1. [Q08495-2]
RefSeq; NP_001310313.1; NM_001323384.1. [Q08495-2]
RefSeq; NP_001310314.1; NM_001323385.1. [Q08495-2]
RefSeq; NP_001310316.1; NM_001323387.1. [Q08495-3]
RefSeq; NP_001310317.1; NM_001323388.1. [Q08495-4]
RefSeq; NP_001310318.1; NM_001323389.1.
RefSeq; NP_001310319.1; NM_001323390.1.
RefSeq; NP_001310320.1; NM_001323391.1.
RefSeq; NP_001310321.1; NM_001323392.1.
RefSeq; NP_001310322.1; NM_001323393.1.
RefSeq; NP_001310323.1; NM_001323394.1.
RefSeq; NP_001310324.1; NM_001323395.1.
RefSeq; NP_001310325.1; NM_001323396.1.
RefSeq; NP_001310326.1; NM_001323397.1.
RefSeq; NP_001310327.1; NM_001323398.1.
RefSeq; NP_001310328.1; NM_001323399.1.
RefSeq; NP_001310329.1; NM_001323400.1.
RefSeq; NP_001310330.1; NM_001323401.1.
RefSeq; NP_001969.2; NM_001978.4. [Q08495-1]
RefSeq; XP_005273489.1; XM_005273432.1. [Q08495-1]
RefSeq; XP_016868678.1; XM_017013189.1. [Q08495-2]
RefSeq; XP_016868682.1; XM_017013193.1. [Q08495-4]
RefSeq; XP_016868683.1; XM_017013194.1. [Q08495-4]
RefSeq; XP_016868684.1; XM_017013195.1. [Q08495-3]
RefSeq; XP_016868685.1; XM_017013196.1. [Q08495-3]
RefSeq; XP_016868686.1; XM_017013197.1. [Q08495-3]
RefSeq; XP_016868687.1; XM_017013198.1. [Q08495-3]
UniGene; Hs.106124; -.
PDB; 1QZP; NMR; -; A=342-405.
PDB; 1ZV6; NMR; -; A=342-405.
PDBsum; 1QZP; -.
PDBsum; 1ZV6; -.
ProteinModelPortal; Q08495; -.
SMR; Q08495; -.
BioGrid; 108353; 20.
CORUM; Q08495; -.
IntAct; Q08495; 10.
MINT; MINT-1390442; -.
STRING; 9606.ENSP00000265800; -.
iPTMnet; Q08495; -.
PhosphoSitePlus; Q08495; -.
BioMuta; DMTN; -.
DMDM; 22654240; -.
MaxQB; Q08495; -.
PaxDb; Q08495; -.
PeptideAtlas; Q08495; -.
PRIDE; Q08495; -.
DNASU; 2039; -.
Ensembl; ENST00000265800; ENSP00000265800; ENSG00000158856. [Q08495-1]
Ensembl; ENST00000358242; ENSP00000350977; ENSG00000158856. [Q08495-1]
Ensembl; ENST00000381470; ENSP00000370879; ENSG00000158856. [Q08495-2]
Ensembl; ENST00000415253; ENSP00000401291; ENSG00000158856. [Q08495-2]
Ensembl; ENST00000432128; ENSP00000416111; ENSG00000158856. [Q08495-1]
Ensembl; ENST00000443491; ENSP00000397904; ENSG00000158856. [Q08495-3]
Ensembl; ENST00000517305; ENSP00000430609; ENSG00000158856. [Q08495-1]
Ensembl; ENST00000517600; ENSP00000430618; ENSG00000158856. [Q08495-4]
Ensembl; ENST00000519907; ENSP00000429377; ENSG00000158856. [Q08495-2]
Ensembl; ENST00000523266; ENSP00000427866; ENSG00000158856. [Q08495-1]
Ensembl; ENST00000523782; ENSP00000429234; ENSG00000158856. [Q08495-3]
GeneID; 2039; -.
KEGG; hsa:2039; -.
UCSC; uc064kwf.1; human. [Q08495-1]
UCSC; uc064kwj.1; human.
CTD; 2039; -.
DisGeNET; 2039; -.
EuPathDB; HostDB:ENSG00000158856.17; -.
GeneCards; DMTN; -.
HGNC; HGNC:3382; DMTN.
HPA; HPA024290; -.
MIM; 125305; gene.
neXtProt; NX_Q08495; -.
OpenTargets; ENSG00000158856; -.
PharmGKB; PA27815; -.
eggNOG; KOG1044; Eukaryota.
eggNOG; ENOG410XRPY; LUCA.
GeneTree; ENSGT00760000119039; -.
HOGENOM; HOG000285997; -.
HOVERGEN; HBG031499; -.
InParanoid; Q08495; -.
OMA; YKQREST; -.
OrthoDB; EOG091G06PE; -.
PhylomeDB; Q08495; -.
TreeFam; TF318042; -.
Reactome; R-HSA-5223345; Miscellaneous transport and binding events.
ChiTaRS; DMTN; human.
EvolutionaryTrace; Q08495; -.
GeneWiki; EPB49; -.
GenomeRNAi; 2039; -.
PRO; PR:Q08495; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000158856; -.
CleanEx; HS_EPB49; -.
ExpressionAtlas; Q08495; baseline and differential.
Genevisible; Q08495; HS.
GO; GO:0015629; C:actin cytoskeleton; TAS:UniProtKB.
GO; GO:0005884; C:actin filament; IDA:UniProtKB.
GO; GO:0031253; C:cell projection membrane; ISS:UniProtKB.
GO; GO:0030863; C:cortical cytoskeleton; IEA:Ensembl.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0031095; C:platelet dense tubular network membrane; IDA:UniProtKB.
GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
GO; GO:0014731; C:spectrin-associated cytoskeleton; IDA:UniProtKB.
GO; GO:0003779; F:actin binding; IDA:UniProtKB.
GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
GO; GO:0005102; F:receptor binding; IDA:UniProtKB.
GO; GO:0030507; F:spectrin binding; IDA:UniProtKB.
GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB.
GO; GO:0051017; P:actin filament bundle assembly; IDA:UniProtKB.
GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
GO; GO:0090527; P:actin filament reorganization; ISS:UniProtKB.
GO; GO:0035585; P:calcium-mediated signaling using extracellular calcium source; ISS:UniProtKB.
GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; ISS:UniProtKB.
GO; GO:0071277; P:cellular response to calcium ion; ISS:UniProtKB.
GO; GO:0071320; P:cellular response to cAMP; IDA:UniProtKB.
GO; GO:0007010; P:cytoskeleton organization; TAS:UniProtKB.
GO; GO:0048821; P:erythrocyte development; ISS:UniProtKB.
GO; GO:0010812; P:negative regulation of cell-substrate adhesion; ISS:UniProtKB.
GO; GO:0051895; P:negative regulation of focal adhesion assembly; ISS:UniProtKB.
GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; ISS:UniProtKB.
GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; ISS:UniProtKB.
GO; GO:0050732; P:negative regulation of peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
GO; GO:0090315; P:negative regulation of protein targeting to membrane; ISS:UniProtKB.
GO; GO:1900025; P:negative regulation of substrate adhesion-dependent cell spreading; ISS:UniProtKB.
GO; GO:0030194; P:positive regulation of blood coagulation; ISS:UniProtKB.
GO; GO:0010763; P:positive regulation of fibroblast migration; ISS:UniProtKB.
GO; GO:2001046; P:positive regulation of integrin-mediated signaling pathway; ISS:UniProtKB.
GO; GO:1901731; P:positive regulation of platelet aggregation; ISS:UniProtKB.
GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISS:UniProtKB.
GO; GO:0090303; P:positive regulation of wound healing; ISS:UniProtKB.
GO; GO:0006461; P:protein complex assembly; IDA:UniProtKB.
GO; GO:0070560; P:protein secretion by platelet; ISS:UniProtKB.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; IDA:UniProtKB.
GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
GO; GO:0051489; P:regulation of filopodium assembly; IMP:UniProtKB.
GO; GO:0010591; P:regulation of lamellipodium assembly; IMP:UniProtKB.
GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
Gene3D; 1.10.950.10; -; 1.
InterPro; IPR032402; AbLIM_anchor.
InterPro; IPR003128; Villin_headpiece.
InterPro; IPR036886; Villin_headpiece_dom_sf.
Pfam; PF16182; AbLIM_anchor; 2.
Pfam; PF02209; VHP; 1.
SMART; SM00153; VHP; 1.
SUPFAM; SSF47050; SSF47050; 1.
PROSITE; PS51089; HP; 1.
1: Evidence at protein level;
3D-structure; Actin capping; Actin-binding; Alternative splicing;
Cell membrane; Cell projection; Complete proteome; Cytoplasm;
Cytoskeleton; Direct protein sequencing; Disulfide bond; Membrane;
Phosphoprotein; Reference proteome; Repeat; Tumor suppressor.
CHAIN 1 405 Dematin.
/FTId=PRO_0000218755.
DOMAIN 337 405 HP. {ECO:0000255|PROSITE-
ProRule:PRU00595}.
REGION 224 308 Interaction with RASGRF2.
{ECO:0000269|PubMed:11856323}.
COMPBIAS 216 222 Poly-Glu.
MOD_RES 16 16 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 18 18 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 26 26 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 92 92 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 96 96 Phosphoserine.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 105 105 Phosphoserine.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 110 110 Phosphoserine.
{ECO:0000250|UniProtKB:Q9WV69}.
MOD_RES 113 113 Phosphoserine.
{ECO:0000250|UniProtKB:Q9WV69}.
MOD_RES 156 156 Phosphoserine.
{ECO:0000244|PubMed:18088087}.
MOD_RES 226 226 Phosphoserine.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:18318008,
ECO:0000244|PubMed:19367720,
ECO:0000244|PubMed:23186163}.
MOD_RES 269 269 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 279 279 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 289 289 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 303 303 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 315 315 Phosphoserine.
{ECO:0000250|UniProtKB:Q9WV69}.
MOD_RES 333 333 Phosphoserine.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:23186163}.
MOD_RES 372 372 Phosphoserine.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 383 383 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 403 403 Phosphoserine; by PKA.
{ECO:0000269|PubMed:16472756,
ECO:0000269|PubMed:22927433,
ECO:0000269|PubMed:23355471}.
VAR_SEQ 7 31 Missing (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044803.
VAR_SEQ 83 97 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_057428.
VAR_SEQ 320 341 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8341682}.
/FTId=VSP_004189.
MUTAGEN 124 124 S->A: Reduces interaction with plasmodium
berghei 14-3-3 protein. Inhibits
phosphorylation and interaction with
plasmodium berghei 14-3-3 protein; when
associated with A-333 and A-403.
{ECO:0000269|PubMed:21084299}.
MUTAGEN 333 333 S->A: Reduces interaction with plasmodium
berghei 14-3-3 protein. Inhibits
phosphorylation and interaction with
plasmodium berghei 14-3-3 protein; when
associated with A-124 and A-403.
{ECO:0000269|PubMed:21084299}.
MUTAGEN 403 403 S->A: Inhibits phosphorylation and
interaction with plasmodium berghei 14-3-
3 protein; when associated with A-124 and
A-333. {ECO:0000269|PubMed:21084299,
ECO:0000269|PubMed:23355471}.
MUTAGEN 403 403 S->E: Reduces F-actin bundling but not F-
actin binding activity.
{ECO:0000269|PubMed:21084299,
ECO:0000269|PubMed:23355471}.
CONFLICT 81 81 S -> Q (in Ref. 1; AAA58438 and 2;
AAC50223). {ECO:0000305}.
CONFLICT 155 155 G -> A (in Ref. 3; BAG52385).
{ECO:0000305}.
CONFLICT 292 292 A -> R (in Ref. 1; AAA58438 and 2;
AAC50223). {ECO:0000305}.
CONFLICT 347 347 M -> V (in Ref. 1; AAA58438).
{ECO:0000305}.
CONFLICT 380 380 F -> S (in Ref. 1; AAA58438).
{ECO:0000305}.
CONFLICT 403 403 S -> P (in Ref. 3; BAG52385).
{ECO:0000305}.
TURN 346 348 {ECO:0000244|PDB:1QZP}.
HELIX 364 366 {ECO:0000244|PDB:1QZP}.
HELIX 368 370 {ECO:0000244|PDB:1QZP}.
HELIX 373 379 {ECO:0000244|PDB:1QZP}.
STRAND 380 382 {ECO:0000244|PDB:1QZP}.
HELIX 384 389 {ECO:0000244|PDB:1QZP}.
HELIX 392 402 {ECO:0000244|PDB:1QZP}.
SEQUENCE 405 AA; 45514 MW; 77D6372E5B16EFF4 CRC64;
MERLQKQPLT SPGSVSPSRD SSVPGSPSSI VAKMDNQVLG YKDLAAIPKD KAILDIERPD
LMIYEPHFTY SLLEHVELPR SRERSLSPKS TSPPPSPEVW ADSRSPGIIS QASAPRTTGT
PRTSLPHFHH PETSRPDSNI YKKPPIYKQR ESVGGSPQTK HLIEDLIIES SKFPAAQPPD
PNQPAKIETD YWPCPPSLAV VETEWRKRKA SRRGAEEEEE EEDDDSGEEM KALRERQREE
LSKVTSNLGK MILKEEMEKS LPIRRKTRSL PDRTPFHTSL HQGTSKSSSL PAYGRTTLSR
LQSTEFSPSG SETGSPGLQN GEGQRGRMDR GNSLPCVLEQ KIYPYEMLVV TNKGRTKLPP
GVDRMRLERH LSAEDFSRVF AMSPEEFGKL ALWKRNELKK KASLF


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