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Q08495 (DEMA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dematin
Alternative name(s):
Dematin actin-binding protein
Erythrocyte membrane protein band 4.9
Gene names
Name:DMTN
Synonyms:DMT, EPB49
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length405 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.7 Ref.8 Ref.9 Ref.13 Ref.17 Ref.19

Subunit structure

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. Ref.2 Ref.8 Ref.9 Ref.13 Ref.16 Ref.17 Ref.18 Ref.19

Subcellular location

Cytoplasm. Cytoplasmcytosol. Cytoplasmperinuclear region By similarity. Cytoplasmcytoskeleton. Cell membrane. Membrane By similarity. Endomembrane system. Cell projection By similarity. 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 vacuol in malaria-infected erythrocytes at late stages of plasmodium berghei or falciparum development. Ref.8 Ref.16 Ref.18

Tissue specificity

Expressed in platelets (at protein level). Expressed in heart, brain, lung, skeletal muscle, and kidney. Ref.18

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.

Post-translational modification

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. Ref.2 Ref.17 Ref.19 Ref.21

The N-terminus is blocked.

Sequence similarities

Belongs to the villin/gelsolin family.

Contains 1 HP (headpiece) domain.

Ontologies

Keywords
   Cellular componentCell membrane
Cell projection
Cytoplasm
Cytoskeleton
Membrane
   Coding sequence diversityAlternative splicing
   DiseaseTumor suppressor
   DomainRepeat
   LigandActin-binding
   Molecular functionActin capping
   PTMDisulfide bond
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton organization

Inferred from sequence or structural similarity. Source: UniProtKB

actin filament bundle assembly

Inferred from direct assay Ref.13Ref.19. Source: UniProtKB

actin filament capping

Inferred from electronic annotation. Source: UniProtKB-KW

actin filament reorganization

Inferred from sequence or structural similarity. Source: UniProtKB

calcium-mediated signaling using extracellular calcium source

Inferred from sequence or structural similarity. Source: UniProtKB

calcium-mediated signaling using intracellular calcium source

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to cAMP

Inferred from direct assay Ref.17. Source: UniProtKB

cellular response to calcium ion

Inferred from sequence or structural similarity. Source: UniProtKB

cytoskeleton organization

Traceable author statement Ref.2. Source: UniProtKB

erythrocyte development

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell-substrate adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of focal adhesion assembly

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of peptidyl-serine phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of peptidyl-threonine phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of peptidyl-tyrosine phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of protein targeting to membrane

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of substrate adhesion-dependent cell spreading

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of blood coagulation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of fibroblast migration

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of integrin-mediated signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of platelet aggregation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of substrate adhesion-dependent cell spreading

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of wound healing

Inferred from sequence or structural similarity. Source: UniProtKB

protein complex assembly

Inferred from direct assay Ref.9. Source: UniProtKB

protein secretion by platelet

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of actin cytoskeleton organization

Inferred from direct assay Ref.17. Source: UniProtKB

regulation of cell shape

Inferred from mutant phenotype Ref.7. Source: UniProtKB

regulation of filopodium assembly

Inferred from mutant phenotype Ref.7. Source: UniProtKB

regulation of lamellipodium assembly

Inferred from mutant phenotype Ref.7. Source: UniProtKB

   Cellular_componentactin cytoskeleton

Traceable author statement Ref.1. Source: UniProtKB

actin filament

Inferred from direct assay Ref.17. Source: UniProtKB

cell projection membrane

Inferred from sequence or structural similarity. Source: UniProtKB

cortical cytoskeleton

Inferred from electronic annotation. Source: Ensembl

cytoplasmic membrane-bounded vesicle

Inferred from direct assay Ref.9. Source: UniProtKB

cytosol

Inferred from direct assay Ref.18. Source: UniProtKB

endomembrane system

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from direct assay Ref.18. Source: UniProtKB

platelet dense tubular network membrane

Inferred from direct assay Ref.18. Source: UniProtKB

spectrin-associated cytoskeleton

Inferred from direct assay Ref.17. Source: UniProtKB

   Molecular_functionactin binding

Inferred from direct assay Ref.17Ref.13Ref.19. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.9Ref.18. Source: UniProtKB

protein self-association

Inferred from direct assay Ref.19. Source: UniProtKB

receptor binding

Inferred from direct assay Ref.9. Source: UniProtKB

spectrin binding

Inferred from direct assay Ref.17. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q08495-1)

Also known as: Long;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q08495-2)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     320-341: Missing.
Isoform 3 (identifier: Q08495-3)

The sequence of this isoform differs from the canonical sequence as follows:
     7-31: Missing.
     320-341: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 405405Dematin
PRO_0000218755

Regions

Domain337 – 40569HP
Region224 – 30885Interaction with RASGRF2
Compositional bias216 – 2227Poly-Glu

Amino acid modifications

Modified residue961Phosphoserine Ref.11 Ref.14
Modified residue1051Phosphoserine Ref.11 Ref.14 Ref.15
Modified residue1561Phosphoserine Ref.11
Modified residue2261Phosphoserine Ref.10 Ref.11 Ref.12
Modified residue3331Phosphoserine Ref.11
Modified residue3721Phosphoserine Ref.11
Modified residue4031Phosphoserine; by PKA Ref.17 Ref.19 Ref.21

Natural variations

Alternative sequence7 – 3125Missing in isoform 3.
VSP_044803
Alternative sequence320 – 34122Missing in isoform 2 and isoform 3.
VSP_004189

Experimental info

Mutagenesis1241S → 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. Ref.16
Mutagenesis3331S → 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. Ref.16
Mutagenesis4031S → A: Inhibits phosphorylation and interaction with plasmodium berghei 14-3-3 protein; when associated with A-124 and A-333. Ref.16 Ref.19
Mutagenesis4031S → E: Reduces F-actin bundling but not F-actin binding activity. Ref.16 Ref.19
Sequence conflict811S → Q in AAA58438. Ref.1
Sequence conflict811S → Q in AAC50223. Ref.2
Sequence conflict1551G → A in BAG52385. Ref.3
Sequence conflict2921A → R in AAA58438. Ref.1
Sequence conflict2921A → R in AAC50223. Ref.2
Sequence conflict3471M → V in AAA58438. Ref.1
Sequence conflict3801F → S in AAA58438. Ref.1
Sequence conflict4031S → P in BAG52385. Ref.3

Secondary structure

.............. 405
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Long) [UniParc].

Last modified August 30, 2002. Version 3.
Checksum: 77D6372E5B16EFF4

FASTA40545,514
        10         20         30         40         50         60 
MERLQKQPLT SPGSVSPSRD SSVPGSPSSI VAKMDNQVLG YKDLAAIPKD KAILDIERPD 

        70         80         90        100        110        120 
LMIYEPHFTY SLLEHVELPR SRERSLSPKS TSPPPSPEVW ADSRSPGIIS QASAPRTTGT 

       130        140        150        160        170        180 
PRTSLPHFHH PETSRPDSNI YKKPPIYKQR ESVGGSPQTK HLIEDLIIES SKFPAAQPPD 

       190        200        210        220        230        240 
PNQPAKIETD YWPCPPSLAV VETEWRKRKA SRRGAEEEEE EEDDDSGEEM KALRERQREE 

       250        260        270        280        290        300 
LSKVTSNLGK MILKEEMEKS LPIRRKTRSL PDRTPFHTSL HQGTSKSSSL PAYGRTTLSR 

       310        320        330        340        350        360 
LQSTEFSPSG SETGSPGLQN GEGQRGRMDR GNSLPCVLEQ KIYPYEMLVV TNKGRTKLPP 

       370        380        390        400 
GVDRMRLERH LSAEDFSRVF AMSPEEFGKL ALWKRNELKK KASLF 

« Hide

Isoform 2 (Short) [UniParc].

Checksum: 3C46AB7704507B6E
Show »

FASTA38343,088
Isoform 3 [UniParc].

Checksum: 1F985F9D3643F995
Show »

FASTA35840,680

References

« Hide 'large scale' references
[1]"Cloning of human erythroid dematin reveals another member of the villin family."
Rana A.P., Ruff P., Maalouf G.J., Speicher D.W., Chishti A.H.
Proc. Natl. Acad. Sci. U.S.A. 90:6651-6655(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PARTIAL PROTEIN SEQUENCE.
Tissue: Reticulocyte.
[2]"Isoform cloning, actin binding, and chromosomal localization of human erythroid dematin, a member of the villin superfamily."
Azim A.C., Knoll J.H.M., Beggs A.H., Chishti A.H.
J. Biol. Chem. 270:17407-17413(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION BY CAPK, SUBUNIT, ALTERNATIVE SPLICING.
Tissue: Reticulocyte.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
Tissue: Amygdala, Brain and Kidney.
[4]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
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.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]"DNA sequence and analysis of human chromosome 8."
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. expand/collapse author list , 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.
Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Brain and Liver.
[7]"Loss of heterozygosity on 8p in prostate cancer implicates a role for dematin in tumor progression."
Lutchman M., Pack S., Kim A.C., Azim A., Emmert-Buck M., van Huffel C., Zhuang Z., Chishti A.H.
Cancer Genet. Cytogenet. 115:65-69(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Dematin interacts with the Ras-guanine nucleotide exchange factor Ras-GRF2 and modulates mitogen-activated protein kinase pathways."
Lutchman M., Kim A.C., Cheng L., Whitehead I.P., Oh S.S., Hanspal M., Boukharov A.A., Hanada T., Chishti A.H.
Eur. J. Biochem. 269:638-649(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RASGRF2, SUBCELLULAR LOCATION.
[9]"Dematin and adducin provide a novel link between the spectrin cytoskeleton and human erythrocyte membrane by directly interacting with glucose transporter-1."
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.
J. Biol. Chem. 283:14600-14609(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH ADD2 AND SLC2A1, INTERACTION WITH SLC2A1.
[10]"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: T-cell.
[11]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96; SER-105; SER-156; SER-226; SER-333 AND SER-372, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[12]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[13]"Dematin exhibits a natively unfolded core domain and an independently folded headpiece domain."
Chen L., Jiang Z.G., Khan A.A., Chishti A.H., McKnight C.J.
Protein Sci. 18:629-636(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH F-ACTIN.
[14]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96 AND SER-105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[15]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Dematin, a component of the erythrocyte membrane skeleton, is internalized by the malaria parasite and associates with Plasmodium 14-3-3."
Lalle M., Curra C., Ciccarone F., Pace T., Cecchetti S., Fantozzi L., Ay B., Breton C.B., Ponzi M.
J. Biol. Chem. 286:1227-1236(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PLASMODIUM BERGHEI 14-3-3 PROTEIN, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-124; SER-333 AND SER-403.
[17]"Identification of a novel role for dematin in regulating red cell membrane function by modulating spectrin-actin interaction."
Koshino I., Mohandas N., Takakuwa Y.
J. Biol. Chem. 287:35244-35250(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT SER-403, IDENTIFICATION IN A COMPLEX WITH SPECTRIN AND F-ACTIN.
[18]"Headpiece domain of dematin regulates calcium mobilization and signaling in platelets."
Wieschhaus A.J., Le Breton G.C., Chishti A.H.
J. Biol. Chem. 287:41218-41231(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DMTN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[19]"The allosteric mechanism induced by protein kinase A (PKA) phosphorylation of dematin (band 4.9)."
Chen L., Brown J.W., Mok Y.F., Hatters D.M., McKnight C.J.
J. Biol. Chem. 288:8313-8320(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, PHOSPHORYLATION AT SER-403, MUTAGENESIS OF SER-403.
[20]"The NMR structure of dematin headpiece reveals a dynamic loop that is conformationally altered upon phosphorylation at a distal site."
Frank B.S., Vardar D., Chishti A.H., McKnight C.J.
J. Biol. Chem. 279:7909-7916(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 342-405.
[21]"A phosphorylation-induced conformation change in dematin headpiece."
Jiang Z.G., McKnight C.J.
Structure 14:379-387(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 342-405, PHOSPHORYLATION AT SER-403.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L19713 mRNA. Translation: AAA58438.1.
U28389 mRNA. Translation: AAC50223.1.
AK055842 mRNA. Translation: BAG51582.1.
AK091581 mRNA. Translation: BAG52385.1.
AK289650 mRNA. Translation: BAF82339.1.
BT007396 mRNA. Translation: AAP36060.1.
AC091171 Genomic DNA. No translation available.
BC006318 mRNA. Translation: AAH06318.1.
BC017445 mRNA. Translation: AAH17445.1.
BC052805 mRNA. Translation: AAH52805.1.
CCDSCCDS47820.1. [Q08495-2]
CCDS47821.1. [Q08495-3]
CCDS6020.1. [Q08495-1]
PIRA48222.
I39062.
RefSeqNP_001107607.1. NM_001114135.2. [Q08495-1]
NP_001107608.1. NM_001114136.1. [Q08495-1]
NP_001107609.1. NM_001114137.1. [Q08495-2]
NP_001107610.1. NM_001114138.1. [Q08495-2]
NP_001107611.1. NM_001114139.1. [Q08495-3]
NP_001969.2. NM_001978.2. [Q08495-1]
XP_005273488.1. XM_005273431.1. [Q08495-1]
XP_005273489.1. XM_005273432.1. [Q08495-1]
XP_005273490.1. XM_005273433.1. [Q08495-1]
XP_005273491.1. XM_005273434.1. [Q08495-1]
XP_005273495.1. XM_005273438.1. [Q08495-2]
UniGeneHs.106124.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QZPNMR-A342-405[»]
1ZV6NMR-A342-405[»]
ProteinModelPortalQ08495.
SMRQ08495. Positions 341-405.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108353. 7 interactions.
IntActQ08495. 5 interactions.
MINTMINT-1390442.
STRING9606.ENSP00000265800.

PTM databases

PhosphoSiteQ08495.

Polymorphism databases

DMDM22654240.

Proteomic databases

MaxQBQ08495.
PaxDbQ08495.
PRIDEQ08495.

Protocols and materials databases

DNASU2039.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265800; ENSP00000265800; ENSG00000158856. [Q08495-1]
ENST00000358242; ENSP00000350977; ENSG00000158856. [Q08495-1]
ENST00000381470; ENSP00000370879; ENSG00000158856. [Q08495-2]
ENST00000415253; ENSP00000401291; ENSG00000158856. [Q08495-2]
ENST00000432128; ENSP00000416111; ENSG00000158856. [Q08495-1]
ENST00000443491; ENSP00000397904; ENSG00000158856. [Q08495-3]
ENST00000519907; ENSP00000429377; ENSG00000158856. [Q08495-2]
ENST00000523266; ENSP00000427866; ENSG00000158856. [Q08495-1]
ENST00000523782; ENSP00000429234; ENSG00000158856. [Q08495-3]
GeneID2039.
KEGGhsa:2039.
UCSCuc022asq.1. human. [Q08495-2]
uc022asr.1. human. [Q08495-1]

Organism-specific databases

CTD2039.
GeneCardsGC08P021907.
HGNCHGNC:3382. DMTN.
HPAHPA024290.
MIM125305. gene.
neXtProtNX_Q08495.
PharmGKBPA27815.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG253396.
HOGENOMHOG000285997.
HOVERGENHBG031499.
OMAWAESRTP.
PhylomeDBQ08495.
TreeFamTF318042.

Gene expression databases

ArrayExpressQ08495.
BgeeQ08495.
CleanExHS_EPB49.
GenevestigatorQ08495.

Family and domain databases

Gene3D1.10.950.10. 1 hit.
InterProIPR003128. Villin_headpiece.
[Graphical view]
PfamPF02209. VHP. 1 hit.
[Graphical view]
SMARTSM00153. VHP. 1 hit.
[Graphical view]
SUPFAMSSF47050. SSF47050. 1 hit.
PROSITEPS51089. HP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEPB49. human.
EvolutionaryTraceQ08495.
GeneWikiEPB49.
GenomeRNAi2039.
NextBio8281.
PROQ08495.
SOURCESearch...

Entry information

Entry nameDEMA_HUMAN
AccessionPrimary (citable) accession number: Q08495
Secondary accession number(s): A8K0T5 expand/collapse secondary AC list , B3KP70, B3KRH3, E9PEJ0, Q13215, Q9BRE3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: August 30, 2002
Last modified: July 9, 2014
This is version 150 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM