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Q08495

- DEMA_HUMAN

UniProt

Q08495 - DEMA_HUMAN

Protein

Dematin

Gene

DMTN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 3 (30 Aug 2002)
      Previous versions | rss
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    Functioni

    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.6 Publications

    GO - Molecular functioni

    1. actin binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. protein self-association Source: UniProtKB
    4. receptor binding Source: UniProtKB
    5. spectrin binding Source: UniProtKB

    GO - Biological processi

    1. actin cytoskeleton organization Source: UniProtKB
    2. actin filament bundle assembly Source: UniProtKB
    3. actin filament capping Source: UniProtKB-KW
    4. actin filament reorganization Source: UniProtKB
    5. calcium-mediated signaling using extracellular calcium source Source: UniProtKB
    6. calcium-mediated signaling using intracellular calcium source Source: UniProtKB
    7. cellular response to calcium ion Source: UniProtKB
    8. cellular response to cAMP Source: UniProtKB
    9. cytoskeleton organization Source: UniProtKB
    10. erythrocyte development Source: UniProtKB
    11. negative regulation of cell-substrate adhesion Source: UniProtKB
    12. negative regulation of focal adhesion assembly Source: UniProtKB
    13. negative regulation of peptidyl-serine phosphorylation Source: UniProtKB
    14. negative regulation of peptidyl-threonine phosphorylation Source: UniProtKB
    15. negative regulation of peptidyl-tyrosine phosphorylation Source: UniProtKB
    16. negative regulation of protein targeting to membrane Source: UniProtKB
    17. negative regulation of substrate adhesion-dependent cell spreading Source: UniProtKB
    18. positive regulation of blood coagulation Source: UniProtKB
    19. positive regulation of fibroblast migration Source: UniProtKB
    20. positive regulation of integrin-mediated signaling pathway Source: UniProtKB
    21. positive regulation of platelet aggregation Source: UniProtKB
    22. positive regulation of substrate adhesion-dependent cell spreading Source: UniProtKB
    23. positive regulation of wound healing Source: UniProtKB
    24. protein complex assembly Source: UniProtKB
    25. protein secretion by platelet Source: UniProtKB
    26. regulation of actin cytoskeleton organization Source: UniProtKB
    27. regulation of cell shape Source: UniProtKB
    28. regulation of filopodium assembly Source: UniProtKB
    29. regulation of lamellipodium assembly Source: UniProtKB

    Keywords - Molecular functioni

    Actin capping

    Keywords - Ligandi

    Actin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dematin
    Alternative name(s):
    Dematin actin-binding protein
    Erythrocyte membrane protein band 4.9
    Gene namesi
    Name:DMTN
    Synonyms:DMT, EPB49
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:3382. DMTN.

    Subcellular locationi

    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.

    GO - Cellular componenti

    1. actin cytoskeleton Source: UniProtKB
    2. actin filament Source: UniProtKB
    3. cell projection membrane Source: UniProtKB
    4. cortical cytoskeleton Source: Ensembl
    5. cytoplasmic membrane-bounded vesicle Source: UniProtKB
    6. cytosol Source: UniProtKB
    7. endomembrane system Source: UniProtKB-SubCell
    8. perinuclear region of cytoplasm Source: UniProtKB
    9. plasma membrane Source: UniProtKB
    10. platelet dense tubular network membrane Source: UniProtKB
    11. spectrin-associated cytoskeleton Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi124 – 1241S → 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. 1 Publication
    Mutagenesisi333 – 3331S → 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. 1 Publication
    Mutagenesisi403 – 4031S → A: Inhibits phosphorylation and interaction with plasmodium berghei 14-3-3 protein; when associated with A-124 and A-333. 2 Publications
    Mutagenesisi403 – 4031S → E: Reduces F-actin bundling but not F-actin binding activity. 2 Publications

    Keywords - Diseasei

    Tumor suppressor

    Organism-specific databases

    PharmGKBiPA27815.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 405405DematinPRO_0000218755Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei96 – 961Phosphoserine3 Publications
    Modified residuei105 – 1051Phosphoserine4 Publications
    Modified residuei156 – 1561Phosphoserine2 Publications
    Modified residuei226 – 2261Phosphoserine4 Publications
    Modified residuei333 – 3331Phosphoserine2 Publications
    Modified residuei372 – 3721Phosphoserine2 Publications
    Modified residuei403 – 4031Phosphoserine; by PKA4 Publications

    Post-translational modificationi

    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.9 Publications
    The N-terminus is blocked.

    Keywords - PTMi

    Disulfide bond, Phosphoprotein

    Proteomic databases

    MaxQBiQ08495.
    PaxDbiQ08495.
    PRIDEiQ08495.

    PTM databases

    PhosphoSiteiQ08495.

    Expressioni

    Tissue specificityi

    Expressed in platelets (at protein level). Expressed in heart, brain, lung, skeletal muscle, and kidney.1 Publication

    Gene expression databases

    ArrayExpressiQ08495.
    BgeeiQ08495.
    CleanExiHS_EPB49.
    GenevestigatoriQ08495.

    Organism-specific databases

    HPAiHPA024290.

    Interactioni

    Subunit structurei

    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.8 PublicationsCurated

    Protein-protein interaction databases

    BioGridi108353. 7 interactions.
    IntActiQ08495. 6 interactions.
    MINTiMINT-1390442.
    STRINGi9606.ENSP00000265800.

    Structurei

    Secondary structure

    1
    405
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni346 – 3483
    Helixi364 – 3663
    Helixi368 – 3703
    Helixi373 – 3797
    Beta strandi380 – 3823
    Helixi384 – 3896
    Helixi392 – 40211

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1QZPNMR-A342-405[»]
    1ZV6NMR-A342-405[»]
    ProteinModelPortaliQ08495.
    SMRiQ08495. Positions 341-405.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ08495.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini337 – 40569HPPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni224 – 30885Interaction with RASGRF2Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi216 – 2227Poly-Glu

    Domaini

    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.

    Sequence similaritiesi

    Belongs to the villin/gelsolin family.Curated
    Contains 1 HP (headpiece) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG253396.
    HOGENOMiHOG000285997.
    HOVERGENiHBG031499.
    OMAiWAESRTP.
    PhylomeDBiQ08495.
    TreeFamiTF318042.

    Family and domain databases

    Gene3Di1.10.950.10. 1 hit.
    InterProiIPR003128. Villin_headpiece.
    [Graphical view]
    PfamiPF02209. VHP. 1 hit.
    [Graphical view]
    SMARTiSM00153. VHP. 1 hit.
    [Graphical view]
    SUPFAMiSSF47050. SSF47050. 1 hit.
    PROSITEiPS51089. HP. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q08495-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MERLQKQPLT SPGSVSPSRD SSVPGSPSSI VAKMDNQVLG YKDLAAIPKD    50
    KAILDIERPD LMIYEPHFTY SLLEHVELPR SRERSLSPKS TSPPPSPEVW 100
    ADSRSPGIIS QASAPRTTGT PRTSLPHFHH PETSRPDSNI YKKPPIYKQR 150
    ESVGGSPQTK HLIEDLIIES SKFPAAQPPD PNQPAKIETD YWPCPPSLAV 200
    VETEWRKRKA SRRGAEEEEE EEDDDSGEEM KALRERQREE LSKVTSNLGK 250
    MILKEEMEKS LPIRRKTRSL PDRTPFHTSL HQGTSKSSSL PAYGRTTLSR 300
    LQSTEFSPSG SETGSPGLQN GEGQRGRMDR GNSLPCVLEQ KIYPYEMLVV 350
    TNKGRTKLPP GVDRMRLERH LSAEDFSRVF AMSPEEFGKL ALWKRNELKK 400
    KASLF 405
    Length:405
    Mass (Da):45,514
    Last modified:August 30, 2002 - v3
    Checksum:i77D6372E5B16EFF4
    GO
    Isoform 2 (identifier: Q08495-2) [UniParc]FASTAAdd to Basket

    Also known as: Short

    The sequence of this isoform differs from the canonical sequence as follows:
         320-341: Missing.

    Show »
    Length:383
    Mass (Da):43,088
    Checksum:i3C46AB7704507B6E
    GO
    Isoform 3 (identifier: Q08495-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         7-31: Missing.
         320-341: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:358
    Mass (Da):40,680
    Checksum:i1F985F9D3643F995
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti81 – 811S → Q in AAA58438. (PubMed:8341682)Curated
    Sequence conflicti81 – 811S → Q in AAC50223. (PubMed:7615546)Curated
    Sequence conflicti155 – 1551G → A in BAG52385. (PubMed:14702039)Curated
    Sequence conflicti292 – 2921A → R in AAA58438. (PubMed:8341682)Curated
    Sequence conflicti292 – 2921A → R in AAC50223. (PubMed:7615546)Curated
    Sequence conflicti347 – 3471M → V in AAA58438. (PubMed:8341682)Curated
    Sequence conflicti380 – 3801F → S in AAA58438. (PubMed:8341682)Curated
    Sequence conflicti403 – 4031S → P in BAG52385. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei7 – 3125Missing in isoform 3. 1 PublicationVSP_044803Add
    BLAST
    Alternative sequencei320 – 34122Missing in isoform 2 and isoform 3. 3 PublicationsVSP_004189Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS47820.1. [Q08495-2]
    CCDS47821.1. [Q08495-3]
    CCDS6020.1. [Q08495-1]
    PIRiA48222.
    I39062.
    RefSeqiNP_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]
    UniGeneiHs.106124.

    Genome annotation databases

    EnsembliENST00000265800; 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]
    GeneIDi2039.
    KEGGihsa:2039.
    UCSCiuc022asq.1. human. [Q08495-2]
    uc022asr.1. human. [Q08495-1]

    Polymorphism databases

    DMDMi22654240.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS47820.1. [Q08495-2 ]
    CCDS47821.1. [Q08495-3 ]
    CCDS6020.1. [Q08495-1 ]
    PIRi A48222.
    I39062.
    RefSeqi NP_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 ]
    UniGenei Hs.106124.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1QZP NMR - A 342-405 [» ]
    1ZV6 NMR - A 342-405 [» ]
    ProteinModelPortali Q08495.
    SMRi Q08495. Positions 341-405.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108353. 7 interactions.
    IntActi Q08495. 6 interactions.
    MINTi MINT-1390442.
    STRINGi 9606.ENSP00000265800.

    PTM databases

    PhosphoSitei Q08495.

    Polymorphism databases

    DMDMi 22654240.

    Proteomic databases

    MaxQBi Q08495.
    PaxDbi Q08495.
    PRIDEi Q08495.

    Protocols and materials databases

    DNASUi 2039.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265800 ; 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 ]
    GeneIDi 2039.
    KEGGi hsa:2039.
    UCSCi uc022asq.1. human. [Q08495-2 ]
    uc022asr.1. human. [Q08495-1 ]

    Organism-specific databases

    CTDi 2039.
    GeneCardsi GC08P021907.
    HGNCi HGNC:3382. DMTN.
    HPAi HPA024290.
    MIMi 125305. gene.
    neXtProti NX_Q08495.
    PharmGKBi PA27815.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG253396.
    HOGENOMi HOG000285997.
    HOVERGENi HBG031499.
    OMAi WAESRTP.
    PhylomeDBi Q08495.
    TreeFami TF318042.

    Miscellaneous databases

    ChiTaRSi EPB49. human.
    EvolutionaryTracei Q08495.
    GeneWikii EPB49.
    GenomeRNAii 2039.
    NextBioi 8281.
    PROi Q08495.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q08495.
    Bgeei Q08495.
    CleanExi HS_EPB49.
    Genevestigatori Q08495.

    Family and domain databases

    Gene3Di 1.10.950.10. 1 hit.
    InterProi IPR003128. Villin_headpiece.
    [Graphical view ]
    Pfami PF02209. VHP. 1 hit.
    [Graphical view ]
    SMARTi SM00153. VHP. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47050. SSF47050. 1 hit.
    PROSITEi PS51089. HP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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. 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.

    Entry informationi

    Entry nameiDEMA_HUMAN
    AccessioniPrimary (citable) accession number: Q08495
    Secondary accession number(s): A8K0T5
    , B3KP70, B3KRH3, E9PEJ0, Q13215, Q9BRE3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: August 30, 2002
    Last modified: October 1, 2014
    This is version 151 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3