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Q08495

- DEMA_HUMAN

UniProt

Q08495 - DEMA_HUMAN

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Protein
Dematin
Gene
DMTN, DMT, EPB49
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 cAMP Source: UniProtKB
  8. cellular response to calcium ion 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
Complete GO annotation...

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.3 Publications

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
Complete GO annotation...

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 – 405405Dematin
PRO_0000218755Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei96 – 961Phosphoserine2 Publications
Modified residuei105 – 1051Phosphoserine3 Publications
Modified residuei156 – 1561Phosphoserine1 Publication
Modified residuei226 – 2261Phosphoserine3 Publications
Modified residuei333 – 3331Phosphoserine1 Publication
Modified residuei372 – 3721Phosphoserine1 Publication
Modified residuei403 – 4031Phosphoserine; by PKA3 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.4 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 Inferred. 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 Publications

Protein-protein interaction databases

BioGridi108353. 7 interactions.
IntActiQ08495. 5 interactions.
MINTiMINT-1390442.
STRINGi9606.ENSP00000265800.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiQ08495.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini337 – 40569HP
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni224 – 30885Interaction with RASGRF2
Add
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.

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei7 – 3125Missing in isoform 3.
VSP_044803Add
BLAST
Alternative sequencei320 – 34122Missing in isoform 2 and isoform 3.
VSP_004189Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti81 – 811S → Q in AAA58438. 1 Publication
Sequence conflicti81 – 811S → Q in AAC50223. 1 Publication
Sequence conflicti155 – 1551G → A in BAG52385. 1 Publication
Sequence conflicti292 – 2921A → R in AAA58438. 1 Publication
Sequence conflicti292 – 2921A → R in AAC50223. 1 Publication
Sequence conflicti347 – 3471M → V in AAA58438. 1 Publication
Sequence conflicti380 – 3801F → S in AAA58438. 1 Publication
Sequence conflicti403 – 4031S → P in BAG52385. 1 Publication

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. 5 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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 150 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

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