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Protein

Dematin

Gene

Dmtn

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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 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.3 Publications

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • protein self-association Source: UniProtKB
  • receptor binding Source: UniProtKB
  • spectrin binding Source: UniProtKB

GO - Biological processi

  • actin cytoskeleton organization Source: UniProtKB
  • actin filament bundle assembly Source: UniProtKB
  • actin filament capping Source: UniProtKB-KW
  • actin filament reorganization Source: UniProtKB
  • calcium-mediated signaling using extracellular calcium source Source: UniProtKB
  • calcium-mediated signaling using intracellular calcium source Source: UniProtKB
  • cellular response to calcium ion Source: UniProtKB
  • cellular response to cAMP Source: UniProtKB
  • erythrocyte development Source: UniProtKB
  • negative regulation of cell-substrate adhesion Source: UniProtKB
  • negative regulation of focal adhesion assembly Source: UniProtKB
  • negative regulation of peptidyl-serine phosphorylation Source: UniProtKB
  • negative regulation of peptidyl-threonine phosphorylation Source: UniProtKB
  • negative regulation of peptidyl-tyrosine phosphorylation Source: UniProtKB
  • negative regulation of protein targeting to membrane Source: UniProtKB
  • negative regulation of substrate adhesion-dependent cell spreading Source: UniProtKB
  • positive regulation of blood coagulation Source: UniProtKB
  • positive regulation of fibroblast migration Source: UniProtKB
  • positive regulation of integrin-mediated signaling pathway Source: UniProtKB
  • positive regulation of platelet aggregation Source: UniProtKB
  • positive regulation of substrate adhesion-dependent cell spreading Source: UniProtKB
  • positive regulation of wound healing Source: UniProtKB
  • protein complex assembly Source: UniProtKB
  • protein secretion by platelet Source: UniProtKB
  • regulation of actin cytoskeleton organization Source: UniProtKB
  • regulation of cell shape Source: UniProtKB
  • regulation of filopodium assembly Source: UniProtKB
  • regulation of lamellipodium assembly Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiREACT_297274. Miscellaneous transport and binding events.

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:Epb4.9, Epb49
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:99670. Dmtn.

Subcellular locationi

  • Cytoplasm By similarity
  • Cytoplasmcytosol 1 Publication
  • Cytoplasmperinuclear region 1 Publication
  • Cytoplasmcytoskeleton By similarity
  • Cell membrane By similarity
  • Membrane 1 Publication
  • Endomembrane system By similarity
  • Cell projection 1 Publication

  • 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 (By similarity).By similarity

GO - Cellular componenti

  • actin filament Source: UniProtKB
  • cell projection membrane Source: UniProtKB
  • cortical cytoskeleton Source: MGI
  • cytoplasmic membrane-bounded vesicle Source: UniProtKB
  • cytosol Source: UniProtKB
  • endomembrane system Source: UniProtKB-SubCell
  • membrane Source: MGI
  • neuronal postsynaptic density Source: MGI
  • perinuclear region of cytoplasm Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • platelet dense tubular network membrane Source: UniProtKB
  • spectrin-associated cytoskeleton Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice are viable and born at the expected Mendelian ratio. Adult mice show compensated anemia and display mild microcytosis and spherocytosis. The erythrocyte plasma membrane association with the spectrin-actin skeleton is fragile and mechanically unstable.1 Publication

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 405405DematinPRO_0000218756Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei16 – 161PhosphoserineBy similarity
Modified residuei18 – 181PhosphoserineBy similarity
Modified residuei96 – 961PhosphoserineBy similarity
Modified residuei114 – 1141Phosphothreonine1 Publication
Modified residuei156 – 1561PhosphoserineBy similarity
Modified residuei226 – 2261Phosphoserine2 Publications
Modified residuei289 – 2891PhosphoserineBy similarity
Modified residuei333 – 3331PhosphoserineBy similarity
Modified residuei372 – 3721Phosphoserine1 Publication
Modified residuei403 – 4031Phosphoserine; by PKABy similarity

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 (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiQ9WV69.
PaxDbiQ9WV69.
PRIDEiQ9WV69.

PTM databases

PhosphoSiteiQ9WV69.

Expressioni

Tissue specificityi

Expressed in platelets. Isoform 1 and isoform 2 are expressed in mature erythrocytes (at protein level).2 Publications

Gene expression databases

CleanExiMM_EPB4.9.
GenevisibleiQ9WV69. MM.

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 and spectrin. Isoform 2 interacts with SLC2A1 (via C-terminus cytoplasmic region) (By similarity). Interacts with RASGRF2.By similarityCurated2 Publications

Protein-protein interaction databases

BioGridi199464. 1 interaction.
IntActiQ9WV69. 2 interactions.
MINTiMINT-4093018.
STRINGi10090.ENSMUSP00000022694.

Structurei

3D structure databases

ProteinModelPortaliQ9WV69.
SMRiQ9WV69. Positions 341-405.
ModBaseiSearch...
MobiDBiSearch...

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 RASGRF2By similarityAdd
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.
GeneTreeiENSGT00760000119039.
HOGENOMiHOG000285997.
HOVERGENiHBG031499.
InParanoidiQ9WV69.
OMAiWAESRTP.
OrthoDBiEOG7PK90G.
PhylomeDBiQ9WV69.
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 (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9WV69-1) [UniParc]FASTAAdd to basket

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

        10         20         30         40         50
MERLQKQPLT SPGSVSSSRD SSVPGSPSSI VAKMDNQVLG YKDLAAIPKD
60 70 80 90 100
KAILDIERPD LMIYEPHFTY SLLEHVELPR SRECSLSPKS TSPPPSPEVW
110 120 130 140 150
AESRTLGIIS QASTPRTTGT PRTSLPHFHH PETTRPDSNI YKKPPIYKQR
160 170 180 190 200
ESVGGSPQSK HLIEDLIIES SKFPAAQPPD PNQPAKIETD YWPCPPSLAV
210 220 230 240 250
VETEWRKRKA SRKGAEEEEE EEDDDSEEEI KAIRERQKEE LSKVTSNLGK
260 270 280 290 300
MILKEEMEKS LPIRRKTRSL PDRTPFHTSL HSGTSKSSSL PSYGRTTLSR
310 320 330 340 350
LQSTEFSPSG SEAGSPGLQN GEGQRGRMDR GNSLPCVLEQ KIYPYEMLVV
360 370 380 390 400
TNKGRTKLPP GVDRMRLERH LSAEDFSRVF AMSPEEFGKL ALWKRNELKK

KASLF
Length:405
Mass (Da):45,468
Last modified:November 1, 1999 - v1
Checksum:iAECA552500BDD19A
GO
Isoform 2 (identifier: Q9WV69-2) [UniParc]FASTAAdd to basket

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

Show »
Length:383
Mass (Da):43,042
Checksum:iC8F3299489322DF1
GO
Isoform 3 (identifier: Q9WV69-3) [UniParc]FASTAAdd to basket

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

Show »
Length:380
Mass (Da):43,071
Checksum:i27E8E56877D0B310
GO
Isoform 4 (identifier: Q9WV69-4) [UniParc]FASTAAdd to basket

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

Show »
Length:358
Mass (Da):40,644
Checksum:i6EF6B051450E509C
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei7 – 3125Missing in isoform 3 and isoform 4. 2 PublicationsVSP_047491Add
BLAST
Alternative sequencei320 – 34122Missing in isoform 2 and isoform 4. 3 PublicationsVSP_047492Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF079846 mRNA. Translation: AAD34233.1.
AF155547 mRNA. Translation: AAD38412.1.
AK158744 mRNA. Translation: BAE34638.1.
AK162866 mRNA. Translation: BAE37092.1.
AK165294 mRNA. Translation: BAE38123.1.
AC154563 Genomic DNA. No translation available.
BC016897 mRNA. Translation: AAH16897.1.
BC037021 mRNA. Translation: AAH37021.1.
CCDSiCCDS27259.1. [Q9WV69-2]
RefSeqiNP_001239591.1. NM_001252662.1. [Q9WV69-1]
NP_001239592.1. NM_001252663.1. [Q9WV69-2]
NP_001239593.1. NM_001252664.1. [Q9WV69-3]
NP_001239594.1. NM_001252665.1. [Q9WV69-4]
NP_001239595.1. NM_001252666.1. [Q9WV69-4]
NP_038542.1. NM_013514.4. [Q9WV69-2]
XP_006518593.1. XM_006518530.2. [Q9WV69-1]
XP_006518594.1. XM_006518531.1. [Q9WV69-1]
XP_006518595.1. XM_006518532.1. [Q9WV69-1]
XP_006518601.1. XM_006518538.2. [Q9WV69-3]
XP_006518602.1. XM_006518539.1. [Q9WV69-3]
XP_006518603.1. XM_006518540.2. [Q9WV69-3]
XP_006518604.1. XM_006518541.1. [Q9WV69-3]
XP_006518605.1. XM_006518542.2. [Q9WV69-4]
UniGeneiMm.210863.

Genome annotation databases

EnsembliENSMUST00000022694; ENSMUSP00000022694; ENSMUSG00000022099. [Q9WV69-2]
ENSMUST00000022695; ENSMUSP00000022695; ENSMUSG00000022099. [Q9WV69-3]
ENSMUST00000110984; ENSMUSP00000106612; ENSMUSG00000022099. [Q9WV69-2]
GeneIDi13829.
KEGGimmu:13829.
UCSCiuc007uom.2. mouse. [Q9WV69-1]
uc007uon.2. mouse.
uc029sln.1. mouse.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF079846 mRNA. Translation: AAD34233.1.
AF155547 mRNA. Translation: AAD38412.1.
AK158744 mRNA. Translation: BAE34638.1.
AK162866 mRNA. Translation: BAE37092.1.
AK165294 mRNA. Translation: BAE38123.1.
AC154563 Genomic DNA. No translation available.
BC016897 mRNA. Translation: AAH16897.1.
BC037021 mRNA. Translation: AAH37021.1.
CCDSiCCDS27259.1. [Q9WV69-2]
RefSeqiNP_001239591.1. NM_001252662.1. [Q9WV69-1]
NP_001239592.1. NM_001252663.1. [Q9WV69-2]
NP_001239593.1. NM_001252664.1. [Q9WV69-3]
NP_001239594.1. NM_001252665.1. [Q9WV69-4]
NP_001239595.1. NM_001252666.1. [Q9WV69-4]
NP_038542.1. NM_013514.4. [Q9WV69-2]
XP_006518593.1. XM_006518530.2. [Q9WV69-1]
XP_006518594.1. XM_006518531.1. [Q9WV69-1]
XP_006518595.1. XM_006518532.1. [Q9WV69-1]
XP_006518601.1. XM_006518538.2. [Q9WV69-3]
XP_006518602.1. XM_006518539.1. [Q9WV69-3]
XP_006518603.1. XM_006518540.2. [Q9WV69-3]
XP_006518604.1. XM_006518541.1. [Q9WV69-3]
XP_006518605.1. XM_006518542.2. [Q9WV69-4]
UniGeneiMm.210863.

3D structure databases

ProteinModelPortaliQ9WV69.
SMRiQ9WV69. Positions 341-405.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199464. 1 interaction.
IntActiQ9WV69. 2 interactions.
MINTiMINT-4093018.
STRINGi10090.ENSMUSP00000022694.

PTM databases

PhosphoSiteiQ9WV69.

Proteomic databases

MaxQBiQ9WV69.
PaxDbiQ9WV69.
PRIDEiQ9WV69.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022694; ENSMUSP00000022694; ENSMUSG00000022099. [Q9WV69-2]
ENSMUST00000022695; ENSMUSP00000022695; ENSMUSG00000022099. [Q9WV69-3]
ENSMUST00000110984; ENSMUSP00000106612; ENSMUSG00000022099. [Q9WV69-2]
GeneIDi13829.
KEGGimmu:13829.
UCSCiuc007uom.2. mouse. [Q9WV69-1]
uc007uon.2. mouse.
uc029sln.1. mouse.

Organism-specific databases

CTDi2039.
MGIiMGI:99670. Dmtn.

Phylogenomic databases

eggNOGiNOG253396.
GeneTreeiENSGT00760000119039.
HOGENOMiHOG000285997.
HOVERGENiHBG031499.
InParanoidiQ9WV69.
OMAiWAESRTP.
OrthoDBiEOG7PK90G.
PhylomeDBiQ9WV69.
TreeFamiTF318042.

Enzyme and pathway databases

ReactomeiREACT_297274. Miscellaneous transport and binding events.

Miscellaneous databases

NextBioi284636.
PROiQ9WV69.
SOURCEiSearch...

Gene expression databases

CleanExiMM_EPB4.9.
GenevisibleiQ9WV69. MM.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA sequence, genomic structure, and expression of the mouse dematin gene (Epb4.9)."
    Azim A.C., Kim A.C., Lutchman M., Andrabi S., Peters L.L., Chishti A.H.
    Mamm. Genome 10:1026-1029(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    Tissue: Erythrocyte and Spleen.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
    Strain: C57BL/6J.
    Tissue: Hypothalamus, Spleen and Visual cortex.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "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 2 AND 4).
    Strain: FVB/N.
    Tissue: Eye and Kidney.
  5. "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: INTERACTION WITH RASGRF2.
  6. "Headpiece domain of dematin is required for the stability of the erythrocyte membrane."
    Khanna R., Chang S.H., Andrabi S., Azam M., Kim A., Rivera A., Brugnara C., Low P.S., Liu S.C., Chishti A.H.
    Proc. Natl. Acad. Sci. U.S.A. 99:6637-6642(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  8. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-372, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-114 AND SER-226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. "The headpiece domain of dematin regulates cell shape, motility, and wound healing by modulating RhoA activation."
    Mohseni M., Chishti A.H.
    Mol. Cell. Biol. 28:4712-4718(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  11. "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: FUNCTION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiDEMA_MOUSE
AccessioniPrimary (citable) accession number: Q9WV69
Secondary accession number(s): F8WIF9
, Q3TYC5, Q8JZV5, Q9WVM2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: November 1, 1999
Last modified: June 24, 2015
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.