DMTN
entrez
2039
canonical
uniprot
Q08495
canonical
ensembl
ENSG00000158856
resolver
ensp
ENSP00000265800
resolver
ensp
ENSP00000350977
resolver
ensp
ENSP00000370879
resolver
ensp
ENSP00000397904
resolver
ensp
ENSP00000401291
resolver
ensp
ENSP00000416111
resolver
ensp
ENSP00000427866
resolver
ensp
ENSP00000429234
resolver
ensp
ENSP00000429377
resolver
ensp
ENSP00000430609
resolver
ensp
ENSP00000430618
resolver
genesymbol
DMTN
resolver
genesymbol_syn
DMT
resolver
genesymbol_syn
EPB49
resolver
hgnc
HGNC:3382
resolver
uniprot
A8K0T5
resolver
uniprot
B3KP70
resolver
uniprot
B3KRH3
resolver
uniprot
B4DI75
resolver
uniprot
E9PEJ0
resolver
uniprot
Q13215
resolver
uniprot
Q9BRE3
resolver
uniprot_entry
DEMA_HUMAN
resolver
uniprot_sec
A8K0T5
resolver
uniprot_sec
B3KP70
resolver
uniprot_sec
B3KRH3
resolver
uniprot_sec
B4DI75
resolver
uniprot_sec
E9PEJ0
resolver
uniprot_sec
Q13215
resolver
uniprot_sec
Q9BRE3
resolver
amino_acid_sequence
MERLQKQPLTSPGSVSPSRDSSVPGSPSSIVAKMDNQVLGYKDLAAIPKDKAILDIERPDLMIYEPHFTYSLLEHVELPRSRERSLSPKSTSPPPSPEVWADSRSPGIISQASAPRTTGTPRTSLPHFHHPETSRPDSNIYKKPPIYKQRESVGGSPQTKHLIEDLIIESSKFPAAQPPDPNQPAKIETDYWPCPPSLAVVETEWRKRKASRRGAEEEEEEEDDDSGEEMKALRERQREELSKVTSNLGKMILKEEMEKSLPIRRKTRSLPDRTPFHTSLHQGTSKSSSLPAYGRTTLSRLQSTEFSPSGSETGSPGLQNGEGQRGRMDRGNSLPCVLEQKIYPYEMLVVTNKGRTKLPPGVDRMRLERHLSAEDFSRVFAMSPEEFGKLALWKRNELKKKASLF
uniprot
proteins
function
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. Also plays a role as a modulator of actin dynamics in fibroblasts; acts as a negative regulator of the RhoA activation pathway. In platelets, functions as a regulator of internal calcium mobilization across the dense tubular system that affects platelet granule secretion pathways and aggregation. Also required for the formation of a diverse set of cell protrusions, such as filopodia and lamellipodia, necessary for platelet cell spreading, motility and migration. Acts as a tumor suppressor and inhibits malignant cell transformation. {ECO:0000269|PubMed:10565303, ECO:0000269|PubMed:11856323, ECO:0000269|PubMed:18347014, ECO:0000269|PubMed:19241372, ECO:0000269|PubMed:22927433, ECO:0000269|PubMed:23355471}.
uniprot
proteins
mass_dalton
45514
uniprot
proteins
mutagenesis
MUTAGEN 124; /note="S->A: Reduces interaction with plasmodium berghei 14-3-3 protein. Inhibits phosphorylation and interaction with plasmodium berghei 14-3-3 protein; when associated with A-333 and A-403."; /evidence="ECO:0000269|PubMed:21084299"; MUTAGEN 333; /note="S->A: Reduces interaction with plasmodium berghei 14-3-3 protein. Inhibits phosphorylation and interaction with plasmodium berghei 14-3-3 protein; when associated with A-124 and A-403."; /evidence="ECO:0000269|PubMed:21084299"; MUTAGEN 403; /note="S->A: Inhibits phosphorylation and interaction with plasmodium berghei 14-3-3 protein; when associated with A-124 and A-333."; /evidence="ECO:0000269|PubMed:21084299, ECO:0000269|PubMed:23355471"; MUTAGEN 403; /note="S->E: Reduces F-actin bundling but not F-actin binding activity."; /evidence="ECO:0000269|PubMed:21084299, ECO:0000269|PubMed:23355471
uniprot
proteins
post_translational_modification
PTM: Phosphorylated. Phosphorylation at Ser-403 by PKA causes the C-terminal headpiece domain to associate with the N-terminal core domain, and leads to the inhibition of its actin bundling activity. {ECO:0000269|PubMed:16472756, ECO:0000269|PubMed:22927433, ECO:0000269|PubMed:23355471, ECO:0000269|PubMed:7615546}.; PTM: The N-terminus is blocked.
uniprot
proteins
protein_family
Villin/gelsolin family
uniprot
proteins
pubmed
10565303
uniprot
proteins
pubmed
11856323
uniprot
proteins
pubmed
14660664
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16421571
uniprot
proteins
pubmed
16472756
uniprot
proteins
pubmed
18088087
uniprot
proteins
pubmed
18318008
uniprot
proteins
pubmed
18347014
uniprot
proteins
pubmed
19241372
uniprot
proteins
pubmed
19367720
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21084299
uniprot
proteins
pubmed
22927433
uniprot
proteins
pubmed
23060452
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23355471
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
7615546
uniprot
proteins
pubmed
8341682
uniprot
proteins
sequence_length
405
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytosol. Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, cytoskeleton. Cell membrane. Membrane {ECO:0000250}. Endomembrane system. Cell projection {ECO:0000250}. Note=Localized at the spectrin-actin junction of erythrocyte plasma membrane. Localized to intracellular membranes and the cytoskeletal network. Localized at intracellular membrane-bounded organelle compartment in platelets that likely represent the dense tubular network membrane. Detected at the cell membrane and at the parasitophorous vacuole in malaria-infected erythrocytes at late stages of plasmodium berghei or falciparum development.
uniprot
proteins