Phospho-DMTN (S403) Antibody

1. When unphosphorylated, dematin's two F-actin binding domains move independent of one another permitting them to bind different F-actin filaments. PMID: 23355471
2. the headpiece domain of dematin regulates calcium mobilization and signaling in platelets PMID: 23060452
3. a novel functional role for dematin in regulating erythrocyte membrane function. PMID: 22927433
4. Fast backbone dynamics probed at amide nitrogen versus carbonyl carbon sites for dematin headpiece C-terminal. The reduction of mobility in the loop region upon the S74E mutation can be seen from the (15)N order parameters. PMID: 20396930
5. results suggest that phosphorylation of the dematin headpiece acts as a conformational switch within this headpiece domain PMID: 14660664
6. a crucial role for this proline residue in structural stability and folding potential of HP (sub)domains consistent with Pro-Trp stacking as a more general determinant of protein stability PMID: 16697408
7. study investigated motions in the backbone of dematin headpiece domain and its mutant DHPS74E using several complementary NMR relaxation techniques PMID: 19030997
8. results suggest that the core domain of dematin exhibits properties typical of a natively unfolded protein, while the headpiece domain is folded in a conformation essentially identical to its native structure PMID: 19241372

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HGNC: 3382

OMIM: 125305

KEGG: hsa:2039

STRING: 9606.ENSP00000265800

UniGene: Hs.106124