SBF1 binds MTMR2

Stable Identifier
Reaction [binding]
Homo sapiens
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MTMR2 forms a heterodimer with SBF1 (MTMR5), an enzymatically inactive myotubularin family member. The interaction of MTMR2 and SBF1 involves coiled-coil domains of both proteins. SBF1 promotes perinuclear localization of MTMR2 (Kim et al. 2003), presumably to the endoplasmic reticulum(ER) membrane, as both proteins can localize to the ER membrane (Berger et al. 2003, Li et al. 2014).

Literature References
PubMed ID Title Journal Year
25522275 SBF-1 exerts strong anticervical cancer effect through inducing endoplasmic reticulum stress-associated cell death via targeting sarco/endoplasmic reticulum Ca(2+)-ATPase 2

Li, W, Xu, Q, Sun, Y, Gu, Y, Yu, B, Zhang, Q, Shu, Y, Shen, Y, Ouyang, Z, Wu, X, Wu, X, Wang, L

Cell Death Dis 2014
14530412 Membrane association of myotubularin-related protein 2 is mediated by a pleckstrin homology-GRAM domain and a coiled-coil dimerization module

Ban, N, Berger, I, Berger, P, Suter, U, Schaffitzel, C

Proc. Natl. Acad. Sci. U.S.A. 2003
12668758 Regulation of myotubularin-related (MTMR)2 phosphatidylinositol phosphatase by MTMR5, a catalytically inactive phosphatase

Vacratsis, PO, Kim, SA, Firestein, R, Cleary, ML, Dixon, JE

Proc. Natl. Acad. Sci. U.S.A. 2003
Orthologous Events
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