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Domain

Both PH domains are essential for its mitochondrial localization.

Function

Controls the stability of the leptin mRNA harboring an AU-rich element (ARE) in its 3' UTR, in cooperation with the RNA stabilizer ELAVL1 (PubMed:29180010). Decreases the stability of the leptin mRNA by antagonizing the function of ELAVL1 by inducing its atypical recruitment from the nucleus to the cytosol (By similarity). Binds to cardiolipin (CL), phosphatidic acid (PA), phosphatidylinositol 4-phosphate (PtdIns(4)P) and phosphatidylserine (PS) (PubMed:18191643). Promotes apoptosis by enhancing BAX-BAK hetero-oligomerization via interaction with BID in colon cancer cells (By similarity) (PubMed:29531808).

Post-translational modifications

Phosphorylation is essential for its mitochondrial localization and regulates its interaction with C1QBP.

Tissue specificity

Ubiquitous (PubMed:18191643). Epressed in several cancer cell lines of differing origin (PubMed:29531808).

Cellular localization

  • Cell membrane
  • Lipid-anchor
  • Mitochondrion
  • Mitochondrion membrane
  • Interaction with C1QBP and phosphorylation is essential for its mitochondrial localization. Localizes on the microtubule in the form of small granules.

Alternative names

CLPABP, PLEKHN1, Pleckstrin homology domain-containing family N member 1, PH domain-containing family N member 1, Cardiolipin and phosphatidic acid-binding protein

Target type

Proteins

Primary research area

Immunology & Infectious Disease

Molecular weight

66409Da

We found 1 product in 1 category

Proteins & Peptides

Target

Species of origin

Search our catalogue for 'PLEKHN1' (1)

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