PLEKHN1
entrez
84069
canonical
uniprot
Q494U1
canonical
ensembl
ENSG00000187583
resolver
ensp
ENSP00000368717
resolver
ensp
ENSP00000368719
resolver
ensp
ENSP00000368720
resolver
ensp
ENSP00000550667
resolver
ensp
ENSP00000550668
resolver
ensp
ENSP00000629671
resolver
ensp
ENSP00000629672
resolver
genesymbol
PLEKHN1
resolver
genesymbol_syn
CLPABP
resolver
hgnc
HGNC:25284
resolver
uniprot
Q494U2
resolver
uniprot
Q5SV98
resolver
uniprot
Q9H0M7
resolver
uniprot_entry
PKHN1_HUMAN
resolver
uniprot_sec
Q494U2
resolver
uniprot_sec
Q5SV98
resolver
uniprot_sec
Q9H0M7
resolver
amino_acid_sequence
MGNSHCVPQAPRRLRASFSRKPSLKGNREDSARMSAGLPGPEAARSGDAAANKLFHYIPGTDILDLENQRENLEQPFLSVFKKGRRRVPVRNLGKVVHYAKVQLRFQHSQDVSDCYLELFPAHLYFQAHGSEGLTFQGLLPLTELSVCPLEGSREHAFQITGPLPAPLLVLCPSRAELDRWLYHLEKQTALLGGPRRCHSAPPQRRLTRLRTASGHEPGGSAVCASRVKLQHLPAQEQWDRLLVLYPTSLAIFSEELDGLCFKGELPLRAVHINLEEKEKQIRSFLIEGPLINTIRVVCASYEDYGHWLLCLRAVTHREGAPPLPGAESFPGSQVMGSGRGSLSSGGQTSWDSGCLAPPSTRTSHSLPESSVPSTVGCSSQHTPDQANSDRASIGRRRTELRRSGSSRSPGSKARAEGRGPVTPLHLDLTQLHRLSLESSPDAPDHTSETSHSPLYADPYTPPATSHRRVTDVRGLEEFLSAMQSARGPTPSSPLPSVPVSVPASDPRSCSSGPAGPYLLSKKGALQSRAAQRHRGSAKDGGPQPPDAPQLVSSAREGSPEPWLPLTDGRSPRRSRDPGYDHLWDETLSSSHQKCPQLGGPEASGGLVQWI
uniprot
proteins
function
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 heterooligomerization via interaction with BID in colon cancer cells (By similarity) (PubMed:29531808). {ECO:0000250|UniProtKB:Q8C886, ECO:0000269|PubMed:18191643, ECO:0000269|PubMed:29180010, ECO:0000269|PubMed:29531808}.
uniprot
proteins
mass_dalton
66409
uniprot
proteins
mutagenesis
MUTAGEN 2; /note="G->A: Loss of myristoylation, reduced protein stability, morphological alterations in mitochondria but no effect on its mitochondrial localization. Loss of cell membrane localization leading to localization to intracellular organelles."; /evidence="ECO:0000269|PubMed:25043870, ECO:0000269|PubMed:29180010"; MUTAGEN 302; /note="Y->F: Loss of phosphorylation and interaction with C1QBP; when associated with F-456."; /evidence="ECO:0000269|PubMed:18191643"; MUTAGEN 456; /note="Y->F: Loss of phosphorylation and interaction with C1QBP; when associated with F-302."; /evidence="ECO:0000269|PubMed:18191643
uniprot
proteins
post_translational_modification
PTM: Phosphorylation is essential for its mitochondrial localization and regulates its interaction with C1QBP. {ECO:0000269|PubMed:18191643}.
uniprot
proteins
pubmed
11230166
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
18191643
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
25043870
uniprot
proteins
pubmed
27616329
uniprot
proteins
pubmed
29180010
uniprot
proteins
pubmed
29531808
uniprot
proteins
sequence_length
611
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25043870}; Lipid-anchor {ECO:0000269|PubMed:25043870}. Mitochondrion {ECO:0000269|PubMed:27616329, ECO:0000269|PubMed:29531808}. Mitochondrion membrane {ECO:0000269|PubMed:18191643, ECO:0000269|PubMed:29180010}. Note=Interaction with C1QBP and phosphorylation is essential for its mitochondrial localization. Localizes on the microtubule in the form of small granules. {ECO:0000269|PubMed:18191643}.
uniprot
proteins