LPIN1
entrez
23175
canonical
uniprot
Q14693
canonical
ensembl
ENSG00000134324
resolver
ensp
ENSP00000256720
resolver
ensp
ENSP00000397908
resolver
ensp
ENSP00000401522
resolver
ensp
ENSP00000501331
resolver
ensp
ENSP00000522487
resolver
ensp
ENSP00000522488
resolver
ensp
ENSP00000522489
resolver
ensp
ENSP00000522499
resolver
ensp
ENSP00000631888
resolver
genesymbol
LPIN1
resolver
genesymbol_syn
KIAA0188
resolver
hgnc
HGNC:13345
resolver
uniprot
A8MU38
resolver
uniprot
B4DET9
resolver
uniprot
B4DGS4
resolver
uniprot
B4DGZ6
resolver
uniprot
B5MC18
resolver
uniprot
B7Z858
resolver
uniprot
D6W506
resolver
uniprot
E7ESE7
resolver
uniprot
F5GY24
resolver
uniprot
Q53T25
resolver
uniprot_entry
LPIN1_HUMAN
resolver
uniprot_sec
A8MU38
resolver
uniprot_sec
B4DET9
resolver
uniprot_sec
B4DGS4
resolver
uniprot_sec
B4DGZ6
resolver
uniprot_sec
B5MC18
resolver
uniprot_sec
B7Z858
resolver
uniprot_sec
D6W506
resolver
uniprot_sec
E7ESE7
resolver
uniprot_sec
F5GY24
resolver
uniprot_sec
Q53T25
resolver
activity_regulation
ACTIVITY REGULATION: Potently inhibited by sphingolipids, in particular, the sphingoid bases sphinganine and sphingosine and ceramide-1-phosphate. Inhibited by concentrations of Mg(2+) and Mn(2+) above their optimums and by Ca(2+), Zn(2+), N-ethylmaleimide and propranolol. {ECO:0000269|PubMed:20231281}.; ACTIVITY REGULATION: [Isoform 1]: Sertraline and propanolol inhibit activity in dose-dependent manners with IC(50) values of 103 uM and 226 uM, respectively. {ECO:0000269|PubMed:39577771}.; ACTIVITY REGULATION: [Isoform 3]: Sertraline and propanolol inhibit activity in dose-dependent manners with IC(50) values of 108 uM and 271 uM, respectively. {ECO:0000269|PubMed:39577771}.; ACTIVITY REGULATION: [Isoform 4]: Sertraline and propanolol inhibit activity in dose-dependent manners with IC(50) values of 143 uM and 227 uM, respectively. {ECO:0000269|PubMed:39577771}.
uniprot
proteins
amino_acid_sequence
MNYVGQLAGQVFVTVKELYKGLNPATLSGCIDIIVIRQPNGNLQCSPFHVRFGKMGVLRSREKVVDIEINGESVDLHMKLGDNGEAFFVQETDNDQEVIPMHLATSPILSEGASRMECQLKRGSVDRMRGLDPSTPAQVIAPSETPSSSSVVKKRRKRRRKSQLDSLKRDDNMNTSEDEDMFPIEMSSDEAMELLESSRTLPNDIPPFQDDIPEENLSLAVIYPQSASYPNSDREWSPTPSPSGSRPSTPKSDSELVSKSTERTGQKNPEMLWLWGELPQAAKSSSPHKMKESSPLSSRKICDKSHFQAIHSESSDTFSDQSPTLVGGALLDQNKPQTEMQFVNEEDLETLGAAAPLLPMIEELKPPSASVVQTANKTDSPSRKRDKRSRHLGADGVYLDDLTDMDPEVAALYFPKNGDPSGLAKHASDNGARSANQSPQSVGSSGVDSGVESTSDGLRDLPSIAISLCGGLSDHREITKDAFLEQAVSYQQFVDNPAIIDDPNLVVKIGSKYYNWTTAAPLLLAMQAFQKPLPKATVESIMRDKMPKKGGRWWFSWRGRNTTIKEESKPEQCLAGKAHSTGEQPPQLSLATRVKHESSSSDEERAAAKPSNAGHLPLLPNVSYKKTLRLTSEQLKSLKLKNGPNDVVFSVTTQYQGTCRCEGTIYLWNWDDKVIISDIDGTITRSDTLGHILPTLGKDWTHQGIAKLYHKVSQNGYKFLYCSARAIGMADMTRGYLHWVNERGTVLPQGPLLLSPSSLFSALHREVIEKKPEKFKVQCLTDIKNLFFPNTEPFYAAFGNRPADVYSYKQVGVSLNRIFTVNPKGELVQEHAKTNISSYVRLCEVVDHVFPLLKRSHSSDFPCSDTFSNFTFWREPLPPFENQDIHSASA
uniprot
proteins
disease_involvement
DISEASE: Myoglobinuria, acute recurrent, autosomal recessive (ARARM) [MIM:268200]: Recurrent myoglobinuria is characterized by recurrent attacks of rhabdomyolysis (necrosis or disintegration of skeletal muscle) associated with muscle pain and weakness and followed by excretion of myoglobin in the urine. Renal failure may occasionally occur. {ECO:0000269|PubMed:18817903}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.1.3.4
uniprot
proteins
function
FUNCTION: Acts as a magnesium-dependent phosphatidate phosphatase enzyme which catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis and therefore controls the metabolism of fatty acids at different levels (PubMed:20231281, PubMed:23426360, PubMed:29765047, PubMed:31695197). Is involved in adipocyte differentiation (By similarity). Recruited at the mitochondrion outer membrane and is involved in mitochondrial fission by converting phosphatidic acid to diacylglycerol (By similarity). Acts also as nuclear transcriptional coactivator for PPARGC1A/PPARA regulatory pathway to modulate lipid metabolism gene expression (By similarity). {ECO:0000250|UniProtKB:Q91ZP3, ECO:0000269|PubMed:20231281, ECO:0000269|PubMed:23426360, ECO:0000269|PubMed:29765047, ECO:0000269|PubMed:31695197}.
uniprot
proteins
mass_dalton
98664
uniprot
proteins
mutagenesis
MUTAGEN 425; /note="K->R: Decreased acetylation by KAT5."; /evidence="ECO:0000269|PubMed:29765047"; MUTAGEN 595; /note="K->R: Decreased acetylation by KAT5."; /evidence="ECO:0000269|PubMed:29765047
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at multiple sites by mTOR in response to insulin, leading to its inactivation (PubMed:23426360). Phosphorylation does not affect the catalytic activity but regulates the localization (By similarity). Phosphorylation is decreased by epinephrine (By similarity). Dephosphorylated by the CTDNEP1-CNEP1R1 complex (By similarity). Dephosphorylation following mTOR inhibition promotes its activity (PubMed:31695197). {ECO:0000250|UniProtKB:Q91ZP3, ECO:0000269|PubMed:23426360, ECO:0000269|PubMed:31695197}.; PTM: Acetylation at Lys-425 and Lys-595 by KAT5 in response to fatty acids promotes translocation to the endoplasmic reticulum and synthesis of diacylglycerol. {ECO:0000269|PubMed:29765047}.; PTM: Sumoylated. {ECO:0000250|UniProtKB:Q91ZP3}.
uniprot
proteins
protein_family
Lipin family
uniprot
proteins
pubmed
12111372
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
17158099
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18817903
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20231281
uniprot
proteins
pubmed
22134922
uniprot
proteins
pubmed
23426360
uniprot
proteins
pubmed
29765047
uniprot
proteins
pubmed
31695197
uniprot
proteins
pubmed
36443312
uniprot
proteins
pubmed
39577771
uniprot
proteins
pubmed
8724849
uniprot
proteins
sequence_length
890
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:29765047}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:29765047}. Nucleus membrane {ECO:0000250|UniProtKB:Q91ZP3}. Note=Translocates from the cytosol to the endoplasmic reticulum following acetylation by KAT5. {ECO:0000269|PubMed:29765047}.
uniprot
proteins