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Phosphatidate phosphatase LPIN1 (EC 3.1.3.4) (Fatty liver dystrophy protein) (Lipin-1)

 LPIN1_MOUSE             Reviewed;         924 AA.
Q91ZP3; Q9CQI2; Q9JLG6;
10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
31-JAN-2018, entry version 140.
RecName: Full=Phosphatidate phosphatase LPIN1;
EC=3.1.3.4;
AltName: Full=Fatty liver dystrophy protein;
AltName: Full=Lipin-1;
Name=Lpin1; Synonyms=Fld;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 38-50;
301-317; 362-369; 425-459; 570-577; 676-693; 708-732; 769-777;
811-843; 868-888 AND 890-908.
STRAIN=BALB/cJ; TISSUE=Liver;
PubMed=11792863; DOI=10.1073/pnas.022634399;
Huffman T.A., Mothe-Satney I., Lawrence J.C. Jr.;
"Insulin-stimulated phosphorylation of lipin mediated by the mammalian
target of rapamycin.";
Proc. Natl. Acad. Sci. U.S.A. 99:1047-1052(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, AND
VARIANT FLD2J ARG-84.
STRAIN=BALB/cJ;
PubMed=11138012; DOI=10.1038/83685;
Peterfy M., Phan J., Xu P., Reue K.;
"Lipodystrophy in the fld mouse results from mutation of a new gene
encoding a nuclear protein, lipin.";
Nat. Genet. 27:121-124(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Skin, and Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
ALTERNATIVE SPLICING, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=16049017; DOI=10.1074/jbc.M503885200;
Peterfy M., Phan J., Reue K.;
"Alternatively spliced lipin isoforms exhibit distinct expression
pattern, subcellular localization, and role in adipogenesis.";
J. Biol. Chem. 280:32883-32889(2005).
[5]
FUNCTION AS COACTIVATOR, MUTAGENESIS OF ASP-712; ILE-726 AND LEU-727,
INDUCTION, AND INTERACTION WITH PPARGC1A AND PPARA.
PubMed=16950137; DOI=10.1016/j.cmet.2006.08.005;
Finck B.N., Gropler M.C., Chen Z., Leone T.C., Croce M.A.,
Harris T.E., Lawrence J.C. Jr., Kelly D.P.;
"Lipin 1 is an inducible amplifier of the hepatic PGC-1alpha/PPARalpha
regulatory pathway.";
Cell Metab. 4:199-210(2006).
[6]
PROTEIN SEQUENCE OF 103-115, PHOSPHORYLATION AT SER-106; SER-150;
SER-285; SER-287; SER-293; THR-298; SER-328; SER-392; SER-468;
SER-472; SER-483; SER-634; SER-635; SER-921 AND SER-923, SUBCELLULAR
LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17105729; DOI=10.1074/jbc.M609537200;
Harris T.E., Huffman T.A., Chi A., Shabanowitz J., Hunt D.F.,
Kumar A., Lawrence J.C. Jr.;
"Insulin controls subcellular localization and multisite
phosphorylation of the phosphatidic acid phosphatase, lipin 1.";
J. Biol. Chem. 282:277-286(2007).
[7]
CATALYTIC ACTIVITY, TISSUE SPECIFICITY, COFACTOR, AND ENZYME
REGULATION.
PubMed=17158099; DOI=10.1074/jbc.M610745200;
Donkor J., Sariahmetoglu M., Dewald J., Brindley D.N., Reue K.;
"Three mammalian lipins act as phosphatidate phosphatases with
distinct tissue expression patterns.";
J. Biol. Chem. 282:3450-3457(2007).
[8]
SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-106.
PubMed=19717560; DOI=10.1074/jbc.M109.023663;
Donkor J., Zhang P., Wong S., O'Loughlin L., Dewald J., Kok B.P.,
Brindley D.N., Reue K.;
"A conserved serine residue is required for the phosphatidate
phosphatase activity but not the transcriptional coactivator functions
of lipin-1 and lipin-2.";
J. Biol. Chem. 284:29968-29978(2009).
[9]
SUMOYLATION AT LYS-599 AND LYS-629, SUBCELLULAR LOCATION, MUTAGENESIS
OF LYS-599 AND LYS-629, TISSUE SPECIFICITY, AND INTERACTION WITH
MEF2C.
PubMed=19753306; DOI=10.1371/journal.pone.0007031;
Liu G.H., Gerace L.;
"Sumoylation regulates nuclear localization of lipin-1alpha in
neuronal cells.";
PLoS ONE 4:E7031-E7031(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and
Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[11]
FUNCTION (ISOFORM 1), SUBCELLULAR LOCATION (ISOFORM 1), AND
MUTAGENESIS OF ASP-712.
PubMed=21397848; DOI=10.1016/j.devcel.2011.01.004;
Huang H., Gao Q., Peng X., Choi S.Y., Sarma K., Ren H., Morris A.J.,
Frohman M.A.;
"piRNA-associated germline nuage formation and spermatogenesis require
MitoPLD profusogenic mitochondrial-surface lipid signaling.";
Dev. Cell 20:376-387(2011).
[12]
TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND DEPHOSPHORYLATION BY
CTDNEP1.
PubMed=22134922; DOI=10.1074/jbc.M111.324350;
Han S., Bahmanyar S., Zhang P., Grishin N., Oegema K., Crooke R.,
Graham M., Reue K., Dixon J.E., Goodman J.M.;
"Nuclear envelope phosphatase-regulatory subunit 1 (formerly TMEM188)
is the metazoan SPO7 ortholog and functions in the lipin activation
pathway.";
J. Biol. Chem. 287:3123-3137(2012).
-!- FUNCTION: Plays important roles in controlling the metabolism of
fatty acids at different levels. Acts as a magnesium-dependent
phosphatidate phosphatase enzyme which catalyzes the conversion of
phosphatidic acid to diacylglycerol during triglyceride,
phosphatidylcholine and phosphatidylethanolamine biosynthesis.
Acts also as nuclear transcriptional coactivator for
PPARGC1A/PPARA regulatory pathway to modulate lipid metabolism
gene expression. Is involved in adipocyte differentiation. Isoform
1 is recruited at the mitochondrion outer membrane and is involved
in mitochondrial fission by converting phosphatidic acid to
diacylglycerol. {ECO:0000269|PubMed:16950137}.
-!- CATALYTIC ACTIVITY: A 1,2-diacylglycerol 3-phosphate + H(2)O = a
1,2-diacyl-sn-glycerol + phosphate. {ECO:0000269|PubMed:17158099}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:17158099};
-!- ENZYME REGULATION: Inhibited by N-ethylmaleimide treatment.
{ECO:0000269|PubMed:17158099}.
-!- SUBUNIT: Interacts (via LXXIL motif) with PPARA. Interacts with
PPARGC1A. Interaction with PPARA and PPARGC1A leads to the
formation of a complex that modulates gene transcription.
Interacts with MEF2C. {ECO:0000269|PubMed:16950137,
ECO:0000269|PubMed:19753306}.
-!- SUBCELLULAR LOCATION: Isoform 1: Mitochondrion outer membrane
{ECO:0000269|PubMed:21397848}. Cytoplasm
{ECO:0000269|PubMed:21397848}. Nucleus membrane
{ECO:0000269|PubMed:21397848}. Note=Recruited at the mitochondrion
outer membrane following phosphatidic acid formation mediated by
PLD6. In neuronals cells, isoform 1 is exclusively cytoplasmic. In
3T3-L1 pre-adipocytes, it primarily located in the cytoplasm.
-!- SUBCELLULAR LOCATION: Isoform 2: Nucleus. Cytoplasm. Endoplasmic
reticulum membrane. Note=Nuclear localization requires both
CNEP1R1 and CTDNEP1. In neuronals cells, localized in both the
cytoplasm and the nucleus. In 3T3-L1 pre-adipocytes, it is
predominantly nuclear.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Lipin-beta;
IsoId=Q91ZP3-1; Sequence=Displayed;
Name=2; Synonyms=Lipin-alpha;
IsoId=Q91ZP3-2; Sequence=VSP_003134;
Note=Mutagenesis of 724:Ser->Leu abolishes phosphatidate
phosphatase activity but does not prevent membrane association.;
-!- TISSUE SPECIFICITY: Specifically expressed in skeletal muscle.
Also expressed prominently in adipose tissue, and testis. Lower
expression also detected in kidney, lung, brain and liver. Isoform
1 is the predominant isoform in the liver. Isoform 2 is the major
form in the brain. {ECO:0000269|PubMed:16049017,
ECO:0000269|PubMed:17158099, ECO:0000269|PubMed:19753306,
ECO:0000269|PubMed:22134922}.
-!- INDUCTION: By fasting, glucocorticoids and diabetes in the liver
in a PPARGC1A-dependent manner. Up-regulated during
differentiation of 3T3-L1 pre-adipocytes.
{ECO:0000269|PubMed:16950137}.
-!- DOMAIN: Contains one Asp-Xaa-Asp-Xaa-Thr (DXDXT) motif, a
catalytic motif essential for phosphatidate phosphatase activity.
-!- DOMAIN: Contains one Leu-Xaa-Xaa-Ile-Leu (LXXIL), a
transcriptional binding motif, which mediates interaction with
PPARA.
-!- PTM: Phosphorylated at multiple sites in response to insulin.
Phosphorylation is controlled by the mTOR signaling pathway.
Phosphorylation is decreased by epinephrine. Phosphorylation may
not directly affect the catalytic activity but may regulate the
localization. Dephosphorylated by the CTDNEP1-CNEP1R1 complex.
{ECO:0000269|PubMed:17105729}.
-!- PTM: Sumoylation is important in brain and is marginal in other
tissues. Sumoylation facilitates nuclear localization of isoform 2
in neuronals cells and its transcriptional coactivator activity.
{ECO:0000269|PubMed:19753306}.
-!- DISEASE: Note=Defects in Lpin1 are the cause of the fatty liver
dystrophy phenotype (fld). Fld mutant mices are characterized by
neonatal fatty liver and hypertriglyceridemia that resolve at
weaning, and neuropathy affecting peripheral nerve in adulthood.
Adipose tissue deficiency, glucose intolerance and increased
susceptibility to atherosclerosis are associated with this
mutation too. Two independent mutant alleles are characterized in
this phenotype, fld and fld2j.
-!- SIMILARITY: Belongs to the lipin family. {ECO:0000305}.
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EMBL; AF412811; AAL07798.1; -; mRNA.
EMBL; AF180471; AAF44296.1; -; mRNA.
EMBL; AK019539; BAB31786.1; -; mRNA.
EMBL; AK014526; BAB29412.1; -; mRNA.
CCDS; CCDS25822.1; -. [Q91ZP3-1]
CCDS; CCDS25823.1; -. [Q91ZP3-2]
RefSeq; NP_001123884.1; NM_001130412.1.
RefSeq; NP_056578.2; NM_015763.4.
RefSeq; NP_766538.2; NM_172950.3.
RefSeq; XP_006515051.1; XM_006514988.3.
UniGene; Mm.153625; -.
ProteinModelPortal; Q91ZP3; -.
BioGrid; 199700; 1.
IntAct; Q91ZP3; 3.
MINT; MINT-4610704; -.
STRING; 10090.ENSMUSP00000070583; -.
SwissLipids; SLP:000000601; -.
iPTMnet; Q91ZP3; -.
PhosphoSitePlus; Q91ZP3; -.
PaxDb; Q91ZP3; -.
PRIDE; Q91ZP3; -.
GeneID; 14245; -.
KEGG; mmu:14245; -.
UCSC; uc007nbs.2; mouse. [Q91ZP3-1]
CTD; 23175; -.
MGI; MGI:1891340; Lpin1.
eggNOG; KOG2116; Eukaryota.
eggNOG; COG5083; LUCA.
HOGENOM; HOG000230954; -.
HOVERGEN; HBG052338; -.
InParanoid; Q91ZP3; -.
KO; K15728; -.
PhylomeDB; Q91ZP3; -.
TreeFam; TF314095; -.
BRENDA; 3.1.3.4; 3474.
ChiTaRS; Lpin1; mouse.
PRO; PR:Q91ZP3; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_LPIN1; -.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005667; C:transcription factor complex; IDA:MGI.
GO; GO:0042826; F:histone deacetylase binding; IDA:MGI.
GO; GO:0042975; F:peroxisome proliferator activated receptor binding; IPI:UniProtKB.
GO; GO:0008195; F:phosphatidate phosphatase activity; IDA:UniProtKB.
GO; GO:0001085; F:RNA polymerase II transcription factor binding; IDA:MGI.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0031532; P:actin cytoskeleton reorganization; IMP:MGI.
GO; GO:0032869; P:cellular response to insulin stimulus; IMP:MGI.
GO; GO:0045444; P:fat cell differentiation; NAS:UniProtKB.
GO; GO:0009062; P:fatty acid catabolic process; IDA:UniProtKB.
GO; GO:0006629; P:lipid metabolic process; IMP:MGI.
GO; GO:0000266; P:mitochondrial fission; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IGI:MGI.
GO; GO:0031065; P:positive regulation of histone deacetylation; IMP:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0045598; P:regulation of fat cell differentiation; IMP:MGI.
GO; GO:0031529; P:ruffle organization; IMP:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0019432; P:triglyceride biosynthetic process; IBA:GO_Central.
GO; GO:0006642; P:triglyceride mobilization; IDA:UniProtKB.
Gene3D; 3.40.50.1000; -; 1.
InterPro; IPR036412; HAD-like_sf.
InterPro; IPR023214; HAD_sf.
InterPro; IPR031703; Lipin_mid.
InterPro; IPR007651; Lipin_N.
InterPro; IPR013209; LNS2.
InterPro; IPR031315; LNS2/PITP.
InterPro; IPR028794; LPIN1.
PANTHER; PTHR12181:SF10; PTHR12181:SF10; 1.
Pfam; PF16876; Lipin_mid; 1.
Pfam; PF04571; Lipin_N; 1.
Pfam; PF08235; LNS2; 1.
SMART; SM00775; LNS2; 1.
SUPFAM; SSF56784; SSF56784; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm;
Direct protein sequencing; Disease mutation; Endoplasmic reticulum;
Hydrolase; Isopeptide bond; Membrane; Mitochondrion;
Mitochondrion outer membrane; Nucleus; Phosphoprotein;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1 924 Phosphatidate phosphatase LPIN1.
/FTId=PRO_0000209880.
REGION 1 108 N-LIP.
REGION 658 864 C-LIP.
MOTIF 153 158 Nuclear localization signal.
{ECO:0000255}.
MOTIF 712 716 DXDXT motif.
MOTIF 723 727 LXXIL motif.
COMPBIAS 632 635 Poly-Ser.
MOD_RES 106 106 Phosphoserine.
{ECO:0000269|PubMed:17105729}.
MOD_RES 150 150 Phosphoserine.
{ECO:0000269|PubMed:17105729}.
MOD_RES 285 285 Phosphoserine.
{ECO:0000269|PubMed:17105729}.
MOD_RES 287 287 Phosphoserine.
{ECO:0000269|PubMed:17105729}.
MOD_RES 293 293 Phosphoserine.
{ECO:0000269|PubMed:17105729}.
MOD_RES 298 298 Phosphothreonine.
{ECO:0000269|PubMed:17105729}.
MOD_RES 328 328 Phosphoserine.
{ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:17105729}.
MOD_RES 392 392 Phosphoserine.
{ECO:0000269|PubMed:17105729}.
MOD_RES 468 468 Phosphoserine.
{ECO:0000269|PubMed:17105729}.
MOD_RES 472 472 Phosphoserine.
{ECO:0000269|PubMed:17105729}.
MOD_RES 483 483 Phosphoserine.
{ECO:0000269|PubMed:17105729}.
MOD_RES 634 634 Phosphoserine.
{ECO:0000269|PubMed:17105729}.
MOD_RES 635 635 Phosphoserine.
{ECO:0000269|PubMed:17105729}.
MOD_RES 921 921 Phosphoserine.
{ECO:0000269|PubMed:17105729}.
MOD_RES 923 923 Phosphoserine.
{ECO:0000269|PubMed:17105729}.
CROSSLNK 599 599 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:19753306}.
CROSSLNK 629 629 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:19753306}.
VAR_SEQ 241 273 Missing (in isoform 2).
{ECO:0000303|PubMed:11138012}.
/FTId=VSP_003134.
VARIANT 84 84 G -> R (in allele FLD2J).
{ECO:0000269|PubMed:11138012}.
MUTAGEN 106 106 S->A: Abolishes phosphorylation in
response to insulin but has no effect on
cellular location.
{ECO:0000269|PubMed:19717560}.
MUTAGEN 599 599 K->R: Reduces sumoylation. Abolishes
sumoylation and nuclear localization;
when associated with R-629.
{ECO:0000269|PubMed:19753306}.
MUTAGEN 629 629 K->R: Reduces sumoylation. Abolishes
sumoylation and nuclear localization;
when associated with R-599.
{ECO:0000269|PubMed:19753306}.
MUTAGEN 712 712 D->A,E: Abolishes phosphatidate
phosphatase activity. No effect on
interaction or coactivation with PPARA.
{ECO:0000269|PubMed:16950137,
ECO:0000269|PubMed:21397848}.
MUTAGEN 726 726 I->F: Diminishes significantly the
interaction and coactivation OF PPARA;
when associated with F-727.
{ECO:0000269|PubMed:16950137}.
MUTAGEN 727 727 L->F: Diminishes significantly the
interaction and coactivation OF PPARA;
when associated with F-726.
{ECO:0000269|PubMed:16950137}.
CONFLICT 175 175 S -> T (in Ref. 3; BAB31786/BAB29412).
{ECO:0000305}.
CONFLICT 223 223 H -> Y (in Ref. 3; BAB31786/BAB29412).
{ECO:0000305}.
CONFLICT 465 465 G -> V (in Ref. 2; AAF44296).
{ECO:0000305}.
SEQUENCE 924 AA; 102002 MW; 175F90E9159A216A CRC64;
MNYVGQLAGQ VFVTVKELYK GLNPATLSGC IDIIVIRQPN GSLQCSPFHV RFGKMGVLRS
REKVVDIEIN GESVDLHMKL GDNGEAFFVQ ETDNDQEIIP MYLATSPILS EGAARMESQL
KRNSVDRIRC LDPTTAAQGL PPSDTPSTGS LGKKRRKRRR KAQLDNLKRD DNVNSSEDED
MFPIEMSSDE DTAPMDGSRT LPNDVPPFQD DIPKENFPSI STHPQSASYP SSDREWSPSP
SSLVDCQRTP PHLAEGVLSS SCPLQSCHFH ASESPSGSRP STPKSDSELV SKSADRLTPK
NNLEMLWLWG ELPQAAKSSS PHKMKESSPL GSRKTPDKMN FQAIHSESSD TFSDQSPTMA
RGLLIHQSKA QTEMQFVNEE DLESLGAAAP PSPVAEELKA PYPNTAQSSS KTDSPSRKKD
KRSRHLGADG VYLDDLTDMD PEVAALYFPK NGDPGGLPKQ ASDNGARSAN QSPQSVGGSG
IDSGVESTSD SLRDLPSIAI SLCGGLSDHR EITKDAFLEQ AVSYQQFADN PAIIDDPNLV
VKVGNKYYNW TTAAPLLLAM QAFQKPLPKA TVESIMRDKM PKKGGRWWFS WRGRNATIKE
ESKPEQCLTG KGHNTGEQPA QLGLATRIKH ESSSSDEEHA AAKPSGSSHL SLLSNVSYKK
TLRLTSEQLK SLKLKNGPND VVFSVTTQYQ GTCRCEGTIY LWNWDDKVII SDIDGTITRS
DTLGHILPTL GKDWTHQGIA KLYHKVSQNG YKFLYCSARA IGMADMTRGY LHWVNERGTV
LPQGPLLLSP SSLFSALHRE VIEKKPEKFK VQCLTDIKNL FFPNTEPFYA AFGNRPADVY
SYKQVGVSLN RIFTVNPKGE LVQEHAKTNI SSYVRLCEVV DHVFPLLKRS HSCDFPCSDT
FSNFTFWREP LPPFENQDMH SASA


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CSB-EL013062MO Mouse Phosphatidate phosphatase LPIN1(LPIN1) ELISA kit 96T
CSB-EL013062HU Human Phosphatidate phosphatase LPIN1(LPIN1) ELISA kit 96T
SNTA1_BOVIN Human ELISA Kit FOR Phosphatidate phosphatase LPIN1 96T
E0702d Human ELISA Kit FOR Phosphatidate phosphatase LPIN1 96T
DL-LPIN1-Mu Mouse Lipin 1 (LPIN1) ELISA Kit 96T
DL-LPIN1-Ra Rat Lipin 1 (LPIN1) ELISA Kit 96T
E2204c ELISA kit Chicken,FABP1,Fatty acid-binding protein 1,Fatty acid-binding protein, liver,Gallus gallus,L-BABP,LB-FABP,L-FABP,Liver basic FABP,Liver bile acid-binding protein,Liver-type fatty acid-bindi 96T
U2204c CLIA kit Chicken,FABP1,Fatty acid-binding protein 1,Fatty acid-binding protein, liver,Gallus gallus,L-BABP,LB-FABP,L-FABP,Liver basic FABP,Liver bile acid-binding protein,Liver-type fatty acid-bindin 96T
E2204r ELISA kit Fabp1,Fatty acid-binding protein 1,Fatty acid-binding protein, liver,L-FABP,Liver-type fatty acid-binding protein,p14,Rat,Rattus norvegicus,SCP,Squalene- and sterol-carrier protein,Z-protei 96T
U2204r CLIA Fabp1,Fatty acid-binding protein 1,Fatty acid-binding protein, liver,L-FABP,Liver-type fatty acid-binding protein,p14,Rat,Rattus norvegicus,SCP,Squalene- and sterol-carrier protein,Z-protein 96T
U2204r CLIA kit Fabp1,Fatty acid-binding protein 1,Fatty acid-binding protein, liver,L-FABP,Liver-type fatty acid-binding protein,p14,Rat,Rattus norvegicus,SCP,Squalene- and sterol-carrier protein,Z-protein 96T
E2204r ELISA Fabp1,Fatty acid-binding protein 1,Fatty acid-binding protein, liver,L-FABP,Liver-type fatty acid-binding protein,p14,Rat,Rattus norvegicus,SCP,Squalene- and sterol-carrier protein,Z-protein 96T
E2204r Fabp1,Fatty acid-binding protein 1,Fatty acid-binding protein, liver,L-FABP,Liver-type fatty acid-binding protein,p14,Rat,Rattus norvegicus,SCP,Squalene- and sterol-carrier protein,Z-protein
E2204c ELISA Chicken,FABP1,Fatty acid-binding protein 1,Fatty acid-binding protein, liver,Gallus gallus,L-BABP,LB-FABP,L-FABP,Liver basic FABP,Liver bile acid-binding protein,Liver-type fatty acid-binding pr 96T
U2204c CLIA Chicken,FABP1,Fatty acid-binding protein 1,Fatty acid-binding protein, liver,Gallus gallus,L-BABP,LB-FABP,L-FABP,Liver basic FABP,Liver bile acid-binding protein,Liver-type fatty acid-binding pro 96T
E2204h ELISA FABP1,FABPL,Fatty acid-binding protein 1,Fatty acid-binding protein, liver,Homo sapiens,Human,L-FABP,Liver-type fatty acid-binding protein 96T
U2204h CLIA kit FABP1,FABPL,Fatty acid-binding protein 1,Fatty acid-binding protein, liver,Homo sapiens,Human,L-FABP,Liver-type fatty acid-binding protein 96T
E2204h ELISA kit FABP1,FABPL,Fatty acid-binding protein 1,Fatty acid-binding protein, liver,Homo sapiens,Human,L-FABP,Liver-type fatty acid-binding protein 96T
U2204h CLIA FABP1,FABPL,Fatty acid-binding protein 1,Fatty acid-binding protein, liver,Homo sapiens,Human,L-FABP,Liver-type fatty acid-binding protein 96T
E96501Ra ELISA Kit for Lipin 1 (LPIN1) 96T/Kit
E96501Mu ELISA Kit for Lipin 1 (LPIN1) 96T/Kit
LPIN3 LPIN1 Gene lipin 1


 

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